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Conserved domains on  [gi|663856869|ref|NP_001287731|]
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ribosomal protein S6 kinase alpha-4 isoform c [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 10145240)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-364 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 694.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYsPPGSPPPG 351
Cdd:cd05614  241 LLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVY-SPAGTPPS 319
                        330
                 ....*....|...
gi 663856869 352 DPRIFQGYSFVAP 364
Cdd:cd05614  320 GARVFQGYSFIAP 332
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
400-707 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14180:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 309  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14180    4 CYELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQsPGVPM 559
Cdd:cd14180   84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHE-AGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQ-GSRPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14180  162 QTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKEGDFSLEGEAWKGVSEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKR 707
Cdd:cd14180  242 AKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPLMTPDVLESSGPAVRTGVNATFMAFNRGKR 309
 
Name Accession Description Interval E-value
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-364 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 694.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYsPPGSPPPG 351
Cdd:cd05614  241 LLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVY-SPAGTPPS 319
                        330
                 ....*....|...
gi 663856869 352 DPRIFQGYSFVAP 364
Cdd:cd05614  320 GARVFQGYSFIAP 332
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
400-707 0e+00

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14180    4 CYELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQsPGVPM 559
Cdd:cd14180   84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHE-AGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQ-GSRPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14180  162 QTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKEGDFSLEGEAWKGVSEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKR 707
Cdd:cd14180  242 AKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPLMTPDVLESSGPAVRTGVNATFMAFNRGKR 309
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
33-301 2.00e-98

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.84  E-value: 2.00e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869    33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKaalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD---KKTGKLVAIKVIKK---KKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEEKE 192
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   193 RTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILKCSPPFPPR---IGPVA 269
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGK-GYGKAVDIWSLGVILYELLTGKPPFP---GDDQLLELFKKIGKPKPPFPPPewdISPEA 227
                          250       260       270
                   ....*....|....*....|....*....|..
gi 663856869   270 QDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-----TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
32-331 4.78e-90

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 285.94  E-value: 4.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREIL-KMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlteeK 191
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV----P 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:PTZ00263 170 DRTFTLCGTPEYLAPEVIQSK-GHGKAVDWWTMGVLLYEFIAGYPPFFDD----TPFRIYEKILAGRLKFPNWFDGRARD 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:PTZ00263 245 LVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNF 304
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
410-667 2.57e-77

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 249.37  E-value: 2.57e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE----ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:smart00220   7 LGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkkdrERILREIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   486 EHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLrpQSPGVPMQTPCFT 565
Cdd:smart00220  86 DLLKKRGRLSEDEARFYLRQILSALEYLH-SKGIVHRDLKPENILLDEDG---HVKLADFGLARQ--LDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqgGQSQAAEIMCKIREGRFSLDGEAWqGVSEEAKELVR 645
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP------GDDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLIR 232
                          250       260
                   ....*....|....*....|..
gi 663856869   646 GLLTVDPAKRLKLEGLRGSSWL 667
Cdd:smart00220 233 KLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
33-301 1.63e-60

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 203.24  E-value: 1.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKE--KIKKKKDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEhlhklgiiyrdlklenvlldseghivltdfglSKEFLTeeke 192
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------------------------------SGSSLT---- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  193 rtfSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcSPPFPPRIGPVAQDL 272
Cdd:pfam00069 119 ---TFVGTPWYMAPEVLGGN-PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYA-FPELPSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....*....
gi 663856869  273 LQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:pfam00069 194 LKKLLKKDPSKRL-----TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-451 6.67e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 182.52  E-value: 6.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRkAALVQRAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDA 109
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARD---LRLGRPVALKVLR-PELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:COG0515   81 RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTGhGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPP----FPPRI 265
Cdd:COG0515  161 TLTQTGTVVGTPGYMAPEQARGEPV-DPRSDVYSLGVTLYELLTGRPPFDGD----SPAELLRAHLREPPPppseLRPDL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 266 GPVAQDLLQRLLCKDPKKRlgagPQGAQEVRNHpffqgLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPP 345
Cdd:COG0515  236 PPALDAIVLRALAKDPEER----YQSAAELAAA-----LRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 346 GSPPPGDPRIFQGYSFVAPSILFDHNNAVMTDGLEAPGAGDRPGRAAVARSAMMQYELDLREPALGQGSFSVCRRCRQRQ 425
Cdd:COG0515  307 AAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALA 386
                        410       420
                 ....*....|....*....|....*.
gi 663856869 426 SGQEFAVKILSRRLEANTQREVAALR 451
Cdd:COG0515  387 AAAAAAAAAAAAALAAAAAAAAAAAA 412
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
410-764 7.76e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 168.27  E-value: 7.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPearerfRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPQSPGVPMQTPC 563
Cdd:COG0515   94 LADLLRRRGPLPPAEALRILAQLAEALAAAHA-AGIVHRDIKPANILLTPD--GR-VKLIDFGIARALGGATLTQTGTVV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEAKEL 643
Cdd:COG0515  170 GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDS-------PAELLRAHLREPPPPPSELRPDLPPALDAI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 644 VRGLLTVDPAKRLK-----LEGLRgSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGFFLKSVENA 718
Cdd:COG0515  243 VLRALAKDPEERYQsaaelAAALR-AVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 719 PLAKRRKQKLRSATASRRGSPAPANPGRAPVASKGAPRRANGPLPP 764
Cdd:COG0515  322 APAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAA 367
Pkinase pfam00069
Protein kinase domain;
410-667 1.94e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 158.95  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR-----LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEkikkkKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  485 LEHIRKKRHFSESEASQILRSLVSAVSfmheeagvvhrdlkpenilyaddtpgapvkiidfgfarlrpqsPGVPMQTPCF 564
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLE-------------------------------------------SGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggQSQAAEIMCKIREGRFsldgeaWQGVSEEAKELV 644
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGN--EIYELIIDQPYAFPEL------PSNLSEEAKDLL 194
                         250       260
                  ....*....|....*....|...
gi 663856869  645 RGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQHPWF 217
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
402-656 3.36e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 136.49  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAA---LRLCQSHPNVVNLHEVHHDQLHTYLVL 476
Cdd:PTZ00263  19 DFEMGE-TLGTGSFGRVRIAKHKGTGEYYAIKCLKKReiLKMKQVQHVAQeksILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSpg 556
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSK-DIIYRDLKPENLLL--DNKGH-VKVTDFGFAKKVPDR-- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 vpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLdgEAWqgV 636
Cdd:PTZ00263 172 --TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDT-------PFRIYEKILAGRLKF--PNW--F 238
                        250       260
                 ....*....|....*....|
gi 663856869 637 SEEAKELVRGLLTVDPAKRL 656
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
431-606 3.41e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.33  E-value: 3.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 431 AVKILSRRLEANT------QREV-AALRLcqSHPNVVNLHEVHHDQLHTYLVlellrggellehIRKKRHFSESEASQIL 503
Cdd:NF033483  36 AVKVLRPDLARDPefvarfRREAqSAASL--SHPNIVSVYDVGEDGGIPYIVmeyvdgrtlkdyIREHGPLSPEEAVEIM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 504 RSLVSAVSFMHeEAGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPQSP--------GvpmqtpcfTLQYAAPElLA 575
Cdd:NF033483 114 IQILSALEHAH-RNGIVHRDIKPQNILITKD--GR-VKVTDFGIARALSSTTmtqtnsvlG--------TVHYLSPE-QA 180
                        170       180       190
                 ....*....|....*....|....*....|..
gi 663856869 576 QQGY-DESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:NF033483 181 RGGTvDARSDIYSLGIVLYEMLTGRPPFDGDS 212
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
141-297 1.17e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 87.16  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 141 YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF----LTEekerTFSFCGTIEYMAPEIIRsktghG 216
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALssttMTQ----TNSVLGTVHYLSPEQAR-----G 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 217 KAV----DWWSLGILLFELLTGASPFTleGErnTQAEVSRRILKCSPPFP----PRIGPVAQDLLQRLLCKDPKKRlgag 288
Cdd:NF033483 183 GTVdarsDIYSLGIVLYEMLTGRPPFD--GD--SPVSVAYKHVQEDPPPPselnPGIPQSLDAVVLKATAKDPDDR---- 254

                 ....*....
gi 663856869 289 PQGAQEVRN 297
Cdd:NF033483 255 YQSAAEMRA 263
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
425-606 8.78e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 65.64  E-value: 8.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   425 QSGQEFAVKILsRRLEANTQREVAALR----LCQ--SHPNVVNL---HEVHHDQLHTylVLELLRGGELLEHIRKKRHFS 495
Cdd:TIGR03903    1 MTGHEVAIKLL-RTDAPEEEHQRARFRretaLCArlYHPNIVALldsGEAPPGLLFA--VFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   496 ESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYA--DDTPGApvKIIDFGFARLRPQSPGVPMQTPCFTL------Q 567
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAHN-QGIVHRDLKPQNIMVSqtGVRPHA--KVLDFGIGTLLPGVRDADVATLTRTTevlgtpT 154
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 663856869   568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:TIGR03903  155 YCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGAS 193
 
Name Accession Description Interval E-value
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-364 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 694.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYsPPGSPPPG 351
Cdd:cd05614  241 LLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVY-SPAGTPPS 319
                        330
                 ....*....|...
gi 663856869 352 DPRIFQGYSFVAP 364
Cdd:cd05614  320 GARVFQGYSFIAP 332
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
400-707 0e+00

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14180    4 CYELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQsPGVPM 559
Cdd:cd14180   84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHE-AGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQ-GSRPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14180  162 QTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKEGDFSLEGEAWKGVSEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKR 707
Cdd:cd14180  242 AKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPLMTPDVLESSGPAVRTGVNATFMAFNRGKR 309
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-304 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 576.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd05583    1 VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIVQKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSF 197
Cdd:cd05583   81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKT-GHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05583  161 CGTIEYMAPEVVRGGSdGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSAEAKDFILKL 240
                        250       260
                 ....*....|....*....|....*...
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGL 304
Cdd:cd05583  241 LEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
400-710 0e+00

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 529.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLeaNTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14092    4 NYELDLREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL--DTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVMELL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSpgVPM 559
Cdd:cd14092   82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMH-SKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKPEN--QPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQ----QGYDESCDLWSLGVILYMMLSGQVPFQGASgqgGQSQAAEIMCKIREGRFSLDGEAWQG 635
Cdd:cd14092  159 KTPCFTLPYAAPEVLKQalstQGYDESCDLWSLGVILYTMLSGQVPFQSPS---RNESAAEIMKRIKSGDFSFDGEEWKN 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGF 710
Cdd:cd14092  236 VSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTPLMTPGVLSSSAAAVSTALRATFDAFHLAFREGF 310
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-320 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 526.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd05613   81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIR-SKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05613  161 ERAYSFCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05613  241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
399-707 7.83e-156

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 455.27  E-value: 7.83e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 399 MQYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14179    4 QHYELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSpGVP 558
Cdd:cd14179   84 LKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHD-VGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPD-NQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSE 638
Cdd:cd14179  162 LKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKKIKQGDFSFEGEAWKNVSQ 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKR 707
Cdd:cd14179  242 EAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGASVHTCVKATFHAFNKYKR 310
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
36-364 3.03e-149

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 438.76  E-value: 3.03e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAERNILEAVKH-PFIVDLHYAFQTGGKLYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEKERTF 195
Cdd:cd05584   80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESI-HDGTVTH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTqaevSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05584  159 TFCGTIEYMAPEIL-TRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKT----IDKILKGKLNLPPYLTNEARDLLKK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 276 LLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPV-YSPPGSPPPGDPR 354
Cdd:cd05584  234 LLKRNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVdSPDDSTLSESANQ 313
                        330
                 ....*....|
gi 663856869 355 IFQGYSFVAP 364
Cdd:cd05584  314 VFQGFTYVAP 323
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
39-301 3.08e-137

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 404.98  E-value: 3.08e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd05123    1 LGKGSFGKVLLVRKK---DTGKLYAMKVLRKKEIIKR-KEVEHTLNERNILERVNH-PFIVKLHYAFQTEEKLYLVLDYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEKERTFSFC 198
Cdd:cd05123   76 PGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELS-SDGDRTYTFC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 199 GTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLC 278
Cdd:cd05123  155 GTPEYLAPEVLLGK-GYGKAVDWWSLGVLLYEMLTGKPPFYAE----NRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQ 229
                        250       260
                 ....*....|....*....|...
gi 663856869 279 KDPKKRLGAGpqGAQEVRNHPFF 301
Cdd:cd05123  230 KDPTKRLGSG--GAEEIKAHPFF 250
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
37-362 9.14e-124

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 372.89  E-value: 9.14e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05582    1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATL--KVRDRVRTKMERDILADVNH-PFIVKLHYAFQTEGKLYLILD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKeRTFS 196
Cdd:cd05582   78 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEK-KAYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEvsrrILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05582  157 FCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTM----ILKAKLGMPQFLSPEAQSLLRAL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPPGSPPPGDPRIF 356
Cdd:cd05582  232 FKRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLF 311

                 ....*.
gi 663856869 357 QGYSFV 362
Cdd:cd05582  312 RGFSFV 317
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
37-341 9.59e-122

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 367.70  E-value: 9.59e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05570    1 KVLGKGSFGKVMLAERKK---TDELYAIKVLKKEVIIEDDDV-ECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTeEKERTFS 196
Cdd:cd05570   77 YVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIW-GGNTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGErnTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05570  156 FCGTPDYIAPEILREQD-YGFSVDWWALGVLLYEMLAGQSPF--EGD--DEDELFEAILNDEVLYPRWLSREAVSILKGL 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPV 341
Cdd:cd05570  231 LTKDPARRLGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPR 295
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
31-331 5.25e-121

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 364.59  E-value: 5.25e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVqRAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDAK 110
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKH---KDSGKYYALKILKKAKII-KLKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltee 190
Cdd:cd05580   76 LYMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQaevsRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05580  152 KDRTYTLCGTPEYLAPEIILSK-GHGKAVDWWALGILIYEMLAGYPPFFDENPMKIY----EKILEGKIRFPSFFDPDAK 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05580  227 DLIKRLLVVDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNF 287
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
37-362 8.48e-113

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 344.69  E-value: 8.48e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRkaggHDA-GKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd05575    1 KVIGKGSFGKVLLAR----HKAeGKLYAVKVLQKKAILKR-NEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEKERTF 195
Cdd:cd05575   76 DYVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGI-EPSDTTS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTqAEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05575  155 TFCGTPEYLAPEVLR-KQPYDRTVDWWCLGAVLYEMLYGLPPFY---SRDT-AEMYDNILHKPLRLRTNVSPSARDLLEG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 276 LLCKDPKKRLGAGpQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPV---------YSPPG 346
Cdd:cd05575  230 LLQKDRTKRLGSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTR-EPVpasvgksadSVAVS 307
                        330
                 ....*....|....*.
gi 663856869 347 SPPPGDPRIFQGYSFV 362
Cdd:cd05575  308 ASVQEADNAFDGFSYV 323
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
37-341 1.92e-111

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 341.26  E-value: 1.92e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05571    1 KVLGKGTFGKVILCRE---KATGELYAIKILKKEVIIAKDEV-AHTLTENRVLQNTRH-PFLTSLKYSFQTNDRLCFVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTeEKERTFS 196
Cdd:cd05571   76 YVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEIS-YGATTKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTlegerNTQAEV-SRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05571  155 FCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFY-----NRDHEVlFELILMEEVRFPSTLSPEAKSLLAG 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 276 LLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPV 341
Cdd:cd05571  229 LLKKDPKKRLGGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTA-ESV 293
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
33-301 2.00e-98

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.84  E-value: 2.00e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869    33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKaalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD---KKTGKLVAIKVIKK---KKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEEKE 192
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   193 RTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILKCSPPFPPR---IGPVA 269
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGK-GYGKAVDIWSLGVILYELLTGKPPFP---GDDQLLELFKKIGKPKPPFPPPewdISPEA 227
                          250       260       270
                   ....*....|....*....|....*....|..
gi 663856869   270 QDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-----TAEEALQHPFF 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
33-327 8.91e-98

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 305.70  E-value: 8.91e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd05574    3 FKKIKLLGKGDVGRVYLVRLKG---TGKLFAMKVLDKEEMIKRNKVK-RVLTEREILATLDH-PFLPTLYASFQTSTHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFtHLYQRQ---YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK----- 184
Cdd:cd05574   78 FVMDYCPGGELF-RLLQKQpgkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 ----------------------EFLTEEK-ERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlE 241
Cdd:cd05574  157 pppvrkslrkgsrrssvksiekETFVAEPsARSNSFVGTEEYIAPEVI-KGDGHGSAVDWWTLGILLYEMLYGTTPF--K 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 242 GErnTQAEVSRRILKCSPPFP--PRIGPVAQDLLQRLLCKDPKKRLGAgPQGAQEVRNHPFFQGLDWVALaaRKIPAPFR 319
Cdd:cd05574  234 GS--NRDETFSNILKKELTFPesPPVSSEAKDLIRKLLVKDPSKRLGS-KRGASEIKRHPFFRGVNWALI--RNMTPPII 308

                 ....*...
gi 663856869 320 PQIRSELD 327
Cdd:cd05574  309 PRPDDPID 316
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
37-364 1.48e-97

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 305.08  E-value: 1.48e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05592    1 KVLGKGSFGKVMLAELKG---TNQYFAIKALKKDVVLEDDDV-ECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfS 196
Cdd:cd05592   77 YLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKAS-T 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05592  156 FCGTPDYIAPEILKGQK-YNQSVDWWSFGVLLYEMLIGQSPFHGEDED----ELFWSICNDTPHYPRWLTKEAASCLSLL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPV--YSPPGSPPPGDPR 354
Cdd:cd05592  231 LERNPEKRLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVltPVDKKLLASMDQE 310
                        330
                 ....*....|
gi 663856869 355 IFQGYSFVAP 364
Cdd:cd05592  311 QFKGFSFTNP 320
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
36-362 4.89e-97

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 303.93  E-value: 4.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKG---TDELYAIKILKKDVIIQDDDV-ECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKErTF 195
Cdd:cd05587   77 EYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKT-TR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05587  156 TFCGTPDYIAPEIIAYQP-YGKSVDWWAYGVLLYEMLAGQPPFDGEDED----ELFQSIMEHNVSYPKSLSKEAVSICKG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 276 LLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVY--SPPGSPPPGDP 353
Cdd:cd05587  231 LLTKHPAKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLtpTDKLVIMNIDQ 310

                 ....*....
gi 663856869 354 RIFQGYSFV 362
Cdd:cd05587  311 SEFEGFSFV 319
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
31-361 8.50e-96

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 300.69  E-value: 8.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRK---KDTGHVYAMKKLRKSEMLEKEQV-AHVRAERDILAEA-DNPWVVKLYYSFQDEEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEE 190
Cdd:cd05599   76 LYLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGL--KK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSP--PFPP--RIG 266
Cdd:cd05599  154 SHLAYSTVGTPDYIAPEVF-LQKGYGKECDWWSLGVIMYEMLIGYPPFCSD----DPQETCRKIMNWREtlVFPPevPIS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 267 PVAQDLLQRLLCkDPKKRLGAGpqGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNFaEEFTRLEPVYSPPG 346
Cdd:cd05599  229 PEAKDLIERLLC-DAEHRLGAN--GVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNF-DEFEEVDLQIPSSP 302
                        330       340
                 ....*....|....*....|.
gi 663856869 347 SPPPGDPRI------FQGYSF 361
Cdd:cd05599  303 EAGKDSKELkskdwvFIGYTY 323
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
31-361 1.09e-95

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 301.51  E-value: 1.09e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRqAPFLVTLHYAFQTDAK 110
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDK---DTGQVYAMKILRKSDMLKREQIA-HVRAERDILADAD-SPWIVRLHYAFQDEDH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF---- 186
Cdd:cd05573   76 LYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnksg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 ------------------------LTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTLEg 242
Cdd:cd05573  156 dresylndsvntlfqdnvlarrrpHKQRRVRAYSAVGTPDYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFPPFYSD- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 243 ernTQAEVSRRIL--KCSPPFP--PRIGPVAQDLLQRLLCkDPKKRLGAgpqgAQEVRNHPFFQGLDWVALaaRKIPAPF 318
Cdd:cd05573  234 ---SLVETYSKIMnwKESLVFPddPDVSPEAIDLIRRLLC-DPEDRLGS----AEEIKAHPFFKGIDWENL--RESPPPF 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 319 RPQIRSELDVGNFaEEFTRLEPVYSPPGSPPPGDPRI----FQGYSF 361
Cdd:cd05573  304 VPELSSPTDTSNF-DDFEDDLLLSEYLSNGSPLLGKGkqlaFVGFTF 349
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
410-666 1.23e-95

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 297.85  E-value: 1.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-----EANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05117    8 LGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlksedEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRpqSPGVPMQTPCF 564
Cdd:cd05117   87 FDRIVKKGSFSEREAAKIMKQILSAVAYLH-SQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIF--EEGEKLKTVCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd05117  164 TPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQ-------ELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd05117  237 KRLLVVDPKKRLTAAEALNHPW 258
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
38-341 4.73e-94

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 295.63  E-value: 4.73e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd05585    1 VIGKGSFGKVMQVRK---KDTSRIYALKTIRKAHIVSRSEV-THTLAERTVLAQV-DCPFIVPLKFSFQSPEKLYLVLAF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEkERTFSF 197
Cdd:cd05585   76 INGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDD-DKTNTF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgerNTQaEVSRRILKCSPPFPPRIGPVAQDLLQRLL 277
Cdd:cd05585  155 CGTPEYLAPELLLGH-GYTKAVDWWTLGVLLYEMLTGLPPFYDE---NTN-EMYRKILQEPLRFPDGFDRDAKDLLIGLL 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 278 CKDPKKRLGAGpqGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPV 341
Cdd:cd05585  230 NRDPTKRLGYN--GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPI 291
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
37-336 4.00e-93

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 293.84  E-value: 4.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05595    1 KLLGKGTFGKVILVREKA---TGRYYAMKILRKEVIIAKDEVA-HTVTESRVLQNTRH-PFLTALKYAFQTHDRLCFVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfS 196
Cdd:cd05595   76 YANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMK-T 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF-TLEGERntqaeVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05595  155 FCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFyNQDHER-----LFELILMEEIRFPRTLSPEAKSLLAG 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 276 LLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFT 336
Cdd:cd05595  229 LLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFT 289
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
42-306 2.30e-92

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 289.89  E-value: 2.30e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  42 GAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYVSGG 121
Cdd:cd05579    4 GAYGRVYLAKK---KSTGDLYAIKVIKKRDMIRKNQV-DSVLAERNILSQA-QNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE------------ 189
Cdd:cd05579   79 DLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRrqiklsiqkksn 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 --EKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFP--PRI 265
Cdd:cd05579  159 gaPEKEDRRIVGTPDYLAPEILLG-QGHGKTVDWWSLGVILYEFLVGIPPF----HAETPEEIFQNILNGKIEWPedPEV 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGAgpQGAQEVRNHPFFQGLDW 306
Cdd:cd05579  234 SDEAKDLISKLLTPDPEKRLGA--KGIEEIKNHPFFKGIDW 272
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
400-703 6.18e-92

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 289.53  E-value: 6.18e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14091    1 EYEI-KEE--IGKGSYSVCKRCIHKATGKEYAVKIIDKS-KRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTpGAP--VKIIDFGFAR-LRPQSpG 556
Cdd:cd14091   77 RGGELLDRILRQKFFSEREASAVMKTLTKTVEYLH-SQGVVHRDLKPSNILYADES-GDPesLRICDFGFAKqLRAEN-G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMqTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgASGQGgqSQAAEIMCKIREGRFSLDGEAWQGV 636
Cdd:cd14091  154 LLM-TPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF--ASGPN--DTPEVILARIGSGKIDLSGGNWDHV 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 637 SEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLEssgpAVRSGLNATFMAFN 703
Cdd:cd14091  229 SDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAA----LVKGAVAATFRAIN 291
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
36-336 9.48e-92

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 290.33  E-value: 9.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRkagGHDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd05604    1 LKVIGKGSFGKVLLAK---RKRDGKYYAVKVLQKKVILNR-KEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTeEKERTF 195
Cdd:cd05604   77 DFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGIS-NSDTTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTqAEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd05604  156 TFCGTPEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPFY---CRDT-AEMYENILHKPLVLRPGISLTAWSILEE 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 276 LLCKDPKKRLGAGpQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFT 336
Cdd:cd05604  231 LLEKDRQLRLGAK-EDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFT 290
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
39-336 6.62e-91

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 288.31  E-value: 6.62e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLE--LVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05586    1 IGKGTFGQVYQVRK---KDTRRIYAMKVLSKKVIVAK-KEVAHTIGERNILVrtALDESPFIVGLKFSFQTPTDLYLVTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKErTFS 196
Cdd:cd05586   77 YMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKT-TNT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEgerNTQaEVSRRILKCSPPFPPR-IGPVAQDLLQR 275
Cdd:cd05586  156 FCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAE---DTQ-QMYRNIAFGKVRFPKDvLSDEGRSFVKG 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 276 LLCKDPKKRLGAgPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFT 336
Cdd:cd05586  232 LLNRNPKHRLGA-HDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFT 291
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
31-333 9.47e-91

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 286.22  E-value: 9.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAALVqRAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDAK 110
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKET---GNYYAMKILDKQKVV-KLKQVEHTLNEKRILQAIN-FPFLVKLEYSFKDNSN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltee 190
Cdd:cd14209   76 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLegerNTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14209  152 KGRTWTLCGTPEYLAPEIILSK-GYNKAVDWWALGVLIYEMAAGYPPFFA----DQPIQIYEKIVSGKVRFPSHFSSDLK 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAE 333
Cdd:cd14209  227 DLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
32-331 4.78e-90

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 285.94  E-value: 4.78e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREIL-KMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlteeK 191
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV----P 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:PTZ00263 170 DRTFTLCGTPEYLAPEVIQSK-GHGKAVDWWTMGVLLYEFIAGYPPFFDD----TPFRIYEKILAGRLKFPNWFDGRARD 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:PTZ00263 245 LVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNF 304
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
33-364 6.27e-90

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 285.35  E-value: 6.27e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLvrkAGGHDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQA--PFLVTLHYAFQTDAK 110
Cdd:cd05589    1 FRCIAVLGRGHFGKVLL---AEYKPTGELFAIKALKKGDIIARDEV-ESLMCEKRIFETVNSArhPFLVNLFACFQTPEH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQrQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEe 190
Cdd:cd05589   77 VCFVMEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGF- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05589  155 GDRTSTFCGTPEFLAPEVL-TDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEE----EVFDSIVNDEVRYPRFLSTEAI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVY---SPPGS 347
Cdd:cd05589  230 SIMRRLLRKNPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLtppKEPRP 309
                        330
                 ....*....|....*..
gi 663856869 348 PPPGDPRIFQGYSFVAP 364
Cdd:cd05589  310 LTEEEQALFKDFDYVAD 326
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
39-306 3.42e-89

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 281.04  E-value: 3.42e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd05572    1 LGVGGFGRVELVQLKS---KGRTFALKCVKKRHIVQT-RQQEHIFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEYC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEEKERTFSFC 198
Cdd:cd05572   76 LGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKL--GSGRKTWTFC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 199 GTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSRRILKCSPP--FPPRIGPVAQDLLQRL 276
Cdd:cd05572  154 GTPEYVAPEIILNK-GYDFSVDYWSLGILLYELLTGRPPFG--GDDEDPMKIYNIILKGIDKieFPKYIDKNAKNLIKQL 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGLDW 306
Cdd:cd05572  231 LRRNPEERLGYLKGGIRDIKKHKWFEGFDW 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
22-336 2.60e-87

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 279.27  E-value: 2.60e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  22 TGHEEKVSVENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQaPFLVTL 101
Cdd:cd05593    6 TTHHKRKTMNDFDYLKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTRH-PFLTSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd05593   81 KYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPF 261
Cdd:cd05593  161 LCKEGITDAATMK-TFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELILMEDIKF 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFT 336
Cdd:cd05593  235 PRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFT 309
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
37-362 4.70e-86

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 275.14  E-value: 4.70e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05591    1 KVLGKGSFGKVMLAERKG---TDEVYAIKVLKKDVILQDDDV-DCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKeRTFS 196
Cdd:cd05591   77 YVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGK-TTTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05591  156 FCGTPDYIAPEILQ-ELEYGPSVDWWALGVLMYEMMAGQPPF----EADNEDDLFESILHDDVLYPVWLSKEAVSILKAF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLG-AGPQGAQE-VRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPPGSPPPGD-- 352
Cdd:cd05591  231 MTKNPAKRLGcVASQGGEDaIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQin 310
                        330
                 ....*....|
gi 663856869 353 PRIFQGYSFV 362
Cdd:cd05591  311 QEEFRGFSFV 320
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
31-331 5.99e-86

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 273.93  E-value: 5.99e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLrKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRIS---EHYYALKVM-AIPEVIRLKQEQHVHNEKRVLKEVSH-PFIIRLFWTEHDQRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltee 190
Cdd:cd05612   76 LYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05612  152 RDRTWTLCGTPEYLAPEVIQSK-GHNKAVDWWALGILIYEMLVGYPPFFDD----NPFGIYEKILAGKLEFPRHLDLYAK 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05612  227 DLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNF 287
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
37-337 6.50e-86

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 274.92  E-value: 6.50e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCD---GKFYAVKVLQKKTILKK-KEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEKERTFS 196
Cdd:cd05603   77 YVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGM-EPEETTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTqAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05603  156 FCGTPEYLAPEVLR-KEPYDRTVDWWCLGAVLYEMLYGLPPFY---SRDV-SQMYDNILHKPLHLPGGKTVAACDLLQGL 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 277 LCKDPKKRLGAGPQgAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTR 337
Cdd:cd05603  231 LHKDQRRRLGAKAD-FLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQ 290
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
37-366 9.12e-86

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 274.48  E-value: 9.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05590    1 RVLGKGSFGKVMLARLK---ESGRLYAVKVLKKDVILQDDDV-ECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKErTFS 196
Cdd:cd05590   77 FVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKT-TST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05590  156 FCGTPDYIAPEILQEML-YGPSVDWWAMGVLLYEMLCGHAPF----EAENEDDLFEAILNDEVVYPTWLSQDAVDILKAF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLGAGPQGAQE-VRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPPGSPPPGDPRI 355
Cdd:cd05590  231 MTKNPTMRLGSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEESLLPMINQ 310
                        330
                 ....*....|...
gi 663856869 356 --FQGYSFVAPSI 366
Cdd:cd05590  311 deFRNFSYTAPEL 323
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
33-331 5.45e-85

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 272.65  E-value: 5.45e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLElvrQA--PFLVTLHYAFQTDAK 110
Cdd:cd05598    3 FEKIKTIGVGAFGEVSLVRK---KDTNALYAMKTLRKKDVLKR-NQVAHVKAERDILA---EAdnEWVVKLYYSFQDKEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL-------- 182
Cdd:cd05598   76 LYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwth 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 -SKEFLTEekertfSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVS--RRILKCsp 259
Cdd:cd05598  156 dSKYYLAH------SLVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKI-- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 260 PFPPRIGPVAQDLLQRLLCkDPKKRLGAGpqGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNF 331
Cdd:cd05598  227 PHEANLSPEAKDLILRLCC-DAEDRLGRN--GADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNF 293
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
32-341 1.24e-84

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 271.89  E-value: 1.24e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHdagKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDE---KFYAVKVLQKKAILKK-KEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEK 191
Cdd:cd05602   84 YFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENI-EPN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTqAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05602  163 GTTSTFCGTPEYLAPEVLH-KQPYDRTVDWWCLGAVLYEMLYGLPPFY---SRNT-AEMYDNILNKPLQLKPNITNSARH 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAgPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPV 341
Cdd:cd05602  238 LLEGLLQKDRTKRLGA-KDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTD-EPV 305
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
37-341 1.37e-83

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 268.90  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAaLVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05588    1 RVIGRGSYAKVLMVELK---KTKRIYAMKVIKKE-LVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLtEEKERTFS 196
Cdd:cd05588   77 FVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGL-RPGDTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEG-----ERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05588  156 FCGTPNYIAPEILRGED-YGFSVDWWALGVLMFEMLAGRSPFDIVGssdnpDQNTEDYLFQVILEKPIRIPRSLSVKAAS 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 272 LLQRLLCKDPKKRLGAGPQ-GAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPV 341
Cdd:cd05588  235 VLKGFLNKNPAERLGCHPQtGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTN-EPV 304
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
18-336 1.54e-83

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 269.59  E-value: 1.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  18 EANLTGHEEKVSVENFELLKVLGTGAYGKVFLVR-KAGGHdagkLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQaP 96
Cdd:cd05594   12 EVSLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKeKATGR----YYAMKILKKEVIVAKDEVA-HTLTENRVLQNSRH-P 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 FLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLH-KLGIIYRDLKLENVLLDSEGHI 175
Cdd:cd05594   86 FLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 176 VLTDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRIL 255
Cdd:cd05594  166 KITDFGLCKEGIKDGATMK-TFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDHEKLFELIL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 256 KCSPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEF 335
Cdd:cd05594  240 MEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEF 319

                 .
gi 663856869 336 T 336
Cdd:cd05594  320 T 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
32-362 1.06e-82

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 266.48  E-value: 1.06e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKG---TDELYAVKILKKDVVIQDDDV-ECTMVEKRVLALSGKPPFLTQLHSCFQTMDRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTeEK 191
Cdd:cd05616   77 YFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIW-DG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGErnTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd05616  156 VTTKTFCGTPDYIAPEIIAYQP-YGKSVDWWAFGVLLYEMLAGQAPF--EGE--DEDELFQSIMEHNVAYPKSMSKEAVA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSElDVGNFAEEFTRLEPVYSPPGSPPPG 351
Cdd:cd05616  231 ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPPDQEVIR 309
                        330
                 ....*....|...
gi 663856869 352 D--PRIFQGYSFV 362
Cdd:cd05616  310 NidQSEFEGFSFV 322
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
32-300 8.35e-81

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 258.60  E-value: 8.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRkaggH-DAGKLYAMKVLRKAALVQraKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLAR----HkLTGEKVAIKIIDKSKLKE--EIEEKIKREIEIMKLLNH-PNIIKLYEVIETENK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEE 190
Cdd:cd14003   74 IYLVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlEGErnTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14003  154 LLKT--FCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPF--DDD--NDSKLFRKILKGKYPIPSHLSPDAR 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14003  228 DLIRRMLVVDPSKRI-----TIEEILNHPW 252
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
26-367 3.33e-80

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 260.31  E-value: 3.33e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  26 EKVSVENFELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAF 105
Cdd:cd05615    5 DRVRLTDFNFLMVLGKGSFGKVMLAERKGSDE---LYAIKILKKDVVIQDDDV-ECTMVEKRVLALQDKPPFLTQLHSCF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05615   81 QTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTeEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRI 265
Cdd:cd05615  161 HMV-EGVTTRTFCGTPDYIAPEIIAYQP-YGRSVDWWAYGVLLYEMLAGQPPFDGEDED----ELFQSIMEHNVSYPKSL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSElDVGNFAEEFTRLEPVYS-- 343
Cdd:cd05615  235 SKEAVSICKGLMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQPVLTpp 313
                        330       340
                 ....*....|....*....|....
gi 663856869 344 PPGSPPPGDPRIFQGYSFVAPSIL 367
Cdd:cd05615  314 DQLVIANIDQADFEGFSYVNPQFV 337
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
39-320 3.11e-79

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 255.53  E-value: 3.11e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd05577    1 LGRGGFGEVCACQVK---ATGKMYACKKLDKKRIKKK-KGETMALNEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEEKERTFS 196
Cdd:cd05577   76 NGGDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF--KGGKKIKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05577  154 RVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 277 LCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05577  234 LQKDPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
31-301 7.52e-78

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 251.75  E-value: 7.52e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKE---KETGKEYAIKVLDKRHIIKEKKVKYVTI-EKEVLSRLAH-PGIVKLYYTFQDESK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK------ 184
Cdd:cd05581   76 LYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpds 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 ---EFLTEEKE-------RTFSFCGTIEYMAPEIIRSKTGhGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRI 254
Cdd:cd05581  156 speSTKGDADSqiaynqaRAASFVGTAEYVSPELLNEKPA-GKSSDLWALGCIIYQMLTGKPPF----RGSNEYLTFQKI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 255 LKCSPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGP-QGAQEVRNHPFF 301
Cdd:cd05581  231 VKLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
28-341 1.07e-77

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 254.57  E-value: 1.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAaLVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQT 107
Cdd:cd05618   17 LGLQDFDLLRVIGRGSYAKVLLVRLK---KTERIYAMKVVKKE-LVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd05618   93 ESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 tEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEG-----ERNTQAEVSRRILKCSPPFP 262
Cdd:cd05618  173 -RPGDTTSTFCGTPNYIAPEILRGED-YGFSVDWWALGVLMFEMMAGRSPFDIVGssdnpDQNTEDYLFQVILEKQIRIP 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLGAGPQ-GAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPV 341
Cdd:cd05618  251 RSLSVKAASVLKSFLNKDPKERLGCHPQtGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTN-EPV 329
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
32-302 1.07e-77

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 250.47  E-value: 1.07e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVR-KagghDAGKLYAMKVLRKAALVqraKTQEHTRTERSVlELVRQA--PFLVTLHYAFQTD 108
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAReK----KSGFIVALKVISKSQLQ---KSGLEHQLRREI-EIQSHLrhPNILRLYGYFEDK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLT 188
Cdd:cd14007   73 KRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH-AP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTfsFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd14007  152 SNRRKT--FCGTLDYLPPEMVEGK-EYDYKVDIWSLGVLCYELLVGKPPF----ESKSHQETYKRIQNVDIKFPSSVSPE 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 269 AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14007  225 AKDLISKLLQKDPSKRL-----SLEQVLNHPWIK 253
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
410-667 2.57e-77

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 249.37  E-value: 2.57e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE----ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:smart00220   7 LGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkkdrERILREIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   486 EHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLrpQSPGVPMQTPCFT 565
Cdd:smart00220  86 DLLKKRGRLSEDEARFYLRQILSALEYLH-SKGIVHRDLKPENILLDEDG---HVKLADFGLARQ--LDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqgGQSQAAEIMCKIREGRFSLDGEAWqGVSEEAKELVR 645
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP------GDDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLIR 232
                          250       260
                   ....*....|....*....|..
gi 663856869   646 GLLTVDPAKRLKLEGLRGSSWL 667
Cdd:smart00220 233 KLLVKDPEKRLTAEEALQHPFF 254
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
28-367 3.61e-77

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 253.02  E-value: 3.61e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFLVRKAGGHdagKLYAMKVLRKAaLVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQT 107
Cdd:cd05617   12 LGLQDFDLIRVIGRGSYAKVLLVRLKKND---QIYAMKVVKKE-LVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd05617   88 TSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 tEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF---TLEGERNTQAEVSRRILKCSPPFPPR 264
Cdd:cd05617  168 -GPGDTTSTFCGTPNYIAPEILRGEE-YGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILEKPIRIPRF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLGAGPQ-GAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRlEPVyS 343
Cdd:cd05617  246 LSVKASHVLKGFLNKDPKERLGCQPQtGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTS-EPV-Q 323
                        330       340
                 ....*....|....*....|....*...
gi 663856869 344 PPGSPPPGDPRI----FQGYSFVAPSIL 367
Cdd:cd05617  324 LTPDDEDVIKRIdqseFEGFEYINPLLL 351
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
27-366 5.08e-77

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 251.77  E-value: 5.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd05619    1 KLTIEDFVLHKMLGKGSFGKVFLAELKG---TNQFFAIKALKKDVVLMDDDV-ECTMVEKRVLSLAWEHPFLTHLFCTFQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:cd05619   77 TKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKEN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKeRTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRIG 266
Cdd:cd05619  157 MLGDA-KTSTFCGTPDYIAPEILLGQK-YNTSVDWWSFGVLLYEMLIGQSPFHGQDEE----ELFQSIRMDNPFYPRWLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 267 PVAQDLLQRLLCKDPKKRLGAgpqgAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEP--VYSP 344
Cdd:cd05619  231 KEAKDILVKLFVREPERRLGV----RGDIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPrlSFAD 306
                        330       340
                 ....*....|....*....|..
gi 663856869 345 PGSPPPGDPRIFQGYSFVAPSI 366
Cdd:cd05619  307 RALINSMDQNMFRNFSFVNPKM 328
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
32-301 7.26e-76

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 245.63  E-value: 7.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd05578    1 HFQILRVIGKGSFGKVCIVQK---KDTKKMFAMKYMNKQKCIEKDSVR-NVLNELEILQELEH-PFLVNLWYSFQDEEDM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd05578   76 YMVVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 erTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlEGERNTQA-EVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05578  156 --ATSTSGTKPYMAPEVFMRA-GYSFAVDWWSLGVTAYEMLRGKRPY--EIHSRTSIeEIRAKFETASVLYPAGWSEEAI 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRLGagpqGAQEVRNHPFF 301
Cdd:cd05578  231 DLINKLLERDPQKRLG----DLSDLKNHPYF 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
32-300 1.65e-73

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 239.69  E-value: 1.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKL 111
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVH---KKTGEEYAVKIIDKKKL--KSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS---EGHIVLTDFGLSKEFLT 188
Cdd:cd05117   75 YLVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIFEE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTfsFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd05117  155 GEKLKT--VCGTPYYVAPEVLKGK-GYGKKCDIWSLGVILYILLCGYPPF----YGETEQELFEKILKGKYSFDSPEWKN 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 269 ----AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd05117  228 vseeAKDLIKRLLVVDPKKRL-----TAAEALNHPW 258
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
37-364 3.47e-73

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 241.00  E-value: 3.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd05620    1 KVLGKGSFGKVLLAELKG---KGEYFAVKALKKDVVLIDDDV-ECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKeRTFS 196
Cdd:cd05620   77 FLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDN-RAST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd05620  156 FCGTPDYIAPEILQGLK-YTFSVDWWSFGVLLYEMLIGQSPFHGDDED----ELFESIRVDTPHYPRWITKESKDILEKL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 277 LCKDPKKRLGAgpqgAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEP--VYSPPGSPPPGDPR 354
Cdd:cd05620  231 FERDPTRRLGV----VGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPrlSYSDKNLIDSMDQS 306
                        330
                 ....*....|
gi 663856869 355 IFQGYSFVAP 364
Cdd:cd05620  307 AFAGFSFINP 316
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
38-320 9.80e-73

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 238.49  E-value: 9.80e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALvqRAKTQEH-TRTERSVLELVRQA---PFLVTLHYAFQTDAKLHL 113
Cdd:cd05606    1 IIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRI--KMKQGETlALNERIMLSLVSTGgdcPFIVCMTYAFQTPDKLCF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlteEKER 193
Cdd:cd05606   76 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF---SKKK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNtQAEVSRRILKCSPPFPPRIGPVAQDLL 273
Cdd:cd05606  153 PHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKD-KHEIDRMTLTMNVELPDSFSPELKSLL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 274 QRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05606  232 EGLLQRDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
33-320 2.09e-72

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 237.64  E-value: 2.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL--VRKAGghdagKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd05605    2 FRQYRVLGKGGFGEVCAcqVRATG-----KMYACKKLEKKRIKKR-KGEAMALNEKQILEKV-NSRFVVSLAYAYETKDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlt 188
Cdd:cd05605   75 LCLVLTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEI-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd05605  153 PEGETIRGRVGTVGYMAPEVVKNER-YTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEE 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 269 AQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05605  232 AKSICSQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
27-336 6.39e-72

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 239.93  E-value: 6.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLeLVRQAPFLVTLHYAFQ 106
Cdd:cd05600    7 RLKLSDFQILTQVGQGGYGSVFLARK---KDTGEICALKIMKKKVLFKLNEVN-HVLTERDIL-TTTNSPWLVKLLYAFQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:cd05600   82 DPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEK-----------------ERT-------------------FSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFE 230
Cdd:cd05600  162 LSPKKiesmkirleevkntaflELTakerrniyramrkedqnyaNSVVGSPDYMAPEVLRGE-GYDLTVDYWSLGCILFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 231 LLTGASPFTLEGERNTQA------EVSRRILKCSPPFPPRIGPVAQDLLQRLLCkDPKKRLgagpQGAQEVRNHPFFQGL 304
Cdd:cd05600  241 CLVGFPPFSGSTPNETWAnlyhwkKTLQRPVYTDPDLEFNLSDEAWDLITKLIT-DPQDRL----QSPEQIKNHPFFKNI 315
                        330       340       350
                 ....*....|....*....|....*....|..
gi 663856869 305 DWVALAARKIPaPFRPQIRSELDVGNFaEEFT 336
Cdd:cd05600  316 DWDRLREGSKP-PFIPELESEIDTSYF-DDFN 345
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
31-331 1.08e-70

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 234.55  E-value: 1.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQEHtRTERSVLelVR-QAPFLVTLHYAFQTDA 109
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKS---TEKVYAMKILNKWEMLKRAETACF-REERDVL--VNgDRRWITKLHYAFQDEN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd05597   75 YLYLVMDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLRE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIR-SKTGHGK---AVDWWSLGILLFELLTGASPFTLEGerntQAEVSRRILKCS-----P 259
Cdd:cd05597  155 DGTVQSSVAVGTPDYISPEILQaMEDGKGRygpECDWWSLGVCMYEMLYGETPFYAES----LVETYGKIMNHKehfsfP 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 260 PFPPRIGPVAQDLLQRLLCkDPKKRLGAGpqGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNF 331
Cdd:cd05597  231 DDEDDVSEEAKDLIRRLIC-SRERRLGQN--GIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNF 297
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
31-341 1.38e-70

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 235.90  E-value: 1.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLeLVRQAPFLVTLHYAFQTDAK 110
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKK---DTGKIYAMKTLLKSEMFKKDQLA-HVKAERDVL-AESDSPWVVSLYYSFQDAQY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF---- 186
Cdd:cd05629   76 LYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFhkqh 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 -------LTEEKERT-----------------------------------FSFCGTIEYMAPEIIrSKTGHGKAVDWWSL 224
Cdd:cd05629  156 dsayyqkLLQGKSNKnridnrnsvavdsinltmsskdqiatwkknrrlmaYSTVGTPDYIAPEIF-LQQGYGQECDWWSL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 225 GILLFELLTGASPFTLEGERNTQaevsRRIL--KCSPPFPPRI--GPVAQDLLQRLLCkDPKKRLGAGpqGAQEVRNHPF 300
Cdd:cd05629  235 GAIMFECLIGWPPFCSENSHETY----RKIInwRETLYFPDDIhlSVEAEDLIRRLIT-NAENRLGRG--GAHEIKSHPF 307
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 663856869 301 FQGLDWVALaaRKIPAPFRPQIRSELDVGNFAEEftRLEPV 341
Cdd:cd05629  308 FRGVDWDTI--RQIRAPFIPQLKSITDTSYFPTD--ELEQV 344
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
36-306 2.32e-70

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 231.60  E-value: 2.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVqrAKTQ-EHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLI 114
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRS---TGDYFAIKVLKKSDMI--AKNQvTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefLTEEKERT 194
Cdd:cd05611   76 MEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR--NGLEKRHN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPR----IGPVAQ 270
Cdd:cd05611  154 KKFVGTPDYLAPETILGV-GDDKMSDWWSLGCVIFEFLFGYPPF----HAETPDAVFDNILSRRINWPEEvkefCSPEAV 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 271 DLLQRLLCKDPKKRLGAgpQGAQEVRNHPFFQGLDW 306
Cdd:cd05611  229 DLINRLLCMDPAKRLGA--NGYQEIKSHPFFKSINW 262
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
409-703 7.09e-70

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 231.07  E-value: 7.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHI 488
Cdd:cd14175    8 TIGVGSYSVCKRCVHKATNMEYAVKVIDKS-KRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 489 RKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAP--VKIIDFGFARLRPQSPGVPMqTPCFTL 566
Cdd:cd14175   87 LRQKFFSEREASSVLHTICKTVEYLHSQ-GVVHRDLKPSNILYVDES-GNPesLRICDFGFAKQLRAENGLLM-TPCYTA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 567 QYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgASGQGGQSQaaEIMCKIREGRFSLDGEAWQGVSEEAKELVRG 646
Cdd:cd14175  164 NFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF--ANGPSDTPE--EILTRIGSGKFTLSGGNWNTVSDAAKDLVSK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 647 LLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVlessgPAVRSGLNATFMAFN 703
Cdd:cd14175  240 MLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQDV-----QLVKGAMAATYSALN 291
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
410-733 1.75e-68

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 229.14  E-value: 1.75e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIR 489
Cdd:cd14176   27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQ-HPNIITLKDVYDDGKYVYVVTELMKGGELLDKIL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 490 KKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAP--VKIIDFGFARLRPQSPGVPMqTPCFTLQ 567
Cdd:cd14176  106 RQKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILYVDES-GNPesIRICDFGFAKQLRAENGLLM-TPCYTAN 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGL 647
Cdd:cd14176  183 FVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF----ANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKM 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 648 LTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDvlesSGPAVRSGLNATFMAFNRGKREgfFLKSVENAPLAKRRKQK 727
Cdd:cd14176  259 LHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQD----APHLVKGAMAATYSALNRNQSP--VLEPVGRSTLAQRRGIK 332

                 ....*.
gi 663856869 728 LRSATA 733
Cdd:cd14176  333 KITSTA 338
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
22-331 2.45e-67

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 226.01  E-value: 2.45e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  22 TGHEEKVSVENFELLKVLGTGAYGKVFLVRKAGGHDAGklYAMKVLRKAALVqRAKTQEHTRTERSVLELVRQaPFLVTL 101
Cdd:PTZ00426  21 PKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFPP--VAIKRFEKSKII-KQKQVDHVFSERKILNYINH-PFCVNL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:PTZ00426  97 YGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTeekeRTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPF 261
Cdd:PTZ00426 177 FAKVVDT----RTYTLCGTPEYIAPEILLN-VGHGKAADWWTLGIFIYEILVGCPPFY----ANEPLLIYQKILEGIIYF 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:PTZ00426 248 PKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNF 317
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
410-666 5.42e-67

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 222.01  E-value: 5.42e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14003    8 LGEGSFGKVKLARHKLTGEKVAIKIIDKsklkeEIEEKIKREIEIMKLLN-HPNIIKLYEVIETENKIYLVMEYASGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYaDDTPGapVKIIDFGFARLrpQSPGVPMQTPCF 564
Cdd:cd14003   87 FDYIVNNGRLSEDEARRFFQQLISAVDYCH-SNGIVHRDLKLENILL-DKNGN--LKIIDFGLSNE--FRGGSLLKTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLdgeaWQGVSEEAKEL 643
Cdd:cd14003  161 TPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDN-------DSKLFRKILKGKYPI----PSHLSPDARDL 229
                        250       260
                 ....*....|....*....|...
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14003  230 IRRMLVVDPSKRITIEEILNHPW 252
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
32-306 7.42e-67

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 222.67  E-value: 7.42e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQEhTRTERSVLELVrQAPFLVTLHYAFQTDAKL 111
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRH---RETRQRFAMKKINKQNLILRNQIQQ-VFVERDILTFA-ENPFVVSMYCSFETKRHL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK------- 184
Cdd:cd05609   76 CMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 ----EFLTEEKERTFS---FCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKC 257
Cdd:cd05609  156 tnlyEGHIEKDTREFLdkqVCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGD----TPEELFGQVISD 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 258 SPPFPPR---IGPVAQDLLQRLLCKDPKKRLGAGpqGAQEVRNHPFFQGLDW 306
Cdd:cd05609  231 EIEWPEGddaLPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
404-703 1.68e-66

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 222.20  E-value: 1.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREPaLGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14177    7 ELKED-IGVGSYSVCKRCIHRATNMEFAVKIIDKS-KRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQSPGVpMQTP 562
Cdd:cd14177   85 LLDRILRQKFFSEREASAVLYTITKTVDYLHCQ-GVVHRDLKPSNILYMDDSANAdSIRICDFGFAKQLRGENGL-LLTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKE 642
Cdd:cd14177  163 CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF----ANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKD 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWLqdgSARSSPPLRTPDVLESSGpAVRSGLNATFMAFN 703
Cdd:cd14177  239 LLSHMLHVDPHQRYTAEQVLKHSWI---ACRDQLPHYQLNRQDAPH-LVKGAMAATYSALN 295
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
410-703 2.79e-66

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 221.81  E-value: 2.79e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIR 489
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYGQ-HPNIITLKDVYDDGKFVYLVMELMRGGELLDRIL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 490 KKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAP--VKIIDFGFARLRPQSPGVPMqTPCFTLQ 567
Cdd:cd14178   90 RQKCFSEREASAVLCTITKTVEYLHSQ-GVVHRDLKPSNILYMDES-GNPesIRICDFGFAKQLRAENGLLM-TPCYTAN 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGL 647
Cdd:cd14178  167 FVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF----ANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVSKM 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 648 LTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVlessgPAVRSGLNATFMAFN 703
Cdd:cd14178  243 LHVDPHQRLTAPQVLRHPWIVNREYLSQNQLSRQDV-----HLVKGAMAATYFALN 293
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
31-333 6.26e-66

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 221.80  E-value: 6.26e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAA-LVQRAKTQehTRTERSVLELvRQAPFLVTLHYAFQTDA 109
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKA---TGDIYAMKVLKKSEtLAQEEVSF--FEEERDIMAK-ANSPWITKLQYAFQDSE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQ-YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLT 188
Cdd:cd05601   75 NLYLVMEYHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG-SAAKLS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSF-CGTIEYMAPEII-----RSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAevsrRIL--KCSPP 260
Cdd:cd05601  154 SDKTVTSKMpVGTPDYIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYS----NIMnfKKFLK 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 261 FP--PRIGPVAQDLLQRLLCkDPKKRLgagpqGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNFAE 333
Cdd:cd05601  230 FPedPKVSESAVDLIKGLLT-DAKERL-----GYEGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFDE 296
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
28-337 1.17e-65

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 221.86  E-value: 1.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlVQRAKTQEHTRTERSVLELVRQA--PFLVTLHYAF 105
Cdd:cd05633    2 LTMNDFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKR-IKMKQGETLALNERIMLSLVSTGdcPFIVCMTYAF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05633   78 HTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FlteEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQaEVSRRILKCSPPFPPRI 265
Cdd:cd05633  158 F---SKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTVNVELPDSF 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQiRSEL------DVGNFAEEFTR 337
Cdd:cd05633  234 SPELKSLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPP-RGEVnaadafDIGSFDEEDTK 310
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
32-337 2.70e-65

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 219.92  E-value: 2.70e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlVQRAKTQEHTRTERSVLELVRQA--PFLVTLHYAFQTDA 109
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKR-IKMKQGETLALNERIMLSLVSTGdcPFIVCMSYAFHTPD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlte 189
Cdd:cd14223   77 KLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQaEVSRRILKCSPPFPPRIGPVA 269
Cdd:cd14223  154 SKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTMAVELPDSFSPEL 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 270 QDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQiRSEL------DVGNFAEEFTR 337
Cdd:cd14223  233 RSLLEGLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPP-RGEVnaadafDIGSFDEEDTK 305
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
27-331 1.36e-64

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 219.17  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVRkaggH-DAGKLYAMKVLRKAALVQRAKTQ---EhtrtERSVLELVRqAPFLVTLH 102
Cdd:cd05596   22 RMNAEDFDVIKVIGRGAFGEVQLVR----HkSTKKVYAMKLLSKFEMIKRSDSAffwE----ERDIMAHAN-SEWIVQLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAKLHLILDYVSGGEMFThLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd05596   93 YAFQDDKYLYMVMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGH---GKAVDWWSLGILLFELLTGASPFTLEGERNTQAevsrRIL--KC 257
Cdd:cd05596  172 CMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGDgvyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYG----KIMnhKN 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 258 SPPFP--PRIGPVAQDLLQRLLCkDPKKRLGAgpQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05596  248 SLQFPddVEISKDAKSLICAFLT-DREVRLGR--NGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF 320
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
421-666 1.61e-64

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 215.61  E-value: 1.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 421 CRQRQSGQEFAVKILSRRLEAntQREVAALRLCQSHPNVVNLHEV----HHDQLHTYLVLELLRGGELLEHI--RKKRHF 494
Cdd:cd14089   20 CFHKKTGEKFALKVLRDNPKA--RREVELHWRASGCPHIVRIIDVyentYQGRKCLLVVMECMEGGELFSRIqeRADSAF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 495 SESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSpgVPMQTPCFTLQYAAPELL 574
Cdd:cd14089   98 TEREAAEIMRQIGSAVAHLHS-MNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTK--KSLQTPCYTPYYVAPEVL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 575 AQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAK 654
Cdd:cd14089  175 GPEKYDKSCDMWSLGVIMYILLCGYPPFY---SNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSE 251
                        250
                 ....*....|..
gi 663856869 655 RLKLEGLRGSSW 666
Cdd:cd14089  252 RLTIEEVMNHPW 263
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
29-331 2.80e-64

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 218.21  E-value: 2.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQEhTRTERSVLELVRqAPFLVTLHYAFQTD 108
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKK---NNSKLYAVKVVKKADMINKNMVHQ-VQAERDALALSK-SPFIVHLYYSLQSA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd05610   77 NNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKE------------------RT----------FSF------------------------CGTIEYMAPEIIRSKtGHG 216
Cdd:cd05610  157 RELNmmdilttpsmakpkndysRTpgqvlslissLGFntptpyrtpksvrrgaarvegeriLGTPDYLAPELLLGK-PHG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 217 KAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFP---PRIGPVAQDLLQRLLCKDPKKRlgagpQGAQ 293
Cdd:cd05610  236 PAVDWWALGVCLFEFLTGIPPFNDE----TPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKR-----AGLK 306
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 663856869 294 EVRNHPFFQGLDWVALAARkiPAPFRPQIRSELDVGNF 331
Cdd:cd05610  307 ELKQHPLFHGVDWENLQNQ--TMPFIPQPDDETDTSYF 342
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
33-320 2.93e-63

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 213.20  E-value: 2.93e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQMRA---TGKLYACKKLNKKRLKKR-KGYEGAMVEKRILAKV-HSRFIVSLAYAFQTKTDLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLY----QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLT 188
Cdd:cd05608   78 LVMTIMNGGDLRYHIYnvdeENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVE-LK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd05608  157 DGQTKTKGYAGTPGFMAPELLLGEE-YDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 269 AQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05608  236 SKSICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
404-656 7.15e-63

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 212.27  E-value: 7.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQ----REVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14090    4 KLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKH-PGHSRsrvfREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFA--------RLR 551
Cdd:cd14090   83 RGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDK-GIAHRDLKPENILCESMDKVSPVKICDFDLGsgiklsstSMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 P-QSPgvPMQTPCFTLQYAAPELL-AQQG----YDESCDLWSLGVILYMMLSGQVPFQGASG------QGGQSQAAEIMC 619
Cdd:cd14090  162 PvTTP--ELLTPVGSAEYMAPEVVdAFVGealsYDKRCDLWSLGVILYIMLCGYPPFYGRCGedcgwdRGEACQDCQELL 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 620 --KIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd14090  240 fhSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRY 278
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
30-361 5.11e-62

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 212.61  E-value: 5.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLeLVRQAPFLVTLHYAFQTDA 109
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKK---DTGHIYAMKILRKADMLEKEQVA-HIRAERDIL-VEADGAWVVKMFYSFQDKR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL------- 182
Cdd:cd05627   76 NLYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkka 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 -SKEF---LTEEKERTFSF-----------------------CGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGA 235
Cdd:cd05627  156 hRTEFyrnLTHNPPSDFSFqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 236 SPFTLEgernTQAEVSRRIL--KCSPPFPPRIgPV---AQDLLQRlLCKDPKKRLGAGpqGAQEVRNHPFFQGLDWVALa 310
Cdd:cd05627  235 PPFCSE----TPQETYRKVMnwKETLVFPPEV-PIsekAKDLILR-FCTDAENRIGSN--GVEEIKSHPFFEGVDWEHI- 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 311 aRKIPAPFRPQIRSELDVGNFAE--EFTRLEPVYSPPGSPPPGDPRIFQGYSF 361
Cdd:cd05627  306 -RERPAAIPIEIKSIDDTSNFDDfpESDILQPAPNTTEPDYKSKDWVFLNYTY 357
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
25-331 5.73e-62

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 213.72  E-value: 5.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  25 EEKVSVENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQEHtRTERSVLeLVRQAPFLVTLHYA 104
Cdd:cd05624   66 EMQLHRDDFEIIKVIGRGAFGEVAVVKM---KNTERIYAMKILNKWEMLKRAETACF-REERNVL-VNGDCQWITTLHYA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd05624  141 FQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSC 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTEEKERTFSFCGTIEYMAPEIIRS-KTGHGK---AVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSp 259
Cdd:cd05624  221 LKMNDDGTVQSSVAVGTPDYISPEILQAmEDGMGKygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQ- 299
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 260 pFPPRIGPV---AQDLLQRLLCKDpKKRLGAgpQGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNF 331
Cdd:cd05624  300 -FPSHVTDVseeAKDLIQRLICSR-ERRLGQ--NGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNF 368
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
33-320 7.42e-62

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 209.49  E-value: 7.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKR-KGEAMALNEKQILEKV-NSRFVVSLAYAYETKDALC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEflTEE 190
Cdd:cd05630   77 LVLTLMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH--VPE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd05630  155 GQTIKGRVGTVGYMAPEVVKNER-YTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQAR 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05630  234 SLCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
Pkinase pfam00069
Protein kinase domain;
33-301 1.63e-60

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 203.24  E-value: 1.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKE--KIKKKKDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEhlhklgiiyrdlklenvlldseghivltdfglSKEFLTeeke 192
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE--------------------------------SGSSLT---- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  193 rtfSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcSPPFPPRIGPVAQDL 272
Cdd:pfam00069 119 ---TFVGTPWYMAPEVLGGN-PYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYA-FPELPSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....*....
gi 663856869  273 LQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:pfam00069 194 LKKLLKKDPSKRL-----TATQALQHPWF 217
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
31-331 4.81e-59

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 206.02  E-value: 4.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQEHtRTERSVLeLVRQAPFLVTLHYAFQTDAK 110
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLK---NADKVFAMKILNKWEMLKRAETACF-REERDVL-VNGDSQWITTLHYAFQDDNN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:cd05623  147 LYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMED 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRS----KTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRilKCSPPFPPRI 265
Cdd:cd05623  227 GTVQSSVAVGTPDYISPEILQAmedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNH--KERFQFPTQV 304
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 266 GPV---AQDLLQRLLCKDpKKRLGAgpQGAQEVRNHPFFQGLDWVALaaRKIPAPFRPQIRSELDVGNF 331
Cdd:cd05623  305 TDVsenAKDLIRRLICSR-EHRLGQ--NGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNF 368
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
33-320 1.18e-58

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 200.60  E-value: 1.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL--VRKAGghdagKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd05631    2 FRHYRVLGKGGFGEVCAcqVRATG-----KMYACKKLEKKRIKKR-KGEAMALNEKRILEKV-NSRFVVSLAYAYETKDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlt 188
Cdd:cd05631   75 LCLVLTIMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd05631  153 PEGETVRGRVGTVGYMAPEVINNEK-YTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSED 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 269 AQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05631  232 AKSICRMLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
31-333 1.67e-58

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 203.35  E-value: 1.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLeLVRQAPFLVTLHYAFQTDAK 110
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQK---KDTGHVYAMKILRKADMLEKEQVG-HIRAERDIL-VEADSLWVVKMFYSFQDKLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDF----GLSKEF 186
Cdd:cd05628   76 LYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFglctGLKKAH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTE------------------------------EKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGAS 236
Cdd:cd05628  156 RTEfyrnlnhslpsdftfqnmnskrkaetwkrnRRQLAFSTVGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGYP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 237 PFTLEgernTQAEVSRRIL--KCSPPFPPRIgPV---AQDLLQRLLCkDPKKRLGAgpQGAQEVRNHPFFQGLDWVALaa 311
Cdd:cd05628  235 PFCSE----TPQETYKKVMnwKETLIFPPEV-PIsekAKDLILRFCC-EWEHRIGA--PGVEEIKTNPFFEGVDWEHI-- 304
                        330       340
                 ....*....|....*....|..
gi 663856869 312 RKIPAPFRPQIRSELDVGNFAE 333
Cdd:cd05628  305 RERPAAIPIEIKSIDDTSNFDE 326
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
33-331 8.80e-58

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 201.39  E-value: 8.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQApFLVTLHYAFQTDAKLH 112
Cdd:cd05626    3 FVKIKTLGIGAFGEVCLACKV---DTHALYAMKTLRKKDVLNRNQVA-HVKAERDILAEADNE-WVVKLYYSFQDKDNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF------ 186
Cdd:cd05626   78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthns 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 --------------------------------------LTEEKERTF--SFCGTIEYMAPEIIRSKtGHGKAVDWWSLGI 226
Cdd:cd05626  158 kyyqkgshirqdsmepsdlwddvsncrcgdrlktleqrATKQHQRCLahSLVGTPNYIAPEVLLRK-GYTQLCDWWSVGV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 227 LLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKdPKKRLGAgpQGAQEVRNHPFFQGLDW 306
Cdd:cd05626  237 ILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCS-AEERLGR--NGADDIKAHPFFSEVDF 313
                        330       340
                 ....*....|....*....|....*
gi 663856869 307 vALAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05626  314 -SSDIRTQPAPYVPKISHPMDTSNF 337
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
31-332 2.08e-57

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 198.27  E-value: 2.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRaKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRA---TGKMYACKRLEKKRIKKR-KGESMALNEKQILEKV-NSQFVVNLAYAYETKDA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlt 188
Cdd:cd05632   77 LCLVLTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd05632  155 PEGESIRGRVGTVGYMAPEVLNNQR-YTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 269 AQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRS-----ELDVGNFA 332
Cdd:cd05632  234 AKSICKMLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAvyckdVLDIEQFS 302
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
39-301 2.15e-56

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 193.92  E-value: 2.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQA---------PFLVTLHYAF---Q 106
Cdd:cd14008    1 LGRGSFGKVKLALDT---ETGQLYAIKIFNKSRLRKRREGKNDRGKIKNALDDVRREiaimkkldhPNIVRLYEVIddpE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDaKLHLILDYVSGGEM--FTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSk 184
Cdd:cd14008   78 SD-KLYLVLEYCEGGPVmeLDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EFLTEEKERTFSFCGTIEYMAPEI--IRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKC--SPP 260
Cdd:cd14008  156 EMFEDGNDTLQKTAGTPAFLAPELcdGDSKTYSGKAADIWALGVTLYCLVFGRLPF----NGDNILELYEAIQNQndEFP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14008  232 IPPELSPELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
401-667 1.18e-55

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 191.80  E-value: 1.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR-----EVAALRLCQSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14106    9 YTVESTP--LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRneilhEIAVLELCKDCPRVVNLHEVYETRSELILI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLrpQSP 555
Cdd:cd14106   87 LELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHER-NIVHLDLKPQNILLTSEFPLGDIKLCDFGISRV--IGE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQG 635
Cdd:cd14106  164 GEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQ-------ETFLNISQCNLDFPEELFKD 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14106  237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
39-299 1.30e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 189.79  E-value: 1.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd00180    1 LGKGSFGKVYKARDKET---GKKVAVKVIPKE---KLKKLLEELLREIEILKKLNH-PNIVKLYDVFETENFLYLVMEYC 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQR-QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSF 197
Cdd:cd00180   74 EGGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELltgaspftlegerntqaevsrrilkcsppfpprigPVAQDLLQRLL 277
Cdd:cd00180  154 GTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRML 198
                        250       260
                 ....*....|....*....|..
gi 663856869 278 CKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd00180  199 QYDPKKRP-----SAKELLEHL 215
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
37-301 2.42e-55

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 190.84  E-value: 2.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAALvQRAKTQEHTRTE----RSVlelvrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMST---GKVYAGKVVPKSSL-TKPKQREKLKSEikihRSL-----KHPNIVKFHDCFEDEENVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEKE 192
Cdd:cd14099   78 ILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAAR-LEYDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPR--IGPVAQ 270
Cdd:cd14099  157 RKKTLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPF----ETSDVKETYKRIKKNEYSFPSHlsISDEAK 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14099  233 DLIRSMLQPDPTKRP-----SLDEILSHPFF 258
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
405-668 1.47e-54

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 189.86  E-value: 1.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRL---EANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14174    5 LTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAghsRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFAR-LRPQSPGVP-- 558
Cdd:cd14174   85 GSILAHIQKRKHFNEREASRVVRDIASALDFLHTK-GIAHRDLKPENILCESPDKVSPVKICDFDLGSgVKLNSACTPit 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 ---MQTPCFTLQYAAPELL---AQQG--YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEI--MCK------IR 622
Cdd:cd14174  164 tpeLTTPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCGWDRGEVcrVCQnklfesIQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 623 EGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd14174  244 EGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
410-659 2.98e-54

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 187.48  E-value: 2.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS--RRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPkrDKKKEAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYAdDTPGAPVKIIDFGFArlRPQSPGVPMQTPCFTLQ 567
Cdd:cd14006   80 LAERGSLSEEEVRTYMRQLLEGLQYLHNH-HILHLDLKPENILLA-DRPSPQIKIIDFGLA--RKLNPGEELKEIFGTPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELVRGL 647
Cdd:cd14006  156 FVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQ-------ETLANISACRVDFSEEYFSSVSQEAKDFIRKL 228
                        250
                 ....*....|..
gi 663856869 648 LTVDPAKRLKLE 659
Cdd:cd14006  229 LVKEPRKRPTAQ 240
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
404-655 8.39e-54

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 186.42  E-value: 8.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14083    6 EFKE-VLGTGAFSEVVLAEDKATGKLVAIKCIDKKAlkgkEDSLENEIAVLRKI-KHPNIVQLLDIYESKSHLYLVMELV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLrpQSPGVpM 559
Cdd:cd14083   84 TGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSL-GIVHRDLKPENLLYYSPDEDSKIMISDFGLSKM--EDSGV-M 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14083  160 STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDEND-------SKLFAQILKAEYEFDSPYWDDISDS 232
                        250
                 ....*....|....*.
gi 663856869 640 AKELVRGLLTVDPAKR 655
Cdd:cd14083  233 AKDFIRHLMEKDPNKR 248
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
410-657 1.02e-53

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 185.80  E-value: 1.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS------RRLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeiikRKEVEHTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPqSPGVPMQTPC 563
Cdd:cd05123   80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSL-GIIYRDLKPENILLDSD--GH-IKLTDFGLAKELS-SDGDRTYTFC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05123  155 GTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYA-------ENRKEIYEKILKSPLKFP----EYVSPEAKSL 223
                        250
                 ....*....|....
gi 663856869 644 VRGLLTVDPAKRLK 657
Cdd:cd05123  224 ISGLLQKDPTKRLG 237
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
410-656 1.26e-53

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 185.99  E-value: 1.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR----LEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14095    8 IGDGNFAVVKECRDKATDKEYALKIIDKAkckgKEHMIENEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELVKGGDLF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQspgvPMQTPCF 564
Cdd:cd14095   87 DAITSSTKFTERDASRMVTDLAQALKYLHSL-SIVHRDIKPENLLVVEHEDGSkSLKLADFGLATEVKE----PLFTVCG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqSQaAEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd14095  162 TPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDR----DQ-EELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                        250
                 ....*....|..
gi 663856869 645 RGLLTVDPAKRL 656
Cdd:cd14095  237 SRMLVVDPEKRY 248
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
33-331 1.58e-53

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 189.87  E-value: 1.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVRQApFLVTLHYAFQTDAKLH 112
Cdd:cd05625    3 FVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVA-HVKAERDILAEADNE-WVVRLYYSFQDKDNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL---------- 182
Cdd:cd05625   78 FVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthds 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 ------------SKEFLTE----------------------EKERTF--SFCGTIEYMAPEIIRsKTGHGKAVDWWSLGI 226
Cdd:cd05625  158 kyyqsgdhlrqdSMDFSNEwgdpencrcgdrlkplerraarQHQRCLahSLVGTPNYIAPEVLL-RTGYTQLCDWWSVGV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 227 LLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRlLCKDPKKRLGAgpQGAQEVRNHPFFQGLDW 306
Cdd:cd05625  237 ILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLGK--NGADEIKAHPFFKTIDF 313
                        330       340
                 ....*....|....*....|....*
gi 663856869 307 VAlAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05625  314 SS-DLRQQSAPYIPKITHPTDTSNF 337
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
396-667 2.13e-53

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 186.51  E-value: 2.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 396 SAMMQYELDLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTqrEVAALRLCQSHPNVVNLHEVH--------- 466
Cdd:cd14171    1 SILEEYEVNWTQ-KLGTGISGPVRVCVKKSTGERFALKILLDRPKART--EVRLHMMCSGHPNIVQIYDVYansvqfpge 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 -HDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTPGAPVKIIDF 545
Cdd:cd14171   78 sSPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCH-SLNIAHRDLKPENLLLKDNSEDAPIKLCDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 546 GFARLRPQSpgvpMQTPCFTLQYAAPELLAQQ-----------------GYDESCDLWSLGVILYMMLSGQVPFQgaSGQ 608
Cdd:cd14171  157 GFAKVDQGD----LMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFY--SEH 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 609 GGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14171  231 PSRTITKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
407-659 2.33e-53

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 185.64  E-value: 2.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EP--ALGQGSFSVCRRCRQRQSGQEFAVKILSR-----------RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTY 473
Cdd:cd14093    6 EPkeILGRGVSSTVRRCIEKETGQEFAVKIIDItgeksseneaeELREATRREIEILRQVSGHPNIIELHDVFESPTFIF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPq 553
Cdd:cd14093   86 LVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSL-NIVHRDLKPENILLDDNL---NVKISDFGFATRLD- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 sPGVPMQTPCFTLQYAAPELLAQQ------GYDESCDLWSLGVILYMMLSGQVPFqgasgqggQSQAAEIMCK-IREGRF 626
Cdd:cd14093  161 -EGEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPF--------WHRKQMVMLRnIMEGKY 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 627 SLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd14093  232 EFGSPEWDDISDTAKDLISKLLVVDPKKRLTAE 264
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
32-301 2.48e-53

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 185.36  E-value: 2.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDAKL 111
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRR---KSDGKLYVLKEIDLSNM--SEKEREEALNEVKLLSKLK-HPNIVKYYESFEENGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQR----QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfL 187
Cdd:cd08215   75 CIVMEYADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKV-L 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRIG 266
Cdd:cd08215  154 ESTTDLAKTVVGTPYYLSPELCENK-PYNYKSDIWALGCVLYELCTLKHPF----EANNLPALVYKIVKGQyPPIPSQYS 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 267 PVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPFF 301
Cdd:cd08215  229 SELRDLVNSMLQKDPEKR----PS-ANEILSSPFI 258
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
25-331 2.82e-53

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 189.83  E-value: 2.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  25 EEKVSVENFELLKVLGTGAYGKVFLVRKAGGHdagKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVrQAPFLVTLHYA 104
Cdd:cd05622   67 DLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTR---KVYAMKLLSKFEMIKRSDSA-FFWEERDIMAFA-NSPWVVQLFYA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd05622  142 FQDDRYLYMVMEYMPGGDL-VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCM 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EFLTEEKERTFSFCGTIEYMAPEIIRSKTG---HGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPF 261
Cdd:cd05622  221 KMNKEGMVRCDTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPD 300
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 262 PPRIGPVAQDLLQRLLcKDPKKRLGAgpQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNF 331
Cdd:cd05622  301 DNDISKEAKNLICAFL-TDREVRLGR--NGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNF 367
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
410-668 4.05e-53

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 184.60  E-value: 4.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14007    8 LGKGKFGNVYLAREKKSGFIVALKVISKSqlqksgLEHQLRREIEIQSHL-RHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENIL--YADDtpgapVKIIDFGFARlrpQSPGVPMQT 561
Cdd:cd14007   87 LYKELKKQKRFDEKEAAKYIYQLALALDYLHSK-NIIHRDIKPENILlgSNGE-----LKLADFGWSV---HAPSNRRKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLdgeaWQGVSEEAK 641
Cdd:cd14007  158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQ-------ETYKRIQNVDIKF----PSSVSPEAK 226
                        250       260
                 ....*....|....*....|....*..
gi 663856869 642 ELVRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd14007  227 DLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
405-667 4.02e-52

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 182.92  E-value: 4.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPALGQGSFSVCRRCRQRQSGQEFAVKILSRR---LEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14173    5 LQEEVLGEGAYARVQTCINLITNKEYAVKIIEKRpghSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFAR-LRPQSPGVPMQ 560
Cdd:cd14173   85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNK-GIAHRDLKPENILCEHPNQVSPVKICDFDLGSgIKLNSDCSPIS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 -----TPCFTLQYAAPELLAQQG-----YDESCDLWSLGVILYMMLSGQVPFQGASG------QGGQSQAAEIMC--KIR 622
Cdd:cd14173  164 tpellTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGsdcgwdRGEACPACQNMLfeSIQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 623 EGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14173  244 EGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
33-285 8.80e-52

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 181.06  E-value: 8.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNT---KTGESVAIKIIDKE-QVAREGMVEQIKREIAIMKLLRH-PNIVELHEVMATKTKIF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS---KEFLTE 189
Cdd:cd14663   77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalsEQFRQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAeVSRRILKCSPPFPPRIGPVA 269
Cdd:cd14663  157 GLLHT--TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFD---DENLMA-LYRKIMKGEFEYPRWFSPGA 230
                        250
                 ....*....|....*.
gi 663856869 270 QDLLQRLLCKDPKKRL 285
Cdd:cd14663  231 KSLIKRILDPNPSTRI 246
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
27-333 1.47e-51

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 184.43  E-value: 1.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVRkaggHDAG-KLYAMKVLRKAALVQRAKTQeHTRTERSVLELVrQAPFLVTLHYAF 105
Cdd:cd05621   48 QMKAEDYDVVKVIGRGAFGEVQLVR----HKASqKVYAMKLLSKFEMIKRSDSA-FFWEERDIMAFA-NSPWVVQLFCAF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05621  122 QDDKYLYMVMEYMPGGDL-VNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMK 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSFCGTIEYMAPEIIRSKTG---HGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRilKCSPPFP 262
Cdd:cd05621  201 MDETGMVHCDTAVGTPDYISPEVLKSQGGdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDH--KNSLNFP 278
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 263 P--RIGPVAQDLLQRLLcKDPKKRLGAgpQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAE 333
Cdd:cd05621  279 DdvEISKHAKNLICAFL-TDREVRLGR--NGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDD 348
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
407-680 1.89e-51

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 181.18  E-value: 1.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14085    8 ESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSpgVPMQTPCFTL 566
Cdd:cd14085   88 RIVEKGYYSERDAADAVKQILEAVAYLHEN-GIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQ--VTMKTVCGTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 567 QYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaAEIMCKIREGRFSLDGEAWQGVSEEAKELVRG 646
Cdd:cd14085  165 GYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGD------QYMFKRILNCDYDFVSPWWDDVSLNAKDLVKK 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 647 LLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRT 680
Cdd:cd14085  239 LIVLDPKKRLTTQQALQHPWVTGKAANFAHMDTA 272
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
410-667 4.25e-51

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 178.99  E-value: 4.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEklskesVLMKVEREIAIMKLIE-HPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLrpQSPGVPMQTPC 563
Cdd:cd14081   88 LFDYLVKKGRLTEKEARKFFRQIISALDYCHSH-SICHRDLKPENLLLDEKN---NIKIADFGMASL--QPEGSLLETSC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEawqgVSEEAKE 642
Cdd:cd14081  162 GSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDN-------LRQLLEKVKRGVFHIPHF----ISPDAQD 230
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14081  231 LLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
37-301 4.84e-51

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 178.87  E-value: 4.84e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLvrkAGGHDAGKLYAMKVLRKAAlvQRAKTQEHTRTERSVL-ELvrQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd06606    6 ELLGKGSFGSVYL---ALNLDTGELMAVKEVELSG--DSEEELEALEREIRILsSL--KHPNIVRYLGTERTENTLNIFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK-ERT 194
Cdd:cd06606   79 EYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATgEGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVSRRILKC--SPPFPPRIGPVAQDL 272
Cdd:cd06606  159 KSLRGTPYWMAPEVIRG-EGYGRAADIWSLGCTVIEMATGKPPW---SELGNPVAALFKIGSSgePPPIPEHLSEEAKDF 234
                        250       260
                 ....*....|....*....|....*....
gi 663856869 273 LQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd06606  235 LRKCLQRDPKKRP-----TADELLQHPFL 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
32-301 5.98e-51

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 178.60  E-value: 5.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVflvrKAGGH-DAGKLYAMKVLRKAALvqrAKTQEHTRTER--SVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14081    2 PYRLGKTLGKGQTGLV----KLAKHcVTGQKVAIKIVNKEKL---SKESVLMKVEReiAIMKLIEH-PNVLKLYDVYENK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd14081   74 KYLYLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRIlkcsPPFPPRIGPV 268
Cdd:cd14081  154 GSLLET--SCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGV----FHIPHFISPD 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 269 AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14081  228 AQDLLRRMLEVNPEKRI-----TIEEIKKHPWF 255
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
409-672 7.70e-51

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 179.42  E-value: 7.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRR---LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14166   10 VLGSGAFSEVYLVKQRSTGKLYALKCIKKSplsRDSSLENEIAVLKRIK-HENIVTLEDIYESTTHYYLVMQLVSGGELF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLrpQSPGVpMQTPCFT 565
Cdd:cd14166   89 DRILERGVYTEKDASRVINQVLSAVKYLHEN-GIVHRDLKPENLLYLTPDENSKIMITDFGLSKM--EQNGI-MSTACGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVR 645
Cdd:cd14166  165 PGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY-------EETESRLFEKIKEGYYEFESPFWDDISESAKDFIR 237
                        250       260
                 ....*....|....*....|....*..
gi 663856869 646 GLLTVDPAKRLKLEGLRGSSWLQDGSA 672
Cdd:cd14166  238 HLLEKNPSKRYTCEKALSHPWIIGNTA 264
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
410-659 2.01e-50

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 177.03  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKI-----LSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEisrkkLNKKLQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFAR-LRPQSpgvpM-QTP 562
Cdd:cd14009   80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRS-KNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARsLQPAS----MaETL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEAKE 642
Cdd:cd14009  155 CGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSN-------HVQLLRNIERSDAVIPFPIAAQLSPDCKD 227
                        250
                 ....*....|....*..
gi 663856869 643 LVRGLLTVDPAKRLKLE 659
Cdd:cd14009  228 LLRRLLRRDPAERISFE 244
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
400-656 2.07e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 178.38  E-value: 2.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKIL-SRRLEANT----QREVAALRLCQsHPNVVNLHEVHHDQLHTYL 474
Cdd:cd14086    2 EYDLKEE---LGKGAFSVVRRCVQKSTGQEFAAKIInTKKLSARDhqklEREARICRLLK-HPNIVRLHDSISEEGFHYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFArlrpqs 554
Cdd:cd14086   78 VFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQN-GIVHRDLKPENLLLASKSKGAAVKLADFGLA------ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 pgVPMQ--TPCF-----TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQaaeimckIREGRFS 627
Cdd:cd14086  151 --IEVQgdQQAWfgfagTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQ-------IKAGAYD 221
                        250       260
                 ....*....|....*....|....*....
gi 663856869 628 LDGEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd14086  222 YPSPEWDTVTPEAKDLINQMLTVNPAKRI 250
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
32-296 2.17e-50

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 177.01  E-value: 2.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRkAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLL---GRPVAIKVLR-PELAEDEEFRERFLREARALARLSH-PNIVRVYDVGEDDGRP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd14014   76 YIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd14014  156 TQTGSVLGTPAYMAPEQARGGPVDPRS-DIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                        250       260
                 ....*....|....*....|....*
gi 663856869 272 LLQRLLCKDPKKRlgagPQGAQEVR 296
Cdd:cd14014  235 IILRALAKDPEER----PQSAAELL 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-451 6.67e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 182.52  E-value: 6.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRkAALVQRAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTDA 109
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARD---LRLGRPVALKVLR-PELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:COG0515   81 RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTGhGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPP----FPPRI 265
Cdd:COG0515  161 TLTQTGTVVGTPGYMAPEQARGEPV-DPRSDVYSLGVTLYELLTGRPPFDGD----SPAELLRAHLREPPPppseLRPDL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 266 GPVAQDLLQRLLCKDPKKRlgagPQGAQEVRNHpffqgLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPP 345
Cdd:COG0515  236 PPALDAIVLRALAKDPEER----YQSAAELAAA-----LRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 346 GSPPPGDPRIFQGYSFVAPSILFDHNNAVMTDGLEAPGAGDRPGRAAVARSAMMQYELDLREPALGQGSFSVCRRCRQRQ 425
Cdd:COG0515  307 AAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALA 386
                        410       420
                 ....*....|....*....|....*.
gi 663856869 426 SGQEFAVKILSRRLEANTQREVAALR 451
Cdd:COG0515  387 AAAAAAAAAAAAALAAAAAAAAAAAA 412
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
404-667 1.38e-49

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 174.91  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQR----EVAALRLCQsHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14074    6 DLEE-TLGRGHFAVVKLARHVFTGEKVAVKVIDKtKLDDVSKAhlfqEVRCMKLVQ-HPNVVRLYEVIDTQTKLYLILEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHI-RKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTpgAPVKIIDFGFARLRpqSPGV 557
Cdd:cd14074   84 GDGGDMYDYImKHENGLNEDLARKYFRQIVSAISYCHK-LHVVHRDLKPENVVFFEKQ--GLVKLTDFGFSNKF--QPGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQTPCFTLQYAAPELLAQQGYDE-SCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEawqgV 636
Cdd:cd14074  159 KLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEAN-------DSETLTMIMDCKYTVPAH----V 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 637 SEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14074  228 SPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
400-666 3.22e-49

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 173.74  E-value: 3.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdLRepALGQGSFSVCRRCRQRQSGQEFAVKILSR------RLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTY 473
Cdd:cd14663    1 RYEL-GR--TLGEGTFAKVKFARNTKTGESVAIKIIDKeqvareGMVEQIKREIAIMKLLR-HPNIVELHEVMATKTKIF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILY-ADDTpgapVKIIDFGFARL-R 551
Cdd:cd14663   77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSR-GVFHRDLKPENLLLdEDGN----LKISDFGLSALsE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 PQSPGVPMQTPCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLdg 630
Cdd:cd14663  152 QFRQDGLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFD-------DENLMALYRKIMKGEFEY-- 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 631 EAWqgVSEEAKELVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14663  223 PRW--FSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
410-667 4.19e-49

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 174.12  E-value: 4.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS-RRLEANTQREVAALRLCQ---------SHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14084   14 LGSGACGEVKLAYDKSTCKKVAIKIINkRKFTIGSRREINKPRNIEteieilkklSHPCIIKIEDFFDAEDDYYIVLELM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPgvPM 559
Cdd:cd14084   94 EGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSN-GIIHRDLKPENVLLSSQEEECLIKITDFGLSKILGETS--LM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLA---QQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQAAEimcKIREGRFSLDGEAWQGV 636
Cdd:cd14084  171 KTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPF---SEEYTQMSLKE---QILSGKYTFIPKAWKNV 244
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 637 SEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14084  245 SEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-284 1.09e-48

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 172.56  E-value: 1.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQEHtrtERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKA---TGKLVAIKCIDKKALKGKEDSLEN---EIAVLRKIKH-PNIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL---LDSEGHIVLTDFGLSKeflTE 189
Cdd:cd14083   78 LVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK---ME 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGErntqAEVSRRILKCS----PPFPPRI 265
Cdd:cd14083  155 DSGVMSTACGTPGYVAPEVLAQK-PYGKAVDCWSIGVISYILLCGYPPFYDEND----SKLFAQILKAEyefdSPYWDDI 229
                        250
                 ....*....|....*....
gi 663856869 266 GPVAQDLLQRLLCKDPKKR 284
Cdd:cd14083  230 SDSAKDFIRHLMEKDPNKR 248
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
410-656 1.66e-48

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 171.95  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN--TQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14087    9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRevCESELNVLRRV-RHTNIIQLIEVFETKERVYMVMELATGGELFDR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQ 567
Cdd:cd14087   88 IIAKGSFTERDATRVLQMVLDGVKYLHG-LGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGPNCLMKTTCGTPE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGL 647
Cdd:cd14087  167 YIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD-------DDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRL 239

                 ....*....
gi 663856869 648 LTVDPAKRL 656
Cdd:cd14087  240 LTVNPGERL 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
31-305 1.83e-48

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 172.01  E-value: 1.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRkaggHD-AGKLYAMKVLrkaALVQRAKTQEHTRTErsvLELVRQA--PFLVTLHYAFQT 107
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVR----HKpTGKIYALKKI---HVDGDEEFRKQLLRE---LKTLRSCesPYVVKCYGAFYK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLH-KLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeF 186
Cdd:cd06623   71 EGEISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISK-V 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtLEGERNTQAEVSRRILKCSPPFPP--R 264
Cdd:cd06623  150 LENTLDQCNTFVGTVTYMSPERIQGES-YSYAADIWSLGLTLLECALGKFPF-LPPGQPSFFELMQAICDGPPPSLPaeE 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLD 305
Cdd:cd06623  228 FSPEFRDFISACLQKDPKKRP-----SAAELLQHPFIKKAD 263
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
405-667 2.59e-48

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 171.71  E-value: 2.59e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAntQREVAALRLCQSHPNVVNLHEV----HHDQLHTYLVLELLR 480
Cdd:cd14172    7 LSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKA--RREVEHHWRASGGPHIVHILDVyenmHHGKRCLLIIMECME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKK--RHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPgvP 558
Cdd:cd14172   85 GGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHS-MNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQN--A 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqgGQSQAAEIMCKIREGRFSLDGEAWQGVSE 638
Cdd:cd14172  162 LQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNT---GQAISPGMKRRIRMGQYGFPNPEWAEVSE 238
                        250       260
                 ....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14172  239 EAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
39-299 3.83e-48

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 170.53  E-value: 3.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVR-KAgghdAGKLYAMKVLRKaalvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14006    1 LGRGRFGVVKRCIeKA----TGREFAAKFIPK-----RDKKKEAVLREISILNQLQH-PRIIQLHEAYESPTELVLILEL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS--EGHIVLTDFGLSKEFLTEEKerTF 195
Cdd:cd14006   71 CSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLNPGEE--LK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd14006  149 EIFGTPEFVAPEIVNGE-PVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRK 227
                        250       260
                 ....*....|....*....|....
gi 663856869 276 LLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd14006  228 LLVKEPRKRP-----TAQEALQHP 246
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
33-320 3.74e-47

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 169.31  E-value: 3.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALvQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVK---NTGQMYACKKLDKKRL-KKKSGEKMALLEKEILEKV-NSPFIVSLAYAFETKTHLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEE 190
Cdd:cd05607   79 LVMSLMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV--KE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP-PRIGPVA 269
Cdd:cd05607  157 GKPITQRAGTNGYMAPEILKEES-YSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVKFEhQNFTEEA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 270 QDLLQRLLCKDPKKRLGAGPQgAQEVRNHPFFQGLDWVALAARKIPAPFRP 320
Cdd:cd05607  236 KDICRLFLAKKPENRLGSRTN-DDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
410-667 4.03e-47

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 168.50  E-value: 4.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANT------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKINRE-KAGSsavkllEREVDILKHVN-HAHIIHLEEVFETPKRMYLVMELCEDGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYA----DDTPGAPVKIIDFGFArLRPQSPGVPM 559
Cdd:cd14097   87 LKELLLRKGFFSENETRHIIQSLASAVAYLHKN-DIVHRDLKLENILVKssiiDNNDKLNIKVTDFGLS-VQKYGLGEDM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 -QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGgqsqaaeIMCKIREGRFSLDGEAWQGVSE 638
Cdd:cd14097  165 lQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEK-------LFEEIRKGDLTFTQSVWQSVSD 237
                        250       260
                 ....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14097  238 AAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
399-672 6.09e-47

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 168.15  E-value: 6.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 399 MQYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYL 474
Cdd:cd14169    3 SVYELKEK---LGEGAFSEVVLAQERGSQRLVALKCIPKKAlrgkEAMVENEIAVLRRIN-HENIVSLEDIYESPTHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQS 554
Cdd:cd14169   79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLH-QLGIVHRDLKPENLLYATPFEDSKIMISDFGLSKIEAQG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 pgvPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIREGRFSLDGEAWQ 634
Cdd:cd14169  158 ---MLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDEND-------SELFNQILKAEYEFDSPYWD 227
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSA 672
Cdd:cd14169  228 DISESAKDFIRHLLERDPEKRFTCEQALQHPWISGDTA 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
410-656 7.76e-47

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 167.78  E-value: 7.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL--------EANTQREVaalrLCQ-SHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd05581    9 LGEGSYSTVVLAKEKETGKEYAIKVLDKRHiikekkvkYVTIEKEV----LSRlAHPGIVKLYYTFQDESKLYFVLEYAP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPqSPGVPMQ 560
Cdd:cd05581   85 NGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLH-SKGIIHRDLKPENILLDED---MHIKITDFGTAKVLG-PDSSPES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TP-----------------CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIRE 623
Cdd:cd05581  160 TKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSN-------EYLTFQKIVK 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 624 GRFSLDgeawQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05581  233 LEYEFP----ENFPPDAKDLIQKLLVLDPSKRL 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
410-661 1.32e-46

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 165.14  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT----QREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleelLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRH-FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFAR-LRPQSPGVPMQTPC 563
Cdd:cd00180   80 DLLKENKGpLSEEEALSILRQLLSALEYLHSN-GIIHRDLKPENILLDSD---GTVKLADFGLAKdLDSDDSLLKTTGGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMlsgqvpfqgasgqggqsqaaeimckiregrfsldgeawqgvsEEAKEL 643
Cdd:cd00180  156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL------------------------------------------EELKDL 193
                        250
                 ....*....|....*...
gi 663856869 644 VRGLLTVDPAKRLKLEGL 661
Cdd:cd00180  194 IRRMLQYDPKKRPSAKEL 211
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
33-299 1.96e-46

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 166.35  E-value: 1.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAalvqRAKTQEH-TRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKAT---DKEYALKIIDKA----KCKGKEHmIENEVAILRRVKH-PNIVQLIEEYDTDTEL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEGHIVLTDFGLSkefl 187
Cdd:cd14095   74 YLVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLA---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCSPPFPP---- 263
Cdd:cd14095  150 TEVKEPLFTVCGTPTYVAPEIL-AETGYGLKVDIWAAGVITYILLCGFPPF--RSPDRDQEELFDLILAGEFEFLSpywd 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHP 299
Cdd:cd14095  227 NISDSAKDLISRMLVVDPEKRYSAG-----QVLDHP 257
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
37-299 5.24e-46

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 165.64  E-value: 5.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAL-VQRAKTQEHTR---TERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14084   12 RTLGSGACGEVKLAYDK---STCKKVAIKIINKRKFtIGSRREINKPRnieTEIEILKKLSH-PCIIKIEDFFDAEDDYY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS---EGHIVLTDFGLSKefLTE 189
Cdd:cd14084   88 IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqeeECLIKITDFGLSK--ILG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILK----CSPPFPP 263
Cdd:cd14084  166 ETSLMKTLCGTPTYLAPEVLRSfgTEGYTRAVDCWSLGVILFICLSGYPPFS---EEYTQMSLKEQILSgkytFIPKAWK 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd14084  243 NVSEEAKDLVKKMLVVDPSRRP-----SIEEALEHP 273
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
39-285 6.94e-46

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 164.43  E-value: 6.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVflvrKAGGHDAGK-LYAMKVLRKAALVQraKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14075   10 LGSGNFSQV----KLGIHQLTKeKVAIKILDKTKLDQ--KTQRLLSREISSMEKLHH-PNIIRLYEVVETLSKLHLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfsF 197
Cdd:cd14075   83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNT--F 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLL 277
Cdd:cd14075  161 CGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAE----TVAKLKKCILEGTYTIPSYVSEPCQELIRGIL 236

                 ....*...
gi 663856869 278 CKDPKKRL 285
Cdd:cd14075  237 QPVPSDRY 244
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
33-284 9.99e-46

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 164.10  E-value: 9.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQeHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14073    3 YELLETLGKGTYGKV---KLAIERATGREVAIKSIKKDKIEDEQDMV-RIRREIEIMSSL-NHPHIIRIYEVFENKDKIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlteeKE 192
Cdd:cd14073   78 IVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLY----SK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTF--SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtleGERNTQaeVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14073  154 DKLlqTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPF---DGSDFK--RLVKQISSGDYREPTQPSDAS 228
                        250
                 ....*....|....
gi 663856869 271 DLLQRLLCKDPKKR 284
Cdd:cd14073  229 GLIRWMLTVNPKRR 242
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
33-301 1.10e-45

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 164.28  E-value: 1.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDAGKLyAMKVLRKAalvqRAKTQEHTR---TERSVLELVRQaPFLVTLHYAFQTDA 109
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGLKEKV-ACKIIDKK----KAPKDFLEKflpRELEILRKLRH-PNIIQVYSIFERGS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlTE 189
Cdd:cd14080   76 KVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLC-PD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFS--FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtleGERNT----QAEVSRRILkcsppFPP 263
Cdd:cd14080  155 DDGDVLSktFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPF---DDSNIkkmlKDQQNRKVR-----FPS 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 264 R---IGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd14080  227 SvkkLSPECKDLIDQLLEPDPTKRATIE-----EILNHPWL 262
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
410-667 1.76e-45

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 163.88  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-RLE----------------ANTQREVAALRLCQsHPNVVNLHEV----HHD 468
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKsRLRkrregkndrgkiknalDDVRREIAIMKKLD-HPNIVRLYEViddpESD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 469 QLhtYLV----LELLRGGELLEHIRKKrhFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILY-ADDTpgapVKII 543
Cdd:cd14008   80 KL--YLVleycEGGPVMELDSGDRVPP--LPEETARKYFRDLVLGLEYLHE-NGIVHRDIKPENLLLtADGT----VKIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 544 DFGFARLRPQSPGVPMQTPCfTLQYAAPELLA--QQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCK 620
Cdd:cd14008  151 DFGVSEMFEDGNDTLQKTAG-TPAFLAPELCDgdSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNIL-------ELYEA 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 621 IREGRFSLDgeaWQG-VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14008  223 IQNQNDEFP---IPPeLSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
29-300 1.94e-45

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 163.59  E-value: 1.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14116    3 ALEDFEIGRPLGKGKFGNVYLARE---KQSKFILALKVLFKAQL-EKAGVEHQLRREVEIQSHLRH-PNILRLYGYFHDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSkefLT 188
Cdd:cd14116   78 TRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS---VH 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPV 268
Cdd:cd14116  155 APSSRRTTLCGTLDYLPPEMIEGRM-HDEKVDLWSLGVLCYEFLVGKPPF----EANTYQETYKRISRVEFTFPDFVTEG 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 269 AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14116  230 ARDLISRLLKHNPSQRP-----MLREVLEHPW 256
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
404-667 2.50e-45

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 163.27  E-value: 2.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14167    6 DFRE-VLGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlegkETSIENEIAVLHKIK-HPNIVALDDIYESGGHLYLIMQLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLrpQSPGVPM 559
Cdd:cd14167   84 SGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHD-MGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKI--EGSGSVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14167  161 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY-------DENDAKLFEQILKAEYEFDSPYWDDISDS 233
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14167  234 AKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
32-300 4.00e-45

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 162.85  E-value: 4.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAalvQRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAKL 111
Cdd:cd14010    1 NYVLYDEIGRGKHSVVYKGRRKG---TIEFVAIKCVDKS---KRPEVLNEVRLTHEL-----KHPNVLKFYEWYETSNHL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEK 191
Cdd:cd14010   70 WLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARR-EGEIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTF----------------SFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRIL 255
Cdd:cd14010  149 KELFgqfsdegnvnkvskkqAKRGTPYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPFVAE----SFTELVEKIL 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 256 KCSPPFPP---RIGPVA--QDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14010  224 NEDPPPPPpkvSSKPSPdfKSLLKGLLEKDPAKRLSWD-----ELVKHPF 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
410-764 7.76e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 168.27  E-value: 7.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:COG0515   15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPearerfRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPQSPGVPMQTPC 563
Cdd:COG0515   94 LADLLRRRGPLPPAEALRILAQLAEALAAAHA-AGIVHRDIKPANILLTPD--GR-VKLIDFGIARALGGATLTQTGTVV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEAKEL 643
Cdd:COG0515  170 GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDS-------PAELLRAHLREPPPPPSELRPDLPPALDAI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 644 VRGLLTVDPAKRLK-----LEGLRgSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGFFLKSVENA 718
Cdd:COG0515  243 VLRALAKDPEERYQsaaelAAALR-AVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 719 PLAKRRKQKLRSATASRRGSPAPANPGRAPVASKGAPRRANGPLPP 764
Cdd:COG0515  322 APAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAA 367
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
33-301 8.84e-45

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 161.22  E-value: 8.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkaggHDA-GKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKL 111
Cdd:cd05122    2 FEILEKIGKGGFGVVYKAR----HKKtGQIVAIKKIN----LESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGG---EMFTHLYQRqyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLT 188
Cdd:cd05122   73 WIVMEFCSGGslkDLLKNTNKT--LTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERtFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPF---PPRI 265
Cdd:cd05122  150 DGKTR-NTFVGTPYWMAPEVIQ-GKPYGFKADIWSLGITAIEMAEGKPPY----SELPPMKALFLIATNGPPGlrnPKKW 223
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd05122  224 SKEFKDFLKKCLQKDPEKRP-----TAEQLLKHPFI 254
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
400-655 1.68e-44

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 160.83  E-value: 1.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCqSHPNVVNLHEVHHDQLHTY 473
Cdd:cd14014    1 RYRLVRL---LGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeefrerFLREARALARL-SHPNIVRVYDVGEDDGRPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQ 553
Cdd:cd14014   77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHR-AGIVHRDIKPANILLTEDGR---VKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAW 633
Cdd:cd14014  153 SGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-------PAAVLAKHLQEAPPPPSPLN 225
                        250       260
                 ....*....|....*....|..
gi 663856869 634 QGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd14014  226 PDVPPALDAIILRALAKDPEER 247
Pkinase pfam00069
Protein kinase domain;
410-667 1.94e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 158.95  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR-----LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEkikkkKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  485 LEHIRKKRHFSESEASQILRSLVSAVSfmheeagvvhrdlkpenilyaddtpgapvkiidfgfarlrpqsPGVPMQTPCF 564
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLE-------------------------------------------SGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggQSQAAEIMCKIREGRFsldgeaWQGVSEEAKELV 644
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGN--EIYELIIDQPYAFPEL------PSNLSEEAKDLL 194
                         250       260
                  ....*....|....*....|...
gi 663856869  645 RGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQHPWF 217
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
410-655 2.57e-44

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 160.33  E-value: 2.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT-------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd14098    8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNdknlqlfQREINILKSLE-HPGIVRLIDWYEDDQHIYLVMEYVEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgAPVKIIDFGFARLrpQSPGVPMQTP 562
Cdd:cd14098   87 DLMDFIMAWGAIPEQHARELTKQILEAMAYTHSM-GITHRDLKPENILITQDDP-VIVKISDFGLAKV--IHTGTFLVTF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQ------GYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGV 636
Cdd:cd14098  163 CGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSS-------QLPVEKRIRKGRYTQPPLVDFNI 235
                        250
                 ....*....|....*....
gi 663856869 637 SEEAKELVRGLLTVDPAKR 655
Cdd:cd14098  236 SEEAIDFILRLLDVDPEKR 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
410-666 3.32e-44

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 160.11  E-value: 3.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQREVAALRLCQ--SHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14185    8 IGDGNFAVVKECRHWNENQEYAMKIIDKsKLKGKEDMIESEILIIKslSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQspgvPMQTPCFT 565
Cdd:cd14185   88 AIIESVKFTEHDAALMIIDLCEALVYIHSKH-IVHRDLKPENLLVQHNPDKStTLKLADFGLAKYVTG----PIFTVCGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgaSGQGGQSQAAEImckIREGRFSLDGEAWQGVSEEAKELVR 645
Cdd:cd14185  163 PTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFR--SPERDQEELFQI---IQLGHYEFLPPYWDNISEAAKDLIS 237
                        250       260
                 ....*....|....*....|.
gi 663856869 646 GLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14185  238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
410-667 3.79e-44

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 160.35  E-value: 3.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEAN--------TQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14105   13 LGSGQFAVVKKCREKSTGLEYAAKfIKKRRSKASrrgvsredIEREVSILRQVL-HPNIITLHDVFENKTDVVLILELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENI-LYADDTPGAPVKIIDFGFARLrpQSPGVPM 559
Cdd:cd14105   92 GGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTK-NIAHFDLKPENImLLDKNVPIPRIKLIDFGLAHK--IEDGNEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14105  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ-------ETLANITAVNYDFDDEYFSNTSEL 241
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14105  242 AKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
424-685 6.54e-44

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 160.59  E-value: 6.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 424 RQSGQEFAVKILSRRLEAntQREVAALRLCQSHPNVVNLHEVHHDQLHT----YLVLELLRGGELLEHI--RKKRHFSES 497
Cdd:cd14170   24 KRTQEKFALKMLQDCPKA--RREVELHWRASQCPHIVRIVDVYENLYAGrkclLIVMECLDGGELFSRIqdRGDQAFTER 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 498 EASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARlrPQSPGVPMQTPCFTLQYAAPELLAQQ 577
Cdd:cd14170  102 EASEIMKSIGEAIQYLHS-INIAHRDVKPENLLYTSKRPNAILKLTDFGFAK--ETTSHNSLTTPCYTPYYVAPEVLGPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 578 GYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLK 657
Cdd:cd14170  179 KYDKSCDMWSLGVIMYILLCGYPPFY---SNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMT 255
                        250       260
                 ....*....|....*....|....*...
gi 663856869 658 LEGLRGSSWLQDGSARSSPPLRTPDVLE 685
Cdd:cd14170  256 ITEFMNHPWIMQSTKVPQTPLHTSRVLK 283
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
410-659 1.02e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 159.37  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS-----------RRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14181   18 IGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeqlEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVFDL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLrpQSPGVP 558
Cdd:cd14181   98 MRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHAN-NIVHRDLKPENILLDDQ---LHIKLSDFGFSCH--LEPGEK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELL------AQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEA 632
Cdd:cd14181  172 LRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFW-------HRRQMLMLRMIMEGRYQFSSPE 244
                        250       260
                 ....*....|....*....|....*..
gi 663856869 633 WQGVSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd14181  245 WDDRSSTVKDLISRLLVVDPEIRLTAE 271
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
43-301 1.10e-43

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 158.67  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  43 AYGKVFLVRKAGGHDAGKLYAMKVLRKAalvQRAKTQEH-TRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSGG 121
Cdd:cd14106   17 GRGKFAVVRKCIHKETGKEYAAKFLRKR---RRGQDCRNeILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAGG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE---GHIVLTDFGLSKefLTEEKERTFSFC 198
Cdd:cd14106   94 ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISR--VIGEGEEIREIL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 199 GTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPFPPR----IGPVAQDLLQ 274
Cdd:cd14106  172 GTPDYVAPEIL-SYEPISLATDMWSIGVLTYVLLTGHSPFG----GDDKQETFLNISQCNLDFPEElfkdVSPLAIDFIK 246
                        250       260
                 ....*....|....*....|....*..
gi 663856869 275 RLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14106  247 RLLVKDPEKRL-----TAKECLEHPWL 268
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
35-300 1.10e-43

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 158.80  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLVRKA--GGHDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14076    5 LGRTLGEGEFGKVKLGWPLpkANHRSGVQVAIKLIRRDTQQENCQTSKIMR-EINILKGLTH-PNIVRLLDVLKTKKYIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKE 192
Cdd:cd14076   83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFSFCGTIEYMAPEIIRSKTG-HGKAVDWWSLGILLFELLTGASPFTLEGErNTQAEVSRRILK--CSPP--FPPRIGP 267
Cdd:cd14076  163 LMSTSCGSPCYAAPELVVSDSMyAGRKADIWSCGVILYAMLAGYLPFDDDPH-NPNGDNVPRLYRyiCNTPliFPEYVTP 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 268 VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14076  242 KARDLLRRILVPNPRKRI-----RLSAIMRHAW 269
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-303 1.45e-43

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 159.00  E-value: 1.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVqRAKTQEHtrtERSVLELVRQAPfLVTLHYAFQTDAK 110
Cdd:cd14166    3 ETFIFMEVLGSGAFSEVYLVKQ---RSTGKLYALKCIKKSPLS-RDSSLEN---EIAVLKRIKHEN-IVTLEDIYESTTH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL---DSEGHIVLTDFGLSKefl 187
Cdd:cd14166   75 YYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd14166  152 MEQNGIMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISE 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 268 VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd14166  231 SAKDFIRHLLEKNPSKRY-----TCEKALSHPWIIG 261
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
33-300 2.49e-43

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 157.64  E-value: 2.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14098    2 YQIIDRLGSGTFAEV---KKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEH-PGIVRLIDWYEDDQHIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG--HIVLTDFGLSKefLTEE 190
Cdd:cd14098   78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAK--VIHT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKT-----GHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPP-- 263
Cdd:cd14098  156 GTFLVTFCGTMAYLAPEILMSKEqnlqgGYSNLVDMWSVGCLVYVMLTGALPF----DGSSQLPVEKRIRKGRYTQPPlv 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 264 --RIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14098  232 dfNISEEAIDFILRLLDVDPEKRMTAA-----QALDHPW 265
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
32-284 2.55e-43

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 157.30  E-value: 2.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALvQRAKTQEHTRTERSVLELvrQAPFLVTLHYAFQTDAKL 111
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHV---LTGREVAIKIIDKTQL-NPSSLQKLFREVRIMKIL--NHPNIVKLFEVIETEKTL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd14072   75 YLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd14072  155 LDT--FCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPF----DGQNLKELRERVLRGKYRIPFYMSTDCEN 228
                        250
                 ....*....|...
gi 663856869 272 LLQRLLCKDPKKR 284
Cdd:cd14072  229 LLKKFLVLNPSKR 241
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
410-667 3.42e-43

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 157.34  E-value: 3.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSG--QEFAVKILSRR------LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14080    8 IGEGSYSKVKLAEYTKSGlkEKVACKIIDKKkapkdfLEKFLPRELEILRKLR-HPNIIQVYSIFERGSKVFIFMEYAEH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILY-ADDTpgapVKIIDFGFARLRPQSPGVPM- 559
Cdd:cd14080   87 GDLLEYIQKRGALSESQARIWFRQLALAVQYLH-SLDIAHRDLKCENILLdSNNN----VKLSDFGFARLCPDDDGDVLs 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQGgqsqaaeiMCKI---REGRFSLDGEawqG 635
Cdd:cd14080  162 KTFCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKK--------MLKDqqnRKVRFPSSVK---K 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14080  231 LSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
31-301 3.58e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 157.52  E-value: 3.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVL----RKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd14093    3 AKYEPKEILGRGVSS---TVRRCIEKETGQEFAVKIIditgEKSSENEAEELREATRREIEILRQVSGHPNIIELHDVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:cd14093   80 SPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERtfSFCGTIEYMAPEIIRSKT-----GHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILK----- 256
Cdd:cd14093  160 DEGEKLR--ELCGTPGYLAPEVLKCSMydnapGYGKEVDMWACGVIMYTLLAGCPPFW----HRKQMVMLRNIMEgkyef 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 257 CSPPFpPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14093  234 GSPEW-DDISDTAKDLISKLLVVDPKKRL-----TAEEALEHPFF 272
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
30-301 6.57e-43

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 156.27  E-value: 6.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVflvrKAGGHD-AGKLYAMKVLRKAaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14079    1 IGNYILGKTLGVGSFGKV----KLAEHElTGHKVAVKILNRQ-KIKSLDMEEKIRREIQILKLFRH-PHIIRLYEVIETP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK---- 184
Cdd:cd14079   75 TDIFMVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNimrd 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 -EFLteekeRTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAeVSRRILKCSPPFPP 263
Cdd:cd14079  155 gEFL-----KT--SCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFD---DEHIPN-LFKKIKSGIYTIPS 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14079  224 HLSPGARDLIKRMLVVDPLKRI-----TIPEIRQHPWF 256
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
410-667 9.68e-43

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 156.25  E-value: 9.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR-----EVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRmeiihEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRH--FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVP--MQ 560
Cdd:cd14197   97 FNQCVADREeaFKEKDVKRLMKQILEGVSFLHNN-NVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELReiMG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEA 640
Cdd:cd14197  176 TP----EYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQ-------ETFLNISQMNVSYSEEEFEHLSESA 244
                        250       260
                 ....*....|....*....|....*..
gi 663856869 641 KELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14197  245 IDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
31-299 1.24e-42

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 155.62  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVflvrKAGGHDA-GKLYAMKVLRKAAL---VQRAKTQEhtrteRSVLELVRQapFLVTLHYAFQ 106
Cdd:cd14078    3 KYYELHETIGSGGFAKV----KLATHILtGEKVAIKIMDKKALgddLPRVKTEI-----EALKNLSHQ--HICRLYHVIE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:cd14078   72 TDNKIFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIG 266
Cdd:cd14078  152 KGGMDHHLETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPF----DDDNVMALYRKIQSGKYEEPEWLS 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 267 PVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd14078  228 PSSKLLLDQMLQVDPKKRI-----TVKELLNHP 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
31-300 2.03e-42

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 154.72  E-value: 2.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKaalvqRAKTQEHTRTERSVLELVRQA--PFLVTLHYAFQTD 108
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYT---GQVVALKFIPK-----RGKSEKELRNLRQEIEILRKLnhPNIIEMLDSFETK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGgEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE--- 185
Cdd:cd14002   73 KEFVVVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAmsc 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 ---FLTEEKertfsfcGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPFP 262
Cdd:cd14002  152 ntlVLTSIK-------GTPLYMAPELVQEQPYDHTA-DLWSLGCILYELFVGQPPFY----TNSIYQLVQMIVKDPVKWP 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLGAgPQgaqeVRNHPF 300
Cdd:cd14002  220 SNMSPEFKSFLQGLLNKDPSKRLSW-PD----LLEHPF 252
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
410-672 2.98e-42

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 155.98  E-value: 2.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14168   18 LGTGAFSEVVLAEERATGKLFAVKCIPKKAlkgkESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGELF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLrpQSPGVPMQTPCFT 565
Cdd:cd14168   97 DRIVEKGFYTEKDASTLIRQVLDAVYYLHR-MGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM--EGKGDVMSTACGT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVR 645
Cdd:cd14168  174 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY-------DENDSKLFEQILKADYEFDSPYWDDISDSAKDFIR 246
                        250       260
                 ....*....|....*....|....*..
gi 663856869 646 GLLTVDPAKRLKLEGLRGSSWLQDGSA 672
Cdd:cd14168  247 NLMEKDPNKRYTCEQALRHPWIAGDTA 273
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-308 3.22e-42

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 155.66  E-value: 3.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRAkTQEHTRTERSVLELvrQAPFLVTLHYAFQTDAK 110
Cdd:cd14086    1 DEYDLKEELGKGAFS---VVRRCVQKSTGQEFAAKIINTKKLSARD-HQKLEREARICRLL--KHPNIVRLHDSISEEGF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE--GHIV-LTDFGLSKEfL 187
Cdd:cd14086   75 HYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKskGAAVkLADFGLAIE-V 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTLEGerntQAEVSRRILKCSPPFPP---- 263
Cdd:cd14086  154 QGDQQAWFGFAGTPGYLSPEVLR-KDPYGKPVDIWACGVILYILLVGYPPFWDED----QHRLYAQIKAGAYDYPSpewd 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLDWVA 308
Cdd:cd14086  229 TVTPEAKDLINQMLTVNPAKRI-----TAAEALKHPWICQRDRVA 268
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
38-301 3.48e-42

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 155.13  E-value: 3.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGkvfLVRKAGGHDAGKLYAMKVLR----KAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHL 113
Cdd:cd14181   17 VIGRGVSS---VVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKER 193
Cdd:cd14181   94 VFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 tfSFCGTIEYMAPEIIR-----SKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILK-----CSPPFPP 263
Cdd:cd14181  174 --ELCGTPGYLAPEILKcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFW----HRRQMLMLRMIMEgryqfSSPEWDD 247
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 264 RiGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14181  248 R-SSTVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-303 6.29e-42

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 153.64  E-value: 6.29e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLvrkAGGHDAGKLYAMKVLRKAALVQRAKTQEHtrtERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVL---AEEKRTQKLVAIKCIAKKALEGKETSIEN---EIAVLHKIKH-PNIVALDDIYESGGH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL---LDSEGHIVLTDFGLSKefl 187
Cdd:cd14167   76 LYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSF-CGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGErntqAEVSRRILKCS----PPFP 262
Cdd:cd14167  153 IEGSGSVMSTaCGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDEND----AKLFEQILKAEyefdSPYW 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd14167  228 DDISDSAKDFIQHLMEKDPEKRF-----TCEQALQHPWIAG 263
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
410-667 1.14e-41

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 152.88  E-value: 1.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQR----EVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKtKLDQKTQRllsrEISSME-KLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLrpQSPGVPMQTPCF 564
Cdd:cd14075   89 YTKISTEGKLSESEAKPLFAQIVSAVKHMHEN-NIIHRDLKAENVFYASNN---CVKVGDFGFSTH--AKRGETLNTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGY-DESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEawqgVSEEAKEL 643
Cdd:cd14075  163 SPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAET-------VAKLKKCILEGTYTIPSY----VSEPCQEL 231
                        250       260
                 ....*....|....*....|....
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14075  232 IRGILQPVPSDRYSIDEIKNSEWL 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
401-667 1.84e-41

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 152.16  E-value: 1.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELdlrEPALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANT----QREVAALRLCqSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14071    2 YDI---ERTIGKGNFAVVKLARHRITKTEVAIKIIDKsQLDEENlkkiYREVQIMKML-NHPHIIKLYQVMETKDMLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLrpQSP 555
Cdd:cd14071   78 TEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKR-HIVHRDLKAENLLLDAN---MNIKIADFGFSNF--FKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GVPMQTPCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDgeawQ 634
Cdd:cd14071  152 GELLKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQ-------TLRDRVLSGRFRIP----F 220
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14071  221 FMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
33-284 2.79e-41

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 151.65  E-value: 2.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVflvrKAGGHDAGKLYAMKVLRKaalvQRAKTQE---HTRTERSVLELVRQaPFLVTLHYAFQTDA 109
Cdd:cd14161    5 YEFLETLGKGTYGRV----KKARDSSGRLVAIKSIRK----DRIKDEQdllHIRREIEIMSSLNH-PHIISVYEVFENSS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:cd14161   76 KIVIVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcSPPFPPRigpvA 269
Cdd:cd14161  156 KFLQT--YCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYR-EPTKPSD----A 228
                        250
                 ....*....|....*
gi 663856869 270 QDLLQRLLCKDPKKR 284
Cdd:cd14161  229 CGLIRWLLMVNPERR 243
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
403-685 4.72e-41

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 152.31  E-value: 4.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 403 LDLREpALGQGSFSVCRRCRQRQSGQEFAVKILS-RRLEANTQREVAAL----RLCQ--SHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14094    5 YELCE-VIGKGPFSVVRRCIHRETGQQFAVKIVDvAKFTSSPGLSTEDLkreaSICHmlKHPHIVELLETYSSDGMLYMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRH----FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLR 551
Cdd:cd14094   84 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 PQSP-------GVPmqtpcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaAEIMCKIREG 624
Cdd:cd14094  163 GESGlvaggrvGTP--------HFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--------ERLFEGIIKG 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 625 RFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDgSARSSPPLRTPDVLE 685
Cdd:cd14094  227 KYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKE-RDRYAYRIHLPETVE 286
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
410-667 6.00e-41

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 151.33  E-value: 6.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT---------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14194   13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgvsrediEREVSILKEIQ-HPNVITLHEVYENKTDVILILELVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYAD-DTPGAPVKIIDFGFArlRPQSPGVPM 559
Cdd:cd14194   92 GGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQ-IAHFDLKPENIMLLDrNVPKPRIKIIDFGLA--HKIDFGNEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14194  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ-------ETLANVSAVNYEFEDEYFSNTSAL 241
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14194  242 AKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
410-668 8.26e-41

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 150.92  E-value: 8.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEAN--------TQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14195   13 LGSGQFAIVRKCREKGTGKEYAAKfIKKRRLSSSrrgvsreeIEREVNILREIQ-HPNIITLHDIFENKTDVVLILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYAD-DTPGAPVKIIDFGFArlRPQSPGVPM 559
Cdd:cd14195   92 GGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKR-IAHFDLKPENIMLLDkNVPNPRIKLIDFGIA--HKIEAGNEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14195  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQ-------ETLTNISAVNYDFDEEYFSNTSEL 241
                        250       260
                 ....*....|....*....|....*....
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd14195  242 AKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
410-667 9.09e-41

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 150.49  E-value: 9.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR---------LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14196   13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvSREEIEREVSILRQVL-HPNIITLHDVYENRTDVVLILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGAP-VKIIDFGFArlRPQSPGVPM 559
Cdd:cd14196   92 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKK-IAHFDLKPENIMLLDKNIPIPhIKLIDFGLA--HEIEDGVEF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14196  169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQ-------ETLANITAVSYDFDEEFFSHTSEL 241
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14196  242 AKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
401-667 9.66e-41

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 150.46  E-value: 9.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRR-----LEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14198    9 YILTSKE--LGRGKFAVVRQCISKSTGQEYAAKFLKKRrrgqdCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHI--RKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQ 553
Cdd:cd14198   87 LEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNN-IVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVP--MQTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGE 631
Cdd:cd14198  166 ACELReiMGTP----EYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQ-------ETFLNISQVNVDYSEE 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 632 AWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14198  235 TFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
410-667 1.56e-40

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 149.63  E-value: 1.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT------QREVA---ALRlcqsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14099    9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPkqreklKSEIKihrSLK----HPNIVKFHDCFEDEENVYILLELCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFA-RLrpQSPGVPM 559
Cdd:cd14099   85 NGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSN-RIIHRDLKLGNLFLDENM---NVKIGDFGLAaRL--EYDGERK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLA-QQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAwqGVSE 638
Cdd:cd14099  159 KTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSD-------VKETYKRIKKNEYSFPSHL--SISD 229
                        250       260
                 ....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14099  230 EAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
39-300 1.83e-40

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 149.29  E-value: 1.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVqrAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14009    1 IGRGSFATVWKGRHK---QTGEVVAIKEISRKKLN--KKLQENLESEIAILKSIKH-PNIVRLYDVQKTEDFIYLVLEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG-HIVL--TDFGLSKEFLTEEKERTf 195
Cdd:cd14009   75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGdDPVLkiADFGFARSLQPASMAET- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 sFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRI----LKCSPPFPPRIGPVAQD 271
Cdd:cd14009  154 -LCGSPLYMAPEILQFQKYDAKA-DLWSVGAILFEMLVGKPPFR----GSNHVQLLRNIersdAVIPFPIAAQLSPDCKD 227
                        250       260
                 ....*....|....*....|....*....
gi 663856869 272 LLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14009  228 LLRRLLRRDPAERI-----SFEEFFAHPF 251
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
410-667 2.90e-40

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 148.53  E-value: 2.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA---VKILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLEllrggelle 486
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAakfIKCRKAKDREDVRNEIEIMNQLR-HPRLLQLYDAFETPREMVLVME--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIR----------KKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAPVKIIDFGFARLrpQSPG 556
Cdd:cd14103   71 YVAggelfervvdDDFELTERDCILFMRQICEGVQYMHKQ-GILHLDLKPENILCVSRT-GNQIKIIDFGLARK--YDPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIREGRFSLDGEAWQGV 636
Cdd:cd14103  147 KKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDND-------AETLANVTRAKWDFDDEAFDDI 219
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 637 SEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14103  220 SDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-303 2.95e-40

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 149.27  E-value: 2.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQEHtrtERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQE---RGSQRLVALKCIPKKALRGKEAMVEN---EIAVLRRI-NHENIVSLEDIYESPTHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS---EGHIVLTDFGLSKeflTE 189
Cdd:cd14169   78 LAMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK---IE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGErntqAEVSRRILKCS----PPFPPRI 265
Cdd:cd14169  155 AQGMLSTACGTPGYVAPELLEQKP-YGKAVDVWAIGVISYILLCGYPPFYDEND----SELFNQILKAEyefdSPYWDDI 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd14169  230 SESAKDFIRHLLERDPEKRF-----TCEQALQHPWISG 262
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
33-300 3.63e-40

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 148.72  E-value: 3.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTqeHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDDVSKA--HLFQEVRCMKLV-QHPNVVRLYEVIDTQTKLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL-DSEGHIVLTDFGLSKEFLTEE 190
Cdd:cd14074   79 LILELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFsfCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegERNtQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14074  159 KLETS--CGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQ---EAN-DSETLTMIMDCKYTVPAHVSPECK 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14074  233 DLIRRMLIRDPKKRASLE-----EIENHPW 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
32-300 5.44e-40

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 148.36  E-value: 5.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKA------ALVQRAKTQEHTRTERSVLE----LVRQAPFLVTL 101
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIR---TGEKCAIKIIPRAsnaglkKEREKRLEKEISRDIRTIREaalsSLLNHPHICRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd14077   79 RDFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcsppF 261
Cdd:cd14077  159 LSNLYDPRRLLRT--FCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVE----Y 232
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14077  233 PSYLSSECKSLISRMLVVDPKKRA-----TLEQVLNHPW 266
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
408-667 9.02e-40

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 147.44  E-value: 9.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 408 PALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT------QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14162    6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDylqkflPREIEVIKGLK-HPNLICFYEAIETTSRVYIIMELAEN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILY-ADDTpgapVKIIDFGFAR--LRPQSPGVP 558
Cdd:cd14162   85 GDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSK-GVVHRDLKCENLLLdKNNN----LKITDFGFARgvMKTKDGKPK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 M-QTPCFTLQYAAPELLAQQGYDES-CDLWSLGVILYMMLSGQVPFqgasgqgGQSQAAEIMCKIREG-RFSLDgeawQG 635
Cdd:cd14162  160 LsETYCGSYAYASPEILRGIPYDPFlSDIWSMGVVLYTMVYGRLPF-------DDSNLKVLLKQVQRRvVFPKN----PT 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 636 VSEEAKELVRGLLTvdPAK-RLKLEGLRGSSWL 667
Cdd:cd14162  229 VSEECKDLILRMLS--PVKkRITIEEIKRDPWF 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
33-303 1.09e-39

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 148.43  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHdagKLYAMKVLRKAAlvqrakTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQKGTQ---KPYAVKKLKKTV------DKKIVRTEIGVLLRLSH-PNIIKLKEIFETPTEIS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH---IVLTDFGLSKefLTE 189
Cdd:cd14085   75 LVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK--IVD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTleGERNTQaEVSRRILKCS----PPFPPRI 265
Cdd:cd14085  153 QQVTMKTVCGTPGYCAPEILRGCA-YGPEVDMWSVGVITYILLCGFEPFY--DERGDQ-YMFKRILNCDydfvSPWWDDV 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd14085  229 SLNAKDLVKKLIVLDPKKRL-----TTQQALQHPWVTG 261
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
410-661 1.59e-39

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 146.23  E-value: 1.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR--RLEANTQREVAALRL---CQSHPNVVNLHEV--HHDQLHTYLVLELLRGG 482
Cdd:cd05118    7 IGEGAFGTVWLARDKVTGEKVAIKKIKNdfRHPKAALREIKLLKHlndVEGHPNIVKLLDVfeHRGGNHLCLVFELMGMN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVKIIDFGFAR-LRPQSPGVPMQT 561
Cdd:cd05118   87 LYELIKDYPRGLPLDLIKSYLYQLLQALDFLHS-NGIIHRDLKPENILI--NLELGQLKLADFGLARsFTSPPYTPYVAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 pcftLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIREgrfsLDGeawqgvSEEA 640
Cdd:cd05118  164 ----RWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSE-------VDQLAKIVR----LLG------TPEA 222
                        250       260
                 ....*....|....*....|.
gi 663856869 641 KELVRGLLTVDPAKRLKLEGL 661
Cdd:cd05118  223 LDLLSKMLKYDPAKRITASQA 243
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
32-284 2.47e-39

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 146.34  E-value: 2.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVrkaggHD--AGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQA---PFLVTLHYAFQ 106
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLA-----VDlrTGRKYAIKCLYKSGPNSKDGNDFQKLPQLREIDLHRRVsrhPNIITLHDVFE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQ-RQYFKEAE-VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-SEGHIVLTDFGLS 183
Cdd:cd13993   76 TEVAIYIVLEYCPNGDLFEAITEnRIYVGKTElIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 kefLTEEKERTFSfCGTIEYMAPEIIRSKTGHGK-----AVDWWSLGILLFELLTGASPFTLEGErntQAEVSRRILKCS 258
Cdd:cd13993  156 ---TTEKISMDFG-VGSEFYMAPECFDEVGRSLKgypcaAGDIWSLGIILLNLTFGRNPWKIASE---SDPIFYDYYLNS 228
                        250       260
                 ....*....|....*....|....*....
gi 663856869 259 PPFPPRIGPVAQD---LLQRLLCKDPKKR 284
Cdd:cd13993  229 PNLFDVILPMSDDfynLLRQIFTVNPNNR 257
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
410-667 4.59e-39

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 146.43  E-value: 4.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-VCRRCRQRQSGQEFAVKILSR----------RLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14096    9 IGEGAFSnVYKAVPLRNTGKPVAIKVVRKadlssdnlkgSSRANILKEVQIMKRL-SHPNIVKLLDFQESDEYYYIVLEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILY--------------ADD---------- 534
Cdd:cd14096   88 ADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLH-EIGVVHRDIKPENLLFepipfipsivklrkADDdetkvdegef 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 535 TPG------APVKIIDFGFAR-LRPQSpgvpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASg 607
Cdd:cd14096  167 IPGvggggiGIVKLADFGLSKqVWDSN----TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDES- 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 608 qggQSQAAEimcKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14096  242 ---IETLTE---KISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
410-667 6.16e-39

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 145.10  E-value: 6.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVAVKILNRQkiksldMEEKIRREIQILKLF-RHPHIIRLYEVIETPTDIFMVMEYVSGGE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLrpQSPGVPMQTPC 563
Cdd:cd14079   89 LFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHM-VVHRDLKPENLLL---DSNMNVKIADFGLSNI--MRDGEFLKTSC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDES-CDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGEawqgVSEEAKE 642
Cdd:cd14079  163 GSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFD-------DEHIPNLFKKIKSGIYTIPSH----LSPGARD 231
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14079  232 LIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
410-667 6.67e-39

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 145.28  E-value: 6.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------------------TQREVAALRLCQsHPNVVNLHEVHHDQLH 471
Cdd:cd14077    9 IGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGlkkerekrlekeisrdirTIREAALSSLLN-HPHICRLRDFLRTPNH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 TYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLr 551
Cdd:cd14077   88 YYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNS-IVHRDLKIENILISKS---GNIKIIDFGLSNL- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 pQSPGVPMQTPCFTLQYAAPELLAQQGY-DESCDLWSLGVILYMMLSGQVPFQGASGQGGQSqaaeimcKIREGRFsldg 630
Cdd:cd14077  163 -YDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHA-------KIKKGKV---- 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 631 EAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14077  231 EYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
410-656 1.88e-38

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 144.29  E-value: 1.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS------------RRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd14182   11 LGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfspeevQELREATLKEIDILRKVSGHPNIIQLKDTYETNTFFFLVFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPqsPGV 557
Cdd:cd14182   91 LMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKL-NIVHRDLKPENILLDDDM---NIKLTDFGFSCQLD--PGE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQTPCFTLQYAAPELLA------QQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGE 631
Cdd:cd14182  165 KLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFW-------HRKQMLMLRMIMSGNYQFGSP 237
                        250       260
                 ....*....|....*....|....*
gi 663856869 632 AWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd14182  238 EWDDRSDTVKDLISRFLVVQPQKRY 262
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
30-300 2.20e-38

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 143.78  E-value: 2.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENF-ELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVL--RKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQ 106
Cdd:cd14105    3 VEDFyDIGEELGSGQFA---VVKKCREKSTGLEYAAKFIkkRRSKASRRGVSREDIEREVSILRQVLH-PNIITLHDVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGL 182
Cdd:cd14105   79 NKTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFltEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP 262
Cdd:cd14105  159 AHKI--EDGNEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYF 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14105  236 SNTSELAKDFIRQLLVKDPRKRM-----TIQESLRHPW 268
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31-284 2.61e-38

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 144.50  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvRKAGGHDAGKLYAMKVLRKAAL-------VQRAKTQEHTRTERSVlelvrQAPFLVTLHY 103
Cdd:cd14096    1 ENYRLINKIGEGAFSNVY--KAVPLRNTGKPVAIKVVRKADLssdnlkgSSRANILKEVQIMKRL-----SHPNIVKLLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS------------ 171
Cdd:cd14096   74 FQESDEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrk 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 172 ---------EGHIV------------LTDFGLSKEFLTEEkerTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFE 230
Cdd:cd14096  154 adddetkvdEGEFIpgvggggigivkLADFGLSKQVWDSN---TKTPCGTVGYTAPEVVKDER-YSKKVDMWALGCVLYT 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 231 LLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14096  230 LLCGFPPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKR 283
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
30-284 2.74e-38

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 143.42  E-value: 2.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVflvrKAGGHD-AGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14070    1 VGSYLIGRKLGEGSFAKV----REGLHAvTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRH-PNITQLLDILETE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd14070   76 NSYYLVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSF-CGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEgERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd14070  156 LGYSDPFSTqCGSPAYAAPELLARKK-YGPKVDVWSIGVNMYAMLTGTLPFTVE-PFSLRALHQKMVDKEMNPLPTDLSP 233
                        250
                 ....*....|....*..
gi 663856869 268 VAQDLLQRLLCKDPKKR 284
Cdd:cd14070  234 GAISFLRSLLEPDPLKR 250
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
410-656 2.89e-38

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 144.26  E-value: 2.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR------RLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05580    9 LGTGSFGRVRLVKHKDSGKYYALKILKKakiiklKQVEHVLNEKRILSEV-RHPFIVNLLGSFQDDRNLYMVMEYVPGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESE----ASQIlrslVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFA-RLRPQSpgvp 558
Cdd:cd05580   88 LFSLLRRSGRFPNDVakfyAAEV----VLALEYLHSL-DIVYRDLKPENLLL--DSDGH-IKITDFGFAkRVKDRT---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 mQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSE 638
Cdd:cd05580  156 -YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFF-------DENPMKIYEKILEGKIRFP----SFFDP 223
                        250
                 ....*....|....*...
gi 663856869 639 EAKELVRGLLTVDPAKRL 656
Cdd:cd05580  224 DAKDLIKRLLVVDLTKRL 241
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
27-317 3.46e-38

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 143.47  E-value: 3.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVRKAGGHdagKLYAMKVLRKAALVQRAktQEHTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd14117    2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSK---FIVALKVLFKSQIEKEG--VEHQLRREIEIQSHLRHPNILRLYNYFH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSkef 186
Cdd:cd14117   77 DRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIG 266
Cdd:cd14117  154 VHAPSLRRRTMCGTLDYLPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPF----ESASHTETYRRIVKVDLKFPPFLS 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 267 PVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPffqgldWVALAARKIPAP 317
Cdd:cd14117  229 DGSRDLISKLLRYHPSERL-----PLKGVMEHP------WVKANSRRVLPP 268
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
404-667 4.48e-38

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 142.52  E-value: 4.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRR-LEAN---TQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14078    6 ELHE-TIGSGGFAKVKLATHILTGEKVAIKIMDKKaLGDDlprVKTEIEALKNL-SHQHICRLYHVIETDNKIFMVLEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARlRPQS-PGVP 558
Cdd:cd14078   84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQ-GYAHRDLKPENLLLDEDQ---NLKLIDFGLCA-KPKGgMDHH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDES-CDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFslDGEAWqgVS 637
Cdd:cd14078  159 LETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPFD-------DDNVMALYRKIQSGKY--EEPEW--LS 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 638 EEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14078  228 PSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
37-300 6.00e-38

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 142.16  E-value: 6.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLvrkAGGHDAGKLYAMKVLRKAALVQRAKtQEHTRTERSVLELVR-QAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd06632    6 QLLGSGSFGSVYE---GFNGDTGDFFAVKEVSLVDDDKKSR-ESVKQLEQEIALLSKlRHPNIVQYYGTEREEDNLYIFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFThLYQR-QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEflTEEKERT 194
Cdd:cd06632   82 EYVPGGSIHK-LLQRyGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH--VEAFSFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGTIEYMAPEIIRSK-TGHGKAVDWWSLGILLFELLTGASPFT-LEGerntqAEVSRRILKCS--PPFPPRIGPVAQ 270
Cdd:cd06632  159 KSFKGSPYWMAPEVIMQKnSGYGLAVDIWSLGCTVLEMATGKPPWSqYEG-----VAAIFKIGNSGelPPIPDHLSPDAK 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRlgagPQgAQEVRNHPF 300
Cdd:cd06632  234 DFIRLCLQRDPEDR----PT-ASQLLEHPF 258
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
32-301 9.12e-38

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 141.59  E-value: 9.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALvqrakTQEHTRTERSVLELVRQA--PFLVTLHYAFQTDA 109
Cdd:cd06627    1 NYQLGDLIGRGAFGSVY---KGLNLNTGEFVAIKQISLEKI-----PKSDLKSVMGEIDLLKKLnhPNIVKYIGSVKTKD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTE 189
Cdd:cd06627   73 SLYIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK-LNE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVSRRILKCSPPFPPRIGPVA 269
Cdd:cd06627  152 VEKDENSVVGTPYWMAPEVIEMS-GVTTASDIWSVGCTVIELLTGNPPY---YDLQPMAALFRIVQDDHPPLPENISPEL 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 270 QDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd06627  228 RDFLLQCFQKDPTLRP-----SAKELLKHPWL 254
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
31-302 9.73e-38

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 142.36  E-value: 9.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVL-----RKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAF 105
Cdd:cd14182    3 EKYEPKEILGRGVSS---VVRRCIHKPTRQEYAVKIIditggGSFSPEEVQELREATLKEIDILRKVSGHPNIIQLKDTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd14182   80 ETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERtfSFCGTIEYMAPEIIR-----SKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILK---- 256
Cdd:cd14182  160 LDPGEKLR--EVCGTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFW----HRKQMLMLRMIMSgnyq 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 257 -CSPPFPPRIGPVaQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14182  234 fGSPEWDDRSDTV-KDLISRFLVVQPQKRY-----TAEEALAHPFFQ 274
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
31-301 2.09e-37

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 141.15  E-value: 2.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGT--GAYGKVFLVRKaggHDAGKLYAMKVLrkaalvqraKTQEHTRTERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:PHA03390  14 KNCEIVKKLKLidGKFGKVSVLKH---KPTQKLFVQKII---------KAKNFNAIEPMVHQLMKDNPNFIKLYYSVTTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-SEGHIVLTDFGLSKEFL 187
Cdd:PHA03390  82 KGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKIIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERtfsfcGTIEYMAPEIIRsktGHGKAV--DWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRI 265
Cdd:PHA03390 162 TPSCYD-----GTLDYFSPEKIK---GHNYDVsfDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLPFIKNV 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGAGpqgaQEVRNHPFF 301
Cdd:PHA03390 234 SKNANDFVQSMLKYNINYRLTNY----NEIIKHPFL 265
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
410-655 2.26e-37

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 140.68  E-value: 2.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKI-----LSRRLEANTQREVAALRLCQsHPNVVNLHE--VHHDQ------------L 470
Cdd:cd08215    8 IGKGSFGSAYLVRRKSDGKLYVLKEidlsnMSEKEREEALNEVKLLSKLK-HPNIVKYYEsfEENGKlcivmeyadggdL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HTYLvlellrggelLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENI-LYADDTpgapVKIIDFGFAR 549
Cdd:cd08215   87 AQKI----------KKQKKKGQPFPEEQILDWFVQICLALKYLHSR-KILHRDLKTQNIfLTKDGV----VKLGDFGISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 LrpQSPGVPM-QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGgqsqaaeIMCKIREGRFSL 628
Cdd:cd08215  152 V--LESTTDLaKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPA-------LVYKIVKGQYPP 222
                        250       260
                 ....*....|....*....|....*..
gi 663856869 629 DGEAWqgvSEEAKELVRGLLTVDPAKR 655
Cdd:cd08215  223 IPSQY---SSELRDLVNSMLQKDPEKR 246
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
33-300 4.00e-37

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 140.08  E-value: 4.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALvqRAKtQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHW---NENQEYAMKIIDKSKL--KGK-EDMIESEILIIKSLSH-PNIVKLFEVYETEKEIY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEGHIVLTDFGLSKEFLT 188
Cdd:cd14185   75 LILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EekerTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTlEGERNtQAEVSRRI----LKCSPPFPPR 264
Cdd:cd14185  155 P----IFTVCGTPTYVAPEIL-SEKGYGLEVDMWAAGVILYILLCGFPPFR-SPERD-QEELFQIIqlghYEFLPPYWDN 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14185  228 ISEAAKDLISRLLVVDPEKRY-----TAKQVLQHPW 258
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
31-300 5.05e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 139.61  E-value: 5.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVR--KAGGHDAGKLYAMKVLRKAALVQRAKTQE--HTRTER-SVLELvrqapflvtlhYAF 105
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARslHTGLEVAIKMIDKKAMQKAGMVQRVRNEVeiHCQLKHpSILEL-----------YNY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAK-LHLILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd14186   70 FEDSNyVYLVLEMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEfLTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQaevsRRILKCSPPFPP 263
Cdd:cd14186  150 TQ-LKMPHEKHFTMCGTPNYISPEIA-TRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTL----NKVVLADYEMPA 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14186  224 FLSREAQDLIHQLLRKNPADRL-----SLSSVLDHPF 255
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
409-669 6.12e-37

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 139.31  E-value: 6.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREvaaLRLCQS--HPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd05578    7 VIGKGSFGKVCIVQKKDTKKMFAMKymnkqkCIEKDSVRNVLNE---LEILQEleHPFLVNLWYSFQDEEDMYMVVDLLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPqsPGVPMQ 560
Cdd:cd05578   84 GGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSK-NIIHRDIKPDNILL--DEQGH-VHITDFNIATKLT--DGTLAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREgrFSldgEAWqgvSEEA 640
Cdd:cd05578  158 STSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVL--YP---AGW---SEEA 229
                        250       260
                 ....*....|....*....|....*....
gi 663856869 641 KELVRGLLTVDPAKRLKleglrGSSWLQD 669
Cdd:cd05578  230 IDLINKLLERDPQKRLG-----DLSDLKN 253
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
409-659 1.20e-36

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 139.39  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEANTQ----REVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd07832    7 RIGEGAHGIVFKAKDRETGETVALKkVALRKLEGGIPnqalREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLSSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEhIRKKRH-FSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQTP 562
Cdd:cd07832   87 SEV-LRDEERpLTEAQVKRYMRMLLKGVAYMH-ANRIMHRDLKPANLLISST---GVLKIADFGLARLFSEEDPRLYSHQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIR----------EGRFSL--- 628
Cdd:cd07832  162 VATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGE------NDIEQLAIVLRtlgtpnektwPELTSLpdy 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 629 --------DGEAWQGV----SEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd07832  236 nkitfpesKGIRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAE 278
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
410-666 1.25e-36

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 138.63  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14184    9 IGDGNFAVVKECVERSTGKEFALKIIDKAKccgkEHLIENEVSILRRVK-HPNIIMLIEEMDTPAELYLVMELVKGGDLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENIL---YADDTPGapVKIIDFGFARLRPQspgvPMQTP 562
Cdd:cd14184   88 DAITSSTKYTERDASAMVYNLASALKYLHG-LCIVHRDIKPENLLvceYPDGTKS--LKLGDFGLATVVEG----PLYTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqSQAAEIMCKIREGRFSLDGEAWQGVSEEAKE 642
Cdd:cd14184  161 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSEN-----NLQEDLFDQILLGKLEFPSPYWDNITDSAKE 235
                        250       260
                 ....*....|....*....|....
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14184  236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
33-301 1.64e-36

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 137.91  E-value: 1.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkaggHDAGKL-YAMKVLRKAALVQraKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd14071    2 YDIERTIGKGNFAVVKLAR----HRITKTeVAIKIIDKSQLDE--ENLKKIYREVQIMKMLNH-PHIIKLYQVMETKDML 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEK 191
Cdd:cd14071   75 YLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQD 271
Cdd:cd14071  155 LKT--WCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPF----DGSTLQTLRDRVLSGRFRIPFFMSTDCEH 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 272 LLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14071  229 LIRRMLVLDPSKRL-----TIEQIKKHKWM 253
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
410-669 1.93e-36

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 138.20  E-value: 1.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS----RRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14183   14 IGDGNFAVVKECVERSTGREYALKIINkskcRGKEHMIQNEVSILRRVK-HPNIVLLIEEMDMPTELYLVMELVKGGDLF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQspgvPMQTPCF 564
Cdd:cd14183   93 DAITSTNKYTERDASGMLYNLASAIKYLHS-LNIVHRDIKPENLLVYEHQDGSkSLKLGDFGLATVVDG----PLYTVCG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqgGQSQAAeIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd14183  168 TPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGS----GDDQEV-LFDQILMGQVDFPSPYWDNVSDSAKELI 242
                        250       260
                 ....*....|....*....|....*
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSWLQD 669
Cdd:cd14183  243 TMMLQVDVDQRYSALQVLEHPWVND 267
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
37-303 2.97e-36

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 138.97  E-value: 2.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRaktqehtrtERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd14092   12 EALGDGSFS---VCRKCVHKKTGQEFAVKIVSRRLDTSR---------EVQLLRLCQGHPNIVKLHEVFQDELHTYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---HIVLTDFGLSKefLTEEKER 193
Cdd:cd14092   80 LLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFAR--LKPENQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIR---SKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP----PRIG 266
Cdd:cd14092  158 LKTPCFTLPYAAPEVLKqalSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDFSFDgeewKNVS 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 267 PVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd14092  238 SEAKSLIQGLLTVDPSKRL-----TMSELRNHPWLQG 269
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-303 3.70e-36

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 138.64  E-value: 3.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQEHtrtERSVLELVRQAPfLVTLHYAFQTDAK 110
Cdd:cd14168   10 KIFEFKEVLGTGAFSEVVLAEERA---TGKLFAVKCIPKKALKGKESSIEN---EIAVLRKIKHEN-IVALEDIYESPNH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL---DSEGHIVLTDFGLSKefL 187
Cdd:cd14168   83 LYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK--M 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd14168  161 EGKGDVMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISD 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 268 VAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFFQG 303
Cdd:cd14168  240 SAKDFIRNLMEKDPNKR-----YTCEQALRHPWIAG 270
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
31-301 5.60e-36

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 136.69  E-value: 5.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGHDAgklYAMKVL---RKAALVQRAKTQE---HTR-TERSVLEL---VRQAPFLvt 100
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEA---VAVKFVdmkRAPGDCPENIKKEvciQKMlSHKNVVRFyghRREGEFQ-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 101 lhyafqtdaklHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDF 180
Cdd:cd14069   76 -----------YLFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEFLTEEKERTF-SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAE--VSRRILKC 257
Cdd:cd14069  145 GLATVFRYKGKERLLnKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSdwKENKKTYL 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 258 SPpfPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14069  225 TP--WKKIDTAALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
410-667 5.78e-36

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 136.36  E-value: 5.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14073    9 LGKGTYGKVKLAIERATGREVAIKsikkdkIEDEQDMVRIRREIEIMSSLN-HPHIIRIYEVFENKDKIVIVMEYASGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLrpQSPGVPMQTPC 563
Cdd:cd14073   88 LYDYISERRRLPEREARRIFRQIVSAVHYCHKN-GVVHRDLKLENILLDQN---GNAKIADFGLSNL--YSKDKLLQTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQaaeimckIREGRFsldGEAWQGvsEEAKE 642
Cdd:cd14073  162 GSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQ-------ISSGDY---REPTQP--SDASG 229
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14073  230 LIRWMLTVNPKRRATIEDIANHWWV 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
31-285 7.77e-36

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 136.69  E-value: 7.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVL--RKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14194    5 DYYDTGEELGSGQFA---VVKKCREKSTGLQYAAKFIkkRRTKSSRRGVSREDIEREVSILKEIQH-PNVITLHEVYENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGLSK 184
Cdd:cd14194   81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 --EFLTEEKertfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP 262
Cdd:cd14194  161 kiDFGNEFK----NIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF 235
                        250       260
                 ....*....|....*....|...
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRL 285
Cdd:cd14194  236 SNTSALAKDFIRRLLVKDPKKRM 258
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
32-286 1.17e-35

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 135.60  E-value: 1.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAALVQRAKtqEHTRTERSVLELVrQAPFLVTLHYAFQTDAKL 111
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSD---NQVYALKEVNLGSLSQKER--EDSVNEIRLLASV-NHPNIIRYKEAFLDGNRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQ----YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFL 187
Cdd:cd08530   75 CIVMEYAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK-VL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSfcGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRIG 266
Cdd:cd08530  154 KKNLAKTQI--GTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPF----EARTMQELRYKVCRGKfPPIPPVYS 226
                        250       260
                 ....*....|....*....|
gi 663856869 267 PVAQDLLQRLLCKDPKKRLG 286
Cdd:cd08530  227 QDLQQIIRSLLQVNPKKRPS 246
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
410-667 1.88e-35

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 134.95  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQ------REVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14072    8 IGKGNFAKVKLARHVLTGREVAIKIIDKT-QLNPSslqklfREVRIMK-ILNHPNIVKLFEVIETEKTLYLVMEYASGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFArlRPQSPGVPMQTPC 563
Cdd:cd14072   86 VFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQK-RIVHRDLKAENLLLDAD---MNIKIADFGFS--NEFTPGNKLDTFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEawqgVSEEAKE 642
Cdd:cd14072  160 GSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN-------LKELRERVLRGKYRIPFY----MSTDCEN 228
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14072  229 LLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
37-300 2.16e-35

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 135.12  E-value: 2.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLvrkAGGHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd06626    6 NKIGEGTFGKVYT---AVNLDTGELMAMKEIRFQDN--DPKTIKEIADEMKVLEGLDH-PNLVRYYGVEVHREEVYIFME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG----LSKEFLTEEKE 192
Cdd:cd06626   80 YCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGsavkLKNNTTTMAPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPF-TLEgerNTQAEVSRRILKCSPPFPPR--IGP 267
Cdd:cd06626  160 EVNSLVGTPAYMAPEVITGnkGEGHGRAADIWSLGCVVLEMATGKRPWsELD---NEWAIMYHVGMGHKPPIPDSlqLSP 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 268 VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd06626  237 EGKDFLSRCLESDPKKRP-----TASELLDHPF 264
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
31-302 2.57e-35

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 134.78  E-value: 2.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAAlvqraKTQEHTRTERSvLELVR--QAPFLVTLHYAFQTD 108
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRP---SGQIMAVKVIRLEI-----DEALQKQILRE-LDVLHkcNSPYIVGFYGAFYSE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMfthlyqRQYFKEAEV---RVYGG---EIVLALEHLH-KLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd06605   72 GDISICMEYMDGGSL------DKILKEVGRipeRILGKiavAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEfLTEEKERTFSfcGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQA--EVSRRILKCSP 259
Cdd:cd06605  146 VSGQ-LVDSLAKTFV--GTRSYMAPERISG-GKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMifELLSYIVDEPP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 260 PFPP--RIGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06605  222 PLLPsgKFSPDFQDFVSQCLQKDPTER-----PSYKELMEHPFIK 261
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
30-300 3.36e-35

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 134.70  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENF-ELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVL--RKAALVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQ 106
Cdd:cd14196    3 VEDFyDIGEELGSGQFA---IVKKCREKSTGLEYAAKFIkkRQSRASRRGVSREEIEREVSILRQV-LHPNIITLHDVYE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGL 182
Cdd:cd14196   79 NRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFltEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP 262
Cdd:cd14196  159 AHEI--EDGVEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFF 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14196  236 SHTSELAKDFIRKLLVKETRKRL-----TIQEALRHPW 268
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
402-656 3.36e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 136.49  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAA---LRLCQSHPNVVNLHEVHHDQLHTYLVL 476
Cdd:PTZ00263  19 DFEMGE-TLGTGSFGRVRIAKHKGTGEYYAIKCLKKReiLKMKQVQHVAQeksILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSpg 556
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSK-DIIYRDLKPENLLL--DNKGH-VKVTDFGFAKKVPDR-- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 vpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLdgEAWqgV 636
Cdd:PTZ00263 172 --TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDT-------PFRIYEKILAGRLKF--PNW--F 238
                        250       260
                 ....*....|....*....|
gi 663856869 637 SEEAKELVRGLLTVDPAKRL 656
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRL 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
33-300 5.44e-35

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 134.29  E-value: 5.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLrkaalvqrakTQEHTRTErsVLELVRQAPFLVTLHYAFQT----- 107
Cdd:cd06609    3 FTLLERIGKGSFGEVY---KGIDKRTNQVVAIKVI----------DLEEAEDE--IEDIQQEIQFLSQCDSPYITkyygs 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 ---DAKLHLILDYVSGGEMFtHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd06609   68 flkGSKLWIIMEYCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EfLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPF-TLEGERntqaeVSRRILKCSPPF-- 261
Cdd:cd06609  147 Q-LTSTMSKRNTFVGTPFWMAPEVIK-QSGYDEKADIWSLGITAIELAKGEPPLsDLHPMR-----VLFLIPKNNPPSle 219
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd06609  220 GNKFSKPFKDFVELCLNKDPKERP-----SAKELLKHKF 253
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
410-667 6.00e-35

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 133.97  E-value: 6.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRC--RQRQSGQEFAVKILSRRLEANTQREVAAlRLCQ--------SHPNVVNLHEVHHDQLHTY-LVLEL 478
Cdd:cd13994    1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDDESKRKDYVK-RLTSeyiissklHHPNIVKVLDLCQDLHGKWcLVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpGApVKIIDFGFA--RLRPQSPG 556
Cdd:cd13994   80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSH-GIAHRDLKPENILLDED--GV-LKLTDFGTAevFGMPAEKE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQT-PCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEimckiREGRFSLDGEAWQ 634
Cdd:cd13994  156 SPMSAgLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYE-----KSGDFTNGPYEPI 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 635 GVS--EEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd13994  231 ENLlpSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
39-299 6.37e-35

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 133.51  E-value: 6.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVF-LVRKAgghdAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14103    1 LGRGKFGTVYrCVEKA----TGKELAAKFIK----CRKAKDREDVRNEIEIMNQLRH-PRLLQLYDAFETPREMVLVMEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYF-KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH-IVLTDFGLSKEFLTEEKERT 194
Cdd:cd14103   72 VAGGELFERVVDDDFElTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 fsFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQ 274
Cdd:cd14103  152 --LFGTPEFVAPEVV-NYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFIS 228
                        250       260
                 ....*....|....*....|....*
gi 663856869 275 RLLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd14103  229 KLLVKDPRKRM-----SAAQCLQHP 248
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
33-288 7.94e-35

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 133.43  E-value: 7.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkaggHDAGKL-YAMKVLRKaalvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVE----HRVTRQpYAIKMIET-----KCRGREVCESELNVLRRVRH-TNIIQLIEVFETKERV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH---IVLTDFGLSKEFLT 188
Cdd:cd14087   73 YMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKC----SPPFPPR 264
Cdd:cd14087  153 GPNCLMKTTCGTPEYIAPEILLRKP-YTQSVDMWAVGVIAYILLSGTMPF----DDDNRTRLYRQILRAkysySGEPWPS 227
                        250       260
                 ....*....|....*....|....
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLGAG 288
Cdd:cd14087  228 VSNLAKDFIDRLLTVNPGERLSAT 251
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
410-661 9.22e-35

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 133.10  E-value: 9.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL----SRRLEANtQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd05122    8 IGKGGFGVVYKARHKKTGQIVAIKKInlesKEKKESI-LNEIAILKKCK-HPNIVKYYGSYLKKDELWIVMEFCSGGSLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRH-FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFA-RLrpqSPGVPMQTPC 563
Cdd:cd05122   86 DLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSH-GIIHRDIKAANILLTSD---GEVKLIDFGLSaQL---SDGKTRNTFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKI-REGRFSL-DGEAWqgvSEEAK 641
Cdd:cd05122  159 GTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS-------ELPPMKALFLIaTNGPPGLrNPKKW---SKEFK 228
                        250       260
                 ....*....|....*....|
gi 663856869 642 ELVRGLLTVDPAKRLKLEGL 661
Cdd:cd05122  229 DFLKKCLQKDPEKRPTAEQL 248
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-301 1.39e-34

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 132.66  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLV-RKAgghDaGKLYAMKVLRKAALVQRAKTQEHTrtERSVL-ELvrQAPFLVTLHYAF--QT 107
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVrRKS---D-GKILVWKEIDYGKMSEKEKQQLVS--EVNILrEL--KHPNIVRYYDRIvdRA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFT----HLYQRQYFKEAEVRVYGGEIVLALEHLHKLG-----IIYRDLKLENVLLDSEGHIVLT 178
Cdd:cd08217   73 NTTLYIVMEYCEGGDLAQlikkCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEfLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlegERNTQAEVSRRIlKCS 258
Cdd:cd08217  153 DFGLARV-LSHDSSFAKTYVGTPYYMSPELLNEQSYDEKS-DIWSLGCLIYELCALHPPF----QAANQLELAKKI-KEG 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 259 --PPFPPRIGPVAQDLLQRLLCKDPKKRlgagPqGAQEVRNHPFF 301
Cdd:cd08217  226 kfPRIPSRYSSELNEVIKSMLNVDPDKR----P-SVEELLQLPLI 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
410-656 1.53e-34

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 133.38  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE-------ANTQREVAALR-LcqSHPNVVNLHEVHHDQLHTYLVlellrg 481
Cdd:cd07829    7 LGEGTYGVVYKAKDKKTGEIVALKKI--RLDneeegipSTALREISLLKeL--KHPNIVKLLDVIHTENKLYLV------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 gelLEHI---------RKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDtpGApVKIIDFGFAR--- 549
Cdd:cd07829   77 ---FEYCdqdlkkyldKRPGPLPPNLIKSIMYQLLRGLAYCH-SHRILHRDLKPQNLLINRD--GV-LKLADFGLARafg 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 --LRPQSPGVpmqtpcFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqgGQSQAAEIMcKIregrF 626
Cdd:cd07829  150 ipLRTYTHEV------VTLWYRAPEiLLGSKHYSTAVDIWSVGCIFAELITGKPLFP------GDSEIDQLF-KI----F 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 627 SLDG----EAWQGVS-------------------------EEAKELVRGLLTVDPAKRL 656
Cdd:cd07829  213 QILGtpteESWPGVTklpdykptfpkwpkndlekvlprldPEGIDLLSKMLQYNPAKRI 271
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
33-301 1.97e-34

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 131.97  E-value: 1.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVR---QAPFLVTLHYAF--QT 107
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARD---KVTGEKVAIKKIK-----NDFRHPKAALREIKLLKHLNdveGHPNIVKLLDVFehRG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYvsggeMFTHLYQ-----RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-SEGHIVLTDFG 181
Cdd:cd05118   73 GNHLCLVFEL-----MGMNLYElikdyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKErtfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGaSPFTLEGERNTQAEVSRRILkcsppf 261
Cdd:cd05118  148 LARSFTSPPYT---PYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTG-RPLFPGDSEVDQLAKIVRLL------ 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 262 ppriG-PVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd05118  218 ----GtPEALDLLSKMLKYDPAKRITAS-----QALAHPYF 249
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
39-300 2.01e-34

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 132.03  E-value: 2.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHD---AGKLYAMKVLRKAALvqraktqEHTRTERSVLELVRQaPFLVTLHyAFQTDAK-LHLI 114
Cdd:cd14121    3 LGSGTYATVYKAYRKSGARevvAVKCVSKSSLNKAST-------ENLLTEIELLKKLKH-PHIVELK-DFQWDEEhIYLI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVL--TDFGLSKeFLTEEKE 192
Cdd:cd14121   74 MEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFGFAQ-HLKPNDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSP---PFPPRIGPVA 269
Cdd:cd14121  153 AH-SLRGSPLYMAPEMILKKK-YDARVDLWSVGVILYECLFGRAPFA----SRSFEELEEKIRSSKPieiPTRPELSADC 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 270 QDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14121  227 RDLLLRLLQRDPDRRI-----SFEEFFAHPF 252
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
45-301 2.66e-34

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 132.37  E-value: 2.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  45 GKVFLVRKAGGHDAGKLYAMKVLRKaalvqRAKTQEhTRTER----SVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSG 120
Cdd:cd14197   20 GKFAVVRKCVEKDSGKEFAAKFMRK-----RRKGQD-CRMEIiheiAVLELAQANPWVINLHEVYETASEMILVLEYAAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 121 GEMFTHLY--QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE---GHIVLTDFGLSKEFLTEEKERtf 195
Cdd:cd14197   94 GEIFNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELR-- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd14197  172 EIMGTPEYVAPEIL-SYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKT 250
                        250       260
                 ....*....|....*....|....*.
gi 663856869 276 LLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd14197  251 LLIKKPENR-----ATAEDCLKHPWL 271
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
39-284 2.87e-34

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 131.12  E-value: 2.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVR-KagghdaGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd13999    1 IGSGSFGEVYKGKwR------GTDVAIKKLKVEDD--NDELLKEFRREVSILSKLRH-PNIVQFIGACLSPPPLCIVTEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKERTFS 196
Cdd:cd13999   72 MPGGSLYDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR-IKNSTTEKMTG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 197 FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd13999  151 VVGTPRWMAPEVLRGEP-YTEKADVYSFGIVLWELLTGEVPF--KELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRC 227

                 ....*...
gi 663856869 277 LCKDPKKR 284
Cdd:cd13999  228 WNEDPEKR 235
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
38-307 4.09e-34

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 132.15  E-value: 4.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAK------TQEHTRTERSVLELVRqapflvtlhyAFQTDAKL 111
Cdd:cd14090    9 LLGEGAYASV---QTCINLYTGKEYAVKIIEKHPGHSRSRvfreveTLHQCQGHPNILQLIE----------YFEDDERF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV---LTDFGL-SKEFL 187
Cdd:cd14090   76 YLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkICDFDLgSGIKL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERT------FSFCGTIEYMAPEIIRSKTG----HGKAVDWWSLGILLFELLTGASPFTLE---------GE--RNT 246
Cdd:cd14090  156 SSTSMTPvttpelLTPVGSAEYMAPEVVDAFVGealsYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrGEacQDC 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 247 QAEVSRRILKCSPPFPPR----IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPffqgldWV 307
Cdd:cd14090  236 QELLFHSIQEGEYEFPEKewshISAEAKDLISHLLVRDASQRY-----TAEQVLQHP------WV 289
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
39-301 4.60e-34

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 131.28  E-value: 4.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLV-RKAGGhdAGKLYAMKVLRKAALVQRAK-TQEHTRTERSVLELVRQaPFLVTLHYAFQT-DAKLHLIL 115
Cdd:cd13994    1 IGKGATSVVRIVtKKNPR--SGVLYAVKEYRRRDDESKRKdYVKRLTSEYIISSKLHH-PNIVKVLDLCQDlHGKWCLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT--EEKER 193
Cdd:cd13994   78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMpaEKESP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFS-FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTL---EGERNTQAEVSRRiLKCSPPFPPR--IGP 267
Cdd:cd13994  158 MSAgLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSakkSDSAYKAYEKSGD-FTNGPYEPIEnlLPS 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 268 VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd13994  237 ECRRLIYRMLHPDPEKRI-----TIDEALNDPWV 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
32-301 8.60e-34

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 130.05  E-value: 8.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFL-VRKAGGHDAgklyAMKVLRKAALVQRAKTQEHTR--TERSVLELVRQ--APFLVTLHYAFQ 106
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSgVRIRDGLPV----AVKFVPKSRVTEWAMINGPVPvpLEIALLLKASKpgVPGVIRLLDWYE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGE-MFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHIVLTDFGlSK 184
Cdd:cd14005   77 RPDGFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-CG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EFLTEEKERTFsfCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegeRNTQAEVSRRILkcsppFPPR 264
Cdd:cd14005  156 ALLKDSVYTDF--DGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPF-----ENDEQILRGNVL-----FRPR 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPFF 301
Cdd:cd14005  224 LSKECCDLISRCLQFDPSKR----PS-LEQILSHPWF 255
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
37-302 1.73e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 130.54  E-value: 1.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRT------ERSVLELVRqapflvtlhyAFQTDAK 110
Cdd:cd14174    8 ELLGEGAYAKV---QGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETlyqcqgNKNILELIE----------FFEDDTR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV---LTDFGLSKEFL 187
Cdd:cd14174   75 FYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpvkICDFDLGSGVK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSF------CGTIEYMAPEIIR----SKTGHGKAVDWWSLGILLFELLTGASPFT---------LEGE--RNT 246
Cdd:cd14174  155 LNSACTPITTpelttpCGSAEYMAPEVVEvftdEATFYDKRCDLWSLGVILYIMLSGYPPFVghcgtdcgwDRGEvcRVC 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 247 QAEVSRRILKCSPPFPPR----IGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFFQ 302
Cdd:cd14174  235 QNKLFESIQEGKYEFPDKdwshISSEAKDLISKLLVRDAKERLSAA-----QVLQHPWVQ 289
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
410-666 1.87e-33

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 129.33  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR--RLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14665    8 IGSGNFGVARLMRDKQTKELVAVKYIERgeKIDENVQREIINHRSLR-HPNIVRFKEVILTPTHLAIVMEYAAGGELFER 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYaDDTPGAPVKIIDFGFAR--LRPQSPGVPMQTPCft 565
Cdd:cd14665   87 ICNAGRFSEDEARFFFQQLISGVSYCH-SMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKssVLHSQPKSTVGTPA-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 lqYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEimcKIREGRFSLDGEAwqGVSEEAKELV 644
Cdd:cd14665  163 --YIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQ---RILSVQYSIPDYV--HISPECRHLI 235
                        250       260
                 ....*....|....*....|..
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14665  236 SRIFVADPATRITIPEIRNHEW 257
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
410-655 2.28e-33

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 129.18  E-value: 2.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilSRRLEANTQREVAALR-----LCQ-SHPNVVNL--HEVHHDQLHTYL------- 474
Cdd:cd06606    8 LGKGSFGSVYLALNLDTGELMAVK--EVELSGDSEEELEALEreiriLSSlKHPNIVRYlgTERTENTLNIFLeyvpggs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLEllrggelleHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFA-RLRPQ 553
Cdd:cd06606   86 LAS---------LLKKFGKLPEPVVRKYTRQILEGLEYLHS-NGIVHRDIKGANILV--DSDGV-VKLADFGCAkRLAEI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqGGQSQAAEIMCKIregrfSLDGEAW 633
Cdd:cd06606  153 ATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW------SELGNPVAALFKI-----GSSGEPP 221
                        250       260
                 ....*....|....*....|....*
gi 663856869 634 Q---GVSEEAKELVRGLLTVDPAKR 655
Cdd:cd06606  222 PipeHLSEEAKDFLRKCLQRDPKKR 246
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
32-301 2.45e-33

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 129.76  E-value: 2.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKvlrKAALVQR-AKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAK 110
Cdd:cd07832    1 RYKILGRIGEGAHGIVF---KAKDRETGETVALK---KVALRKLeGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGG--EMFTHlyQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFlT 188
Cdd:cd07832   75 FVLVFEYMLSSlsEVLRD--EERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLF-S 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRI----LKCSP---- 259
Cdd:cd07832  152 EEDPRLYSHqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLgtpnEKTWPelts 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 260 -P------FPPRIG-----------PVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07832  232 lPdynkitFPESKGirleeifpdcsPEAIDLLKGLLVYNPKKRL-----SAEEALRHPYF 286
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
410-656 2.67e-33

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 130.80  E-value: 2.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-------EAnTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLKKEViiedddvEC-TMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRpQSPGVPMQTP 562
Cdd:cd05570   82 DLMFHIQRARRFTEERARFYAAEICLALQFLHER-GIIYRDLKLDNVLL--DAEGH-IKIADFGMCKEG-IWGGNTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGrfslDGEAWQGVSEEAKE 642
Cdd:cd05570  157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDED-------ELFEAILND----EVLYPRWLSREAVS 225
                        250
                 ....*....|....
gi 663856869 643 LVRGLLTVDPAKRL 656
Cdd:cd05570  226 ILKGLLTKDPARRL 239
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
410-667 2.73e-33

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 128.99  E-value: 2.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA-----NTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14069    9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPgdcpeNIKKEVCIQKML-SHKNVVRFYGHRREGEFQYLFLEYASGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFA-RLRPQSPGVPMQTPC 563
Cdd:cd14069   88 FDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSC-GITHRDIKPENLLL--DENDN-LKISDFGLAtVFRYKGKERLLNKMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGASgqggqSQAAEIMCKIREGRFSLDgeAWQGVSEEAKE 642
Cdd:cd14069  164 GTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPWDQPS-----DSCQEYSDWKENKKTYLT--PWKKIDTAALS 236
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14069  237 LLRKILTENPNKRITIEDIKKHPWY 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
410-667 3.40e-33

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 128.86  E-value: 3.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANT-QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14114   10 LGTGAFGVVHRCTERATGNNFAAKFImtPHESDKETvRKEIQIMNQLH-HPKLINLHDAFEDDNEMVLILEFLSGGELFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRH-FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTpGAPVKIIDFGFA-RLRPQSPgVPMQTPcf 564
Cdd:cd14114   89 RIAAEHYkMSEAEVINYMRQVCEGLCHMHENN-IVHLDIKPENIMCTTKR-SNEVKLIDFGLAtHLDPKES-VKVTTG-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd14114  164 TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDD-------ETLRNVKSCDWNFDDSAFSGISEEAKDFI 236
                        250       260
                 ....*....|....*....|...
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14114  237 RKLLLADPNKRMTIHQALEHPWL 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
33-321 3.58e-33

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 129.68  E-value: 3.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL-VRKAgghdAGKLYAMKVLRKAalvQRAKTQEhtrtersVLELVR--QAPFLVTLHYAFQTDA 109
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRcIHKA----TGKEYAVKIIDKS---KRDPSEE-------IEILLRygQHPNIITLRDVYDDGN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH----IVLTDFGLSKE 185
Cdd:cd14091   68 SVYLVTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 fLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFtLEGERNTQAEVSRRI----LKCSPPF 261
Cdd:cd14091  148 -LRAENGLLMTPCYTANFVAPEVLK-KQGYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILARIgsgkIDLSGGN 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFFQglDWVALAARKIPAPFRPQ 321
Cdd:cd14091  225 WDHVSDSAKDLVRKMLHVDPSQRPTAA-----QVLQHPWIR--NRDSLPQRQLTDPQDAA 277
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
33-302 4.34e-33

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 128.10  E-value: 4.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRA---TGKEVAIKKMR-----LRKQNKELIINEILIMKECKH-PNIVDYYDSYLVGDELW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEK 191
Cdd:cd06614   73 VVMEYMDGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQ-LTKEK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASP-FTLEGERNTQAEVSRRIlkcsPPF--PPRIGPV 268
Cdd:cd06614  152 SKRNSVVGTPYWMAPEVIKRKD-YGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKGI----PPLknPEKWSPE 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 269 AQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06614  227 FKDFLNKCLVKDPEKR-----PSAEELLQHPFLK 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
420-667 4.48e-33

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 128.60  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 420 RCRQRQSGQEFAVKIL----SRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFS 495
Cdd:cd14088   19 RAKDKTTGKLYTCKKFlkrdGRKVRKAAKNEINILKMVK-HPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 496 ESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSpgvpMQTPCFTLQYAAPELLA 575
Cdd:cd14088   98 ERDTSNVIRQVLEAVAYLHS-LKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKLENGL----IKEPCGTPEYLAPEVVG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 576 QQGYDESCDLWSLGVILYMMLSGQVPF-QGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAK 654
Cdd:cd14088  173 RQRYGRPVDCWAIGVIMYILLSGNPPFyDEAEEDDYENHDKNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQ 252
                        250
                 ....*....|...
gi 663856869 655 RLKLEGLRGSSWL 667
Cdd:cd14088  253 RITAEEAISHEWI 265
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
33-285 5.17e-33

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 128.58  E-value: 5.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALV--QRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd14195    7 YEMGEELGSGQFA---IVRKCREKGTGKEYAAKFIKKRRLSssRRGVSREEIEREVNILREIQH-PNIITLHDIFENKTD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGLSKEF 186
Cdd:cd14195   83 VVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 ltEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIG 266
Cdd:cd14195  163 --EAGNEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTS 239
                        250
                 ....*....|....*....
gi 663856869 267 PVAQDLLQRLLCKDPKKRL 285
Cdd:cd14195  240 ELAKDFIRRLLVKDPKKRM 258
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
29-284 5.49e-33

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 128.50  E-value: 5.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTG--AYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQehTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd14198    1 SMDNFNNFYILTSKelGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAE--ILHEIAVLELAKSNPRVVNLHEVYE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLY--QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS---EGHIVLTDFG 181
Cdd:cd14198   79 TTSEIILILEYAAGGEIFNLCVpdLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIVDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERtfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPF 261
Cdd:cd14198  159 MSRKIGHACELR--EIMGTPEYLAPEILNYDP-ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEET 235
                        250       260
                 ....*....|....*....|...
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14198  236 FSSVSQLATDFIQKLLVKNPEKR 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
410-656 5.58e-33

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 128.11  E-value: 5.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKcvkkrhIVQTRQQEHIFSEKEILEEC-NSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSpGVPMQTPC 563
Cdd:cd05572   80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSR-GIIYRDLKPENLLL--DSNGY-VKLVDFGFAK-KLGS-GRKTWTFC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqggQSQAAEIMCKIREGRFSLdgEAWQGVSEEAKEL 643
Cdd:cd05572  154 GTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGD-----DEDPMKIYNIILKGIDKI--EFPKYIDKNAKNL 226
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05572  227 IKQLLRRNPEERL 239
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
410-667 6.23e-33

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 128.01  E-value: 6.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR-------LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKkakkdsyVTKNLRREGRIQQMIR-HPNITQLLDILETENSYYLVMELCPGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTpgaPVKIIDFGFAR-LRPQSPGVPMQT 561
Cdd:cd14070   89 NLMHRIYDKKRLEEREARRYIRQLVSAVEHLH-RAGVVHRDLKIENLLLDEND---NIKLIDFGLSNcAGILGYSDPFST 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqggqsqAAEIMCKIREGRFSLDGEAW---QGVSE 638
Cdd:cd14070  165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF-----------TVEPFSLRALHQKMVDKEMNplpTDLSP 233
                        250       260
                 ....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14070  234 GAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
410-666 7.26e-33

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 127.91  E-value: 7.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLR---- 480
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKlrfptKQESQLRNEVAILQQL-SHPGVVNLECMFETPERVFVVMEKLHgdml 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 -GGELLEHIRKKRHFSESEASQILrslvSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSP---- 555
Cdd:cd14082   90 eMILSSEKGRLPERITKFLVTQIL----VALRYLHSK-NIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSfrrs 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 --GVPmqtpcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqggqSQAAEIMCKIREGRFSLDGEAW 633
Cdd:cd14082  165 vvGTP--------AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF---------NEDEDINDQIQNAAFMYPPNPW 227
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 634 QGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14082  228 KEISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
33-301 7.52e-33

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 127.80  E-value: 7.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKaalvQRAK---TQEHTRTERSVLELVRQaPFLVTLHYAFQTDA 109
Cdd:cd14162    2 YIVGKTLGHGSYAVV---KKAYSTKHKCKVAIKIVSK----KKAPedyLQKFLPREIEVIKGLKH-PNLICFYEAIETTS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK-EFLT 188
Cdd:cd14162   74 RVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgVMKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFS--FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRilkcsPPFP--PR 264
Cdd:cd14162  154 KDGKPKLSetYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRR-----VVFPknPT 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 265 IGPVAQDLLQRLLCKdPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14162  229 VSEECKDLILRMLSP-VKKRI-----TIEEIKRDPWF 259
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
409-667 8.61e-33

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 127.38  E-value: 8.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREV---AALRlcqsHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14116   12 PLGKGKFGNVYLAREKQSKFILALKVLFKAqlekagVEHQLRREVeiqSHLR----HPNILRLYGYFHDATRVYLILEYA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPgvpM 559
Cdd:cd14116   88 PLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKR-VIHRDIKPENLLLGSA---GELKIADFGWSVHAPSSR---R 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEawqgVSEE 639
Cdd:cd14116  161 TTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQ-------ETYKRISRVEFTFPDF----VTEG 229
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14116  230 ARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
32-284 1.05e-32

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 127.14  E-value: 1.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVF-LVRKAGGHdagkLYAMKV--LRKAAlvqrAKTQEHTRTERSVLELVRqAPFLVTLHYAFQTD 108
Cdd:cd08529    1 DFEILNKLGKGSFGVVYkVVRKVDGR----VYALKQidISRMS----RKMREEAIDEARVLSKLN-SPYVIKYYDSFVDK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEM--FTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeF 186
Cdd:cd08529   72 GKLNIVMEYAENGDLhsLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK-I 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRI 265
Cdd:cd08529  151 LSDTTNFAQTIVGTPYYLSPELCEDKPYNEKS-DVWALGCVLYELCTGKHPF----EAQNQGALILKIVRGKyPPISASY 225
                        250
                 ....*....|....*....
gi 663856869 266 GPVAQDLLQRLLCKDPKKR 284
Cdd:cd08529  226 SQDLSQLIDSCLTKDYRQR 244
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
37-285 1.10e-32

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 128.62  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKaalvqraKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd14179   13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSK-------RMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---HIVLTDFGLSKeFLTEEKER 193
Cdd:cd14179   83 LLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFAR-LKPPDNQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTLEGER---NTQAEVSRRILKCSPPFP----PRIG 266
Cdd:cd14179  162 LKTPCFTLHYAAPELLN-YNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltcTSAEEIMKKIKQGDFSFEgeawKNVS 240
                        250
                 ....*....|....*....
gi 663856869 267 PVAQDLLQRLLCKDPKKRL 285
Cdd:cd14179  241 QEAKDLIQGLLTVDPNKRI 259
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
410-668 1.36e-32

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 126.94  E-value: 1.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRkqllRELKTLRSCE-SPYVVKCYGAFYKEGEISIVLEYMDGGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPQSpGVPMQTPCFT 565
Cdd:cd06623   88 DLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLINSK--GE-VKIADFGISKVLENT-LDQCNTFVGT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgASGQGGQsqaAEIMCKIREG-RFSLDGEAWqgvSEEAKELV 644
Cdd:cd06623  164 VTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFL-PPGQPSF---FELMQAICDGpPPSLPAEEF---SPEFRDFI 236
                        250       260
                 ....*....|....*....|....
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd06623  237 SACLQKDPKKRPSAAELLQHPFIK 260
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
39-301 1.76e-32

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 126.82  E-value: 1.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQT-DAKLHLILDY 117
Cdd:cd14165    9 LGEGSYAKV---KSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPR-ELEILARLNH-KSIIKTYEIFETsDGKVYIVMEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTF-- 195
Cdd:cd14165   84 GVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRIVls 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 -SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQaEVSRRILKCSPPFPPRIGPVAQ--DL 272
Cdd:cd14165  164 kTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYD---DSNVK-KMLKIQKEHRVRFPRSKNLTSEckDL 239
                        250       260
                 ....*....|....*....|....*....
gi 663856869 273 LQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14165  240 IYRLLQPDVSQRL-----CIDEVLSHPWL 263
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
33-300 2.18e-32

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 126.25  E-value: 2.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRD---KQTKELVAVKYIERGEKIDE-NVQREIINHRSL-----RHPNIVRFKEVILTPTHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG--HIVLTDFGLSKEFLTEE 190
Cdd:cd14665   73 IVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERtfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPP--RIGPV 268
Cdd:cd14665  153 QPK--STVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQYSIPDyvHISPE 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 269 AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14665  231 CRHLISRIFVADPATRI-----TIPEIRNHEW 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
410-659 2.20e-32

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 126.25  E-value: 2.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-VCRRCRQRQSGQEFAVK-ILSRRLEA----NTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14121    3 LGSGTYAtVYKAYRKSGAREVVAVKcVSKSSLNKasteNLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYAddTPGAPV-KIIDFGFARLrpQSPGVPMQTP 562
Cdd:cd14121   82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREH-NISHMDLKPQNLLLS--SRYNPVlKLADFGFAQH--LKPNDEAHSL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRfSLDGEAWQGVSEEAKE 642
Cdd:cd14121  157 RGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRS-------FEELEEKIRSSK-PIEIPTRPELSADCRD 228
                        250
                 ....*....|....*..
gi 663856869 643 LVRGLLTVDPAKRLKLE 659
Cdd:cd14121  229 LLLRLLQRDPDRRISFE 245
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
37-284 2.77e-32

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 126.20  E-value: 2.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALV---QRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAKLHL 113
Cdd:cd14187   13 RFLGKGGFAKCYEITDA---DTKEVFAGKIVPKSLLLkphQKEKMSMEIAIHRSL-----AHQHVVGFHGFFEDNDFVYV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEKER 193
Cdd:cd14187   85 VLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATK-VEYDGER 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLL 273
Cdd:cd14187  164 KKTLCGTPNYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLI 238
                        250
                 ....*....|.
gi 663856869 274 QRLLCKDPKKR 284
Cdd:cd14187  239 QKMLQTDPTAR 249
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
410-660 4.13e-32

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 125.56  E-value: 4.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQ-SGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQnllgKEIKILKELS-HENVVALLDCQETSSSVYLVMEYCNGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAP------VKIIDFGFARLRPQspGVP 558
Cdd:cd14120   80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSK-GIVHRDLKPQNILLSHNSGRKPspndirLKIADFGFARFLQD--GMM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQS---QAAEIMCKIREgrfsldgeawqG 635
Cdd:cd14120  157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAfyeKNANLRPNIPS-----------G 225
                        250       260
                 ....*....|....*....|....*
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEG 660
Cdd:cd14120  226 TSPALKDLLLGLLKRNPKDRIDFED 250
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
31-302 4.20e-32

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 126.01  E-value: 4.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVlrkaALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd06611    5 DIWEIIGELGDGAFGKVYKAQH---KETGLFAAAKI----IQIESEEELEDFMVEIDILSECKH-PNIVGLYEAYFYENK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTE 189
Cdd:cd06611   77 LWILIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAK-NKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTGHGKAVDW----WSLGILLFELLTGASPftlegerNTQAEVSR---RILKCSPPF- 261
Cdd:cd06611  156 TLQKRDTFIGTPYWMAPEVVACETFKDNPYDYkadiWSLGITLIELAQMEPP-------HHELNPMRvllKILKSEPPTl 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 262 --PPRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFFQ 302
Cdd:cd06611  229 dqPSKWSSSFNDFLKSCLVKDPDDRPTAA-----ELLKHPFVS 266
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
410-656 4.28e-32

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 126.40  E-value: 4.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSrrleantQREVAALRLCQ------------SHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd05612    9 IGTGTFGRVHLVRDRISEHYYALKVMA-------IPEVIRLKQEQhvhnekrvlkevSHPFIIRLFWTEHDQRFLYMLME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFAR-LRPQSpg 556
Cdd:cd05612   82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSK-EIVYRDLKPENILLDKE---GHIKLTDFGFAKkLRDRT-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 vpmQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFsldgEAWQGV 636
Cdd:cd05612  156 ---WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFD-------DNPFGIYEKILAGKL----EFPRHL 221
                        250       260
                 ....*....|....*....|
gi 663856869 637 SEEAKELVRGLLTVDPAKRL 656
Cdd:cd05612  222 DLYAKDLIKKLLVVDRTRRL 241
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
32-301 4.74e-32

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 125.55  E-value: 4.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVlrkaalVQRAKTQEHTRTERSVLElvRQAPFLVTLHY-------- 103
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDA---DTGRELAVKQ------VEIDPINTEASKEVKALE--CEIQLLKNLQHerivqyyg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd06625   70 CLQDEKSLSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLT-EEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegernTQAEVSRRILK-----C 257
Cdd:cd06625  150 KRLQTiCSSTGMKSVTGTPYWMSPEVI-NGEGYGRKADIWSVGCTVVEMLTTKPPW-------AEFEPMAAIFKiatqpT 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 258 SPPFPPRIGPVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPFF 301
Cdd:cd06625  222 NPQLPPHVSEDARDFLSLIFVRNKKQR----PS-AEELLSHSFV 260
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
410-606 6.37e-32

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 124.57  E-value: 6.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-VCR-RCRqrqsGQEFAVKIL-SRRLEANT----QREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd13999    1 IGSGSFGeVYKgKWR----GTDVAIKKLkVEDDNDELlkefRREVSILSKL-RHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRH-FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgapVKIIDFGFARLrPQSPGVPMQT 561
Cdd:cd13999   76 SLYDLLHKKKIpLSWSLRLKIALDIARGMNYLHSP-PIIHRDLKSLNILLDENFT---VKIADFGLSRI-KNSTTEKMTG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd13999  151 VVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELS 195
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
33-301 7.34e-32

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 124.81  E-value: 7.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKA-ALVQ---RAKTQEHTRTERSVLELVRQA--PFLVTLHYAFQ 106
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKS---KGKEVVIKFIFKErILVDtwvRDRKLGTVPLEIHILDTLNKRshPNIVKLLDFFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILD-YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKE 185
Cdd:cd14004   79 DDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG-SAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF-----TLEGERNTQAEVSRRilkcspp 260
Cdd:cd14004  158 YIKSGPFDT--FVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFynieeILEADLRIPYAVSED------- 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 261 fpprigpvAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14004  229 --------LIDLISRMLNRDVGDRP-----TIEELLTDPWL 256
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
66-301 1.26e-31

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 124.20  E-value: 1.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  66 VLRKAALVQRAKTQE------------HTRTERSVLElvRQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQ---- 129
Cdd:cd05576   11 VIDKVLLVMDTRTQEtfilkglrksseYSRERKTIIP--RCVPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKflnd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 130 ------------------RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEflTEEk 191
Cdd:cd05576   89 keihqlfadlderlaaasRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE--VED- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ertfSFCG-TIE--YMAPEI--IRSKTghgKAVDWWSLGILLFELLTGASpftlegerntqaevsrrILKCSPP------ 260
Cdd:cd05576  166 ----SCDSdAIEnmYCAPEVggISEET---EACDWWSLGALLFELLTGKA-----------------LVECHPAgintht 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 261 ---FPPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFF 301
Cdd:cd05576  222 tlnIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-284 1.40e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 123.77  E-value: 1.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd08218    5 IKKIGEGSFGKALLVKS---KEDGKQYVIKEINISKM--SPKEREESRKEVAVLSKMKH-PNIVQYQESFEENGNLYIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQ--YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKER 193
Cdd:cd08218   79 DYCDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR-VLNSTVEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRIGPVAQDL 272
Cdd:cd08218  158 ARTCIGTPYYLSPEICENKPYNNKS-DIWALGCVLYEMCTLKHAF----EAGNMKNLVLKIIRGSyPPVPSRYSYDLRSL 232
                        250
                 ....*....|..
gi 663856869 273 LQRLLCKDPKKR 284
Cdd:cd08218  233 VSQLFKRNPRDR 244
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
421-656 1.70e-31

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 124.25  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 421 CRQRQSGQEFAVKILSRR--LEANTQREVAALR--LCQSH-PNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFS 495
Cdd:cd05579   12 AKKKSTGDLYAIKVIKKRdmIRKNQVDSVLAERniLSQAQnPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSLLENVGALD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 496 ESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFAR--------------LRPQSPGVPMQT 561
Cdd:cd05579   92 EDVARIYIAEIVLALEYLHSH-GIIHRDLKPDNILIDAN---GHLKLTDFGLSKvglvrrqiklsiqkKSNGAPEKEDRR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSL--DGEawqgVSEE 639
Cdd:cd05579  168 IVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAET-------PEEIFQNILNGKIEWpeDPE----VSDE 236
                        250
                 ....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRL 656
Cdd:cd05579  237 AKDLISKLLTPDPEKRL 253
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
33-287 1.94e-31

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 124.12  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrkAGGHDA-GKLYAMKVLR------KAALVQRaktqehtrtERSVLELVRQAPF--LVTLHY 103
Cdd:cd06917    3 YRRLELVGRGSYGAVY----RGYHVKtGRVVALKVLNldtdddDVSDIQK---------EVALLSQLKLGQPknIIKYYG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGEMFThLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd06917   70 SYLKGPSLWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegernTQAEVSRRILKCSPPFPP 263
Cdd:cd06917  149 ASLNQNSSKRS-TFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY-------SDVDALRAVMLIPKSKPP 220
                        250       260
                 ....*....|....*....|....*....
gi 663856869 264 RI-----GPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd06917  221 RLegngySPLLKEFVAACLDEEPKDRLSA 249
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
33-300 2.18e-31

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 123.34  E-value: 2.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkagGHDAGKLYAMKVLRKAAlvqraKTQEHTRTE----RSVlelvrQAPFLVTLHYAFQTD 108
Cdd:cd14662    2 YELVKDIGSGNFGVARLMR---NKETKELVAVKYIERGL-----KIDENVQREiinhRSL-----RHPNIIRFKEVVLTP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE--GHIVLTDFGLSKEF 186
Cdd:cd14662   69 THLAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERtfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFT-LEGERNTQAEVSrRILKCSPPFPP-- 263
Cdd:cd14662  149 VLHSQPK--STVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEdPDDPKNFRKTIQ-RIMSVQYKIPDyv 225
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14662  226 RVSQDCRHLLSRIFVANPAKRITIP-----EIKNHPW 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
410-656 2.27e-31

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 124.18  E-value: 2.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVlellrggelL 485
Cdd:cd07830    7 LGDGTFGSVYLARNKETGELVAIKKMKKKFysweECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFV---------F 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHI----------RKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYADDTpgaPVKIIDFGFAR-LRPQS 554
Cdd:cd07830   78 EYMegnlyqlmkdRKGKPFSESVIRSIIYQILQGLAHIH-KHGFFHRDLKPENLLVSGPE---VVKIADFGLAReIRSRP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PgvpmqtpcFTLQ-----YAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaaEI-----MCKI-- 621
Cdd:cd07830  154 P--------YTDYvstrwYRAPEiLLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSS---------EIdqlykICSVlg 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 622 -------REG-------RFSLDGEAWQG-------VSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07830  217 tptkqdwPEGyklasklGFRFPQFAPTSlhqlipnASPEAIDLIKDMLRWDPKKRP 272
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
39-307 2.29e-31

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 124.01  E-value: 2.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRA---------KTQEHTRTERSVLELVRQA---------PFLVT 100
Cdd:cd14118    2 IGKGSYG---IVKLAYNEEDNTLYAMKILSKKKLLKQAgffrrppprRKPGALGKPLDPLDRVYREiailkkldhPNVVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 101 LHYAFQTDAK--LHLILDYVSGGEMFtHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLT 178
Cdd:cd14118   79 LVEVLDDPNEdnLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEFLTEEKERTfSFCGTIEYMAPEIIR--SKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILK 256
Cdd:cd14118  158 DFGVSNEFEGDDALLS-STAGTPAFMAPEALSesRKKFSGKALDIWAMGVTLYCFVFGRCPF----EDDHILGLHEKIKT 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 257 CSPPFP--PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPffqgldWV 307
Cdd:cd14118  233 DPVVFPddPVVSEQLKDLILRMLDKNPSERI-----TLPEIKEHP------WV 274
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
400-666 3.16e-31

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 122.96  E-value: 3.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSR--RLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd14662    1 RYEL-VKD--IGSGNFGVARLMRNKETKELVAVKYIERglKIDENVQREIINHRSLR-HPNIIRFKEVVLTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYaDDTPGAPVKIIDFGFAR--LRPQSP 555
Cdd:cd14662   77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCH-SMQICHRDLKLENTLL-DGSPAPRLKICDFGYSKssVLHSQP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GVPMQTPCftlqYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREGRFSLDGeaWQ 634
Cdd:cd14662  155 KSTVGTPA----YIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFE---DPDDPKNFRKTIQRIMSVQYKIPD--YV 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14662  226 RVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
31-301 5.00e-31

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 122.47  E-value: 5.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd06610    1 DDYELIEVIGSGATAVVY---AAYCLPKKEKVAIKRID---LEKCQTSMDELRKEIQAMSQC-NHPNVVSYYTSFVVGDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMF---THLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd06610   74 LWLVMPLLSGGSLLdimKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 T---EEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPFPP- 263
Cdd:cd06610  154 TggdRTRKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYS----KYPPMKVLMLTLQNDPPSLEt 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 264 -----RIGPVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPFF 301
Cdd:cd06610  230 gadykKYSKSFRKMISLCLQKDPSKR----PT-AEELLKHKFF 267
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
31-300 5.55e-31

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 123.22  E-value: 5.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLrkaalvqraKTQEHTRTERSVLELVRQA----PFLVTLHYAFQ 106
Cdd:cd06644   12 EVWEIIGELGDGAFGKVY---KAKNKETGALAAAKVI---------ETKSEEELEDYMVEIEILAtcnhPYIVKLLGAFY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEM-FTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd06644   80 WDGKLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDW----WSLGILLFELLTGASPftlEGERNTQaEVSRRILKCSPPF 261
Cdd:cd06644  160 NVKTLQRRD-SFIGTPYWMAPEVVMCETMKDTPYDYkadiWSLGITLIEMAQIEPP---HHELNPM-RVLLKIAKSEPPT 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 262 ---PPRIGPVAQDLLQRLLCKDPKKRlgagPQGAQeVRNHPF 300
Cdd:cd06644  235 lsqPSKWSMEFRDFLKTALDKHPETR----PSAAQ-LLEHPF 271
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
410-677 6.29e-31

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 123.96  E-value: 6.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsRRLEANTQREVAALR-----LCQSH-PNVVNLHEVHHDQLHTYLVLELlrgge 483
Cdd:cd05601    9 IGRGHFGEVQVVKEKATGDIYAMKVL-KKSETLAQEEVSFFEeerdiMAKANsPWITKLQYAFQDSENLYLVMEY----- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 lleH---------IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFG-FARLRPQ 553
Cdd:cd05601   83 ---HpggdllsllSRYDDIFEESMARFYLAELVLAIHSLHS-MGYVHRDIKPENILI--DRTGH-IKLADFGsAAKLSSD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 ---SPGVPMQTPcftlQYAAPELL------AQQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQAAEIMCKIREG 624
Cdd:cd05601  156 ktvTSKMPVGTP----DYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPF---TEDTVIKTYSNIMNFKKFL 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 625 RFSLDgeawQGVSEEAKELVRGLLTvDPAKRLKLEGLRGSSWLQD---GSARSSPP 677
Cdd:cd05601  229 KFPED----PKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGidwNNLRQTVP 279
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
59-284 6.87e-31

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 127.06  E-value: 6.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  59 GKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQapFLVTLHYA-FQTDAKLHLILDYVSGGEMFTHLYQRQY----F 133
Cdd:PTZ00267  89 GSDPKEKVVAKFVMLNDERQAAYARSELHCLAACDH--FGIVKHFDdFKSDDKLLLIMEYGSGGDLNKQIKQRLKehlpF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 134 KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL-TEEKERTFSFCGTIEYMAPEIIRSK 212
Cdd:PTZ00267 167 QEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSdSVSLDVASSFCGTPYYLAPELWERK 246
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 213 TgHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:PTZ00267 247 R-YSKKADMWSLGVILYELLTLHRPF----KGPSQREIMQQVLYGKyDPFPCPVSSGMKALLDPLLSKNPALR 314
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
31-301 7.84e-31

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 122.81  E-value: 7.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvQRAKTQEHTRT---ERSVLELVRQaPFLVTLHYAFQT 107
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVL---KCRNKATGEIVAIKKFK-----ESEDDEDVKKTalrEVKVLRQLRH-ENIVNLKEAFRR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVsGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeF 186
Cdd:cd07833   72 KGRLYLVFEYV-ERTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFAR-A 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTF-SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTleGErntqAEVSR--RILKCSPPFPP 263
Cdd:cd07833  150 LTARPASPLtDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFP--GD----SDIDQlyLIQKCLGPLPP 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 264 R--------------------------------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07833  224 ShqelfssnprfagvafpepsqpeslerrypgkVSSPALDFLKACLRMDPKERL-----TCDELLQHPYF 288
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
31-301 8.53e-31

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 121.92  E-value: 8.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLrkaaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERA---TGNNFAAKFI----MTPHESDKETVRKEIQIMNQLHH-PKLINLHDAFEDDNE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD--SEGHIVLTDFGLSKEFL 187
Cdd:cd14114   74 MVLILEFLSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSfcGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRrilkCSPPFP----P 263
Cdd:cd14114  154 PKESVKVTT--GTAEFAAPEIVEREP-VGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKS----CDWNFDdsafS 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14114  227 GISEEAKDFIRKLLLADPNKRM-----TIHQALEHPWL 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
31-301 1.02e-30

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 121.60  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLR-KAALVQRAKtqehtrtERSVLELVRqAPFLVTLHYAFQTDA 109
Cdd:cd06612    3 EVFDILEKLGEGSYGSVY---KAIHKETGQVVAIKVVPvEEDLQEIIK-------EISILKQCD-SPYIVKYYGSYFKNT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQ-YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLT 188
Cdd:cd06612   72 DLWIVMEYCGAGSVSDIMKITNkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ-LT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegerntqAEV--SRRIL--KCSPP---- 260
Cdd:cd06612  151 DTMAKRNTVIGTPFWMAPEVI-QEIGYNNKADIWSLGITAIEMAEGKPPY---------SDIhpMRAIFmiPNKPPptls 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd06612  221 DPEKWSPEFNDFVKKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
410-683 1.14e-30

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 123.93  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL------EAN--TQREVAAlrlCQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05573    9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDmlkreqIAHvrAERDILA---DADSPWIVRLHYAFQDEDHLYLVMEYMPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFA------------- 548
Cdd:cd05573   86 GDLMNLLIKYDVFPEETARFYIAELVLALDSLHK-LGFIHRDIKPDNILL--DADGH-IKLADFGLCtkmnksgdresyl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 --------RLRPQSPGVPMQ-------TPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQ 613
Cdd:cd05573  162 ndsvntlfQDNVLARRRPHKqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPF---YSDSLVET 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 614 AAEIMCKIREGRFSLDgeawQGVSEEAKELVRGLLTvDPAKRLK-LEGLRGSSWLQ----DGSARSSPPLRtPDV 683
Cdd:cd05573  239 YSKIMNWKESLVFPDD----PDVSPEAIDLIRRLLC-DPEDRLGsAEEIKAHPFFKgidwENLRESPPPFV-PEL 307
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
31-300 1.39e-30

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 121.29  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAalvqRAKTQEH-TRTERSVLELVRQaPFLVTLHYAFQTDA 109
Cdd:cd14184    1 EKYKIGKVIGDGNFA---VVKECVERSTGKEFALKIIDKA----KCCGKEHlIENEVSILRRVKH-PNIIMLIEEMDTPA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEGHIVLTDFGLSke 185
Cdd:cd14184   73 ELYLVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLA-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 flTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCSPPFPP-- 263
Cdd:cd14184  151 --TVVEGPLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPF--RSENNLQEDLFDQILLGKLEFPSpy 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 264 --RIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14184  226 wdNITDSAKELISHMLQVNVEARYTAE-----QILSHPW 259
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
410-667 1.43e-30

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 121.22  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL---SRRLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKIIkvkGAKEREEVKNEINIMNQL-NHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HI-RKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTpGAPVKIIDFGFAR-LRPQSP-GVPMQTPc 563
Cdd:cd14192   91 RItDESYQLTELDAILFTRQICEGVHYLHQHY-ILHLDLKPENILCVNST-GNQIKIIDFGLARrYKPREKlKVNFGTP- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 ftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIREGRFSLDGEAWQGVSEEAKEL 643
Cdd:cd14192  168 ---EFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETD-------AETMNNIVNCKWDFDAEAFENLSEEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14192  238 ISRLLVKEKSCRMSATQCLKHEWL 261
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
410-656 1.52e-30

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 121.74  E-value: 1.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR----RLE-----ANTQREVAALRLcqshPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14209    9 LGTGSFGRVMLVRHKETGNYYAMKILDKqkvvKLKqvehtLNEKRILQAINF----PFLVKLEYSFKDNSNLYMVMEYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFA-RLRPQSpgvpm 559
Cdd:cd14209   85 GGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHS-LDLIYRDLKPENLLI--DQQGY-IKVTDFGFAkRVKGRT----- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgeawQGVSEE 639
Cdd:cd14209  156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA-------DQPIQIYEKIVSGKVRFP----SHFSSD 224
                        250
                 ....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRL 656
Cdd:cd14209  225 LKDLLRNLLQVDLTKRF 241
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
401-667 1.65e-30

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 120.69  E-value: 1.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDlrEPALGQGSFSVCRRCRQRQSGQEFAVKIlsRRLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14109    5 YEIG--EEDEKRAAQGAPFHVTERSTGRNFLAQL--RYGDPFLMREVDIHNSL-DHPNIVQMHDAYDDEKLAVTVIDNLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHI---RKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgapVKIIDFGFAR--LRPQSP 555
Cdd:cd14109   80 STIELVRDnllPGKDYYTERQVAVFVRQLLLALKHMHDL-GIAHLDLRPEDILLQDDK----LKLADFGQSRrlLRGKLT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GVPMQTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQG 635
Cdd:cd14109  155 TLIYGSP----EFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR-------ETLTNVRSGKWSFDSSPLGN 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14109  224 ISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
39-287 1.91e-30

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 121.12  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrKAGGHDAGKLYAMK-VLRKAALVQRAKTQEHtrtERSVLELVRQApFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14097    9 LGQGSFGVVI---EATHKETQTKWAIKkINREKAGSSAVKLLER---EVDILKHVNHA-HIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG-------HIVLTDFGLSKEFLTEE 190
Cdd:cd14097   82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQKYGLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14097  162 EDMLQETCGTPIYMAPEVI-SAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAK 240
                        250
                 ....*....|....*..
gi 663856869 271 DLLQRLLCKDPKKRLGA 287
Cdd:cd14097  241 NVLQQLLKVDPAHRMTA 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
38-300 2.05e-30

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 120.72  E-value: 2.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLvrkagGHDA--GKLYAMKVLRKAALvqrakTQEHTRTERSVLE-LVRQAPFLVTLHY-------AFQT 107
Cdd:cd06628    7 LIGSGSFGSVYL-----GMNAssGELMAVKQVELPSV-----SAENKDRKKSMLDaLQREIALLRELQHenivqylGSSS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAK-LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE- 185
Cdd:cd06628   77 DANhLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 ----FLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRI-LKCSPP 260
Cdd:cd06628  157 eansLSTKNNGARPSLQGSVFWMAPEVVK-QTSYTRKADIWSLGCLVVEMLTGTHPFP----DCTQMQAIFKIgENASPT 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPF 300
Cdd:cd06628  232 IPSNISSEARDFLEKTFEIDHNKR----PT-ADELLKHPF 266
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
25-284 2.14e-30

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 125.75  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  25 EEKVSVENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQAPF-LVTLHY 103
Cdd:PTZ00283  26 TAKEQAKKYWISRVLGSGATGTVLCAKRVSD---GEPFAVKVVD----MEGMSEADKNRAQAEVCCLLNCDFFsIVKCHE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AF-QTDAK-------LHLILDYVSGGEMFTHLYQR----QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS 171
Cdd:PTZ00283  99 DFaKKDPRnpenvlmIALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 172 EGHIVLTDFGLSKEF---LTEEKERTfsFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGErNTQA 248
Cdd:PTZ00283 179 NGLVKLGDFGFSKMYaatVSDDVGRT--FCGTPYYVAPEIWRRKP-YSKKADMFSLGVLLYELLTLKRPF--DGE-NMEE 252
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 249 EVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:PTZ00283 253 VMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRR 288
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
400-608 3.12e-30

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 120.50  E-value: 3.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDlREPALGQGSFSVCRRCRQRQSGQ-EFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYL 474
Cdd:cd14202    1 KFEFS-RKDLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQtllgKEIKILKELK-HENIVALYDFQEIANSVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDT--PGAP----VKIIDFGFA 548
Cdd:cd14202   79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSK-GIIHRDLKPQNILLSYSGgrKSNPnnirIKIADFGFA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 RLRPQSpgVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQ 608
Cdd:cd14202  158 RYLQNN--MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQ 215
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
410-656 3.13e-30

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 120.84  E-value: 3.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL----EANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYL-VLELLRGGEL 484
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHFksleQVNNLREIQALRRLSPHPNILRLIEVLFDRKTGRLaLVFELMDMNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIR-KKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgapVKIIDFGFARLRPQSPgvPMQTPC 563
Cdd:cd07831   87 YELIKgRKRPLPEKRVKNYMYQLLKSLDHMHRN-GIFHRDIKPENILIKDDI----LKLADFGSCRGIYSKP--PYTEYI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQG-YDESCDLWSLGVILYMMLSGQVPFQGASgQGGQ---------SQAAEIMCKIREGR-FSLD--- 629
Cdd:cd07831  160 STRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTN-ELDQiakihdvlgTPDAEVLKKFRKSRhMNYNfps 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 630 ----GEAW--QGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07831  239 kkgtGLRKllPNASAEGLDLLKKLLAYDPDERI 271
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
410-656 3.95e-30

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 121.74  E-value: 3.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGS----FSVcRRCRQRQSGQEFAVKILSRRLEANTQREVAALRL------CQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05584    4 LGKGGygkvFQV-RKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAernileAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGVpM 559
Cdd:cd05584   83 SGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSL-GIIYRDLKPENILL--DAQGH-VKLTDFGLCKESIHDGTV-T 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEawqgVSEE 639
Cdd:cd05584  158 HTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRK-------KTIDKILKGKLNLPPY----LTNE 226
                        250
                 ....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRL 656
Cdd:cd05584  227 ARDLLKKLLKRNVSSRL 243
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
410-655 6.62e-30

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 119.31  E-value: 6.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ--REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQvtHELGVLQSLQ-HPQLVGLLDTFETPTSYILVLEMADQGRLLDY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILyADDTPGAP-VKIIDFGFArlrpqspgVPMQTPCFTL 566
Cdd:cd14113   94 VVRWGNLTEEKIRFYLREILEALQYLHN-CRIAHLDLKPENIL-VDQSLSKPtIKLADFGDA--------VQLNTTYYIH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 567 Q------YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEA 640
Cdd:cd14113  164 QllgspeFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDES-------VEETCLNICRLDFSFPDDYFKGVSQKA 236
                        250
                 ....*....|....*
gi 663856869 641 KELVRGLLTVDPAKR 655
Cdd:cd14113  237 KDFVCFLLQMDPAKR 251
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
400-667 6.69e-30

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 119.25  E-value: 6.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLREpALGQGSFSVCRRCRQRQSGQEFAVKILSRRleANTQREVAALRL----CQSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14190    3 TFSIHSKE-VLGGGKFGKVHTCTEKRTGLKLAAKVINKQ--NSKDKEMVLLEIqvmnQLNHRNLIQLYEAIETPNEIVLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHI-RKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTpGAPVKIIDFGFARlrPQS 554
Cdd:cd14190   80 MEYVEGGELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQ-MRVLHLDLKPENILCVNRT-GHQVKIIDFGLAR--RYN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDGEAWQ 634
Cdd:cd14190  156 PREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLG-------DDDTETLNNVLMGNWYFDEETFE 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14190  229 HVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
410-655 7.15e-30

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 119.18  E-value: 7.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS-RRL-EANTQ---REVAALRLCQsHPNVVNLHEVHHDQLHT--YLV----LEL 478
Cdd:cd08217    8 IGKGSFGTVRKVRRKSDGKILVWKEIDyGKMsEKEKQqlvSEVNILRELK-HPNIVRYYDRIVDRANTtlYIVmeycEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG----VVHRDLKPENI-LYADDTpgapVKIIDFGFARLRPQ 553
Cdd:cd08217   87 DLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSVgggkILHRDLKPANIfLDSDNN----VKLGDFGLARVLSH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SpGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEimcKIREGRFS-LDgea 632
Cdd:cd08217  163 D-SSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAAN----QLELAK---KIKEGKFPrIP--- 231
                        250       260
                 ....*....|....*....|...
gi 663856869 633 wQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd08217  232 -SRYSSELNEVIKSMLNVDPDKR 253
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
33-301 8.04e-30

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 119.51  E-value: 8.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKaalvqrakTQEH---TRT---ERSVL-ELvrQAPFLVTLHYAF 105
Cdd:cd07829    1 YEKLEKLGEGTYGVVY---KAKDKKTGEIVALKKIRL--------DNEEegiPSTalrEISLLkEL--KHPNIVKLLDVI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVsggEM----FTHLYQRQyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd07829   68 HTENKLYLVFEYC---DQdlkkYLDKRPGP-LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEF------LTEEKErtfsfcgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGER----------- 244
Cdd:cd07829  144 LARAFgiplrtYTHEVV-------TLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIdqlfkifqilg 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 245 ----NTQAEVSRRILKcSPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07829  217 tpteESWPGVTKLPDY-KPTFPkwpkndlekvlPRLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
410-675 9.46e-30

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 119.19  E-value: 9.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL--EANTQREVAALRLCQsHPNVVNLHEVH--HDQLhtYLVLELLRGGELL 485
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKGadQVLVKKEISILNIAR-HRNILRLHESFesHEEL--VMIFEFISGVDIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKR-HFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTpGAPVKIIDFGfaRLRPQSPGVPMQTPCF 564
Cdd:cd14104   85 ERITTARfELNEREIVSYVRQVCEALEFLHSKN-IGHFDIRPENIIYCTRR-GSYIKIIEFG--QSRQLKPGDKFRLQYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd14104  161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQ-------QTIENIRNAEYAFDDEAFKNISIEALDFV 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSWLQDGSARSS 675
Cdd:cd14104  234 DRLLVKERKSRMTAQEALNHPWLKQGMETVS 264
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
37-300 9.81e-30

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 119.75  E-value: 9.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHT------RTERSVLELVRqapflvtlhyAFQTDAK 110
Cdd:cd14173    8 EVLGEGAYARV---QTCINLITNKEYAVKIIEKRPGHSRSRVFREVemlyqcQGHRNVLELIE----------FFEEEDK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV---LTDFGL----- 182
Cdd:cd14173   75 FYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSpvkICDFDLgsgik 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 ---------SKEFLTEekertfsfCGTIEYMAPEIIRS----KTGHGKAVDWWSLGILLFELLTGASPFT---------- 239
Cdd:cd14173  155 lnsdcspisTPELLTP--------CGSAEYMAPEVVEAfneeASIYDKRCDLWSLGVILYIMLSGYPPFVgrcgsdcgwd 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 240 -LEGERNTQAEVSRRILKCSPPFPPR----IGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14173  227 rGEACPACQNMLFESIQEGKYEFPEKdwahISCAAKDLISKLLVRDAKQRLSAA-----QVLQHPW 287
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
31-300 1.01e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 120.90  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAalvQRAKTQEhtrteRSVLELVRQAPFLVTLHYAFQTDAK 110
Cdd:cd14176   19 DGYEVKEDIGVGSYS---VCKRCIHKATNMEFAVKIIDKS---KRDPTEE-----IEILLRYGQHPNIITLKDVYDDGKY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH---IVLTDFGLSKEf 186
Cdd:cd14176   88 VYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQ- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlEGERNTQAEVSRRI----LKCSPPFP 262
Cdd:cd14176  167 LRAENGLLMTPCYTANFVAPEVLE-RQGYDAACDIWSLGVLLYTMLTGYTPFA-NGPDDTPEEILARIgsgkFSLSGGYW 244
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd14176  245 NSVSDTAKDLVSKMLHVDPHQRLTAA-----LVLRHPW 277
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
410-667 1.15e-29

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 118.52  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqSGQEFAVKILSRRLEANTQ------REVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14161   11 LGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQdllhirREIEIMS-SLNHPHIISVYEVFENSSKIVIVMEYASRGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQspGVPMQTPC 563
Cdd:cd14161   89 LYDYISERQRLSELEARHFFRQIVSAVHYCHAN-GIVHRDLKLENILL--DANGN-IKIADFGLSNLYNQ--DKFLQTYC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGY-DESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAwqgvsEEAKE 642
Cdd:cd14161  163 GSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYK-------ILVKQISSGAYREPTKP-----SDACG 230
                        250       260
                 ....*....|....*....|....*
gi 663856869 643 LVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14161  231 LIRWLLMVNPERRATLEDVASHWWV 255
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
410-677 1.33e-29

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 118.81  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAaLRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKFIVALKVLFKSqiekegVEHQLRREIE-IQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFArlrPQSPGVPMQTPC 563
Cdd:cd14117   93 LYKELQKHGRFDEQRTATFMEELADALHYCHEKK-VIHRDIKPENLLMGYK---GELKIADFGWS---VHAPSLRRRTMC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIregrFSLDGEAWQGVSEEAKEL 643
Cdd:cd14117  166 GTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESAS-------HTETYRRI----VKVDLKFPPFLSDGSRDL 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPP 677
Cdd:cd14117  235 ISKLLRYHPSERLPLKGVMEHPWVKANSRRVLPP 268
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
31-298 1.40e-29

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 118.59  E-value: 1.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIF---RAKDKTTGKLYTCKKFLKR---DGRKVRKAAKNEINILKMVKH-PNILQLVDVFETRKE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE---GHIVLTDFGLSKEFL 187
Cdd:cd14088   74 YFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlknSKIVISDFHLAKLEN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERtfsfCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGE----RNTQAEVSRRIL----KCSP 259
Cdd:cd14088  154 GLIKEP----CGTPEYLAPEVV-GRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyENHDKNLFRKILagdyEFDS 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 260 PFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNH 298
Cdd:cd14088  229 PYWDDISQAAKDLVTRLMEVEQDQRI-----TAEEAISH 262
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
410-667 1.82e-29

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 118.36  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-----VCRRCRQRQSGQEFAVKILSRRL------EANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14076    9 LGEGEFGkvklgWPLPKANHRSGVQVAIKLIRRDTqqencqTSKIMREINILKGL-THPNIVRLLDVLKTKKYIGIVLEF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGAPVkIIDFGFARLRPQSPGVP 558
Cdd:cd14076   88 VSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKK-GVVHRDLKLENLLL--DKNRNLV-ITDFGFANTFDHFNGDL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELL-AQQGYDES-CDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDgeawQGV 636
Cdd:cd14076  164 MSTSCGSPCYAAPELVvSDSMYAGRkADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLYRYICNTPLIFP----EYV 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 637 SEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14076  240 TPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
33-301 1.83e-29

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 117.68  E-value: 1.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKG---NGECCAAKFIP-----LRSSTRARAFQERDILARLSH-RRLTCLLDQFETRKTLI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH--IVLTDFGLSKEFLTEE 190
Cdd:cd14107   75 LILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEITPSE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KErtFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQ 270
Cdd:cd14107  155 HQ--FSKYGSPEFVAPEIV-HQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAK 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd14107  232 DFIKRVLQPDPEKR-----PSASECLSHEWF 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-284 2.22e-29

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 117.75  E-value: 2.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRkagghdaGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVR-QAPFLVTLHYAFQTDAK 110
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAK-------AKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKmKHPNIVTFFASFQENGR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLyQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSKEf 186
Cdd:cd08225   74 LFIVMEYCDGGDLMKRI-NRQRgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIARQ- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCS-PPFPPRI 265
Cdd:cd08225  152 LNDSMELAYTCVGTPYYLSPEICQNRPYNNK-TDIWSLGCVLYELCTLKHPF----EGNNLHQLVLKICQGYfAPISPNF 226
                        250
                 ....*....|....*....
gi 663856869 266 GPVAQDLLQRLLCKDPKKR 284
Cdd:cd08225  227 SRDLRSLISQLFKVSPRDR 245
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
411-661 2.33e-29

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 117.35  E-value: 2.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVKILSRRLE-----ANTQREVAALR-LcqSHPNVVNLH-------------EVHHDQLH 471
Cdd:cd14002   10 GEGSFGKVYKGRRKYTGQVVALKFIPKRGKsekelRNLRQEIEILRkL--NHPNIIEMLdsfetkkefvvvtEYAQGELF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 TYLvlellrggellehiRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLR 551
Cdd:cd14002   88 QIL--------------EDDGTLPEEEVRSIAKQLVSALHYLHSNR-IIHRDMKPQNILI---GKGGVVKLCDFGFARAM 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 PQS-------PGVPMqtpcftlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREg 624
Cdd:cd14002  150 SCNtlvltsiKGTPL--------YMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNS-------IYQLVQMIVK- 213
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 625 rfslDGEAW-QGVSEEAKELVRGLLTVDPAKRLKLEGL 661
Cdd:cd14002  214 ----DPVKWpSNMSPEFKSFLQGLLNKDPSKRLSWPDL 247
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
410-656 4.06e-29

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 116.98  E-value: 4.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ--REVAALRLCQSHPNVVNLHEVH------HDQlHTYLVLELLRG 481
Cdd:cd14133    7 LGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQslDEIRLLELLNKKDKADKYHIVRlkdvfyFKN-HLCIVFELLSQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEH-IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPgAPVKIIDFGFARLRPQSPGVPMQ 560
Cdd:cd14133   86 NLYEFLkQNKFQYLSLPRIRKIAQQILEALVFLHS-LGLIHCDLKPENILLASYSR-CQIKIIDFGSSCFLTQRLYSYIQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TpcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqgGQSQAAEIMCKIreGRFSLdGEAWQGVS--E 638
Cdd:cd14133  164 S----RYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGAS---EVDQLARIIGTI--GIPPA-HMLDQGKAddE 233
                        250
                 ....*....|....*...
gi 663856869 639 EAKELVRGLLTVDPAKRL 656
Cdd:cd14133  234 LFVDFLKKLLEIDPKERP 251
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-287 4.34e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 116.61  E-value: 4.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHV---NSDQKYAMKEIR---LPKSSSAVEDSRKEAVLLAKMKH-PNIVAFKESFEADGHL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTE 189
Cdd:cd08219   74 YIVMEYCDGGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLTS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQAEVSRrilKCSPPFPPRIGPVA 269
Cdd:cd08219  153 PGAYACTYVGTPYYVPPEIWENMPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQ---GSYKPLPSHYSYEL 228
                        250
                 ....*....|....*...
gi 663856869 270 QDLLQRLLCKDPKKRLGA 287
Cdd:cd08219  229 RSLIKQMFKRNPRSRPSA 246
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
410-667 4.45e-29

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 116.59  E-value: 4.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS-RRL------EANTQREVAALRLCQsHPNVVNLHEVHHDQL--HTYLVLELLR 480
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKkRKLrripngEANVKREIQILRRLN-HRNVIKLVDVLYNEEkqKLYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRH-FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILY-ADDTpgapVKIIDFGFA-RLRPQSPGV 557
Cdd:cd14119   80 GGLQEMLDSAPDKrLPIWQAHGYFVQLIDGLEYLHSQ-GIIHKDIKPGNLLLtTDGT----LKISDFGVAeALDLFAEDD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQTPCFTLQYAAPELLAQQGYDE--SCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEawqg 635
Cdd:cd14119  155 TCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGDN-------IYKLFENIGKGEYTIPDD---- 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14119  224 VDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
32-297 5.62e-29

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 116.33  E-value: 5.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKaalvQRAKTQEHTRTERSV--LELVRQAPFLVTLHYAFQTDA 109
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRS---KVDGCLYAVKKSKK----PFRGPKERARALREVeaHAALGQHPNIVRYYSSWEEGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEM---FTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG----L 182
Cdd:cd13997   74 HLYIQMELCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGlatrL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEkertfsfcGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGaSPFTlegernTQAEVSRRILKCSPPFP 262
Cdd:cd13997  154 ETSGDVEE--------GDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATG-EPLP------RNGQQWQQLRQGKLPLP 218
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 263 PriGPVAQDLLQRLLC----KDPKKRlgagPQGAQEVRN 297
Cdd:cd13997  219 P--GLVLSQELTRLLKvmldPDPTRR----PTADQLLAH 251
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-284 5.81e-29

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 116.83  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGhdAGKLYAMKVLRKAALVQRAKTQEHTRTERSVL---ELVRQA---PFLVTLHYAF 105
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKSN--GQTLLALKEINMTNPAFGRTEQERDKSVGDIIsevNIIKEQlrhPNIVRYYKTF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSG---GEMFTHLYQR-QYFKEAEVRVYGGEIVLALEHLHK-LGIIYRDLKLENVLLDSEGHIVLTDF 180
Cdd:cd08528   79 LENDRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEgerNTQAEVSRRILKCSPP 260
Cdd:cd08528  159 GLAKQKGPESSKMT-SVVGTILYSCPEIVQNEP-YGEKADIWALGCILYQMCTLQPPFYST---NMLTLATKIVEAEYEP 233
                        250       260
                 ....*....|....*....|....*
gi 663856869 261 FPP-RIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd08528  234 LPEgMYSDDITFVIRSCLTPDPEAR 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
39-301 6.10e-29

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 116.20  E-value: 6.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKV-------FLVRkagghdagklYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDA-- 109
Cdd:cd14119    1 LGEGSYGKVkevldteTLCR----------RAVKILKKRKLRRIPNGEANVKREIQILRRLNH-RNVIKLVDVLYNEEkq 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGG--EMFTHLYQRQyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSkEFL 187
Cdd:cd14119   70 KLYMVMEYCVGGlqEMLDSAPDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVA-EAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 T--EEKERTFSFCGTIEYMAPEIIR-SKTGHGKAVDWWSLGILLFELLTGASPFtlEGErnTQAEVSRRILKCSPPFPPR 264
Cdd:cd14119  148 DlfAEDDTCTTSQGSPAFQPPEIANgQDSFSGFKVDIWSAGVTLYNMTTGKYPF--EGD--NIYKLFENIGKGEYTIPDD 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14119  224 VDPDLQDLLRGMLEKDPEKRF-----TIEQIRQHPWF 255
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
407-667 6.98e-29

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 116.26  E-value: 6.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEFA---VKILSRRLEANTQREVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14191    7 EERLGSGKFGQVFRLVEKKTKKVWAgkfFKAYSAKEKENIRQEISIMN-CLHHPKLVQCVDAFEEKANIVMVLEMVSGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHI-RKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAPVKIIDFGFARlRPQSPG---VPM 559
Cdd:cd14191   86 LFERIiDEDFELTERECIKYMRQISEGVEYIHKQ-GIVHLDLKPENIMCVNKT-GTKIKLIDFGLAR-RLENAGslkVLF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14191  163 GTP----EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN-------ETLANVTSATWDFDDEAFDEISDD 231
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14191  232 AKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
400-667 1.05e-28

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 115.41  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDlrePALGQGSFSVCRRCRQRQSGQEFAVKILSRrlEANTQR-----------EVAALRLC--QSHPNVVNLHEVH 466
Cdd:cd14005    1 QYEVG---DLLGKGGFGTVYSGVRIRDGLPVAVKFVPK--SRVTEWamingpvpvplEIALLLKAskPGVPGVIRLLDWY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLHTYLVLELLRGGE-LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVKIIDF 545
Cdd:cd14005   76 ERPDGFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQ-RGVLHRDIKDENLLI--NLRTGEVKLIDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 546 GFARLRPQSPgvpMQTPCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFqgasgqggqSQAAEIMckirEG 624
Cdd:cd14005  153 GCGALLKDSV---YTDFDGTRVYSPPEWIRHGRYHgRPATVWSLGILLYDMLCGDIPF---------ENDEQIL----RG 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 625 RFSLdgeaWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14005  217 NVLF----RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
37-300 1.23e-28

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 115.94  E-value: 1.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQA---------PFLVTLHYAFQT 107
Cdd:cd06629    7 ELIGKGTYGRVYLAMNA---TTGEMLAVKQVE----LPKTSSDRADSRQKTVVDALKSEidtlkdldhPNIVQYLGFEET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfl 187
Cdd:cd06629   80 EDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKK-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEE---KERTFSFCGTIEYMAPEIIRS-KTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRI--LKCSPPF 261
Cdd:cd06629  158 SDDiygNNGATSMQGSVFWMAPEVIHSqGQGYSAKVDIWSLGCVVLEMLAGRRPWS----DDEAIAAMFKLgnKRSAPPV 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 262 PP--RIGPVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPF 300
Cdd:cd06629  234 PEdvNLSPEALDFLNACFAIDPRDR----PT-AAELLSHPF 269
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
37-301 1.45e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 115.11  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALvqrAKTQEHTRTERSV-LELVRQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd14188    7 KVLGKGGFAKCYEMTDL---TTNKVYAAKIIPHSRV---SKPHQREKIDKEIeLHRILHHKHVVQFYHYFEDKENIYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTf 195
Cdd:cd14188   81 EYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRR- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQR 275
Cdd:cd14188  160 TICGTPNYLSPEVL-NKQGHGCESDIWALGCVMYTMLLGRPPF----ETTNLKETYRCIREARYSLPSSLLAPAKHLIAS 234
                        250       260
                 ....*....|....*....|....*.
gi 663856869 276 LLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd14188  235 MLSKNPEDR-----PSLDEIIRHDFF 255
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
410-656 1.68e-28

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 116.73  E-value: 1.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS---VCRRCRQRQSGQEFAVKILSR-------RLEANTQREV-AALRlcqsHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd05582    3 LGQGSFGkvfLVRKITGPDAGTLYAMKVLKKatlkvrdRVRTKMERDIlADVN----HPFIVKLHYAFQTEGKLYLILDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVP 558
Cdd:cd05582   79 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHS-LGIIYRDLKPENILLDED---GHIKLTDFGLSK-ESIDHEKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDgeawQGVSE 638
Cdd:cd05582  154 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRK-------ETMTMILKAKLGMP----QFLSP 222
                        250
                 ....*....|....*...
gi 663856869 639 EAKELVRGLLTVDPAKRL 656
Cdd:cd05582  223 EAQSLLRALFKRNPANRL 240
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
410-656 1.80e-28

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 116.69  E-value: 1.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL------EANTQREVAALRLCqSHPNVVNLHevHHDQLHTYL--VLELLRG 481
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEViiakdeVAHTLTENRVLQNT-RHPFLTSLK--YSFQTNDRLcfVMEYVNG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQT 561
Cdd:cd05571   80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQ-GIVYRDLKLENLLL--DKDGH-IKITDFGLCK-EEISYGATTKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqggQSQAAEIMCKI---REGRFSldgeawQGVSE 638
Cdd:cd05571  155 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--------YNRDHEVLFELilmEEVRFP------STLSP 220
                        250
                 ....*....|....*...
gi 663856869 639 EAKELVRGLLTVDPAKRL 656
Cdd:cd05571  221 EAKSLLAGLLKKDPKKRL 238
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
39-285 1.94e-28

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 115.10  E-value: 1.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVF-LVRKAgghdAGKLYAMKVLRKAAlvqrAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14191   10 LGSGKFGQVFrLVEKK----TKKVWAGKFFKAYS----AKEKENIRQEISIMNCLHH-PKLVQCVDAFEEKANIVMVLEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEG-HIVLTDFGLSKEFltEEKERT 194
Cdd:cd14191   81 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRL--ENAGSL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQ 274
Cdd:cd14191  159 KVLFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFIS 237
                        250
                 ....*....|.
gi 663856869 275 RLLCKDPKKRL 285
Cdd:cd14191  238 NLLKKDMKARL 248
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
37-301 2.26e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 114.64  E-value: 2.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFlvrKAGGHDAGKLYAMKVL---RKAALVQRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAKLHL 113
Cdd:cd14189    7 RLLGKGGFARCY---EMTDLATNKTYAVKVIphsRVAKPHQREKIVNEIELHRDL-----HHKHVVKFSHHFEDAENIYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMfTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEkE 192
Cdd:cd14189   79 FLELCSRKSL-AHIWKaRHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPE-Q 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDL 272
Cdd:cd14189  157 RKKTICGTPNYLAPEVL-LRQGHGPESDVWSLGCVMYTLLCGNPPF----ETLDLKETYRCIKQVKYTLPASLSLPARHL 231
                        250       260
                 ....*....|....*....|....*....
gi 663856869 273 LQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14189  232 LAGILKRNPGDRL-----TLDQILEHEFF 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
410-667 2.67e-28

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 114.41  E-value: 2.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEANTQRE-------------VAALRLcQSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14004    8 MGEGAYGQVNLAIYKSKGKEVVIKfIFKERILVDTWVRdrklgtvpleihiLDTLNK-RSHPNIVKLLDFFEDDEFYYLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELL-EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLrpQS 554
Cdd:cd14004   87 MEKHGSGMDLfDFIERKPNMDEKEAKYIFRQVADAVKHLHD-QGIVHRDIKDENVILDGN---GTIKLIDFGSAAY--IK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGvPMQTPCFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFqgasgqggqsqaaeimCKIREGrfsLDGE-- 631
Cdd:cd14004  161 SG-PFDTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLVFKENPF----------------YNIEEI---LEADlr 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 632 AWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14004  221 IPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
410-667 2.84e-28

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 114.49  E-value: 2.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCQsHPNVVNLHEVHH-DQLHTYLVLELLRGG 482
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKkapddfVEKFLPRELEILARLN-HKSIIKTYEIFEtSDGKVYIVMELGVQG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPgapVKIIDFGFAR--LRPQSPGVPM- 559
Cdd:cd14165   88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHE-LDIVHRDLKCENLLLDKDFN---IKLTDFGFSKrcLRDENGRIVLs 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESC-DLWSLGVILYMMLSGQVPFQGASgqggqsqaAEIMCKIREgRFSLDGEAWQGVSE 638
Cdd:cd14165  164 KTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSN--------VKKMLKIQK-EHRVRFPRSKNLTS 234
                        250       260
                 ....*....|....*....|....*....
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14165  235 ECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
31-308 3.08e-28

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 115.33  E-value: 3.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRAK-TQEHTRTERSVLELVrQAPFLVTLHYAFQTDA 109
Cdd:cd14094    3 DVYELCEVIGKGPFS---VVRRCIHRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHML-KHPHIVELLETYSSDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQ----YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL---DSEGHIVLTDFGL 182
Cdd:cd14094   79 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEfLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTLEGERnTQAEVSRRILKCSPPFP 262
Cdd:cd14094  159 AIQ-LGESGLVAGGRVGTPHFMAPEVVK-REPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQW 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 263 PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLDWVA 308
Cdd:cd14094  236 SHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWIKERDRYA 276
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
94-301 3.08e-28

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 114.46  E-value: 3.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  94 QAPFLVTLHYAFQTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd06648   62 QHPNIVEMYSSYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKEfLTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAevSRR 253
Cdd:cd06648  141 RVKLSDFGFCAQ-VSKEVPRRKSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMVDGEPPYF--NEPPLQA--MKR 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 254 ILKCSPPF---PPRIGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd06648  215 IRDNEPPKlknLHKVSPRLRSFLDRMLVRDPAQR-----ATAAELLNHPFL 260
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
410-655 3.57e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 114.70  E-value: 3.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRlCQSHPNVVNLHE--VHHDQLhtYLVLELLRGGE 483
Cdd:cd13996   14 LGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASekvlREVKALA-KLNHPNIVRYYTawVEEPPL--YIQMELCEGGT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFS---ESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGapVKIIDFGFARL---------- 550
Cdd:cd13996   91 LRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSK-GIVHRDLKPSNIFLDNDDLQ--VKIGDFGLATSignqkrelnn 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 --RPQSPGVPMQTP-CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLsgqVPFQgasgqgGQSQAAEIMCKIREGRFS 627
Cdd:cd13996  168 lnNNNNGNTSNNSVgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFK------TAMERSTILTDLRNGILP 238
                        250       260
                 ....*....|....*....|....*...
gi 663856869 628 LDGEAWQgvSEEAKeLVRGLLTVDPAKR 655
Cdd:cd13996  239 ESFKAKH--PKEAD-LIQSLLSKNPEER 263
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
410-662 3.66e-28

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 114.37  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsRRLEANTQ-----------REVAALRLCQSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCL-YKSGPNSKdgndfqklpqlREIDLHRRVSRHPNIITLHDVFETEVAIYIVLEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESE--ASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpGAPVKIIDFGFARLRPQSpg 556
Cdd:cd13993   87 CPNGDLFEAITENRIYVGKTelIKNVFLQLIDAVKHCHSL-GIYHRDIKPENILLSQD--EGTVKLCDFGLATTEKIS-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 vpMQTPCFTLQYAAPELLAQ-----QGYD-ESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCkiregRFSLDG 630
Cdd:cd13993  162 --MDFGVGSEFYMAPECFDEvgrslKGYPcAAGDIWSLGIILLNLTFGRNPWKIA------SESDPIFY-----DYYLNS 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 631 EA----WQGVSEEAKELVRGLLTVDPAKRLKLEGLR 662
Cdd:cd13993  229 PNlfdvILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
39-300 3.69e-28

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 115.12  E-value: 3.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGkvflVRKAGGHDAGKL-YAMKVLRKaalvqrakTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14175    9 IGVGSYS----VCKRCVHKATNMeYAVKVIDK--------SKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH---IVLTDFGLSKEfLTEEKER 193
Cdd:cd14175   77 MRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQ-LRAENGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlEGERNTQAEVSRRIlkCSPPFPPR------IGP 267
Cdd:cd14175  156 LMTPCYTANFVAPEVLK-RQGYDEGCDIWSLGILLYTMLAGYTPFA-NGPSDTPEEILTRI--GSGKFTLSggnwntVSD 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 268 VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14175  232 AAKDLVSKMLHVDPHQRL-----TAKQVLQHPW 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
410-667 4.14e-28

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 113.93  E-value: 4.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCqSHPNVVNLHEV-HHDQLHTYLVLELLRGG 482
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeefIQRFLPRELQIVERL-DHKNIIHVYEMlESADGKIYLVMELAEDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYAddtpGAPVKIIDFGFARLRPQSPGVPMQTP 562
Cdd:cd14163   87 DVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHG-CGVAHRDLKCENALLQ----GFTLKLTDFGFAKQLPKGGRELSQTF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGrFSLDGEAwqGVSEEAK 641
Cdd:cd14163  162 CGSTAYAAPEVLQGVPHDsRKGDIWSMGVVLYVMLCAQLPFD-------DTDIPKMLCQQQKG-VSLPGHL--GVSRTCQ 231
                        250       260
                 ....*....|....*....|....*.
gi 663856869 642 ELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14163  232 DLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
30-300 5.21e-28

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 114.48  E-value: 5.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELL--KVLGTGAYGKVFLVRKaggHDAGKLYAMKVLrkaalVQRAKTQehtrTERSVLELVRQAPFLVTLHYAFQT 107
Cdd:cd14171    3 LEEYEVNwtQKLGTGISGPVRVCVK---KSTGERFALKIL-----LDRPKAR----TEVRLHMMCSGHPNIVQIYDVYAN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 D----------AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL---DSEGH 174
Cdd:cd14171   71 SvqfpgessprARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 175 IVLTDFGLSKEFLTEEKERTFsfcgTIEYMAPEII-------RSKTG---------HGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14171  151 IKLCDFGFAKVDQGDLMTPQF----TPYYVAPQVLeaqrrhrKERSGiptsptpytYDKSCDMWSLGVIIYIMLCGYPPF 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 239 TLEG-ERNTQAEVSRRILKCSPPFPPR----IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14171  227 YSEHpSRTITKDMKRKIMTGSYEFPEEewsqISEMAKDIVRKLLCVDPEERM-----TIEEVLHHPW 288
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
410-661 5.32e-28

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 114.34  E-value: 5.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN-----TQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd07833    9 VGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvkktALREVKVLRQL-RHENIVNLKEAFRRKGRLYLVFEYVERTLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPMQTPCF 564
Cdd:cd07833   88 ELLEASPGGLPPDAVRSYIWQLLQAIAYCHSH-NIIHRDIKPENILV---SESGVLKLCDFGFARALTARPASPLTDYVA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGAS------------GQGGQSQAA--------------EI 617
Cdd:cd07833  164 TRWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSdidqlyliqkclGPLPPSHQElfssnprfagvafpEP 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 618 MCKI-REGRFSldgeawQGVSEEAKELVRGLLTVDPAKRLKLEGL 661
Cdd:cd07833  244 SQPEsLERRYP------GKVSSPALDFLKACLRMDPKERLTCDEL 282
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31-305 5.34e-28

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 114.35  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvqrAKTQEHTRTERSVLELVRQA--PFLVTLHYAFQTD 108
Cdd:cd06643    5 DFWEIVGELGDGAFGKVY---KAQNKETGILAAAKVID-------TKSEEELEDYMVEIDILASCdhPNIVKLLDAFYYE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEM-FTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFl 187
Cdd:cd06643   75 NNLWILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKN- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDW----WSLGILLFELLTGASPftlEGERNTQaEVSRRILKCSPPF-- 261
Cdd:cd06643  154 TRTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYkadvWSLGVTLIEMAQIEPP---HHELNPM-RVLLKIAKSEPPTla 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 262 -PPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLD 305
Cdd:cd06643  230 qPSRWSPEFKDFLRKCLEKNVDARW-----TTSQLLQHPFVSVLV 269
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
410-665 6.17e-28

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 113.26  E-value: 6.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQRE--VAALRLCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd08530    8 LGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREdsVNEIRLLASvnHPNIIRYKEAFLDGNRLCIVMEYAPFGDLS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRK----KRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtpGAPVKIIDFGFAR-LRPQSPGVPMQ 560
Cdd:cd08530   88 KLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQ-KILHRDLKSANILLSA---GDLVKIGDLGISKvLKKNLAKTQIG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCftlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSldgEAWQGVSEEA 640
Cdd:cd08530  164 TPL----YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQ-------ELRYKVCRGKFP---PIPPVYSQDL 229
                        250       260
                 ....*....|....*....|....*
gi 663856869 641 KELVRGLLTVDPAKRLKLEGLRGSS 665
Cdd:cd08530  230 QQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
33-301 6.80e-28

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 114.20  E-value: 6.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKaalvqrakTQEHT---RT---ERSVLELVRQAPFL-----VTL 101
Cdd:cd07840    1 YEKIAQIGEGTYGQVY---KARNKKTGELVALKKIRM--------ENEKEgfpITairEIKLLQKLDHPNVVrlkeiVTS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVS---GGEMFTHLYQrqyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLT 178
Cdd:cd07840   70 KGSAKYKGSIYMVFEYMDhdlTGLLDNPEVK---FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGE--------------- 243
Cdd:cd07840  147 DFGLARPYTKENNADYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTEleqlekifelcgspt 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 244 RNTQAEVSR----RILKCSPPFPPR--------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07840  227 EENWPGVSDlpwfENLKPKKPYKRRlrevfknvIDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-284 7.50e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 113.29  E-value: 7.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKagghdagklyamKVLRKAALVQRAKTQEHTRTER-------SVLELVrQAPFLVTLHYA 104
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRR------------KDDNKLVIIKQIPVEQMTKEERqaalnevKVLSML-HHPNIIEYYES 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFG 181
Cdd:cd08220   68 FLEDKALMIVMEYAPGGTLFEYIQQRkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVkIGDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERTfsFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlEGErNTQAEVSRRILKCSPPF 261
Cdd:cd08220  148 ISKILSSKSKAYT--VVGTPCYISPELCEGKPYNQKS-DIWALGCVLYELASLKRAF--EAA-NLPALVLKIMRGTFAPI 221
                        250       260
                 ....*....|....*....|...
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd08220  222 SDRYSEELRHLILSMLHLDPNKR 244
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31-284 7.52e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 113.54  E-value: 7.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVR-QAPFLVTLHYAFQTDA 109
Cdd:cd13996    6 NDFEEIELLGSGGFGSVYKVRNKVD---GVTYAIKKIR-----LTEKSSASEKVLREVKALAKlNHPNIVRYYTAWVEEP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQR---QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSKE 185
Cdd:cd13996   78 PLYIQMELCEGGTLRDWIDRRnssSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkIGDFGLATS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTF-------------SFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLtgaSPFTLEGER-NTQAEVS 251
Cdd:cd13996  158 IGNQKRELNNlnnnnngntsnnsVGIGTPLYASPEQL-DGENYNEKADIYSLGIILFEML---HPFKTAMERsTILTDLR 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 252 RRILkcsPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd13996  234 NGIL---PESFKAKHPKEADLIQSLLSKNPEER 263
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
33-301 1.21e-27

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 112.78  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd06613    2 YELIQRIGSGTYGDVY---KARNIATGELAAVKVIK----LEPGDDFEIIQQEISMLKECRH-PNIVAYFGSYLRRDKLW 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMfTHLYQR-QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEK 191
Cdd:cd06613   74 IVMEYCGGGSL-QDIYQVtGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQ-LTATI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEII--RSKTGHGKAVDWWSLGILLFELLTGASP-FTLEGERntqaeVSRRILKCSPPfPPRI--- 265
Cdd:cd06613  152 AKRKSFIGTPYWMAPEVAavERKGGYDGKCDIWALGITAIELAELQPPmFDLHPMR-----ALFLIPKSNFD-PPKLkdk 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 266 ---GPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd06613  226 ekwSPDFHDFIKKCLTKNPKKRPTAT-----KLLQHPFV 259
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
410-684 1.64e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 113.62  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE-------ANTQREVAALRLCQsHPNVVNLHEV----HHDQLhtYLVLEL 478
Cdd:cd07845   15 IGEGTYGIVYRARDTTSGEIVALKKV--RMDnerdgipISSLREITLLLNLR-HPNIVELKEVvvgkHLDSI--FLVMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADdtpGAPVKIIDFGFARlRPQSPGVP 558
Cdd:cd07845   90 CEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENF-IIHRDLKVSNLLLTD---KGCLKIADFGLAR-TYGLPAKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MqTPCF-TLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMC--------KIREG---- 624
Cdd:cd07845  165 M-TPKVvTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKS----EIEQLDLIIqllgtpneSIWPGfsdl 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 625 ----RFSLDGEAWQG-------VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDgsarsSPPLRTPDVL 684
Cdd:cd07845  240 plvgKFTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE-----KPLPCEPEMM 305
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
409-666 1.72e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 112.39  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEanTQREVaalRLCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14010    7 EIGRGKHSVVYKGRRKGTIEFVAIKCVdkSKRPE--VLNEV---RLTHElkHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQS---------- 554
Cdd:cd14010   82 ETLLRQDGNLPESSVRKFGRDLVRGLHYIHSK-GIIYCDLKPSNILL--DGNGT-LKLSDFGLARREGEIlkelfgqfsd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 ---------PGVPMQTPCftlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAE-IMCKIREg 624
Cdd:cd14010  158 egnvnkvskKQAKRGTPY----YMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAES----FTELVEkILNEDPP- 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 625 rfSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSS-W 666
Cdd:cd14010  229 --PPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
37-287 1.75e-27

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 112.36  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAKLHLILD 116
Cdd:cd14192   10 EVLGGGRFGQV---HKCTELSTGLTLAAKIIK----VKGAKEREEVKNEINIMNQLNHVN-LIQLYDAFESKTNLTLIME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH-IVLTDFGLSKEFLTEEKER 193
Cdd:cd14192   82 YVDGGELFDRITDESYqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TfSFcGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKCSPPFPP----RIGPVA 269
Cdd:cd14192  162 V-NF-GTPEFLAPEVVNYDF-VSFPTDMWSVGVITYMLLSGLSPFLGE----TDAETMNNIVNCKWDFDAeafeNLSEEA 234
                        250
                 ....*....|....*...
gi 663856869 270 QDLLQRLLCKDPKKRLGA 287
Cdd:cd14192  235 KDFISRLLVKEKSCRMSA 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
410-663 1.79e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 112.60  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEF-AVKILS------RRLEANTQR-------EVAALRLCQSHPNVVNLHE--VHHDQLhtY 473
Cdd:cd08528    8 LGSGAFGCVYKVRKKSNGQTLlALKEINmtnpafGRTEQERDKsvgdiisEVNIIKEQLRHPNIVRYYKtfLENDRL--Y 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELLEHI----RKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDTpgaPVKIIDFGFAR 549
Cdd:cd08528   86 IVMELIEGAPLGEHFsslkEKNEHFTEDRIWNIFVQMVLALRYLHKEKQIVHRDLKPNNIMLGEDD---KVTITDFGLAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 LRpQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFS-L 628
Cdd:cd08528  163 QK-GPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYS-------TNMLTLATKIVEAEYEpL 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 629 DGEAWqgvSEEAKELVRGLLTVDPAKR---LKLEGLRG 663
Cdd:cd08528  235 PEGMY---SDDITFVIRSCLTPDPEARpdiVEVSSMIS 269
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
31-308 1.95e-27

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 113.19  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvflVRKAGGHDAGKL-YAMKVLRKaalvqrakTQEHTRTERSVLELVRQAPFLVTLHYAFQTDA 109
Cdd:cd14178    3 DGYEIKEDIGIGSYS----VCKRCVHKATSTeYAVKIIDK--------SKRDPSEEIEILLRYGQHPNIITLKDVYDDGK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH---IVLTDFGLSKE 185
Cdd:cd14178   71 FVYLVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 fLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlEGERNTQAEVSRRI----LKCSPPF 261
Cdd:cd14178  151 -LRAENGLLMTPCYTANFVAPEVLK-RQGYDAACDIWSLGILLYTMLAGFTPFA-NGPDDTPEEILARIgsgkYALSGGN 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLDWVA 308
Cdd:cd14178  228 WDSISDAAKDIVSKMLHVDPHQRL-----TAPQVLRHPWIVNREYLS 269
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
33-300 2.08e-27

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 112.74  E-value: 2.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDA--- 109
Cdd:cd14200    2 YKLQSEIGKGSYG---VVKLAYNESDDKYYAMKVLSKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPLERVYQEIAilk 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 --------------------KLHLILDYVSGGEMFtHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14200   79 kldhvnivklievlddpaedNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIrSKTGH---GKAVDWWSLGILLFELLTGASPFTLEgernT 246
Cdd:cd14200  158 GDDGHVKIADFGVSNQFEGNDALLS-STAGTPAFMAPETL-SDSGQsfsGKALDVWAMGVTLYCFVYGKCPFIDE----F 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 247 QAEVSRRILKCSPPFP--PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14200  232 ILALHNKIKNKPVEFPeePEISEELKDLILKMLDKNPETRI-----TVPEIKVHPW 282
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
410-656 2.17e-27

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 113.56  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL---EANTQREVAALRLCQS--HPNVVNLHEVH--HDQLhtYLVLELLRGG 482
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEViiaKDEVAHTVTESRVLQNtrHPFLTALKYAFqtHDRL--CFVMEYANGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVPMQTP 562
Cdd:cd05595   81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSR-DVVYRDIKLENLMLDKD---GHIKITDFGLCK-EGITDGATMKTF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMckIREGRFSldgeawQGVSEEAKE 642
Cdd:cd05595  156 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY---NQDHERLFELIL--MEEIRFP------RTLSPEAKS 224
                        250
                 ....*....|....
gi 663856869 643 LVRGLLTVDPAKRL 656
Cdd:cd05595  225 LLAGLLKKDPKQRL 238
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
410-656 2.17e-27

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 113.46  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-------EAnTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVilqdddvEC-TMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpGVPMQTP 562
Cdd:cd05590   82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDK-GIIYRDLKLDNVLLDHE---GHCKLADFGMCKEGIFN-GKTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMCKiREGRFSldgeAWqgVSEEAKE 642
Cdd:cd05590  157 CGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAEN----EDDLFEAILN-DEVVYP----TW--LSQDAVD 225
                        250
                 ....*....|....
gi 663856869 643 LVRGLLTVDPAKRL 656
Cdd:cd05590  226 ILKAFMTKNPTMRL 239
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
406-608 2.64e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 112.02  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQ-SGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14201   10 RKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLSKSQillgKEIKILKELQ-HENIVALYDVQEMPNSVFLVMEYCN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENIL--YAD----DTPGAPVKIIDFGFARLRPQS 554
Cdd:cd14201   89 GGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSK-GIIHRDLKPQNILlsYASrkksSVSGIRIKIADFGFARYLQSN 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 555 pgVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQ 608
Cdd:cd14201  168 --MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQ 219
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
410-656 3.10e-27

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 113.18  E-value: 3.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAA----LRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKaiLKRNEVKHIMAernvLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05575   83 LFFHLQRERHFPEPRARFYAAEIASALGYLHS-LNIIYRDLKPENILL--DSQGH-VVLTDFGLCK-EGIEPSDTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqggQSQA-AEIMCKIREGRFSLDGeawqGVSEEAKE 642
Cdd:cd05575  158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPF--------YSRDtAEMYDNILHKPLRLRT----NVSPSARD 225
                        250
                 ....*....|....
gi 663856869 643 LVRGLLTVDPAKRL 656
Cdd:cd05575  226 LLEGLLQKDRTKRL 239
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
412-667 4.19e-27

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 111.16  E-value: 4.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 412 QGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ--REVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIR 489
Cdd:cd14110   13 RGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLvlREYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 490 KKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYA 569
Cdd:cd14110   92 ERNSYSEAEVTDYLWQILSAVDYLHSRR-ILHLDLRSENMII---TEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVETM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 570 APELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgEAWQGVSEEAKELVRGLLT 649
Cdd:cd14110  168 APELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSS-------DLNWERDRNIRKGKVQLS-RCYAGLSGGAVNFLKSTLC 239
                        250
                 ....*....|....*...
gi 663856869 650 VDPAKRLKLEGLRGSSWL 667
Cdd:cd14110  240 AKPWGRPTASECLQNPWL 257
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
412-660 4.73e-27

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 111.03  E-value: 4.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 412 QGSFSVCRRCRQRQSGQEFAVKIL------SRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd05611    6 KGAFGSVYLAKKRSTGDYFAIKVLkksdmiAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFAR---LRPQSPGVpMQTP 562
Cdd:cd05611   86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQR-GIIHRDIKPENLLI--DQTGH-LKLTDFGLSRnglEKRHNKKF-VGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 cftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKE 642
Cdd:cd05611  161 ----DYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPD-------AVFDNILSRRINWPEEVKEFCSPEAVD 229
                        250
                 ....*....|....*...
gi 663856869 643 LVRGLLTVDPAKRLKLEG 660
Cdd:cd05611  230 LINRLLCMDPAKRLGANG 247
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
39-285 4.89e-27

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 112.27  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKaalvqraKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14180   14 LGEGSFS---VCRKCRHRQSGQEYAVKIISR-------RMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL--DSEGHIV-LTDFGLSKEFlTEEKERTF 195
Cdd:cd14180   84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadESDGAVLkVIDFGFARLR-PQGSRPLQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQ---AEVSRRILKCSPPFPPR----IGPV 268
Cdd:cd14180  163 TPCFTLQYAAPELFSNQ-GYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHnhaADIMHKIKEGDFSLEGEawkgVSEE 241
                        250
                 ....*....|....*..
gi 663856869 269 AQDLLQRLLCKDPKKRL 285
Cdd:cd14180  242 AKDLVRGLLTVDPAKRL 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
39-300 4.89e-27

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 110.92  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHDagKLYAMKVLRKAALvqrAKTQEHTRTERSVL-ELvrQAPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPD--LPVAIKCITKKNL---SKSQNLLGKEIKILkEL--SHENVVALLDCQETSSSVYLVMEY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD---------SEGHIVLTDFGLSKeFLT 188
Cdd:cd14120   74 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShnsgrkpspNDIRLKIADFGFAR-FLQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEkERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFtlegERNTQAEV-----SRRILKcsPPFPP 263
Cdd:cd14120  153 DG-MMAATLCGSPMYMAPEVIMSLQYDAKA-DLWSIGTIVYQCLTGKAPF----QAQTPQELkafyeKNANLR--PNIPS 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14120  225 GTSPALKDLLLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
33-298 5.83e-27

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 111.31  E-value: 5.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAggHDaGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVR-QAPFLVTLHYAFQTDAKL 111
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNK--LD-GRYYAIKKIK-----LRSESKNNSRILREVMLLSRlNHQHVVRYYQAWIERANL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK------E 185
Cdd:cd14046   80 YIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsnklnvE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSFC-----------GTIEYMAPEI-IRSKTGHGKAVDWWSLGILLFELltgASPFTLEGERntqAEVSRR 253
Cdd:cd14046  160 LATQDINKSTSAAlgssgdltgnvGTALYVAPEVqSGTKSTYNEKVDMYSLGIIFFEM---CYPFSTGMER---VQILTA 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 254 ILKCSPPFPPRI----GPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNH 298
Cdd:cd14046  234 LRSVSIEFPPDFddnkHSKQAKLIRWLLNHDPAKR-----PSAQELLKS 277
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
39-302 7.20e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 111.35  E-value: 7.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGghdAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd06655   27 IGQGASGTVFTAIDVA---TGQEVAIKQIN----LQKQPKKELIINEILVMKELKN-PNIVNFLDSFLVGDELFVVMEYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfSFC 198
Cdd:cd06655   99 AGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 199 GTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEgerNTQAEVSRRILKCSPPF--PPRIGPVAQDLLQRL 276
Cdd:cd06655  177 GTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE---NPLRALYLIATNGTPELqnPEKLSPIFRDFLNRC 252
                        250       260
                 ....*....|....*....|....*.
gi 663856869 277 LCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06655  253 LEMDVEKR-----GSAKELLQHPFLK 273
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
405-670 8.81e-27

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 110.41  E-value: 8.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT-QREVAALRLC----QSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14187   10 VRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPhQKEKMSMEIAihrsLAHQHVVGFHGFFEDNDFVYVVLELC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFARlRPQSPGVPM 559
Cdd:cd14187   90 RRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNR-VIHRDLKLGNLFLNDDME---VKIGDFGLAT-KVEYDGERK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSEE 639
Cdd:cd14187  165 KTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE-------TSCLKETYLRIKKNEYSIP----KHINPV 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQDG 670
Cdd:cd14187  234 AASLIQKMLQTDPTARPTINELLNDEFFTSG 264
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
37-299 1.28e-26

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 109.69  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLV--RKAGGHdagklYAMKVLR---KA----ALVQRAKTQEHTRTERSVLELVrqapflvtlhyaFQT 107
Cdd:cd14089    7 QVLGLGINGKVLECfhKKTGEK-----FALKVLRdnpKArrevELHWRASGCPHIVRIIDVYENT------------YQG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH---IVLTDFGL 182
Cdd:cd14089   70 RKCLLVVMECMEGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEflTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVS----RRILKCS 258
Cdd:cd14089  150 AKE--TTTKKSLQTPCYTPYYVAPEVLGPEK-YDKSCDMWSLGVIMYILLCGYPPFY----SNHGLAISpgmkKRIRNGQ 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 259 PPFP----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd14089  223 YEFPnpewSNVSEEAKDLIRGLLKTDPSERL-----TIEEVMNHP 262
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
411-667 1.55e-26

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 109.53  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVKIlsRRLEANTQR----EVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKI--VPYQAEEKQgvlqEYEILKSLH-HERIMALHEAYITPRYLVLIAEFCSGKELLH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFA-RLRPQSPGvPMQTPCFT 565
Cdd:cd14111   89 SLIDRFRYSEDDVVGYLVQILQGLEYLHGRR-VLHLDIKPDNIMVTNLNA---IKIVDFGSAqSFNPLSLR-QLGRRTGT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSlDGEAWQGVSEEAKELVR 645
Cdd:cd14111  164 LEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQ-------ETEAKILVAKFD-AFKLYPNVSQSASLFLK 235
                        250       260
                 ....*....|....*....|..
gi 663856869 646 GLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14111  236 KVLSSYPWSRPTTKDCFAHAWL 257
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
410-667 1.74e-26

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 109.18  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR------LEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14164    8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRraspdfVQKFLPRELSILRRVN-HPNIVQMFECIEVANGRLYIVMEAAATD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpGAPVKIIDFGFARLRPQSPGVPmQTPC 563
Cdd:cd14164   87 LLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDM-NIVHRDLKCENILLSAD--DRKIKIADFGFARFVEDYPELS-TTFC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQGasgqggqsqaaeimCKIREGRFSLDGEAWQ---GVSEE 639
Cdd:cd14164  163 GSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPFDE--------------TNVRRLRLQQRGVLYPsgvALEEP 228
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14164  229 CRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
39-301 2.09e-26

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 110.08  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKV--LRKaalvqraktqeHTRTERSVLELV----RQAPFLVTLHYAFQTDAKLH 112
Cdd:cd06659   29 IGEGSTGVVCIAREK---HSGRQVAVKMmdLRK-----------QQRRELLFNEVVimrdYQHPNVVEMYKSYLVGEELW 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKE 192
Cdd:cd06659   95 VLMEYLQGGAL-TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTfSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRiLKCSPPfPP-----RIGP 267
Cdd:cd06659  174 RK-SLVGTPYWMAPEVI-SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSD----SPVQAMKR-LRDSPP-PKlknshKASP 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 268 VAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd06659  246 VLRDFLERMLVRDPQER-----ATAQELLDHPFL 274
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
33-302 2.59e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 108.94  E-value: 2.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDAGklYAMKVLRKAALvqrAKTQEHTRTERSVLELVRQAPfLVTLhYAFQTDAK-L 111
Cdd:cd14202    4 FSRKDLIGHGAFAVVFKGRHKEKHDLE--VAVKCINKKNL---AKSQTLLGKEIKILKELKHEN-IVAL-YDFQEIANsV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---------HIVLTDFGL 182
Cdd:cd14202   77 YLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTfsFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQA--EVSRRIlkcSPP 260
Cdd:cd14202  157 ARYLQNNMMAAT--LCGSPMYMAPEVIMSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSPQDLRLfyEKNKSL---SPN 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14202  231 IPRETSSHLRQLLLGLLQRNQKDRM-----DFDEFFHHPFLD 267
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
33-301 2.83e-26

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 109.16  E-value: 2.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLEL--VRQAPFLVTLHYAFQTDAK 110
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARN---KETGELVAIKKMK-----KKFYSWEECMNLREVKSLrkLNEHPNIVKLKEVFRENDE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGgemftHLYQ------RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd07830   73 LYFVFEYMEG-----NLYQlmkdrkGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EflTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLT------GASPF--------TL---------E 241
Cdd:cd07830  148 E--IRSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTlrplfpGSSEIdqlykicsVLgtptkqdwpE 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 242 GERNTQAeVSRRILKCSPPFP----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07830  226 GYKLASK-LGFRFPQFAPTSLhqliPNASPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
410-656 3.08e-26

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 110.09  E-value: 3.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05616    8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQdddvecTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05616   88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSK-GIIYRDLKLDNVML--DSEGH-IKIADFGMCK-ENIWDGVTTKTFC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05616  163 GTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEG-------EDEDELFQSIMEHNVAYP----KSMSKEAVAI 231
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05616  232 CKGLMTKHPGKRL 244
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
409-656 3.16e-26

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 109.29  E-value: 3.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRRLE-----ANTQREVAALRLCQS--HPNVVNLHEV---------------- 465
Cdd:cd07838    6 EIGEGAYGTVYKARDLQDGRFVALKKVRVPLSeegipLSTIREIALLKQLESfeHPNVVRLLDVchgprtdrelkltlvf 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 -HHDQ-LHTYLvlellrggellehiRK--KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVK 541
Cdd:cd07838   86 eHVDQdLATYL--------------DKcpKPGLPPETIKDLMRQLLRGLDFLHSHR-IVHRDLKPQNILVTSD---GQVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 542 IIDFGFARLRpqspGVPMQ-TPCF-TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMC 619
Cdd:cd07838  148 LADFGLARIY----SFEMAlTSVVvTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFR---GSSEADQLGKIFD 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 620 KIreGRFSldGEAW-----------------------QGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07838  221 VI--GLPS--EEEWprnsalprssfpsytprpfksfvPEIDEEGLDLLKKMLTFNPHKRI 276
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
410-682 3.44e-26

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 110.17  E-value: 3.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEAN----TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKALKKDvvLEDDdvecTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSpGVPMQTPC 563
Cdd:cd05592   83 LMFHIQQSGRFDEDRARFYGAEIICGLQFLHSR-GIIYRDLKLDNVLL--DREGH-IKIADFGMCKENIYG-ENKASTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQAAEIMckiregrfslDGEAW--QGVSEEAK 641
Cdd:cd05592  158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPF---HGEDEDELFWSIC----------NDTPHypRWLTKEAA 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 642 ELVRGLLTVDPAKRLkleglrGSSWLQDGSARSSPPLRTPD 682
Cdd:cd05592  225 SCLSLLLERNPEKRL------GVPECPAGDIRDHPFFKTID 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
406-667 4.41e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 108.08  E-value: 4.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKIL---SRRLEANTQREVAALRLCqSHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd14193    8 KEEILGGGRFGQVHKCEEKSSGLKLAAKIIkarSQKEKEEVKNEIEVMNQL-NHANLIQLYDAFESRNDIVLVMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRH-FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTpGAPVKIIDFGFAR-LRPQSP-GVPM 559
Cdd:cd14193   87 ELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMY-ILHLDLKPENILCVSRE-ANQVKIIDFGLARrYKPREKlRVNF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14193  165 GTP----EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLG-------EDDNETLNNILACQWDFEDEEFADISEE 233
                        250       260
                 ....*....|....*....|....*...
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14193  234 AKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
410-656 5.16e-26

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 108.81  E-value: 5.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEanTQRE---VAALRLCQ-----SHPNVVNLHEVHHDQLH------TYLV 475
Cdd:cd07840    7 IGEGTYGQVYKARNKKTGELVALKKI--RME--NEKEgfpITAIREIKllqklDHPNVVRLKEIVTSKGSakykgsIYMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSP 555
Cdd:cd07840   83 FEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHS-NGILHRDIKGSNILINND---GVLKLADFGLARPYTKEN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GVPMQTPCFTLQYAAPELL--AQQgYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMckireGrfSLDGEAW 633
Cdd:cd07840  159 NADYTNRVITLWYRPPELLlgATR-YGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELC-----G--SPTEENW 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 634 QGVSE---------------------------EAKELVRGLLTVDPAKRL 656
Cdd:cd07840  231 PGVSDlpwfenlkpkkpykrrlrevfknvidpSALDLLDKLLTLDPKKRI 280
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
38-300 6.40e-26

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 107.91  E-value: 6.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLvrkaGGHDAGKLYAMK-VLRKAALVQRAKtQEHTRTERSV--LELVRQAPFLVTLHYAFQtDAKLHLI 114
Cdd:cd06631    8 VLGKGAYGTVYC----GLTSTGQLIAVKqVELDTSDKEKAE-KEYEKLQEEVdlLKTLKHVNIVGYLGTCLE-DNVVSIF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERT 194
Cdd:cd06631   82 MEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 F-----SFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAEV----SRRILKcsPPFPPRI 265
Cdd:cd06631  162 QsqllkSMRGTPYWMAPEVIN-ETGHGRKSDIWSIGCTVFEMATGKPPWA---DMNPMAAIfaigSGRKPV--PRLPDKF 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd06631  236 SPEARDFVHACLTRDQDERP-----SAEQLLKHPF 265
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
37-301 6.85e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 107.90  E-value: 6.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGghdAGKLYAMKVLR--KAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLI 114
Cdd:cd06630    6 PLLGTGAFSSCYQARDVK---TGTLMAVKQVSfcRNSSSEQEEVVEAIREEIRMMARLNH-PNIVRMLGATQHKSHFNIF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSKEF---LTEE 190
Cdd:cd06630   82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLrIADFGAAARLaskGTGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRriLKCS---PPFPPRIGP 267
Cdd:cd06630  162 GEFQGQLLGTIAFMAPEVLRGEQ-YGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFK--IASAttpPPIPEHLSP 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 268 VAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd06630  239 GLRDVTLRCLELQPEDR-----PPARELLKHPVF 267
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
33-238 1.06e-25

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 107.39  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQAPFLVTLHYAFQT----- 107
Cdd:cd06608    8 FELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMDIIE-----DEEEEIKLEINILRKFSNHPNIATFYGAFIKkdppg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 -DAKLHLILDYVSGGEMfTHLYQR-----QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd06608   80 gDDQLWLVMEYCGGGSV-TDLVKGlrkkgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 182 LSKEfLTEEKERTFSFCGTIEYMAPEIIRSK----TGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd06608  159 VSAQ-LDSTLGRRNTFIGTPYWMAPEVIACDqqpdASYDARCDVWSLGITAIELADGKPPL 218
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
408-656 1.14e-25

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 108.63  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 408 PALGQGSFSVCRRCRQRQSGQEFAVKILSRR-------LE-ANTQREVAALRlcQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05587    2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDviiqdddVEcTMVEKRVLALS--GKPPFLTQLHSCFQTMDRLYFVMEYV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRpQSPGVPM 559
Cdd:cd05587   80 NGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVML--DAEGH-IKIADFGMCKEG-IFGGKTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgeawQGVSEE 639
Cdd:cd05587  155 RTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG-------EDEDELFQSIMEHNVSYP----KSLSKE 223
                        250
                 ....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRL 656
Cdd:cd05587  224 AVSICKGLLTKHPAKRL 240
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
410-651 1.69e-25

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 106.14  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT--QREVAALRLCQsHPNVVNLHEVHhDQLHTYLVLELLRGGELLEH 487
Cdd:cd14108   10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTsaRRELALLAELD-HKSIVRFHDAF-EKRRVVIIVTELCHEELLER 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgAPVKIIDFGFARlrPQSPGVPMQTPCFTLQ 567
Cdd:cd14108   88 ITKRPTVCESEVRSYMRQLLEGIEYLHQND-VLHLDLKPENLLMADQKT-DQVRICDFGNAQ--ELTPNEPQYCKYGTPE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELVRGL 647
Cdd:cd14108  164 FVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDR-------TTLMNIRNYNVAFEESMFKDLCREAKGFIIKV 236

                 ....
gi 663856869 648 LTVD 651
Cdd:cd14108  237 LVSD 240
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
410-656 1.69e-25

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 107.21  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ-------REVAALRLCqSHPNVVNLHEVHHDQLHTYLVlellrgg 482
Cdd:cd07860    8 IGEGTYGVVYKARNKLTGEVVALKKI--RLDTETEgvpstaiREISLLKEL-NHPNIVKLLDVIHTENKLYLV------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQI--------LRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFARlrpqS 554
Cdd:cd07860   78 FEFLHQDLKKFMDASALTGIplpliksyLFQLLQGLAFCHSHR-VLHRDLKPQNLLI--NTEGA-IKLADFGLAR----A 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaaEI--MCKIREGRFSL 628
Cdd:cd07860  150 FGVPVRTythEVVTLWYRAPEiLLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDS---------EIdqLFRIFRTLGTP 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 629 DGEAWQGVS-------------------------EEAKELVRGLLTVDPAKRL 656
Cdd:cd07860  221 DEVVWPGVTsmpdykpsfpkwarqdfskvvppldEDGRDLLSQMLHYDPNKRI 273
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
33-301 1.81e-25

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 106.23  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAA----LVQRAKTQEhtrtersvLELVRQAPFLVTLH-YAF-- 105
Cdd:cd14163    2 YQLGKTIGEGTYSKV---KEAFSKKHQRKVAIKIIDKSGgpeeFIQRFLPRE--------LQIVERLDHKNIIHvYEMle 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEgHIVLTDFGLSKE 185
Cdd:cd14163   71 SADGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILKCSPPFPPRI 265
Cdd:cd14163  150 LPKGGRELSQTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFD---DTDIPKMLCQQQKGVSLPGHLGV 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 266 GPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd14163  227 SRTCQDLLKRLLEPDMVLR-----PSIEEVSWHPWL 257
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
33-304 1.97e-25

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 108.00  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKA-ALVQRAKtqehtRTERSVlELVR--QAPFLVTLHYAFQTDA 109
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDK---RTGRKVAIKKISNVfDDLIDAK-----RILREI-KILRhlKHENIIGLLDILRPPS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 K-----LHLILDYvsggeMFTHLYQ------------RQYFkeaevrVYggEIVLALEHLHKLGIIYRDLKLENVLLDSE 172
Cdd:cd07834   73 PeefndVYIVTEL-----METDLHKvikspqpltddhIQYF------LY--QILRGLKYLHSAGVIHRDLKPSNILVNSN 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GHIVLTDFGLSKEFLTEEKERTFS-FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFT------------ 239
Cdd:cd07834  140 CDLKICDFGLARGVDPDEDKGFLTeYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPgrdyidqlnliv 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 240 ----------LEGERNTQAevsRRILKCSPPFPPR--------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07834  220 evlgtpseedLKFISSEKA---RNYLKSLPKKPKKplsevfpgASPEAIDLLEKMLVFNPKKRI-----TADEALAHPYL 291

                 ...
gi 663856869 302 QGL 304
Cdd:cd07834  292 AQL 294
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
32-301 2.01e-25

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 107.27  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKvlrKAALVQRAKTQEH-TRT---ERSVL-ELvrQAPFLVTLHYAFQ 106
Cdd:cd07841    1 RYEKGKKLGEGTYAVVY---KARDKETGRIVAIK---KIKLGERKEAKDGiNFTalrEIKLLqEL--KHPNIIGLLDVFG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYvsggeMFTHLYQ-----RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd07841   73 HKSNINLVFEF-----METDLEKvikdkSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGAsPFtLEGERN-TQAEVSRRIL----- 255
Cdd:cd07841  148 LARSFGSPNRKMT-HQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRV-PF-LPGDSDiDQLGKIFEALgtpte 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 256 ------KCSP------PFPPR--------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07841  225 enwpgvTSLPdyvefkPFPPTplkqifpaASDDALDLLQRLLTLNPNKRI-----TARQALEHPYF 285
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
32-300 2.01e-25

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 106.15  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAKL 111
Cdd:cd14193    5 NVNKEEILGGGRFGQV---HKCEEKSSGLKLAAKIIK----ARSQKEKEEVKNEIEVMNQLNHAN-LIQLYDAFESRNDI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE--GHIVLTDFGLSKEFLT 188
Cdd:cd14193   77 VLVMEYVDGGELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRYKP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTfSFcGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGErntqAEVSRRILKCSPPFPPR---- 264
Cdd:cd14193  157 REKLRV-NF-GTPEFLAPEVVNYEF-VSFPTDMWSLGVIAYMLLSGLSPFLGEDD----NETLNNILACQWDFEDEefad 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 265 IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14193  230 ISEEAKDFISKLLIKEKSWRM-----SASEALKHPW 260
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
29-300 2.21e-25

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 108.37  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVL--RKAALVQRAKTQEhtrtersvLELVRQA--PFLVTLHYA 104
Cdd:PLN00034  72 SLSELERVNRIGSGAGGTVYKVIH---RPTGRLYALKVIygNHEDTVRRQICRE--------IEILRDVnhPNVVKCHDM 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEM-FTHLYQRQYFKEAEVRVYGGeivlaLEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:PLN00034 141 FDHNGEIQVLLEFMDGGSLeGTHIADEQFLADVARQILSG-----IAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVS 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KeFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGK----AVDWWSLGILLFELLTGASPFTLeGERNTQAEVSRRILKCSP 259
Cdd:PLN00034 216 R-ILAQTMDPCNSSVGTIAYMSPERINTDLNHGAydgyAGDIWSLGVSILEFYLGRFPFGV-GRQGDWASLMCAICMSQP 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 260 PFPPR-IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:PLN00034 294 PEAPAtASREFRHFISCCLQREPAKRW-----SAMQLLQHPF 330
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
39-284 2.50e-25

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 105.87  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRAKTQE-HTRTERSVlelvrqAPFLV-TLHYAFQTDAKLHLILD 116
Cdd:cd13987    1 LGEGTYGKVLLAVHKG---SGTKMALKFVPKPSTKLKDFLREyNISLELSV------HPHIIkTYDVAFETEDYYVFAQE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL-DSE-GHIVLTDFGLSKEFLTEEKERT 194
Cdd:cd13987   72 YAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRRVGSTVKRVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 fsfcGTIEYMAPEIIRSKTGHGKAV----DWWSLGILLFELLTGASPFTLEGERNTQ----AEVSRRILKCSPPFPPRIG 266
Cdd:cd13987  152 ----GTIPYTAPEVCEAKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWEKADSDDQFyeefVRWQKRKNTAVPSQWRRFT 227
                        250
                 ....*....|....*...
gi 663856869 267 PVAQDLLQRLLCKDPKKR 284
Cdd:cd13987  228 PKALRMFKKLLAPEPERR 245
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
96-301 2.60e-25

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 105.67  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 PFLVTLHYAFQTDAK-LHLILDYVSGGEMFTH--LYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLdSE 172
Cdd:cd14109   56 PNIVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GHIVLTDFGLSKEfLTEEKERTFSFcGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVsr 252
Cdd:cd14109  135 DKLKLADFGQSRR-LLRGKLTTLIY-GSPEFVSPEIVNSY-PVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNV-- 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 253 RILKCS---PPFPPrIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14109  210 RSGKWSfdsSPLGN-ISDDARDFIKKLLVYIPESRL-----TVDEALNHPWF 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
33-284 2.60e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 105.98  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVR-QAPFLVTLHYAFQT-DAK 110
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRD---RKQYVIKKLN----LKNASKRERKAAEQEAKLLSKlKHPNIVSYKESFEGeDGF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLT 188
Cdd:cd08223   75 LYIVMGFCEGGDLYTRLKEQkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR-VLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEgERNTqaeVSRRILKCS-PPFPPRIGP 267
Cdd:cd08223  154 SSSDMATTLIGTPYYMSPELFSNKPYNHKS-DVWALGCCVYEMATLKHAFNAK-DMNS---LVYKILEGKlPPMPKQYSP 228
                        250
                 ....*....|....*..
gi 663856869 268 VAQDLLQRLLCKDPKKR 284
Cdd:cd08223  229 ELGELIKAMLHQDPEKR 245
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
410-659 3.28e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 105.33  E-value: 3.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL---EANTQREVAALRL-CQ-SHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd14186    9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAmqkAGMVQRVRNEVEIhCQlKHPSILELYNYFEDSNYVYLVLEMCHNGEM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIR-KKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgapVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd14186   89 SRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSH-GILHRDLTLSNLLLTRNMN---IKIADFGLAT-QLKMPHEKHFTMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEawqgVSEEAKEL 643
Cdd:cd14186  164 GTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVK-------NTLNKVVLADYEMPAF----LSREAQDL 232
                        250
                 ....*....|....*.
gi 663856869 644 VRGLLTVDPAKRLKLE 659
Cdd:cd14186  233 IHQLLRKNPADRLSLS 248
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
32-284 5.14e-25

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 105.05  E-value: 5.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQrAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd08224    1 NYEIEKKIGKGQFSVVY---RARCLLDGRLVALKKVQIFEMMD-AKARQDCLKEIDLLQQLNH-PNIIKYLASFIENNEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGE---MFTHL-YQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFL 187
Cdd:cd08224   76 NIVLELADAGDlsrLIKHFkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR-FF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCS-PPFPPRIG 266
Cdd:cd08224  155 SSKTTAAHSLVGTPYYMSPERIR-EQGYDFKSDIWSLGCLLYEMAALQSPF--YGEKMNLYSLCKKIEKCEyPPLPADLY 231
                        250
                 ....*....|....*....
gi 663856869 267 PVA-QDLLQRLLCKDPKKR 284
Cdd:cd08224  232 SQElRDLVAACIQPDPEKR 250
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
410-656 6.82e-25

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 104.78  E-value: 6.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGS----FSVCRRCRQRQsGQEFAVKIL--------SRRLE-ANTQREVaaLRLCQSHPNVVNLHEVHHDQLHTYLVL 476
Cdd:cd05583    2 LGTGAygkvFLVRKVGGHDA-GKLYAMKVLkkativqkAKTAEhTMTERQV--LEAVRQSPFLVTLHYAFQTDAKLHLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPG 556
Cdd:cd05583   79 DYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHK-LGIIYRDIKLENILL--DSEGH-VVLTDFGLSKEFLPGEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCFTLQYAAPELL--AQQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQAAEIMCKIREGRFSLDgeawQ 634
Cdd:cd05583  155 DRAYSFCGTIEYMAPEVVrgGSDGHDKAVDWWSLGVLTYELLTGASPF---TVDGERNSQSEISKRILKSHPPIP----K 227
                        250       260
                 ....*....|....*....|..
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05583  228 TFSAEAKDFILKLLEKDPKKRL 249
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
36-284 7.17e-25

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 104.72  E-value: 7.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLrkaaLVQRAKTQEHTRTERSVLELVRQAPFLVTL--HYAFQTDAKLH- 112
Cdd:cd13985    5 TKQLGEGGFSYVYLAHD---VNTGRRYALKRM----YFNDEEQLRVAIKEIEIMKRLCGHPNIVQYydSAILSSEGRKEv 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 -LILDYVSGgemftHLYQ------RQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLLDSEGHIVLTDFGlS 183
Cdd:cd13985   78 lLLMEYCPG-----SLVDilekspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG-S 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTEEKERTfSFCGTIE----------YMAPEIIR--SKTGHGKAVDWWSLGILLFELLTGASPFtlegerntQAEVS 251
Cdd:cd13985  152 ATTEHYPLERA-EEVNIIEeeiqknttpmYRAPEMIDlySKKPIGEKADIWALGCLLYKLCFFKLPF--------DESSK 222
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 252 RRIL--KCSPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd13985  223 LAIVagKYSIPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
410-656 7.66e-25

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 106.21  E-value: 7.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAALR--LCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtiLKKKEQNHIMAERnvLLKNlkHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSL-NIIYRDLKPENILL--DCQGH-VVLTDFGLCK-EGMEPEETTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGeawqGVSEEAKEL 643
Cdd:cd05603  158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFY-------SRDVSQMYDNILHKPLHLPG----GKTVAACDL 226
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05603  227 LQGLLHKDQRRRL 239
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
410-656 8.81e-25

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 106.23  E-value: 8.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05615   18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQdddvecTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05615   98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKK-GIIYRDLKLDNVML--DSEGH-IKIADFGMCK-EHMVEGVTTRTFC 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05615  173 GTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDG-------EDEDELFQSIMEHNVSYP----KSLSKEAVSI 241
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05615  242 CKGLMTKHPAKRL 254
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
410-655 1.01e-24

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 104.20  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL----SRRLEANTQREVAAlRLcqSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14107   10 IGRGTFGFVKRVTHKGNGECCAAKFIplrsSTRARAFQERDILA-RL--SHRRLTCLLDQFETRKTLILILELCSSEELL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgAPVKIIDFGFAR----LRPQSP--GVPm 559
Cdd:cd14107   87 DRLFLKGVVTEAEVKLYIQQVLEGIGYLHGM-NILHLDIKPDNILMVSPTR-EDIKICDFGFAQeitpSEHQFSkyGSP- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 qtpcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGgqsqaaeIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd14107  164 -------EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRA-------TLLNVAEGVVSWDTPEITHLSED 229
                        250
                 ....*....|....*.
gi 663856869 640 AKELVRGLLTVDPAKR 655
Cdd:cd14107  230 AKDFIKRVLQPDPEKR 245
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
410-656 1.05e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 106.27  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAnTQREVAAL----RLCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05594   33 LGKGTFGKVILVKEKATGRYYAMKILKKEVIV-AKDEVAHTltenRVLQNsrHPFLTALKYSFQTHDRLCFVMEYANGGE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05594  112 LFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKD---GHIKITDFGLCK-EGIKDGATMKTFC 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMCkIREGRFSldgeawQGVSEEAKEL 643
Cdd:cd05594  188 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD----HEKLFELIL-MEEIRFP------RTLSPEAKSL 256
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05594  257 LSGLLKKDPKQRL 269
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
37-288 1.11e-24

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 104.03  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFlvrkAGGH-DAGKLYAMKVLRKaaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd14082    9 EVLGSGQFGIVY----GGKHrKTGRDVAIKVIDK--LRFPTKQESQLRNEVAILQQLSH-PGVVNLECMFETPERVFVVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGG--EMFTHlYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---HIVLTDFGLSKefLTEE 190
Cdd:cd14082   82 EKLHGDmlEMILS-SEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR--IIGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFtlegerNTQAEVSRRILKCSPPFPP----RIG 266
Cdd:cd14082  159 KSFRRSVVGTPAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPF------NEDEDINDQIQNAAFMYPPnpwkEIS 231
                        250       260
                 ....*....|....*....|..
gi 663856869 267 PVAQDLLQRLLCKDPKKRLGAG 288
Cdd:cd14082  232 PDAIDLINNLLQVKMRKRYSVD 253
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
37-288 1.19e-24

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 103.85  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKaalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd14190   10 EVLGGGKFGKV---HTCTEKRTGLKLAAKVINK----QNSKDKEMVLLEIQVMNQLNH-RNLIQLYEAIETPNEIVLFME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL-DSEGHIV-LTDFGLSKEFLTEEKER 193
Cdd:cd14190   82 YVEGGELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQVkIIDFGLARRYNPREKLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 TfSFcGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGASPFTleGERNTqaEVSRRILKCSPPFPPR----IGPVA 269
Cdd:cd14190  162 V-NF-GTPEFLSPEVVNYDQVSFP-TDMWSMGVITYMLLSGLSPFL--GDDDT--ETLNNVLMGNWYFDEEtfehVSDEA 234
                        250
                 ....*....|....*....
gi 663856869 270 QDLLQRLLCKDPKKRLGAG 288
Cdd:cd14190  235 KDFVSNLIIKERSARMSAT 253
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
31-300 1.28e-24

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 103.92  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAalvqRAKTQEHT-RTERSVLELVRQaPFLVTLHYAFQTDA 109
Cdd:cd14183    6 ERYKVGRTIGDGNFA---VVKECVERSTGREYALKIINKS----KCRGKEHMiQNEVSILRRVKH-PNIVLLIEEMDMPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEGHIVLTDFGLSke 185
Cdd:cd14183   78 ELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLA-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 flTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCSPPFP--- 262
Cdd:cd14183  156 --TVVDGPLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPF--RGSGDDQEVLFDQILMGQVDFPspy 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 263 -PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14183  231 wDNVSDSAKELITMMLQVDVDQRY-----SALQVLEHPW 264
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
39-302 1.36e-24

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 103.85  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFL-VRKAGGHDAGklyamkvLRKAALVQRAKtQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd06647   15 IGQGASGTVYTaIDVATGQEVA-------IKQMNLQQQPK-KELIINEILVMRENKN-PNIVNYLDSYLVGDELWVVMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfSF 197
Cdd:cd06647   86 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEgerNTQAEVSRRILKCSPPF--PPRIGPVAQDLLQR 275
Cdd:cd06647  164 VGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNE---NPLRALYLIATNGTPELqnPEKLSAIFRDFLNR 239
                        250       260
                 ....*....|....*....|....*..
gi 663856869 276 LLCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06647  240 CLEMDVEKR-----GSAKELLQHPFLK 261
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
410-655 1.56e-24

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 104.30  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-IL--SRRLEANTQREVAALRLCQsHPNVVNL--HEV--HHDQLHT-YLVLELLRG 481
Cdd:cd13986    8 LGEGGFSFVYLVEDLSTGRLYALKkILchSKEDVKEAMREIENYRLFN-HPNILRLldSQIvkEAGGKKEvYLLLPYYKR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIR----KKRHFSESEASQILRSLVSAVSFMHE--EAGVVHRDLKPENILYADDtpGAPVkIIDFGFAR-----L 550
Cdd:cd13986   87 GSLQDEIErrlvKGTFFPEDRILHIFLGICRGLKAMHEpeLVPYAHRDIKPGNVLLSED--DEPI-LMDLGSMNparieI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RPQSPGVPMQ----TPCfTLQYAAPELL---AQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAeimckIRE 623
Cdd:cd13986  164 EGRREALALQdwaaEHC-TMPYRAPELFdvkSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLALA-----VLS 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 624 GRFSLDGEAwqGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd13986  238 GNYSFPDNS--RYSEELHQLVKSMLVVNPAER 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
34-284 1.79e-24

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 103.40  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869    34 ELLKVLGTGAYGKVFLVR-KAGGHDAGKLYAMKVLRKAAlvqraktqehtrTERSVLELVRQA--------PFLVTLHYA 104
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlKGKGDGKEVEVAVKTLKEDA------------SEQQIEEFLREArimrkldhPNIVKLLGV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   105 FQTDAKLHLILDYVSGGEMFTHL--YQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:smart00221  70 CTEEEPLMIVMEYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   183 SKEfLTEEKERTFSFC-GTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRI-----L 255
Cdd:smart00221 150 SRD-LYDDDYYKVKGGkLPIRWMAPESLKEGK-FTSKSDVWSFGVLLWEIFTlGEEPY----PGMSNAEVLEYLkkgyrL 223
                          250       260
                   ....*....|....*....|....*....
gi 663856869   256 KCSPPFPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:smart00221 224 PKPPNCPPEL----YKLMLQCWAEDPEDR 248
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
33-301 1.88e-24

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 103.50  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLR--KAALVQRAKtqehtrtERSVLELVRQAP-----FLVTLHYAF 105
Cdd:cd14133    1 YEVLEVLGKGTFGQVV---KCYDLLTGEEVALKIIKnnKDYLDQSLD-------EIRLLELLNKKDkadkyHIVRLKDVF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTdaKLHLILdyVSggEMFT-HLYQ------RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL--DSEGHIV 176
Cdd:cd14133   71 YF--KNHLCI--VF--ELLSqNLYEflkqnkFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 177 LTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILK 256
Cdd:cd14133  145 IIDFGSS----CFLTQRLYSYIQSRYYRAPEVILG-LPYDEKIDMWSLGCILAELYTGEPLFP----GASEVDQLARIIG 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 257 CSPPFPPRI---GPVAQ----DLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd14133  216 TIGIPPAHMldqGKADDelfvDFLKKLLEIDPKERPTAS-----QALSHPWL 262
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
412-656 1.89e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 104.23  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 412 QGSFSVCRRCRQRQSGQEFAVKilsrRLEANTQRE---VAALR-----LCQSHPNVVNLHEV----HHDQLhtYLVLELL 479
Cdd:cd07843   15 EGTYGVVYRARDKKTGEIVALK----KLKMEKEKEgfpITSLReinilLKLQHPNIVTVKEVvvgsNLDKI--YMVMEYV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVPM 559
Cdd:cd07843   89 EHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNW-ILHRDLKTSNLLLNNR---GILKICDFGLAR-EYGSPLKPY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaaEI--MCKIregrFSLDG----EA 632
Cdd:cd07843  164 TQLVVTLWYRAPElLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKS---------EIdqLNKI----FKLLGtpteKI 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 633 WQGV----------------------------SEEAKELVRGLLTVDPAKRL 656
Cdd:cd07843  231 WPGFselpgakkktftkypynqlrkkfpalslSDNGFDLLNRLLTYDPAKRI 282
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
31-300 1.92e-24

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 103.53  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLK-VLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQRaKTQEHTRTERSVlELVRQAPFLVTLHYAFQTda 109
Cdd:cd14172    3 DDYKLSKqVLGLGVNGKVL---ECFHRRTGQKCALKLLYDSPKARR-EVEHHWRASGGP-HIVHILDVYENMHHGKRC-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 kLHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE---GHIVLTDFGLSK 184
Cdd:cd14172   76 -LLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EflTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP-P 263
Cdd:cd14172  155 E--TTVQNALQTPCYTPYYVAPEVLGPEK-YDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRMGQYGFPnP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 264 RIGPVAQD---LLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14172  232 EWAEVSEEakqLIRHLLKTDPTERM-----TITQFMNHPW 266
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
36-301 2.00e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 103.28  E-value: 2.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAGGHdagklyaMKVLRKAALVQRAKTQEH--TRTERSVLELVRQAPfLVTLHYAFQTDAKLHL 113
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDN-------SLVVWKEVNLSRLSEKERrdALNEIDILSLLNHDN-IITYYNHFLDGESLFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEK 191
Cdd:cd08221   77 EMEYCNGGNLHDKIAQqkNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKV-LDSES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILK-CSPPFPPRIgpvaQ 270
Cdd:cd08221  156 SMAESIVGTPYYMSPELVQGVKYNFK-SDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdIDEQYSEEI----I 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 271 DLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd08221  231 QLVHDCLHQDPEDR-----PTAEELLERPLL 256
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
134-300 2.15e-24

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 103.26  E-value: 2.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 134 KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS-EGHIVLTDFGLSKEfLTEEKERTFSFCGTIEYMAPEII-RS 211
Cdd:cd06624  106 NENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKR-LAGINPCTETFTGTLQYMAPEVIdKG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 212 KTGHGKAVDWWSLGILLFELLTGASPFTLEGErnTQAEVSR-RILKCSPPFPPRIGPVAQDLLQRLLCKDPKKRlgagpQ 290
Cdd:cd06624  185 QRGYGPPADIWSLGCTIIEMATGKPPFIELGE--PQAAMFKvGMFKIHPEIPESLSEEAKSFILRCFEPDPDKR-----A 257
                        170
                 ....*....|
gi 663856869 291 GAQEVRNHPF 300
Cdd:cd06624  258 TASDLLQDPF 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
410-659 2.42e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 103.08  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQRE--VAALRLCQS--HPNVVNLHEVHHDQLHTYlVLELLRGGEL 484
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHsRVAKPHQREkiVNEIELHRDlhHKHVVKFSHHFEDAENIY-IFLELCSRKS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRH-FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgapVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd14189   88 LAHIWKARHtLLEPEVRYYLKQIISGLKYLHLK-GILHRDLKLGNFFINENME---LKVGDFGLAA-RLEPPEQRKKTIC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGeawqGVSEEAKEL 643
Cdd:cd14189  163 GTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFE-------TLDLKETYRCIKQVKYTLPA----SLSLPARHL 231
                        250
                 ....*....|....*.
gi 663856869 644 VRGLLTVDPAKRLKLE 659
Cdd:cd14189  232 LAGILKRNPGDRLTLD 247
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
33-301 2.67e-24

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 103.74  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkagGHDAGKLYAMKvlrKAALVQRAKTQEhtrtersvLELVRQA--PFLVTLHYAFQT--- 107
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAK---LLETGEVVAIK---KVLQDKRYKNRE--------LQIMRRLkhPNIVKLKYFFYSsge 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 ---DAKLHLILDYVSggemfTHLYQ--RQYFKEAE------VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHI 175
Cdd:cd14137   72 kkdEVYLNLVMEYMP-----ETLYRviRHYSKNKQtipiiyVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 176 VLTDFGLSKEFLTEEKERTFsFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlEGErnTQAEVSRRIL 255
Cdd:cd14137  147 KLCDFGSAKRLVPGEPNVSY-IC-SRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLF--PGE--SSVDQLVEII 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 256 KC--SPP---------------------------FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14137  221 KVlgTPTreqikamnpnytefkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFF 290
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
410-656 2.69e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 104.53  E-value: 2.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRrCRQRQSGQEFAVK---------ILSRRleanTQREVAALRLCQsHPNVVNLHEV-HHDQLHT----YL 474
Cdd:cd07834    8 IGSGAYgVVCS-AYDKRTGRKVAIKkisnvfddlIDAKR----ILREIKILRHLK-HENIIGLLDIlRPPSPEEfndvYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLellrggellehirkkrHFSESEASQILRS---------------LVSAVSFMHEeAGVVHRDLKPENILYADDtpgAP 539
Cdd:cd07834   82 VT----------------ELMETDLHKVIKSpqpltddhiqyflyqILRGLKYLHS-AGVIHRDLKPSNILVNSN---CD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 540 VKIIDFGFARLRPQSPGVPMQTP-CFTLQYAAPEL-LAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS----------- 606
Cdd:cd07834  142 LKICDFGLARGVDPDEDKGFLTEyVVTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnlivev 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 607 ---------GQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07834  222 lgtpseedlKFISSEKARNYLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRI 280
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
410-656 2.72e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 104.66  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN--TQREVAALR--LCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNrkEQKHIMAERnvLLKNvkHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVkIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05604   84 LFFHLQRERSFPEPRARFYAAEIASALGYLHS-INIVYRDLKPENILL--DSQGHIV-LTDFGLCK-EGISNSDTTTTFC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05604  159 GTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFY-------CRDTAEMYENILHKPLVLR----PGISLTAWSI 227
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05604  228 LEELLEKDRQLRL 240
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
410-655 2.97e-24

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 102.35  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ--REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQaaHEAALLQHLQ-HPQYITLHDTYESPTSYILVLELMDDGRLLDY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFA------RLRPQSPGVPmqt 561
Cdd:cd14115   80 LMNHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAvqisghRHVHHLLGNP--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 pcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMCKIregRFSLDGEAWQGVSEEAK 641
Cdd:cd14115  156 -----EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDES----KEETCINVCRV---DFSFPDEYFGDVSQAAR 223
                        250
                 ....*....|....
gi 663856869 642 ELVRGLLTVDPAKR 655
Cdd:cd14115  224 DFINVILQEDPRRR 237
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
410-656 3.45e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 104.71  E-value: 3.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05602   15 IGKGSFGKVLLARHKSDEKFYAVKvlqkkaILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVkIIDFGFARLRPQsPGVPMQTPC 563
Cdd:cd05602   95 LFYHLQRERCFLEPRARFYAAEIASALGYLHS-LNIVYRDLKPENILL--DSQGHIV-LTDFGLCKENIE-PNGTTSTFC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05602  170 GTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFY-------SRNTAEMYDNILNKPLQLK----PNITNSARHL 238
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05602  239 LEGLLQKDRTKRL 251
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
33-301 3.51e-24

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 103.12  E-value: 3.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMK--------------VLRKAALVQRAKTQEHTrtersvlELVRqapfL 98
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQD---GRFVALKkvrvplseegiplsTIREIALLKQLESFEHP-------NVVR----L 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  99 VTLHYAFQTDAKLHLILdyvsggeMFTHLYQ--RQYFK--------EAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL 168
Cdd:cd07838   67 LDVCHGPRTDRELKLTL-------VFEHVDQdlATYLDkcpkpglpPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNIL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 169 LDSEGHIVLTDFGLSKEFlTEEKERTfSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERN--- 245
Cdd:cd07838  140 VTSDGQVKLADFGLARIY-SFEMALT-SVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADqlg 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 246 ---------TQAEVSRRILKCSPPFPPR-----------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07838  217 kifdviglpSEEEWPRNSALPRSSFPSYtprpfksfvpeIDEEGLDLLKKMLTFNPHKRI-----SAFEALQHPYF 287
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
407-667 4.23e-24

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 101.74  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFsvcrRCRQRQSGQEFAVKILSRRLEANTQRevAALRLcQSHPNVVNLHEV-------------HHDQLHTY 473
Cdd:cd13976    2 EPAEGSSLY----RCVDIHTGEELVCKVVPVPECHAVLR--AYFRL-PSHPNISGVHEViagetkayvfferDHGDLHSY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 lvlellrggellehIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtpGAPVKIidfgfaRLRPQ 553
Cdd:cd13976   75 --------------VRSRKRLREPEAARLFRQIASAVAHCHRN-GIVLRDLKLRKFVFAD---EERTKL------RLESL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTPCFTLQ-------YAAPELL-AQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREG 624
Cdd:cd13976  131 EDAVILEGEDDSLSdkhgcpaYVSPEILnSGATYSgKAADVWSLGVILYTMLVGRYPFH-------DSEPASLFAKIRRG 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 625 RFSLDgeawQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd13976  204 QFAIP----ETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
406-659 4.24e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 102.40  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQREVA----ALRLCQSHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd14188    5 RGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHsRVSKPHQREKIdkeiELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFA-RLRPQspGVPM 559
Cdd:cd14188   85 RRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQE-ILHRDLKLGNFFINENME---LKVGDFGLAaRLEPL--EHRR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSEE 639
Cdd:cd14188  159 RTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE-------TTNLKETYRCIREARYSLP----SSLLAP 227
                        250       260
                 ....*....|....*....|
gi 663856869 640 AKELVRGLLTVDPAKRLKLE 659
Cdd:cd14188  228 AKHLIASMLSKNPEDRPSLD 247
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
410-679 5.01e-24

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 103.85  E-value: 5.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE------ANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05619   13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVlmdddvECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05619   93 LMFHIQSCHKFDLPRATFYAAEIICGLQFLHSK-GIVYRDLKLDNILL--DKDGH-IKIADFGMCK-ENMLGDAKTSTFC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIRegrfsLDGEAW-QGVSEEAKE 642
Cdd:cd05619  168 GTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEE-------ELFQSIR-----MDNPFYpRWLEKEAKD 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 643 LVRGLLTVDPAKRLKLEG-------LRGSSWLQDGSARSSPPLR 679
Cdd:cd05619  236 ILVKLFVREPERRLGVRGdirqhpfFREINWEALEEREIEPPFK 279
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
39-238 5.30e-24

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 102.91  E-value: 5.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaalvQRAKTQEHTRtERSVLE-----------LVRQApfLVTLHYAFQT 107
Cdd:cd13989    1 LGSGGFGYVTLWKH---QDTGEYVAIKKCR-----QELSPSDKNR-ERWCLEvqimkklnhpnVVSAR--DVPPELEKLS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLI-LDYVSGGEMFTHLYQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL-DSEGHIV--LTDF 180
Cdd:cd13989   70 PNDLPLLaMEYCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRVIykLIDL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 181 GLSKEFltEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd13989  150 GYAKEL--DQGSLCTSFVGTLQYLAPELFESKK-YTCTVDYWSFGTLAFECITGYRPF 204
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
410-660 7.43e-24

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 103.03  E-value: 7.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANT--QREVAALRLCqshPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKtirkahIVSRSEVTHTlaERTVLAQVDC---PFIVPLKFSFQSPEKLYLVLAFING 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRpQSPGVPMQT 561
Cdd:cd05585   79 GELFHHLQREGRFDLSRARFYTAELLCALECLHK-FNVIYRDLKPENILL--DYTGH-IALCDFGLCKLN-MKDDDKTNT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDGeawqGVSEEAK 641
Cdd:cd05585  154 FCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFY-------DENTNEMYRKILQEPLRFPD----GFDRDAK 222
                        250
                 ....*....|....*....
gi 663856869 642 ELVRGLLTVDPAKRLKLEG 660
Cdd:cd05585  223 DLLIGLLNRDPTKRLGYNG 241
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
410-656 7.48e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 103.62  E-value: 7.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL------EANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05593   23 LGKGTFGKVILVREKASGKYYAMKILKKEViiakdeVAHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNGGE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05593  102 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHS-GKIVYRDLKLENLMLDKD---GHIKITDFGLCK-EGITDAATMKTFC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaeimcKIREGRFSLDGEAWQGVSEEAKEL 643
Cdd:cd05593  177 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-----------KLFELILMEDIKFPRTLSADAKSL 245
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05593  246 LSGLLIKDPNKRL 258
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
33-302 8.55e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 102.35  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAALVQRA------------KTQEHTRTERSVLELVRQA----- 95
Cdd:cd14199    4 YKLKDEIGKGSYG---VVKLAYNEDDNTYYAMKVLSKKKLMRQAgfprrppprgarAAPEGCTQPRGPIERVYQEiailk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 ----PFLVTLHYAFQ--TDAKLHLILDYVSGGEMFtHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14199   81 kldhPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQ 247
Cdd:cd14199  160 GEDGHIKIADFGVSNEFEGSDALLT-NTVGTPAFMAPETLSEtrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 248 AEVSRRILKCspPFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14199  239 SKIKTQPLEF--PDQPDISDDLKDLLFRMLDKNPESRI-----SVPEIKLHPWVT 286
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
410-656 8.85e-24

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 101.98  E-value: 8.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVlELLRGG 482
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKI--RLETEDEgvpstaiREISLLKELN-HPNIVRLLDVVHSENKLYLV-FEFLDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSeSEASQI---LRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlrpqSPGVPM 559
Cdd:cd07835   83 DLKKYMDSSPLTG-LDPPLIksyLYQLLQGIAFCHSH-RVLHRDLKPQNLLI--DTEGA-LKLADFGLAR----AFGVPV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaaEI--MCKIregrFSL----D 629
Cdd:cd07835  154 RTythEVVTLWYRAPEiLLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDS---------EIdqLFRI----FRTlgtpD 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 630 GEAWQGVS-------------------------EEAKELVRGLLTVDPAKRL 656
Cdd:cd07835  221 EDVWPGVTslpdykptfpkwarqdlskvvpsldEDGLDLLSQMLVYDPAKRI 272
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
410-666 9.28e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 101.67  E-value: 9.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR---------------------------LEaNTQREVAALRLCqSHPNVVNL 462
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKkllkqagffrrppprrkpgalgkpldpLD-RVYREIAILKKL-DHPNVVKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 463 HEVHHD--QLHTYLVLELLRGGELLEHIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPV 540
Cdd:cd14118   80 VEVLDDpnEDNLYMVFELVDKGAVMEVPTDNP-LSEETARSYFRDIVLGIEYLHYQ-KIIHRDIKPSNLLLGDD---GHV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 541 KIIDFGFAR-------LRPQSPGvpmqTPCFTlqyaAPELLAQQGYDES---CDLWSLGVILYMMLSGQVPFQGASgqgg 610
Cdd:cd14118  155 KIADFGVSNefegddaLLSSTAG----TPAFM----APEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDH---- 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 611 qsqaaeIMC---KIR--EGRFSLDGEawqgVSEEAKELVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd14118  223 ------ILGlheKIKtdPVVFPDDPV----VSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
31-287 1.16e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 102.02  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvflVRKAGGHDAGKL-YAMKVLRKAalvQRAKTQEhtrteRSVLELVRQAPFLVTLHYAFQTDA 109
Cdd:cd14177    4 DVYELKEDIGVGSYS----VCKRCIHRATNMeFAVKIIDKS---KRDPSEE-----IEILMRYGQHPNIITLKDVYDDGR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSEGH---IVLTDFGLSKE 185
Cdd:cd14177   72 YVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 fLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTlEGERNTQAEVSRRI----LKCSPPF 261
Cdd:cd14177  152 -LRGENGLLLTPCYTANFVAPEVLM-RQGYDAACDIWSLGVLLYTMLAGYTPFA-NGPNDTPEEILLRIgsgkFSLSGGN 228
                        250       260
                 ....*....|....*....|....*.
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd14177  229 WDTVSDAAKDLLSHMLHVDPHQRYTA 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
400-655 1.28e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 101.88  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYEldlREPALGQGSFSVCRRCRQRQSGQEFAVK-I-LSRRLEANTQREVAALR---LCQ--SHPNVVNLHEV--HHDQL 470
Cdd:cd07841    1 RYE---KGKKLGEGTYAVVYKARDKETGRIVAIKkIkLGERKEAKDGINFTALReikLLQelKHPNIIGLLDVfgHKSNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HtyLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARL 550
Cdd:cd07841   78 N--LVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSN-WILHRDLKPNNLLIASD---GVLKLADFGLARS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RPqSPGVPMQTPCFTLQYAAPELL--AQQgYDESCDLWSLGVILYMMLSgQVPFqgASGQGGQSQAAEImckiregrFSL 628
Cdd:cd07841  152 FG-SPNRKMTHQVVTRWYRAPELLfgARH-YGVGVDMWSVGCIFAELLL-RVPF--LPGDSDIDQLGKI--------FEA 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 629 DG----EAWQGV------------------------SEEAKELVRGLLTVDPAKR 655
Cdd:cd07841  219 LGtpteENWPGVtslpdyvefkpfpptplkqifpaaSDDALDLLQRLLTLNPNKR 273
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
410-656 1.42e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 101.62  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS---VCRRCRQRQSGQEFAVKILSR-------RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05613    8 LGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKativqkaKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHLILDYI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYadDTPGAPVkIIDFGFARLRPQSPGVPM 559
Cdd:cd05613   88 NGGELFTHLSQRERFTENEVQIYIGEIVLALEHLH-KLGIIYRDIKLENILL--DSSGHVV-LTDFGLSKEFLLDENERA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELL--AQQGYDESCDLWSLGVILYMMLSGQVPFqgaSGQGGQSQAAEIMCKIREGrfslDGEAWQGVS 637
Cdd:cd05613  164 YSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPF---TVDGEKNSQAEISRRILKS----EPPYPQEMS 236
                        250
                 ....*....|....*....
gi 663856869 638 EEAKELVRGLLTVDPAKRL 656
Cdd:cd05613  237 ALAKDIIQRLLMKDPKKRL 255
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
410-656 1.51e-23

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 101.93  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL--------EANTQREVAALrlcQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05574    9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEmikrnkvkRVLTEREILAT---LDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRH--FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILY----------------ADDTPGAPVKII 543
Cdd:cd05574   86 GELFRLLQKQPGkrLPEEVARFYAAEVLLALEYLHLL-GFVYRDLKPENILLhesghimltdfdlskqSSVTPPPVRKSL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 544 DFGFARLRPQSPGVPM-------QTPCF--TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqa 614
Cdd:cd05574  165 RKGSRRSSVKSIEKETfvaepsaRSNSFvgTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD------ 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 615 aEIMCKIREGRFSLDGEAwqGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05574  239 -ETFSNILKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRL 277
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
34-284 1.66e-23

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 100.68  E-value: 1.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869    34 ELLKVLGTGAYGKVFLVR-KAGGHDAGKLYAMKVLRKaalvqraktqEHTRTERSvlELVRQA--------PFLVTLHYA 104
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKKKVEVAVKTLKE----------DASEQQIE--EFLREArimrkldhPNVVKLLGV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   105 FQTDAKLHLILDYVSGGEMFTHL-YQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:smart00219  70 CTEEEPLYIVMEYMEGGDLLSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   184 KEflTEEKERTFSFCG--TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPFtlEGERNTQAE---VSRRILKC 257
Cdd:smart00219 150 RD--LYDDDYYRKRGGklPIRWMAPESLKEGK-FTSKSDVWSFGVLLWEIFTlGEQPY--PGMSNEEVLeylKNGYRLPQ 224
                          250       260
                   ....*....|....*....|....*..
gi 663856869   258 SPPFPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:smart00219 225 PPNCPPEL----YDLMLQCWAEDPEDR 247
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
110-300 1.70e-23

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 100.51  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH--IV-LTDFGLSKEF 186
Cdd:cd14012   78 KVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgIVkLTDYSLGKTL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 L---TEEKERTFSFCGtieYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFpp 263
Cdd:cd14012  158 LdmcSRGSLDEFKQTY---WLPPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVL----EKYTSPNPVLVSLDLSASL-- 228
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 663856869 264 rigpvaQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14012  229 ------QDFLSKCLSLDPKKRP-----TALELLPHEF 254
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
30-302 1.74e-23

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 100.85  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLK--VLGTGAYGKVFLVRKAGGHDAGklYAMKVLRKAALvqrAKTQEHTRTERSVLELVrQAPFLVTLHYAFQT 107
Cdd:cd14201    3 VGDFEYSRkdLVGHGAFAVVFKGRHRKKTDWE--VAIKSINKKNL---SKSQILLGKEIKILKEL-QHENIVALYDVQEM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---------HIVLT 178
Cdd:cd14201   77 PNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEFLTEEKERTfsFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQA--EVSRRILk 256
Cdd:cd14201  157 DFGFARYLQSNMMAAT--LCGSPMYMAPEVIMSQHYDAKA-DLWSIGTVIYQCLVGKPPFQANSPQDLRMfyEKNKNLQ- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 257 csPPFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14201  233 --PSIPRETSPYLADLLLGLLQRNQKDRM-----DFEAFFSHPFLE 271
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
32-300 1.80e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 100.50  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKvlrkaaLVQRAKTQEHTRTERSVLELVRQapFLVTL-------HYA 104
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDA---DTGRELAVK------QVQFDPESPETSKEVNALECEIQ--LLKNLlherivqYYG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAK---LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd06652   72 CLRDPQertLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERT--FSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegernTQAEVSRRILKCS- 258
Cdd:cd06652  152 ASKRLQTICLSGTgmKSVTGTPYWMSPEVI-SGEGYGRKADIWSVGCTVVEMLTEKPPW-------AEFEAMAAIFKIAt 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 259 ----PPFPPRIGPVAQDLLQRLLCkDPKKRlgagpQGAQEVRNHPF 300
Cdd:cd06652  224 qptnPQLPAHVSDHCRDFLKRIFV-EAKLR-----PSADELLRHTF 263
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
31-300 1.82e-23

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 100.48  E-value: 1.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMK-VLRKAALVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQ--T 107
Cdd:cd06653    2 VNWRLGKLLGRGAFGEVYLCYDA---DTGRELAVKqVPFDPDSQETSKEVNALECEIQLLKNLRHDR-IVQYYGCLRdpE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd06653   78 EKKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTF--SFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtlegernTQAEVSRRILKCS-----PP 260
Cdd:cd06653  158 TICMSGTGikSVTGTPYWMSPEVI-SGEGYGRKADVWSVACTVVEMLTEKPPW-------AEYEAMAAIFKIAtqptkPQ 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKRLgagpqgAQEVRNHPF 300
Cdd:cd06653  230 LPDGVSDACRDFLRQIFVEEKRRPT------AEFLLRHPF 263
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
410-656 1.86e-23

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 101.80  E-value: 1.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQdddvdcTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05591   83 LMFQIQRARKFDEPRARFYAAEVTLALMFLHRH-GVIYRDLKLDNILL--DAEGH-CKLADFGMCK-EGILNGKTTTTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggqsqaAEIMCKIREGRFSLD--GEAWqgVSEEAK 641
Cdd:cd05591  158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE-----------ADNEDDLFESILHDDvlYPVW--LSKEAV 224
                        250
                 ....*....|....*
gi 663856869 642 ELVRGLLTVDPAKRL 656
Cdd:cd05591  225 SILKAFMTKNPAKRL 239
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
411-661 2.31e-23

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 101.92  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANTQREVAALR--LCQS-HPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd05599   10 GRGAFGEVRLVRKKDTGHVYAMKKLrkSEMLEKEQVAHVRAERdiLAEAdNPWVVKLYYSFQDEENLYLIMEFLPGGDMM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGF------ARLRPQSPGVPm 559
Cdd:cd05599   90 TLLMKKDTLTEEETRFYIAETVLAIESIHK-LGYIHRDIKPDNLLL--DARGH-IKLSDFGLctglkkSHLAYSTVGTP- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 qtpcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd05599  165 -------DYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQ-------ETCRKIMNWRETLVFPPEVPISPE 230
                        250       260
                 ....*....|....*....|..
gi 663856869 640 AKELVRGLLTvDPAKRLKLEGL 661
Cdd:cd05599  231 AKDLIERLLC-DAEHRLGANGV 251
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
39-238 3.01e-23

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 99.11  E-value: 3.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLvrkagghdaGKLYAMKVLRKaalvqraKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14059    1 LGSGAQGAVFL---------GKFRGEEVAVK-------KVRDEKETDIKHLRKL-NHPNIIKFKGVCTQAPCYCILMEYC 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFltEEKERTFSFC 198
Cdd:cd14059   64 PYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL--SEKSTKMSFA 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663856869 199 GTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGASPF 238
Cdd:cd14059  142 GTVAWMAPEVIRNEPCSEK-VDIWSFGVVLWELLTGEIPY 180
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
31-302 3.21e-23

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 100.59  E-value: 3.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDA- 109
Cdd:cd06620    5 QDLETLKDLGAGNGGSVSKVLHI---PTGTIMAKKVIH---IDAKSSVRKQILRELQILHEC-HSPYIVSFYGAFLNENn 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLH-KLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLT 188
Cdd:cd06620   78 NIIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFGVSGE-LI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTfsFCGTIEYMAPEIIRsktGHGKAV--DWWSLGILLFELLTGASPFTLEGERNTQA-------EVSRRILKCSP 259
Cdd:cd06620  157 NSIADT--FVGTSTYMSPERIQ---GGKYSVksDVWSLGLSIIELALGEFPFAGSNDDDDGYngpmgilDLLQRIVNEPP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 260 PFPP---RIGPVAQDLLQRLLCKDPKKRlgagPQGAQEVRNHPFFQ 302
Cdd:cd06620  232 PRLPkdrIFPKDLRDFVDRCLLKDPRER----PSPQLLLDHDPFIQ 273
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
407-656 3.22e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 100.42  E-value: 3.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPA--LGQGSFSVCRRCRQRQSGQEFAVKilSRRLEAN-------TQREVAALRLCQS--HPNVVNLHEV---------- 465
Cdd:cd07863    3 EPVaeIGVGAYGTVYKARDPHSGHFVALK--SVRVQTNedglplsTVREVALLKRLEAfdHPNIVRLMDVcatsrtdret 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 -------HHDQ-LHTYLvLELLRGGELLEHIRkkrhfseseasQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPG 537
Cdd:cd07863   81 kvtlvfeHVDQdLRTYL-DKVPPPGLPAETIK-----------DLMRQFLRGLDFLHANC-IVHRDLKPENILV---TSG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 538 APVKIIDFGFARLrpQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEI 617
Cdd:cd07863  145 GQVKLADFGLARI--YSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNS-------EADQ 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 618 MCKIregrFSLDG----EAW-------------QG----------VSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07863  216 LGKI----FDLIGlppeDDWprdvtlprgafspRGprpvqsvvpeIEESGAQLLLEMLTFNPHKRI 277
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
410-655 3.35e-23

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 100.09  E-value: 3.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIlsRRLEANTQREVA------ALRLCQ-----SHPNVVNLH---EVHHDQLHTylV 475
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKI--HQLNKDWSEEKKqnyikhALREYEihkslDHPRIVKLYdvfEIDTDSFCT--V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQS 554
Cdd:cd13990   84 LEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEiKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDDE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGvPMQTPCFTLQ------YAAPE--LLAQQGYDESC--DLWSLGVILYMMLSGQVPFqgasGQgGQSQAAE----IMCK 620
Cdd:cd13990  164 SY-NSDGMELTSQgagtywYLPPEcfVVGKTPPKISSkvDVWSVGVIFYQMLYGRKPF----GH-NQSQEAIleenTILK 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 621 IREGRFSldgeAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd13990  238 ATEVEFP----SKPVVSSEAKDFIRRCLTYRKEDR 268
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
32-301 4.52e-23

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 99.89  E-value: 4.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQA--PFLVTLHYAFQTDA 109
Cdd:cd07860    1 NFQKVEKIGEGTYGVVY---KARNKLTGEVVALKKIR-----LDTETEGVPSTAIREISLLKELnhPNIVKLLDVIHTEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGG-EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd07860   73 KLYLVFEFLHQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSR--------------RI 254
Cdd:cd07860  153 PVRTYTHEVV-TLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRtlgtpdevvwpgvtSM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 255 LKCSPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07860  232 PDYKPSFPkwarqdfskvvPPLDEDGRDLLSQMLHYDPNKRI-----SAKAALAHPFF 284
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
410-655 5.54e-23

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 99.33  E-value: 5.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS----RRLEAnTQREVAALRLCQSHPNVVNL--HEVHHDQLHTYLVLELLRGGE 483
Cdd:cd13985    8 LGEGGFSYVYLAHDVNTGRRYALKRMYfndeEQLRV-AIKEIEIMKRLCGHPNIVQYydSAILSSEGRKEVLLLMEYCPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKR---HFSESEASQILRSLVSAVSFMHEEA-GVVHRDLKPENILYADDTpgaPVKIIDFGFA--RLRPQSPG- 556
Cdd:cd13985   87 SLVDILEKSppsPLSEEEVLRIFYQICQAVGHLHSQSpPIIHRDIKIENILFSNTG---RFKLCDFGSAttEHYPLERAe 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 --------VPMQTpcfTLQYAAPELLAQQGYDESC---DLWSLGVILYMMLSGQVPFQGASgqggqsqaaeIMcKIREGR 625
Cdd:cd13985  164 evniieeeIQKNT---TPMYRAPEMIDLYSKKPIGekaDIWALGCLLYKLCFFKLPFDESS----------KL-AIVAGK 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 626 FSldGEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd13985  230 YS--IPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
410-665 5.95e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 99.52  E-value: 5.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQ-----SHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIilekvSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRK--KRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQspGVPMQTP 562
Cdd:cd05577   81 KYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNR-FIVYRDLKPENILLDDH---GHVRISDLGLAVEFKG--GKKIKGR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQ-GYDESCDLWSLGVILYMMLSGQVPFQgASGQGGQSQAAEIMCKIREGRFSLDgeawqgVSEEAK 641
Cdd:cd05577  155 VGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFR-QRKEKVDKEELKRRTLEMAVEYPDS------FSPEAR 227
                        250       260
                 ....*....|....*....|....
gi 663856869 642 ELVRGLLTVDPAKRLkleGLRGSS 665
Cdd:cd05577  228 SLCEGLLQKDPERRL---GCRGGS 248
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
410-606 6.05e-23

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 99.75  E-value: 6.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilsRRLEANTQ--------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIK---KFVESEDDpvikkialREIRMLKQLK-HPNLVNLIEVFRRKRKLHLVFEYCDH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLrpQSPGVPMQT 561
Cdd:cd07847   85 TVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKH-NCIHRDVKPENILI---TKQGQIKLCDFGFARI--LTGPGDDYT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 562 PCF-TLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07847  159 DYVaTRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKS 205
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
37-284 7.27e-23

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 98.77  E-value: 7.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALvqrAKTQEHTRTERSVLELVRQaPFLVTLhYAFQTDA-KLHLIL 115
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDAS---ESERKDFLKEARVMKKLGH-PNVVRL-LGVCTEEePLYLVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHL---------YQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEf 186
Cdd:cd00192   76 EYMEGGDLLDFLrksrpvfpsPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 lTEEKERTFSFCGT---IEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPFtleGERNTQaEVSRRILKCS-PPF 261
Cdd:cd00192  155 -IYDDDYYRKKTGGklpIRWMAPESLKDGI-FTSKSDVWSFGVLLWEIFTlGATPY---PGLSNE-EVLEYLRKGYrLPK 228
                        250       260
                 ....*....|....*....|...
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd00192  229 PENCPDELYELMLSCWQLDPEDR 251
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
52-302 7.69e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 99.80  E-value: 7.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  52 KAGGHDAGKLY-AMKVLR-KAALVQRAKTQEHTRTERSVLELV----RQAPFLVTLHYAFQTDAKLHLILDYVSGGEMfT 125
Cdd:cd06654   27 KIGQGASGTVYtAMDVATgQEVAIRQMNLQQQPKKELIINEILvmreNKNPNIVNYLDSYLVGDELWVVMEYLAGGSL-T 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 126 HLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfSFCGTIEYMA 205
Cdd:cd06654  106 DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMVGTPYWMA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 206 PEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEgerNTQAEVSRRILKCSPPF--PPRIGPVAQDLLQRLLCKDPKK 283
Cdd:cd06654  185 PEVV-TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE---NPLRALYLIATNGTPELqnPEKLSAIFRDFLNRCLEMDVEK 260
                        250
                 ....*....|....*....
gi 663856869 284 RlgagpQGAQEVRNHPFFQ 302
Cdd:cd06654  261 R-----GSAKELLQHQFLK 274
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
73-302 8.38e-23

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 99.41  E-value: 8.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  73 VQRAKTQEHTRTERSVLELV----RQAPFLVTLHYAFQTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLA 148
Cdd:cd06656   49 IKQMNLQQQPKKELIINEILvmreNKNPNIVNYLDSYLVGDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 149 LEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILL 228
Cdd:cd06656  128 LDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMA 205
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 229 FELLTGASPFTLEgerNTQAEVSRRILKCSPPF--PPRIGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06656  206 IEMVEGEPPYLNE---NPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQHPFLK 273
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
31-319 8.63e-23

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 100.13  E-value: 8.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKA-ALVQRAKtqehtRTERSvLELVR--QAPFLVTLHYAFQT 107
Cdd:cd07855    5 DRYEPIETIGSGAYG---VVCSAIDTKSGQKVAIKKIPNAfDVVTTAK-----RTLRE-LKILRhfKHDNIIAIRDILRP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILD-YVSGGEMFTHLYQ----RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd07855   76 KVPYADFKDvYVVLDLMESDLHHiihsDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTF---SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFE------LLTGASP-------FTLEGE--- 243
Cdd:cd07855  156 ARGLCTSPEEHKYfmtEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEmlgrrqLFPGKNYvhqlqliLTVLGTpsq 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 244 ---RNTQAEVSRRILKCSPPFPPR--------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGLDWVALAAR 312
Cdd:cd07855  236 aviNAIGADRVRRYIQNLPNKQPVpwetlypkADQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAKYHDPDDEPD 310

                 ....*..
gi 663856869 313 KIPaPFR 319
Cdd:cd07855  311 CAP-PFD 316
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
410-660 9.98e-23

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 100.08  E-value: 9.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAALR--LCQS-HPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05598    9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKdvLKRNQVAHVKAERdiLAEAdNEWVVKLYYSFQDKENLYFVMDYIPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFA---RLRPQSPGVPMQT 561
Cdd:cd05598   89 MSLLIKKGIFEEDLARFYIAELVCAIESVHK-MGFIHRDIKPDNILIDRD---GHIKLTDFGLCtgfRWTHDSKYYLAHS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEAK 641
Cdd:cd05598  165 LVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQT-------PAETQLKVINWRTTLKIPHEANLSPEAK 237
                        250
                 ....*....|....*....
gi 663856869 642 ELVRGLLTvDPAKRLKLEG 660
Cdd:cd05598  238 DLILRLCC-DAEDRLGRNG 255
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
144-301 1.07e-22

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 98.50  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLD---SEGHI--VLTDFGLSK--EFLTEEKERTFSFCGTIEYMAPEIIRS--KTG 214
Cdd:cd13982  107 QIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVraMISDFGLCKklDVGRSSFSRRSGVAGTSGWIAPEMLSGstKRR 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 215 HGKAVDWWSLGILLFELLTGAS-PF--TLEGERNtqaevsrrILK--CSPPFPPRIG---PVAQDLLQRLLCKDPKKRlg 286
Cdd:cd13982  187 QTRAVDIFSLGCVFYYVLSGGShPFgdKLEREAN--------ILKgkYSLDKLLSLGehgPEAQDLIERMIDFDPEKR-- 256
                        170
                 ....*....|....*
gi 663856869 287 agPQgAQEVRNHPFF 301
Cdd:cd13982  257 --PS-AEEVLNHPFF 268
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
410-655 1.28e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 98.05  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK--ILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd06614    8 IGEGASGEVYKATDRATGKEVAIKkmRLRKQNKELIINEILIMKECK-HPNIVDYYDSYLVGDELWVVMEYMDGGSLTDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRH-FSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLrpqSPGVPMQ----- 560
Cdd:cd06614   87 ITQNPVrMNESQIAYVCREVLQGLEYLHS-QNVIHRDIKSDNILLSKD---GSVKLADFGFaAQL---TKEKSKRnsvvg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTlqyaAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaAEIMCKIR-EGRFSL-DGEAWqgvSE 638
Cdd:cd06614  160 TPYWM----APEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPP-------LRALFLITtKGIPPLkNPEKW---SP 225
                        250
                 ....*....|....*..
gi 663856869 639 EAKELVRGLLTVDPAKR 655
Cdd:cd06614  226 EFKDFLNKCLVKDPEKR 242
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-284 1.75e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 97.79  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQrAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd08228    3 NFQIEKKIGRGQFSEVY---RATCLLDRKPVALKKVQIFEMMD-AKARQDCVKEIDLLKQLNH-PNVIKYLDSFIEDNEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGG---EMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFL 187
Cdd:cd08228   78 NIVLELADAGdlsQMIKYFKkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR-FF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSRRILKCS-PPFP-PRI 265
Cdd:cd08228  157 SSKTTAAHSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFY--GDKMNLFSLCQKIEQCDyPPLPtEHY 233
                        250
                 ....*....|....*....
gi 663856869 266 GPVAQDLLQRLLCKDPKKR 284
Cdd:cd08228  234 SEKLRELVSMCIYPDPDQR 252
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
410-696 1.98e-22

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 99.22  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS---VCRRCRQRQSGQEFAVKILSR-------RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05614    8 LGTGAYGkvfLVRKVSGHDANKLYAMKVLRKaalvqkaKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLHLILDYV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYadDTPGAPVkIIDFGFARLRPQSPGVPM 559
Cdd:cd05614   88 SGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLH-KLGIVYRDIKLENILL--DSEGHVV-LTDFGLSKEFLTEEKERT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLdgeawqgVSE 638
Cdd:cd05614  164 YSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSF-------IGP 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 639 EAKELVRGLLTVDPAKRLKlEGLRGSS------------WLQDGSARSSPPLRtpdvlessgPAVRSGLN 696
Cdd:cd05614  237 VARDLLQKLLCKDPKKRLG-AGPQGAQeikehpffkgldWEALALRKVNPPFR---------PSIRSELD 296
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
410-656 2.00e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 99.17  E-value: 2.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK----ILSRRLEAN-TQREVAALRLCQSHPNVVNLHEVHH--DQLHTYLVLellrgg 482
Cdd:cd07852   15 LGKGAYGIVWKAIDKKTGEVVALKkifdAFRNATDAQrTFREIMFLQELNDHPNIIKLLNVIRaeNDKDIYLVF------ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ellehirkkrHFSESEASQILRS--------------LVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFA 548
Cdd:cd07852   89 ----------EYMETDLHAVIRAniledihkqyimyqLLKALKYLHS-GGVIHRDLKPSNILLNSD---CRVKLADFGLA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 RL---RPQSPGVPMQTP-CFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG---------------- 607
Cdd:cd07852  155 RSlsqLEEDDENPVLTDyVATRWYRAPEiLLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTlnqlekiievigrpsa 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 608 ---QGGQSQAAEIM---CKIREgRFSLDgEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07852  235 ediESIQSPFAATMlesLPPSR-PKSLD-ELFPKASPDALDLLKKLLVFNPNKRL 287
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
34-300 2.20e-22

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 98.00  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  34 ELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlvqraktqEHTRTERSVLELV----RQAPFLVTLHYAFQTDA 109
Cdd:cd06622    4 EVLDELGKGNYGSVYKVLHR---PTGVTMAMKEIRLEL--------DESKFNQIIMELDilhkAVSPYIVDFYGAFFIEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMfTHLY----QRQYFKEAEVRVYGGEIVLALEHL-HKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd06622   73 AVYMCMEYMDAGSL-DKLYaggvATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EFlteEKERTFSFCGTIEYMAPEIIRSKTGHGKAV-----DWWSLGILLFELLTGASPFTLEGERNTQAEVSrRILKCSP 259
Cdd:cd06622  152 NL---VASLAKTNIGCQSYMAPERIKSGGPNQNPTytvqsDVWSLGLSILEMALGRYPYPPETYANIFAQLS-AIVDGDP 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 260 P-FPPRIGPVAQDLLQRLLCKDPKKRlgagPQGAQeVRNHPF 300
Cdd:cd06622  228 PtLPSGYSDDAQDFVAKCLNKIPNRR----PTYAQ-LLEHPW 264
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
410-659 2.21e-22

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 97.39  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL--EANTQREVA-ALRLCqSHPNVVNLHEVHHdQLHTYLVLELLRGGELLE 486
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStkLKDFLREYNiSLELS-VHPHIIKTYDVAF-ETEDYYVFAQEYAPYGDL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 H--IRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpGAPVKIIDFGFARLRpqspGVPMQTPCF 564
Cdd:cd13987   79 FsiIPPQVGLPEERVKRCAAQLASALDFMHSK-NLVHRDIKPENVLLFDKD-CRRVKLCDFGLTRRV----GSTVKRVSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELL---AQQGY--DESCDLWSLGVILYMMLSGQVPFQGASgqgGQSQAAEIMCKIREGRFSLDGEAWQGVSEE 639
Cdd:cd13987  153 TIPYTAPEVCeakKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWEKAD---SDDQFYEEFVRWQKRKNTAVPSQWRRFTPK 229
                        250       260
                 ....*....|....*....|
gi 663856869 640 AKELVRGLLTVDPAKRLKLE 659
Cdd:cd13987  230 ALRMFKKLLAPEPERRCSIK 249
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
29-284 2.25e-22

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 97.41  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd14147    1 SFQELRLEEVIGIGGFGKVYR-----GSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAH-PNIIALKAVCLEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRvYGGEIVLALEHLHK---LGIIYRDLKLENVLL------DSEGHIVL-- 177
Cdd:cd14147   75 PNLCLVMEYAAGGPLSRALAGRRVPPHVLVN-WAVQIARGMHYLHCealVPVIHRDLKSNNILLlqpienDDMEHKTLki 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFGLSKEFlteEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKC 257
Cdd:cd14147  154 TDFGLAREW---HKTTQMSAAGTYAWMAPEVIKAST-FSKGSDVWSFGVLLWELLTGEVPY--RGIDCLAVAYGVAVNKL 227
                        250       260
                 ....*....|....*....|....*...
gi 663856869 258 SPPFPPRI-GPVAQdLLQRLLCKDPKKR 284
Cdd:cd14147  228 TLPIPSTCpEPFAQ-LMADCWAQDPHRR 254
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
31-301 2.28e-22

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 97.98  E-value: 2.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAalVQRAKTQEHTRTERSVLELVRQAPFLVTL----HYAFQ 106
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVY---KARDKNTGKLVALKKTRLE--MEEEGVPSTALREVSLLQMLSQSIYIVRLldveHVEEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGG-EMFTHLYQRQYFKEAE---VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHIVLTDFG 181
Cdd:cd07837   76 GKPLLYLVFEYLDTDlKKFIDSYGRGPHNPLPaktIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEFLTEEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFE------LLTGASP-------FTLEGERNTQA 248
Cdd:cd07837  156 LGRAFTIPIKSYTHEIV-TLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEmsrkqpLFPGDSElqqllhiFRLLGTPNEEV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 249 EVSRRILKCSPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07837  235 WPGVSKLRDWHEYPqwkpqdlsravPDLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
409-656 2.43e-22

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 99.29  E-value: 2.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSF-SVCRrCRQRQSGQEFAVKILSRRLEAN-----TQREVAALRLCQsHPNVVNLHEVHHDQLHT------YLVL 476
Cdd:cd07851   22 PVGSGAYgQVCS-AFDTKTGRKVAIKKLSRPFQSAihakrTYRELRLLKHMK-HENVIGLLDVFTPASSLedfqdvYLVT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELleHIRKKRHFSESE----ASQILRSLvsavSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRP 552
Cdd:cd07851  100 HLMGADLN--NIVKCQKLSDDHiqflVYQILRGL----KYIHS-AGIIHRDLKPSNLAVNED---CELKILDFGLARHTD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSpgvpMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS------------G-------QGGQS 612
Cdd:cd07851  170 DE----MTGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDhidqlkrimnlvGtpdeellKKISS 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 613 QAA----EIMCKIREGRFSldgEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07851  246 ESArnyiQSLPQMPKKDFK---EVFSGANPLAIDLLEKMLVLDPDKRI 290
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
33-284 2.84e-22

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 96.80  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   33 FELLKVLGTGAYGKVFL-VRKAGGHDAGKLYAMKVLRKAAlvqraktqehtrTERSVLELVRQA--------PFLVTLHY 103
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKgTLKGEGENTKIKVAVKTLKEGA------------DEEEREDFLEEAsimkkldhPNIVKLLG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  104 AFQTDAKLHLILDYVSGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:pfam07714  69 VCTQGEPLYIVTEYMPGGDLLDFLRKHKRkLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  183 SKEFLTEEKERTFSFCGT-IEYMAPEIIRsktgHGK---AVDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRI--- 254
Cdd:pfam07714 149 SRDIYDDDYYRKRGGGKLpIKWMAPESLK----DGKftsKSDVWSFGVLLWEIFTlGEQPY----PGMSNEEVLEFLedg 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 663856869  255 --LKCSPPFPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:pfam07714 221 yrLPQPENCPDEL----YDLMKQCWAYDPEDR 248
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
20-302 3.09e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 97.83  E-value: 3.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  20 NLTGHEEKVSVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAalvQRAKTQEHTRTERSVLELVRQAPFLV 99
Cdd:cd06618    4 TIDGKKYKADLNDLENLGEIGSGTCGQVY---KMRHKKTGHVMAVKQMRRS---GNKEENKRILMDLDVVLKSHDCPYIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQTDAKLHLILDYVSggEMFTHLYQR--QYFKEaevRVYGGEIVLALEHLHKL----GIIYRDLKLENVLLDSEG 173
Cdd:cd06618   78 KCYGYFITDSDVFICMELMS--TCLDKLLKRiqGPIPE---DILGKMTVSIVKALHYLkekhGVIHRDVKPSNILLDESG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKeFLTEEKERTFSfCGTIEYMAPEIIRSKTGHGKAV--DWWSLGILLFELLTGASPFTlegERNTQAEVS 251
Cdd:cd06618  153 NVKLCDFGISG-RLVDSKAKTRS-AGCAAYMAPERIDPPDNPKYDIraDVWSLGISLVELATGQFPYR---NCKTEFEVL 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 252 RRILKCSPP-FPPRIG--PVAQDLLQRLLCKDPKKRlgagPQgAQEVRNHPFFQ 302
Cdd:cd06618  228 TKILNEEPPsLPPNEGfsPDFCSFVDLCLTKDHRYR----PK-YRELLQHPFIR 276
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
410-656 3.24e-22

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 98.41  E-value: 3.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL------EANT--QREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVivakkeVAHTigERNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARLRpQSPGVPMQT 561
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKN-DIVYRDLKPENILL--DANGH-IALCDFGLSKAD-LTDNKTTNT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsQAAEIMC--KIREGRFSLdgeawqgvSE 638
Cdd:cd05586  156 FCGTTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQ----QMYRNIAfgKVRFPKDVL--------SD 223
                        250
                 ....*....|....*...
gi 663856869 639 EAKELVRGLLTVDPAKRL 656
Cdd:cd05586  224 EGRSFVKGLLNRNPKHRL 241
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
410-661 3.96e-22

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 96.30  E-value: 3.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-----EANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrgpkeRARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRK---KRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPMQT 561
Cdd:cd13997   88 QDALEElspISKLSEAEVWDLLLQVALGLAFIHSK-GIVHLDIKPDNIFI---SNKGTCKIGDFGLATRLETSGDVEEGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PcftlQYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQGasGQGGQsqaaeimcKIREGRFSLDGEAwqGVSEEA 640
Cdd:cd13997  164 S----RYLAPELLNEnYTHLPKADIFSLGVTVYEAATGEPLPRN--GQQWQ--------QLRQGKLPLPPGL--VLSQEL 227
                        250       260
                 ....*....|....*....|.
gi 663856869 641 KELVRGLLTVDPAKRLKLEGL 661
Cdd:cd13997  228 TRLLKVMLDPDPTRRPTADQL 248
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
33-302 4.63e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 98.01  E-value: 4.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMK----VLRKAALVQRaktqehtrTERSV--LELVRQAPFLVTLH--YA 104
Cdd:cd07852    9 YEILKKLGKGAYGIVW---KAIDKKTGEVVALKkifdAFRNATDAQR--------TFREImfLQELNDHPNIIKLLnvIR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYvsggeMFTHLY-----------QRQYFkeaevrVYggEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd07852   78 AENDKDIYLVFEY-----METDLHaviranilediHKQYI------MY--QLLKALKYLHSGGVIHRDLKPSNILLNSDC 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKEFLTEEKERTFS----FCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFT-------LE- 241
Cdd:cd07852  145 RVKLADFGLARSLSQLEEDDENPvltdYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPgtstlnqLEk 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 242 -----GERNTQ---------AEVSRRILKCSPPFP-----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd07852  225 iieviGRPSAEdiesiqspfAATMLESLPPSRPKSldelfPKASPDALDLLKKLLVFNPNKRL-----TAEEALRHPYVA 299
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
401-655 6.67e-22

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 96.28  E-value: 6.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDLREPA-LGQGSFSVCRRCRQRQSGQEFAVKILSRR----LEANTQREVAAL-RLcqSHPNVVNLHEVHHDQLHTYL 474
Cdd:cd14046    4 YLTDFEELQvLGKGAFGQVVKVRNKLDGRYYAIKKIKLRseskNNSRILREVMLLsRL--NHQHVVRYYQAWIERANLYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILY--ADDtpgapVKIIDFGFARLRP 552
Cdd:cd14046   82 QMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQ-GIIHRDLKPVNIFLdsNGN-----VKIGDFGLATSNK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSPGVPMQTPCF-----------------TLQYAAPELLAQQG--YDESCDLWSLGVILYMMLsgqVPFQGAsgqggqSQ 613
Cdd:cd14046  156 LNVELATQDINKstsaalgssgdltgnvgTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC---YPFSTG------ME 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 614 AAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd14046  227 RVQILTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKR 268
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
45-287 7.59e-22

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 95.41  E-value: 7.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  45 GKVFLVRKAGGHDAGKLYAMKVLRKaalvqRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYVSGGEMF 124
Cdd:cd14115    4 GRFSIVKKCLHKATRKDVAVKFVSK-----KMKKKEQAAHEAALLQHL-QHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 125 THLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD---SEGHIVLTDFG----LSKEFlteekeRTFSF 197
Cdd:cd14115   78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEdavqISGHR------HVHHL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLL 277
Cdd:cd14115  152 LGNPEFAAPEVIQG-TPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVIL 230
                        250
                 ....*....|
gi 663856869 278 CKDPKKRLGA 287
Cdd:cd14115  231 QEDPRRRPTA 240
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
45-284 9.42e-22

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 95.37  E-value: 9.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  45 GKVFLVRKAGGHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYVSGGEMF 124
Cdd:cd14110   14 GRFSVVRQCEEKRSGQMLAAKIIP-----YKPEDKQLVLREYQVLRRLSH-PRIAQLHSAYLSPRHLVLIEELCSGPELL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 125 THLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEEKERTFSFCGTI-EY 203
Cdd:cd14110   88 YNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPFNQGKVLMTDKKGDYvET 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 204 MAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPvAQDLLQRLLCKDPKK 283
Cdd:cd14110  167 MAPELLEGQ-GAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCYAGLSGG-AVNFLKSTLCAKPWG 244

                 .
gi 663856869 284 R 284
Cdd:cd14110  245 R 245
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
410-656 9.76e-22

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 97.78  E-value: 9.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05617   23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDdedidwVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05617  103 LMFHMQRQRKLPEEHARFYAAEICIALNFLHER-GIIYRDLKLDNVLLDAD---GHIKLTDYGMCK-EGLGPGDTTSTFC 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd05617  178 GTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIP----RFLSVKASHV 253
                        250
                 ....*....|...
gi 663856869 644 VRGLLTVDPAKRL 656
Cdd:cd05617  254 LKGFLNKDPKERL 266
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
38-238 9.88e-22

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 95.54  E-value: 9.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14061    1 VIGVGGFGKVYR-----GIWRGEEVAVKAARQDPDEDISVTLENVRQEARLFWMLRH-PNIIALRGVCLQPPNLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYfkEAEVRV-YGGEIVLALEHLHKLG---IIYRDLKLENVLL------DSEGHIVL--TDFGLSKE 185
Cdd:cd14061   75 ARGGALNRVLAGRKI--PPHVLVdWAIQIARGMNYLHNEApvpIIHRDLKSSNILIleaienEDLENKTLkiTDFGLARE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 186 FlteEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14061  153 W---HKTTRMSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGEVPY 201
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
37-318 1.06e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 96.26  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVF--LVRKAGGHdagklYAMKVLRKAALVQRaKTQEHTRTErsvlelvrQAPFLVTL----HYAFQTDAK 110
Cdd:cd14170    8 QVLGLGINGKVLqiFNKRTQEK-----FALKMLQDCPKARR-EVELHWRAS--------QCPHIVRIvdvyENLYAGRKC 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE---GHIVLTDFGLSKE 185
Cdd:cd14170   74 LLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTfsFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFP--- 262
Cdd:cd14170  154 TTSHNSLTT--PCYTPYYVAPEVLGPEK-YDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPnpe 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 263 -PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPffqgldWVALAARKIPAPF 318
Cdd:cd14170  231 wSEVSEEVKMLIRNLLKTEPTQRM-----TITEFMNHP------WIMQSTKVPQTPL 276
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
31-314 1.10e-21

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 95.95  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAA--LVQRAKTQEhtrtersvLELVR--QAPFLVTLHYAF- 105
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNT---KTIFALKTITTDPnpDVQKQILRE--------LEINKscASPYIVKYYGAFl 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 -QTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEV--RVYG--GEIVL-ALEHLHKLGIIYRDLKLENVLLDSEGHIVLTD 179
Cdd:cd06621   70 dEQDSSIGIAMEYCEGGSL-DSIYKKVKKKGGRIgeKVLGkiAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 180 FGLSKEFLTEEKErtfSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQA-EVSRRILKCS 258
Cdd:cd06621  149 FGVSGELVNSLAG---TFTGTSYYMAPERIQGGPYSITS-DVWSLGLTLLEVAQNRFPFPPEGEPPLGPiELLSYIVNMP 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 259 PPF---PPRIGPV----AQDLLQRLLCKDPKKRlgAGPqgaQEVRNHPFfqgldWVALAARKI 314
Cdd:cd06621  225 NPElkdEPENGIKwsesFKDFIEKCLEKDGTRR--PGP---WQMLAHPW-----IKAQEKKKV 277
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
31-238 1.43e-21

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 95.83  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQraktqEHTRTERSVLELVRQAPFLVTLHYAF-QTD- 108
Cdd:cd06639   22 DTWDIIETIGKGTYGKVY---KVTNKKDGSLAAVKILDPISDVD-----EEIEAEYNILRSLPNHPNVVKFYGMFyKADq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 ---AKLHLILDYVSGG---EMFTHLYQR-QYFKEAEVR--VYGGeiVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTD 179
Cdd:cd06639   94 yvgGQLWLVLELCNGGsvtELVKGLLKCgQRLDEAMISyiLYGA--LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 180 FGLSKEfLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKA----VDWWSLGILLFELLTGASPF 238
Cdd:cd06639  172 FGVSAQ-LTSARLRRNTSVGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDPPL 233
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
411-618 1.61e-21

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 95.65  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVK--ILSRRLEantQREVAALRLCQsHPNVVNL--HEVHHDQ----------------- 469
Cdd:cd14137   13 GSGSFGVVYQAKLLETGEVVAIKkvLQDKRYK---NRELQIMRRLK-HPNIVKLkyFFYSSGEkkdevylnlvmeympet 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 470 LHTYLVLellrggelleHIRKKRHFSESEAS----QILRSLvsavSFMHEeAGVVHRDLKPENILYADDTpgAPVKIIDF 545
Cdd:cd14137   89 LYRVIRH----------YSKNKQTIPIIYVKlysyQLFRGL----AYLHS-LGICHRDIKPQNLLVDPET--GVLKLCDF 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 546 GFA-RLRPQSPGVPMQtpCfTLQYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQGASGQGgqsQAAEIM 618
Cdd:cd14137  152 GSAkRLVPGEPNVSYI--C-SRYYRAPELIFGaTDYTTAIDIWSAGCVLAELLLGQPLFPGESSVD---QLVEII 220
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
33-300 1.61e-21

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 94.97  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGhdagKLYAMKVLR--------KAALVQRAKTQEHTRTERSVLELVRqapflvtlHYA 104
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVLNPKK----KIYALKRVDlegadeqtLQSYKNEIELLKKLKGSDRIIQLYD--------YEV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYvsgGEM-FTHLYQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLdSEGHIVLTDF 180
Cdd:cd14131   71 TDEDDYLYMVMEC---GEIdLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEFLTEE----KErtfSFCGTIEYMAPEIIR--SKTGHGKAV-------DWWSLGILLFELLTGASPFtlegerntq 247
Cdd:cd14131  147 GIAKAIQNDTtsivRD---SQVGTLNYMSPEAIKdtSASGEGKPKskigrpsDVWSLGCILYQMVYGKTPF--------- 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 248 AEVSRRILK----CSP----PFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd14131  215 QHITNPIAKlqaiIDPnheiEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPELLNHPF 270
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
32-300 1.62e-21

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 96.32  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLR---KAALVQRA----KTQEHTRTERSV-----LELVRQAPFLV 99
Cdd:cd07857    1 RYELIKELGQGAYGIVCSARNAETSEEETVAIKKITNvfsKKILAKRAlrelKLLRHFRGHKNItclydMDIVFPGNFNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQTDAKLHLILDyvSGgemfthlyqrQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTD 179
Cdd:cd07857   81 LYLYEELMEADLHQIIR--SG----------QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 180 FGLSK----------EFLTEekertfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLtGASPFtLEGE------ 243
Cdd:cd07857  149 FGLARgfsenpgenaGFMTE-------YVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELL-GRKPV-FKGKdyvdql 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 244 -----------RNTQAEV-SRRILKC--SPPFPPRI---------GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd07857  220 nqilqvlgtpdEETLSRIgSPKAQNYirSLPNIPKKpfesifpnaNPLALDLLEKLLAFDPTKRI-----SVEEALEHPY 294
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
39-302 1.65e-21

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 95.31  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHdagKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQAPFLVtLHYAFQTDAKLHLILDYV 118
Cdd:cd14104    8 LGRGQFGIVHRCVETSSK---KTYMAKFVK-----VKGADQVLVKKEISILNIARHRNILR-LHESFESHEELVMIFEFI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE--GHIVLTDFGLSKEFLTEEKERtF 195
Cdd:cd14104   79 SGVDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQLKPGDKFR-L 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 SFCgTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlEGERNTQAEVSRRILKCS---PPFpPRIGPVAQDL 272
Cdd:cd14104  158 QYT-SAEFYAPEVHQHES-VSTATDMWSLGCLVYVLLSGINPF--EAETNQQTIENIRNAEYAfddEAF-KNISIEALDF 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 273 LQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14104  233 VDRLLVKERKSRM-----TAQEALNHPWLK 257
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
410-660 1.72e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 95.48  E-value: 1.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQ-----SHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05630    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQilekvNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRK--KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQspGVPMQTP 562
Cdd:cd05630   88 KFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRER-IVYRDLKPENILLDDH---GHIRISDLGLAVHVPE--GQTIKGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREgrfsldgEAWQGVSEEAKE 642
Cdd:cd05630  162 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPE-------EYSEKFSPQARS 234
                        250
                 ....*....|....*...
gi 663856869 643 LVRGLLTVDPAKRLKLEG 660
Cdd:cd05630  235 LCSMLLCKDPAERLGCRG 252
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
31-239 1.94e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 95.14  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd06641    4 ELFTKLEKIGKGSFGEVF---KGIDNRTQKVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKDTK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFThLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEE 190
Cdd:cd06641   77 LWIIMEYLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ-LTDT 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFT 239
Cdd:cd06641  155 QIKRN*FVGTPFWMAPEVIKQSAYDSKA-DIWSLGITAIELARGEPPHS 202
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
410-656 2.07e-21

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 96.64  E-value: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05618   28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDdedidwVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPGVPMQTPC 563
Cdd:cd05618  108 LMFHMQRQRKLPEEHARFYSAEISLALNYLHER-GIIYRDLKLDNVLL--DSEGH-IKLTDYGMCK-EGLRPGDTTSTFC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ--GASGQGGQSQAAEIMCKIREGRFSLDgeawQGVSEEAK 641
Cdd:cd05618  183 GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivGSSDNPDQNTEDYLFQVILEKQIRIP----RSLSVKAA 258
                        250
                 ....*....|....*
gi 663856869 642 ELVRGLLTVDPAKRL 656
Cdd:cd05618  259 SVLKSFLNKDPKERL 273
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
98-302 2.59e-21

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 95.11  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  98 LVTLHYAFQTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVL 177
Cdd:cd06658   81 VVDMYNSYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEgernTQAEVSRRILKC 257
Cdd:cd06658  160 SDFGFCAQVSKEVPKRK-SLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNE----PPLQAMRRIRDN 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 258 SPPFPP---RIGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd06658  234 LPPRVKdshKVSSVLRGFLDLMLVREPSQR-----ATAQELLQHPFLK 276
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
410-683 2.73e-21

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 95.40  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE------ANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05620    3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVlidddvECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGvPMQTPC 563
Cdd:cd05620   83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSK-GIIYRDLKLDNVMLDRD---GHIKIADFGMCKENVFGDN-RASTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIRegrfsLDGEAW-QGVSEEAKE 642
Cdd:cd05620  158 GTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHG-------DDEDELFESIR-----VDTPHYpRWITKESKD 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 643 LVRGLLTVDPAKRLKLEG-LRGSS------WLQDGSARSSPPLRtPDV 683
Cdd:cd05620  226 ILEKLFERDPTRRLGVVGnIRGHPffktinWTALEKRELDPPFK-PKV 272
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
96-284 2.77e-21

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 94.69  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 PFLVTLHYAFQTDA-KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHL--HKLGIIYRDLKLENVLLDSE 172
Cdd:cd13990   64 PRIVKLYDVFEIDTdSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 ---GHIVLTDFGLSKEFLTEEK-----ERTFSFCGTIEYMAPEI---------IRSKtghgkaVDWWSLGILLFELLTGA 235
Cdd:cd13990  144 nvsGEIKITDFGLSKIMDDESYnsdgmELTSQGAGTYWYLPPECfvvgktppkISSK------VDVWSVGVIFYQMLYGR 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 236 SPFtleGERNTQAEVSRR--ILKC---SPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd13990  218 KPF---GHNQSQEAILEEntILKAtevEFPSKPVVSSEAKDFIRRCLTYRKEDR 268
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
410-683 3.04e-21

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 95.91  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRrLEANTQREVAAL---RLCQSHPN---VVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05596   34 IGRGAFGEVQLVRHKSTKKVYAMKLLSK-FEMIKRSDSAFFweeRDIMAHANsewIVQLHYAFQDDKYLYMVMDYMPGGD 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLeHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGVPMQTPC 563
Cdd:cd05596  113 LV-NLMSNYDVPEKWARFYTAEVVLALDAIHS-MGFVHRDVKPDNMLL--DASGH-LKLADFGTCMKMDKDGLVRSDTAV 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQG----YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQaaeIMCKIREGRFSLDGEawqgVSEE 639
Cdd:cd05596  188 GTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGK---IMNHKNSLQFPDDVE----ISKD 260
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 640 AKELVRGLLTvDPAKRLKLEGL---------RGSSWLQDgSARSSPPLRTPDV 683
Cdd:cd05596  261 AKSLICAFLT-DREVRLGRNGIeeikahpffKNDQWTWD-NIRETVPPVVPEL 311
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
431-606 3.41e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.33  E-value: 3.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 431 AVKILSRRLEANT------QREV-AALRLcqSHPNVVNLHEVHHDQLHTYLVlellrggellehIRKKRHFSESEASQIL 503
Cdd:NF033483  36 AVKVLRPDLARDPefvarfRREAqSAASL--SHPNIVSVYDVGEDGGIPYIVmeyvdgrtlkdyIREHGPLSPEEAVEIM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 504 RSLVSAVSFMHeEAGVVHRDLKPENILYADDtpGApVKIIDFGFARLRPQSP--------GvpmqtpcfTLQYAAPElLA 575
Cdd:NF033483 114 IQILSALEHAH-RNGIVHRDIKPQNILITKD--GR-VKVTDFGIARALSSTTmtqtnsvlG--------TVHYLSPE-QA 180
                        170       180       190
                 ....*....|....*....|....*....|..
gi 663856869 576 QQGY-DESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:NF033483 181 RGGTvDARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
31-287 3.44e-21

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 93.89  E-value: 3.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKV----LGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKAaLVQRaktqEHTRTERSVLELVrQAPFLVTLHYAFQ 106
Cdd:cd14113    3 DNFDSFYSevaeLGRGRFS---VVKKCDQRGTKRAVATKFVNKK-LMKR----DQVTHELGVLQSL-QHPQLVGLLDTFE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD---SEGHIVLTDFGLS 183
Cdd:cd14113   74 TPTSYILVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTeeKERTFSFCGTIEYMAPEIIRsktghGKAV----DWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSP 259
Cdd:cd14113  154 VQLNT--TYYIHQLLGSPEFAAPEIIL-----GNPVsltsDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPD 226
                        250       260
                 ....*....|....*....|....*...
gi 663856869 260 PFPPRIGPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd14113  227 DYFKGVSQKAKDFVCFLLQMDPAKRPSA 254
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
49-288 3.58e-21

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 94.39  E-value: 3.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  49 LVRKAGghdAGKLYAMKVLrkaALVQRAKTQEHTR-------TERSVLELVRQAPFLVTLHYAFQTDA------------ 109
Cdd:cd13974   16 LARKEG---TDDFYTLKIL---TLEEKGEETQEDRqgkmllhTEYSLLSLLHDQDGVVHHHGLFQDRAceikedkssnvy 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 ------KLHLILDYVSGGEM---------FTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd13974   90 tgrvrkRLCLVLDCLCAHDFsdktadlinLQHYVIREKrLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 H-IVLTDFGLSKEFLTEEK----ERtfsfcGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQA 248
Cdd:cd13974  170 RkITITNFCLGKHLVSEDDllkdQR-----GSPAYISPDVLSGKPYLGKPSDMWALGVVLFTMLYGQFPFY----DSIPQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 249 EVSRRILKC--SPPFPPRIGPVAQDLLQRLLCKDPKKRLGAG 288
Cdd:cd13974  241 ELFRKIKAAeyTIPEDGRVSENTVCLIRKLLVLNPQKRLTAS 282
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
39-247 4.07e-21

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 93.67  E-value: 4.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKtqEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd13978    1 LGSGGFGTVSKARHV---SWFGMVAIKCLHSSPNCIEER--KALLKEAEKMERARH-SYVLPLLGVCVERRSLGLVMEYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMfTHLYQRQY--------FKEAEvrvyggEIVLALEHLHKL--GIIYRDLKLENVLLDSEGHIVLTDFGLSK---- 184
Cdd:cd13978   75 ENGSL-KSLLEREIqdvpwslrFRIIH------EIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmk 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 185 EFLTEEKERTFSFCGTIEYMAPEIIRskTGHGK---AVDWWSLGILLFELLTGASPFtlEGERNTQ 247
Cdd:cd13978  148 SISANRRRGTENLGGTPIYMAPEAFD--DFNKKptsKSDVYSFAIVIWAVLTRKEPF--ENAINPL 209
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
410-602 4.16e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 94.44  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA---NTQR---EVAAL-RLcqSHPNVVNLHEVhhdQLHTYLVLELLRGG 482
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPsdkNRERwclEVQIMkKL--NHPNVVSARDV---PPELEKLSPNDLPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKK--RH----------FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGAPVKIIDFGFARL 550
Cdd:cd13989   76 LAMEYCSGGdlRKvlnqpenccgLKESEVRTLLSDISSAISYLHENR-IIHRDLKPENIVLQQGGGRVIYKLIDLGYAKE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 551 RPQspgvpmQTPCF----TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd13989  155 LDQ------GSLCTsfvgTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
31-301 4.76e-21

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 93.06  E-value: 4.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVR----KAGGHDAGKLYAMKVLRKAALVQRaktqehTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEdklhDLYDRNKGRLVALKHIYPTSSPSR------ILNELECLERLGGSNNVSGLITAFR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYvsggemFTHLYQRQYFKE---AEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHIVLTDFGL 182
Cdd:cd14019   75 NEDQVVAVLPY------IEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SkEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGA-SPFTLEGERNTQAEVSRRILKcsppf 261
Cdd:cd14019  149 A-QREEDRPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATIFGS----- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 262 pprigPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14019  223 -----DEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
33-301 5.70e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 93.91  E-value: 5.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAAlvQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAKLH 112
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKE---IVAIKKFKDSE--ENEEVKETTLRELKMLRTLKQEN-IVELKEAFRRRGKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGgEMFTHLYQRQYFKEAE-VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEK 191
Cdd:cd07848   77 LVFEYVEK-NMLELLEEMPNGVPPEkVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARN-LSEGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTFS-FCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNtQAEVSRRILKCSPP---------- 260
Cdd:cd07848  155 NANYTeYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGELSDGQPLFPGESEID-QLFTIQKVLGPLPAeqmklfysnp 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 261 ------FPPRIGP-------------VAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07848  233 rfhglrFPAVNHPqslerrylgilsgVLLDLMKNLLKLNPTDRY-----LTEQCLNHPAF 287
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
410-672 6.16e-21

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 93.69  E-value: 6.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE----ANTQREVA---ALRLCQShPNVVNLHevhhdqlHTYLVLELLRGG 482
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDdddvSDIQKEVAllsQLKLGQP-KNIIKYY-------GSYLKGPSLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEH---IR---KKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYAddTPGApVKIIDFGFARLRPQSPG 556
Cdd:cd06917   81 MDYCEggsIRtlmRAGPIAERYIAVIMREVLVALKFIHK-DGIIHRDIKAANILVT--NTGN-VKLCDFGVAASLNQNSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 vPMQTPCFTLQYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMCKIREGRfsLDGEAWqg 635
Cdd:cd06917  157 -KRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVD----ALRAVMLIPKSKPPR--LEGNGY-- 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 636 vSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSA 672
Cdd:cd06917  228 -SPLLKEFVAACLDEEPKDRLSADELLKSKWIKQHSK 263
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
33-300 8.68e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 92.87  E-value: 8.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDAGKLyamKVLRKAAL--VQRAKTQEHTRTERSVLELvrQAPFLVTLHYAFQTDAK 110
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEEL---KVLKEISVgeLQPDETVDANREAKLLSKL--DHPAIVKFHDSFVEKES 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMfthlyqrqYFKEAEVRVYGGEI------------VLALEHLHKLGIIYRDLKLENVLLdSEGHIVLT 178
Cdd:cd08222   77 FCIVTEYCEGGDL--------DDKISEYKKSGTTIdenqildwfiqlLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEFLTEEKERTfSFCGTIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNtqaeVSRRILKC- 257
Cdd:cd08222  148 DFGISRILMGTSDLAT-TFTGTPYYMSPEVLKHE-GYNSKSDIWSLGCILYEMCCLKHAFDGQNLLS----VMYKIVEGe 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 258 SPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPF 300
Cdd:cd08222  222 TPSLPDKYSKELNAIYSRMLNKDPALRPSAA-----EILKIPF 259
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
34-250 1.01e-20

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 92.58  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  34 ELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHtrterSVLELVRQAPfLVTLHYAFQTDAKLHL 113
Cdd:cd14111    3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEY-----EILKSLHHER-IMALHEAYITPRYLVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKER 193
Cdd:cd14111   77 IAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQ 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 194 TFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEV 250
Cdd:cd14111  157 LGRRTGTLEYMAPEMVKGEP-VGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKI 212
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
98-301 1.27e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 93.16  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  98 LVTLHYAFQTDAKLHLILDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVL 177
Cdd:cd06657   79 VVEMYNSYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFGLSKEfLTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRIlkc 257
Cdd:cd06657  158 SDFGFCAQ-VSKEVPRRKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL--- 232
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 258 sppfPPR------IGPVAQDLLQRLLCKDPKKRlgagpQGAQEVRNHPFF 301
Cdd:cd06657  233 ----PPKlknlhkVSPSLKGFLDRLLVRDPAQR-----ATAAELLKHPFL 273
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
33-284 1.77e-20

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 92.10  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAggHDAGKLYAMKVLRKAALvqRAKTQEHTRTERSVL-ELVRQA-PFLVTLHYAFQTDAK 110
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSER--VPTGKVYAVKKLKPNYA--GAKDRLRRLEEVSILrELTLDGhDNIVQLIDSWEYHGH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEM--FTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF- 186
Cdd:cd14052   78 LYIQTELCENGSLdvFLSELgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTfsfcGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFEL--------------------LTGASpfTLEGERNT 246
Cdd:cd14052  158 LIRGIERE----GDREYIAPEILSEHM-YDKPADIFSLGLILLEAaanvvlpdngdawqklrsgdLSDAP--RLSSTDLH 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 247 QAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14052  231 SASSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRR 268
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
31-302 1.85e-20

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 92.10  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRkaALVQrakTQEHTR-------TERSVlelvrQAPFLVTLHY 103
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHV---PTGTIMAVKRIR--ATVN---SQEQKRllmdldiSMRSV-----DCPYTVTFYG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AF--QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRvygGEI----VLALEHLH-KLGIIYRDLKLENVLLDSEGHIV 176
Cdd:cd06617   68 ALfrEGDVWICMEVMDTSLDKFYKKVYDKGLTIPEDIL---GKIavsiVKALEYLHsKLSVIHRDVKPSNVLINRNGQVK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 177 LTDFGLSKeFLTEEKERTFSfCGTIEYMAPEII---RSKTGHGKAVDWWSLGILLFELLTGASPFTLEGernTQAEVSRR 253
Cdd:cd06617  145 LCDFGISG-YLVDSVAKTID-AGCKPYMAPERInpeLNQKGYDVKSDVWSLGITMIELATGRFPYDSWK---TPFQQLKQ 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 254 ILKCSPPFPP--RIGPVAQDLLQRLLCKDPKKRlgagPQGAqEVRNHPFFQ 302
Cdd:cd06617  220 VVEEPSPQLPaeKFSPEFQDFVNKCLKKNYKER----PNYP-ELLQHPFFE 265
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
31-284 1.96e-20

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 92.38  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLV-RKAGGHDAgklyAMKVLRKAALVQraktqEHTRTERSVLELVRQAPFLVTLHYAF---- 105
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVlNKKNGSKA----AVKILDPIHDID-----EEIEAEYNILKALSDHPNVVKFYGMYykkd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 -QTDAKLHLILDYVSGGEMFT----HLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDF 180
Cdd:cd06638   89 vKNGDQLWLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEfLTEEKERTFSFCGTIEYMAPEIIRSK----TGHGKAVDWWSLGILLFELLTGASPFtlegernTQAEVSRRILK 256
Cdd:cd06638  169 GVSAQ-LTSTRLRRNTSVGTPFWMAPEVIACEqqldSTYDARCDVWSLGITAIELGDGDPPL-------ADLHPMRALFK 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 257 CSPPFPPRI------GPVAQDLLQRLLCKDPKKR 284
Cdd:cd06638  241 IPRNPPPTLhqpelwSNEFNDFIRKCLTKDYEKR 274
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
410-664 2.06e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 92.36  E-value: 2.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCQSHpNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05631    8 LGKGGFGEVCACQVRATGKMYACKklekkrIKKRKGEAMALNEKRILEKVNSR-FVVSLAYAYETKDALCLVLTIMNGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRH--FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQspGVPMQT 561
Cdd:cd05631   87 LKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRER-IVYRDLKPENILLDDR---GHIRISDLGLAVQIPE--GETVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREgrfslDGEAW-QGVSEEA 640
Cdd:cd05631  161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFR---KRKERVKREEVDRRVKE-----DQEEYsEKFSEDA 232
                        250       260
                 ....*....|....*....|....
gi 663856869 641 KELVRGLLTVDPAKRLkleGLRGS 664
Cdd:cd05631  233 KSICRMLLTKNPKERL---GCRGN 253
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
31-300 2.08e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 92.04  E-value: 2.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd06640    4 ELFTKLERIGKGSFGEVF---KGIDNRTQQVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKGTK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFThLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEE 190
Cdd:cd06640   77 LWIIMEYLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQ-LTDT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPftlegerNTQAEvSRRILKCSPPFPPR--IGPV 268
Cdd:cd06640  155 QIKRNTFVGTPFWMAPEVIQQSAYDSKA-DIWSLGITAIELAKGEPP-------NSDMH-PMRVLFLIPKNNPPtlVGDF 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 269 A---QDLLQRLLCKDPKKRlgagpQGAQEVRNHPF 300
Cdd:cd06640  226 SkpfKEFIDACLNKDPSFR-----PTAKELLKHKF 255
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
33-238 2.25e-20

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 91.99  E-value: 2.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQAPFLVTLHYAF------Q 106
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHV---KTGQLAAIKVMDVTE-----DEEEEIKLEINMLKKYSHHRNIATYYGAFikksppG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMfTHLYQR---QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd06636   90 HDDQLWLVMEFCGAGSV-TDLVKNtkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 184 KEfLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDW----WSLGILLFELLTGASPF 238
Cdd:cd06636  169 AQ-LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYrsdiWSLGITAIEMAEGAPPL 226
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
424-656 2.28e-20

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 92.73  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 424 RQSGQEFAVKILSRRLEANTQ------REVAALRLCqSHPNVVNLHEVH----------------HDQLH--TYlvlell 479
Cdd:cd07842   24 GKDGKEYAIKKFKGDKEQYTGisqsacREIALLREL-KHENVVSLVEVFlehadksvyllfdyaeHDLWQiiKF------ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 rggelleHIRKKRH-FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTP-GAPVKIIDFGFARLRpQSPGV 557
Cdd:cd07842   97 -------HRQAKRVsIPPSMVKSLLWQILNGIHYLHSNW-VLHRDLKPANILVMGEGPeRGVVKIGDLGLARLF-NAPLK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQT---PCFTLQYAAPEL-LAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG--------QGGQSQA----------- 614
Cdd:cd07842  168 PLADldpVVVTIWYRAPELlLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfQRDQLERifevlgtptek 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 615 -----------AEIMCKIREGRFSLDGEA-----WQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07842  248 dwpdikkmpeyDTLKSDTKASTYPNSLLAkwmhkHKKPDSQGFDLLRKLLEYDPTKRI 305
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
122-302 2.61e-20

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 91.06  E-value: 2.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHIVLTDFGlSKEFLTEEKERTFSfcGT 200
Cdd:cd14101   94 DLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKLIDFG-SGATLKDSMYTDFD--GT 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 201 IEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegERNTQaevsrrILKCSPPFPPRIGPVAQDLLQRLLCKD 280
Cdd:cd14101  171 RVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPF----ERDTD------ILKAKPSFNKRVSNDCRSLIRSCLAYN 240
                        170       180
                 ....*....|....*....|..
gi 663856869 281 PKKRlgagpQGAQEVRNHPFFQ 302
Cdd:cd14101  241 PSDR-----PSLEQILLHPWMM 257
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
33-301 2.67e-20

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 91.95  E-value: 2.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAF--QTDAK 110
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSR---KTGKYYAIKCMKKHF---KSLEQVNNLREIQALRRLSPHPNILRLIEVLfdRKTGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYvsggeMFTHLY-----QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEgHIVLTDFG---- 181
Cdd:cd07831   75 LALVFEL-----MDMNLYelikgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGscrg 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 -LSKEFLTEekertfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEV-------SRR 253
Cdd:cd07831  149 iYSKPPYTE-------YISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhdvlgtpDAE 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 254 ILK-------CSPPFPPRIG-----------PVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07831  222 VLKkfrksrhMNYNFPSKKGtglrkllpnasAEGLDLLKKLLAYDPDERI-----TAKQALRHPYF 282
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
33-284 2.89e-20

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 91.59  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkagGHDAGKLYAMKvlrkAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAK-- 110
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVE---DLSTGRLYALK----KILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGgk 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 --LHLILDYVSGGEMFTHLYQR----QYFKEAEVRVYGGEIVLALEHLHKL---GIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd13986   75 keVYLLLPYYKRGSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 L----------SKEFLTEEKERTFSfcGTIEYMAPE--------IIRSKTghgkavDWWSLGILLFELLTGASPFTLEGE 243
Cdd:cd13986  155 SmnparieiegRREALALQDWAAEH--CTMPYRAPElfdvkshcTIDEKT------DIWSLGCTLYALMYGESPFERIFQ 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 244 RNT---QAEVSRRIlkcSPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd13986  227 KGDslaLAVLSGNY---SFPDNSRYSEELHQLVKSMLVVNPAER 267
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
37-302 3.16e-20

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 91.30  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAgghDAGKLYAMKvlrkaaLVQRAKTQEHTRTERSVLE----LVRQAPFLVTLHYAF----QTD 108
Cdd:cd06651   13 KLLGQGAFGRVYLCYDV---DTGRELAAK------QVQFDPESPETSKEVSALEceiqLLKNLQHERIVQYYGclrdRAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd06651   84 KTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERT--FSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVSRRILK-CSPPFPPRI 265
Cdd:cd06651  164 ICMSGTgiRSVTGTPYWMSPEVI-SGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHI 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 266 GPVAQDLLQRLLCKDPKKrlgagpQGAQEVRNHPFFQ 302
Cdd:cd06651  240 SEHARDFLGCIFVEARHR------PSAEELLRHPFAQ 270
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
400-655 3.27e-20

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 91.27  E-value: 3.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdlREPaLGQGSFSVCRRCRQRQSGQEFAVKILSrrLEA------NTQREVAALRLCqSHPNVVNLHE--VHHDQLh 471
Cdd:cd06610    2 DYEL--IEV-IGSGATAVVYAAYCLPKKEKVAIKRID--LEKcqtsmdELRKEIQAMSQC-NHPNVVSYYTsfVVGDEL- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 tYLVLELLRGGELL---EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpGApVKIIDFGFA 548
Cdd:cd06610   75 -WLVMPLLSGGSLLdimKSSYPRGGLDEAIIATVLKEVLKGLEYLHSN-GQIHRDVKAGNILLGED--GS-VKIADFGVS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 -----------RLRPQSPGvpmqTPCftlqYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAE 616
Cdd:cd06610  150 aslatggdrtrKVRKTFVG----TPC----WMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYS-------KYPPMK 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 663856869 617 IMCKIREGRF-SLDGEAWQGV-SEEAKELVRGLLTVDPAKR 655
Cdd:cd06610  215 VLMLTLQNDPpSLETGADYKKySKSFRKMISLCLQKDPSKR 255
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
410-656 3.34e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 92.34  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQ-----SHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05632   10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQilekvNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRH--FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQspGVPMQTP 562
Cdd:cd05632   90 KFHIYNMGNpgFEEERALFYAAEILCGLEDLHRE-NTVYRDLKPENILLDDY---GHIRISDLGLAVKIPE--GESIRGR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAaeimckirEGRFSLDGEAWQG-VSEEAK 641
Cdd:cd05632  164 VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEV--------DRRVLETEEVYSAkFSEEAK 235
                        250
                 ....*....|....*
gi 663856869 642 ELVRGLLTVDPAKRL 656
Cdd:cd05632  236 SICKMLLTKDPKQRL 250
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
39-284 3.73e-20

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 90.67  E-value: 3.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTD-AKLHLILDY 117
Cdd:cd14064    1 IGSGSFGKVY-----KGRCRNKIVAIKRYRANTYCSKSDVDMFCR-EVSILCRLNH-PCVIQFVGACLDDpSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERT 194
Cdd:cd14064   74 VSGGSLFSLLHeQKRVIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcsPPFPPRIGPVAQDLLQ 274
Cdd:cd14064  154 TKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIR--PPIGYSIPKPISSLLM 231
                        250
                 ....*....|
gi 663856869 275 RLLCKDPKKR 284
Cdd:cd14064  232 RGWNAEPESR 241
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
410-655 4.18e-20

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 91.15  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSrrLEANT------QREVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd06609    9 IGKGSFGEVYKGIDKRTNQVVAIKVID--LEEAEdeiediQQEIQFLSQCDS-PYITKYYGSFLKGSKLWIIMEYCGGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLeHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFG------FARLRpqspgv 557
Cdd:cd06609   86 VL-DLLKPGPLDETYIAFILREVLLGLEYLHSE-GKIHRDIKAANILLSEE---GDVKLADFGvsgqltSTMSK------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 pMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKI-REGRFSLDGEAWqgv 636
Cdd:cd06609  155 -RNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLH-------PMRVLFLIpKNNPPSLEGNKF--- 223
                        250
                 ....*....|....*....
gi 663856869 637 SEEAKELVRGLLTVDPAKR 655
Cdd:cd06609  224 SKPFKDFVELCLNKDPKER 242
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
31-302 5.21e-20

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 91.98  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLV--RKAGGHDAGK--------LYAMKVLRKAALVQRAKtqeHtrtER--SVLELVRqAPFL 98
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAvhKPTGQKVAIKkispfehqTYCLRTLREIKILLRFK---H---ENiiGILDIQR-PPTF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  99 VTLHyafqtdaKLHLILDYvsggeMFTHLY-----QR------QYFkeaevrVYggEIVLALEHLHKLGIIYRDLKLENV 167
Cdd:cd07849   78 ESFK-------DVYIVQEL-----METDLYkliktQHlsndhiQYF------LY--QILRGLKYIHSANVLHRDLKPSNL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 168 LLDSEGHIVLTDFGLSK---------EFLTEekertfsFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd07849  138 LLNTNCDLKICDFGLARiadpehdhtGFLTE-------YVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLF 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 239 ----------------------TLEGERNTQAEVSRRILKCSPPFP-----PRIGPVAQDLLQRLLCKDPKKRLgagpqG 291
Cdd:cd07849  211 pgkdylhqlnlilgilgtpsqeDLNCIISLKARNYIKSLPFKPKVPwnklfPNADPKALDLLDKMLTFNPHKRI-----T 285
                        330
                 ....*....|.
gi 663856869 292 AQEVRNHPFFQ 302
Cdd:cd07849  286 VEEALAHPYLE 296
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
33-301 5.43e-20

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 91.45  E-value: 5.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQApflvtlhyafQTDAKLH 112
Cdd:cd14210   15 YEVLSVLGKGSFGQVV---KCLDHKTGQLVAIKIIR-----NKKRFHQQALVEVKILKHLNDN----------DPDDKHN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LI--LDYVsggeMF------------THLY---QRQYFKE---AEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE 172
Cdd:cd14210   77 IVryKDSF----IFrghlcivfellsINLYellKSNNFQGlslSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GH--IVLTDFGlSKEFlteEKERTFSFcgtIE---YMAPEIIrskTGH--GKAVDWWSLGILLFELLTGASPFTLEGER- 244
Cdd:cd14210  153 SKssIKVIDFG-SSCF---EGEKVYTY---IQsrfYRAPEVI---LGLpyDTAIDMWSLGCILAELYTGYPLFPGENEEe 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 245 --NTQAEV----SRRILKCSP-------------PFPPRIG------------------PVAQDLLQRLLCKDPKKRLga 287
Cdd:cd14210  223 qlACIMEVlgvpPKSLIDKASrrkkffdsngkprPTTNSKGkkrrpgskslaqvlkcddPSFLDFLKKCLRWDPSERM-- 300
                        330
                 ....*....|....
gi 663856869 288 gpqGAQEVRNHPFF 301
Cdd:cd14210  301 ---TPEEALQHPWI 311
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
410-656 5.77e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 91.71  E-value: 5.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN------TQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDdedidwVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFAR--LRPqspGVPMQT 561
Cdd:cd05588   83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEK-GIIYRDLKLDNVLL--DSEGH-IKLTDYGMCKegLRP---GDTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAE------IMCK-IREGRfsldgeawq 634
Cdd:cd05588  156 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNPDQNTEdylfqvILEKpIRIPR--------- 226
                        250       260
                 ....*....|....*....|..
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05588  227 SLSVKAASVLKGFLNKNPAERL 248
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
33-300 6.75e-20

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 90.50  E-value: 6.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLH 112
Cdd:cd06642    6 FTKLERIGKGSFGEVY---KGIDNRTKEVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYITRYYGSYLKGTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFThLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEfLTEEKE 192
Cdd:cd06642   79 IIMEYLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQ-LTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFT-LEGERntqaeVSRRILKCSPP-FPPRIGPVAQ 270
Cdd:cd06642  157 KRNTFVGTPFWMAPEVIKQSAYDFKA-DIWSLGITAIELAKGEPPNSdLHPMR-----VLFLIPKNSPPtLEGQHSKPFK 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 271 DLLQRLLCKDPKKRlgagpQGAQEVRNHPF 300
Cdd:cd06642  231 EFVEACLNKDPRFR-----PTAKELLKHKF 255
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
32-301 7.14e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 90.62  E-value: 7.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd07836    1 NFKQLEKLGEGTYATVY---KGRNRTTGEIVALKEIH---LDAEEGTPSTAIREISLMKELKH-ENIVRLHDVIHTENKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGG---EMFTHLYQRQyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd07836   74 MLVFEYMDKDlkkYMDTHGVRGA-LDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKerTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTleGERN-----------------TQAEV 250
Cdd:cd07836  153 PVN--TFSNeVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFP--GTNNedqllkifrimgtptesTWPGI 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 251 SR--RILKCSPPFP--------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07836  229 SQlpEYKPTFPRYPpqdlqqlfPHADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
407-667 7.48e-20

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 89.55  E-value: 7.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFsvcrRCRQRQSGQEFAVKILSRRleaNTQREVAALRLCQSHPNVVNLHEV-------------HHDQLHTy 473
Cdd:cd14024    2 EPWEGQELY----RAEHYQTEKEYTCKVLSLR---SYQECLAPYDRLGPHEGVCSVLEVvigqdrayaffsrHYGDMHS- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 lvlellrggelleHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVkiidfgfarLRPQ 553
Cdd:cd14024   74 -------------HVRRRRRLSEDEARGLFTQMARAVAHCHQH-GVILRDLKLRRFVFTDELRTKLV---------LVNL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTPCFTL-------QYAAPELL-AQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREG 624
Cdd:cd14024  131 EDSCPLNGDDDSLtdkhgcpAYVGPEILsSRRSYSgKAADVWSLGVCLYTMLLGRYPFQ-------DTEPAALFAKIRRG 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 625 RFSLDgeawQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14024  204 AFSLP----AWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
29-284 7.54e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 90.86  E-value: 7.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQrAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTD 108
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVY---RATCLLDGVPVALKKVQIFDLMD-AKARADCIKEIDLLKQLNH-PNVIKYYASFIED 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGE---MFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd08229   97 NELNIVLELADAGDlsrMIKHFKkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 eFLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSRRILKCS-PPFPP 263
Cdd:cd08229  177 -FFSSKTTAAHSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFY--GDKMNLYSLCKKIEQCDyPPLPS 252
                        250       260
                 ....*....|....*....|..
gi 663856869 264 -RIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd08229  253 dHYSEELRQLVNMCINPDPEKR 274
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
410-656 7.59e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 90.89  E-value: 7.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK--ILSRRLEA---NTQREVAALRLCQsHPNVVNLHEVHH--------DQLHTYLVL 476
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIVALKkvLMENEKEGfpiTALREIKILQLLK-HENVVNLIEICRtkatpynrYKGSIYLVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFArlRPQSPG 556
Cdd:cd07865   99 EFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNK-ILHRDMKAANILITKD---GVLKLADFGLA--RAFSLA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCF-----TLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQgGQSQAAEIMCKiregrfSLDG 630
Cdd:cd07865  173 KNSQPNRYtnrvvTLWYRPPElLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQ-HQLTLISQLCG------SITP 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 631 EAWQGV----------------------------SEEAKELVRGLLTVDPAKRL 656
Cdd:cd07865  246 EVWPGVdklelfkkmelpqgqkrkvkerlkpyvkDPYALDLIDKLLVLDPAKRI 299
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
33-301 8.01e-20

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 90.43  E-value: 8.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRT-ERSVLELVRQaPFLVTLHYAFQTDAKL 111
Cdd:cd07835    1 YQKLEKIGEGTYGVVY---KARDKLTGEIVALKKIR---LETEDEGVPSTAIrEISLLKELNH-PNIVRLLDVVHSENKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVS---GGEMFTHlyQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd07835   74 YLVFEFLDldlKKYMDSS--PLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERN----------TQAEVS----RRI 254
Cdd:cd07835  152 PVRTYTHEVV-TLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDqlfrifrtlgTPDEDVwpgvTSL 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 255 LKCSPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07835  231 PDYKPTFPkwarqdlskvvPSLDEDGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
410-683 8.15e-20

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 91.25  E-value: 8.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05597    9 IGRGAFGEVAVVKLKSTEKVYAMKILNKwemlkRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRK-KRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGfARLRPQSPG-----VP 558
Cdd:cd05597   89 LTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQ-LGYVHRDIKPDNVLL--DRNGH-IRLADFG-SCLKLREDGtvqssVA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPcftlQYAAPELL-AQQG----YDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKI--REGRFSLDGE 631
Cdd:cd05597  164 VGTP----DYISPEILqAMEDgkgrYGPECDWWSLGVCMYEMLYGETPFYAES-------LVETYGKImnHKEHFSFPDD 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 632 AwQGVSEEAKELVRGLLTvDPAKRLKLEGL---RGSSW---LQDGSARSSPPLRTPDV 683
Cdd:cd05597  233 E-DDVSEEAKDLIRRLIC-SRERRLGQNGIddfKKHPFfegIDWDNIRDSTPPYIPEV 288
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
410-602 1.12e-19

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 89.21  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRrleanTQREVAALRLCQS---------HPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTGEFVAIKQISL-----EKIPKSDLKSVMGeidllkklnHPNIVKYIGSVKTKDSLYIILEYVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEA----SQILRSLVsavsFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFArLRPQSPG 556
Cdd:cd06627   83 NGSLASIIKKFGKFPESLVavyiYQVLEGLA----YLHEQ-GVIHRDIKGANILTTKD---GLVKLADFGVA-TKLNEVE 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06627  154 KDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY 199
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
27-300 1.27e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 90.25  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvqraktQEHTRtERSVLELVRQAPFLVTLHYA-- 104
Cdd:cd07864    3 KRCVDKFDIIGIIGEGTYGQVY---KAKDKDTGELVALKKVR----------LDNEK-EGFPITAIREIKILRQLNHRsv 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 ---------------FQTDAK-LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL 168
Cdd:cd07864   69 vnlkeivtdkqdaldFKKDKGaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 169 LDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERnTQA 248
Cdd:cd07864  149 LNNKGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQEL-AQL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 249 EVSRRIlkCSPPFP----------------PR-------------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHP 299
Cdd:cd07864  228 ELISRL--CGSPCPavwpdviklpyfntmkPKkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRC-----TAEQALNSP 300

                 .
gi 663856869 300 F 300
Cdd:cd07864  301 W 301
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31-300 1.64e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 89.33  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAK 110
Cdd:cd06645   11 EDFELIQRIGSGTYGDVY---KARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDC-----KHSNIVAYFGSYLRRDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEE 190
Cdd:cd06645   83 LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTfSFCGTIEYMAPEI--IRSKTGHGKAVDWWSLGILLFELLTGASP-FTLEGERntqaevSRRILKCSPPFPPRIGP 267
Cdd:cd06645  163 AKRK-SFIGTPYWMAPEVaaVERKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMR------ALFLMTKSNFQPPKLKD 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 268 VAQ------DLLQRLLCKDPKKRlgagpQGAQEVRNHPF 300
Cdd:cd06645  236 KMKwsnsfhHFVKMALTKNPKKR-----PTAEKLLQHPF 269
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
410-655 1.71e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 89.02  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL--EANTQREVAALRLCQ-----SHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd08222    8 LGSGNFGTVYLVSDLKATADEELKVLKEISvgELQPDETVDANREAKllsklDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSES-EASQILR---SLVSAVSFMHEEaGVVHRDLKPENILYADDTpgapVKIIDFGFARLRPQSPGVP 558
Cdd:cd08222   88 DLDDKISEYKKSGTTiDENQILDwfiQLLLAVQYMHER-RILHRDLKAKNIFLKNNV----IKVGDFGISRILMGTSDLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 mQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGgqsqaaeIMCKIREGRFSLDGEAWqgvSE 638
Cdd:cd08222  163 -TTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLS-------VMYKIVEGETPSLPDKY---SK 231
                        250
                 ....*....|....*..
gi 663856869 639 EAKELVRGLLTVDPAKR 655
Cdd:cd08222  232 ELNAIYSRMLNKDPALR 248
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
410-606 1.76e-19

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 89.40  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVA--ALRLCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd07846    9 VGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAmrEIKMLKQlrHENLVNLIEVFRRKKRWYLVFEFVDHTVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRpQSPGVPMQTPCFT 565
Cdd:cd07846   89 DLEKYPNGLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILV---SQSGVVKLCDFGFARTL-AAPGEVYTDYVAT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 566 LQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07846  164 RWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDS 205
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
507-656 1.87e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 89.39  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 507 VSAVSFMHEeAGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPM--------------QTPCFTLQYAAPE 572
Cdd:cd05609  110 VLALEYLHS-YGIVHRDLKPDNLLI---TSMGHIKLTDFGLSKIGLMSLTTNLyeghiekdtrefldKQVCGTPEYIAPE 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 573 LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQG--GQSQAAEIMCkiregrfsLDGEAWqgVSEEAKELVRGLLTV 650
Cdd:cd05609  186 VILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEElfGQVISDEIEW--------PEGDDA--LPDDAQDLITRLLQQ 255

                 ....*.
gi 663856869 651 DPAKRL 656
Cdd:cd05609  256 NPLERL 261
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
26-238 2.19e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 88.95  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  26 EKVSVENFELLKVLGTGAYGKVFlvRKAGGhdaGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAF 105
Cdd:cd14145    1 LEIDFSELVLEEIIGIGGFGKVY--RAIWI---GDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKH-PNIIALRGVC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRvYGGEIVLALEHLHKLGI---IYRDLKLENVLL-------DSEGHI 175
Cdd:cd14145   75 LKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIvpvIHRDLKSSNILIlekvengDLSNKI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 176 V-LTDFGLSKEFlteEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14145  154 LkITDFGLAREW---HRTTKMSAAGTYAWMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGEVPF 213
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
33-238 2.20e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 88.38  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVrkagghdAGKLYAMKVLRKAALVQRAK---TQEHTRTERSVLELVRQaPFLVTLHYAFQ-TD 108
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLA-------TSQKYCCKVAIKIVDRRRASpdfVQKFLPRELSILRRVNH-PNIVQMFECIEvAN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDyVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG-HIVLTDFGLSKeFL 187
Cdd:cd14164   74 GRLYIVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFAR-FV 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 188 TEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14164  152 EDYPELSTTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPF 202
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
410-668 2.20e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 88.56  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ------REVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd06605    9 LGEGNGGVVSKVRHRPSGQIMAVKVI--RLEIDEAlqkqilRELDVLHKCNS-PYIVGFYGAFYSEGDISICMEYMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGvpmQTPC 563
Cdd:cd06605   86 LDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILV--NSRGQ-VKLCDFGVSGQLVDSLA---KTFV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWqgvSEEAKEL 643
Cdd:cd06605  160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFELLSYIVDEPPPLLPSGKF---SPDFQDF 236
                        250       260
                 ....*....|....*....|....*
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd06605  237 VSQCLQKDPTERPSYKELMEHPFIK 261
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
406-655 2.25e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 88.64  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSrrLEANTQRE-VAALRLCQ-----SHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd08220    4 KIRVVGRGAYGTVYLCRRKDDNKLVIIKQIP--VEQMTKEErQAALNEVKvlsmlHHPNIIEYYESFLEDKALMIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHI--RKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGAPVKIIDFGFAR-LRPQSPG 556
Cdd:cd08220   82 PGGTLFEYIqqRKGSLLSEEEILHFFVQILLALHHVHSKQ-ILHRDLKTQNILL--NKKRTVVKIGDFGISKiLSSKSKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VP-MQTPCftlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWqg 635
Cdd:cd08220  159 YTvVGTPC----YISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAAN-------LPALVLKIMRGTFAPISDRY-- 225
                        250       260
                 ....*....|....*....|
gi 663856869 636 vSEEAKELVRGLLTVDPAKR 655
Cdd:cd08220  226 -SEELRHLILSMLHLDPNKR 244
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
31-301 2.76e-19

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 88.97  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMK---------VLRKAAL--VQRAKTQEHtrtersvlelvrqaPFLV 99
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRN---RETGQIVAIKkfveseddpVIKKIALreIRMLKQLKH--------------PNLV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQTDAKLHLILDYVSGgEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLT 178
Cdd:cd07847   64 NLIEVFRRKRKLHLVFEYCDH-TVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLC 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 179 DFGLSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF--------------TLeGE- 243
Cdd:cd07847  143 DFGFARILTGPGDDYT-DYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWpgksdvdqlylirkTL-GDl 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 244 --RNTQAEVSRRILK-CSPPFP----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07847  221 ipRHQQIFSTNQFFKgLSIPEPetrepleskfPNISSPALSFLKGCLQMDPTERL-----SCEELLEHPYF 286
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
410-656 3.14e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 88.63  E-value: 3.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLE--LLR 480
Cdd:cd07861    8 IGEGTYGVVYKGRNKKTGQIVAMKKI--RLESEEEgvpstaiREISLLKELQ-HPNIVCLEDVLMQENRLYLVFEflSMD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFARlrpqSPGVPMQ 560
Cdd:cd07861   85 LKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRR-VLHRDLKPQNLLI--DNKGV-IKLADFGLAR----AFGIPVR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 T---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqaaEI--MCKIREGRFSLDGEAWQ 634
Cdd:cd07861  157 VythEVVTLWYRAPEvLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDS---------EIdqLFRIFRILGTPTEDIWP 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 635 GVS-------------------------EEAKELVRGLLTVDPAKRL 656
Cdd:cd07861  228 GVTslpdykntfpkwkkgslrtavknldEDGLDLLEKMLIYDPAKRI 274
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
411-667 3.89e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 88.13  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQR-------EVAALRLCqSHPNVVNLH--EVHHDQLhtYLVLELLRG 481
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEI--RFQDNDPKtikeiadEMKVLEGL-DHPNLVRYYgvEVHREEV--YIFMEYCQE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADdtpGAPVKIIDFGFA-RLRPQS---PGV 557
Cdd:cd06626   84 GTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHE-NGIVHRDIKPANIFLDS---NGLIKLGDFGSAvKLKNNTttmAPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQTPCFTLQYAAPELLAQQ---GYDESCDLWSLGVILYMMLSGQVP-------FQgasgqggqsqaaeIMCKIREGRFS 627
Cdd:cd06626  160 EVNSLVGTPAYMAPEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPwseldneWA-------------IMYHVGMGHKP 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 628 LDGEAWQgVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd06626  227 PIPDSLQ-LSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
31-301 4.51e-19

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 88.25  E-value: 4.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGkvfLVRKAGGHDAGKLYAMKVLRKA---ALVQRAKTQEhtrtersvLELVRQAPF--LVTLHYAF 105
Cdd:cd07846    1 EKYENLGLVGEGSYG---MVMKCRHKETGQIVAIKKFLESeddKMVKKIAMRE--------IKMLKQLRHenLVNLIEVF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSggemFTHLYQRQYF----KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd07846   70 RRKKRWYLVFEFVD----HTVLDDLEKYpnglDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKeFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKC---- 257
Cdd:cd07846  146 FAR-TLAAPGEVYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFP----GDSDIDQLYHIIKClgnl 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 258 ----------SPPFP-----------------PRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd07846  221 iprhqelfqkNPLFAgvrlpevkeveplerryPKLSGVVIDLAKKCLHIDPDKRPSCS-----ELLHHEFF 286
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
29-302 5.06e-19

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 88.37  E-value: 5.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKaalVQRAKTqehtRTERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:cd14132   16 SQDDYEIIRKIGRGKYSEVFEGINIG---NNEKVVIKVLKP---VKKKKI----KREIKILQNLRGGPNIVKLLDVVKDP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLH--LILDYVSGgEMFTHLYQrqYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSkE 185
Cdd:cd14132   86 QSKTpsLIFEYVNN-TDFKTLYP--TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLrLIDWGLA-E 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKE---RTfsfcGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtLEGERNT---------------- 246
Cdd:cd14132  162 FYHPGQEynvRV----ASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPF-FHGHDNYdqlvkiakvlgtddly 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 247 ------QAEVSRRILKCSPPFPPR-------------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14132  237 ayldkyGIELPPRLNDILGRHSKKpwerfvnsenqhlVTPEALDLLDKLLRYDHQERI-----TAKEAMQHPYFD 306
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
410-677 5.67e-19

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 89.32  E-value: 5.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQS-----------------GQEFAVKILSRRLEANTQ-----REVAALRlCQSHPNVVNLHEVHH 467
Cdd:cd07876   12 VADSTFTVLKRYQQLKPigsgaqgivcaafdtvlGINVAVKKLSRPFQNQTHakrayRELVLLK-CVNHKNIISLLNVFT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 468 DQ------LHTYLVLELLRGGE-LLEHIrkkrHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPV 540
Cdd:cd07876   91 PQksleefQDVYLVMELMDANLcQVIHM----ELDHERMSYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSD---CTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 541 KIIDFGFARLRPQSPgvpMQTP-CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS--GQGGQ------ 611
Cdd:cd07876  163 KILDFGLARTACTNF---MMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDhiDQWNKvieqlg 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 612 SQAAEIMCKIREG--RFSLDGEAWQGVS---------------------EEAKELVRGLLTVDPAKRLKL-EGLRG---S 664
Cdd:cd07876  240 TPSAEFMNRLQPTvrNYVENRPQYPGISfeelfpdwifpseserdklktSQARDLLSKMLVIDPDKRISVdEALRHpyiT 319
                        330
                 ....*....|...
gi 663856869 665 SWLQDGSARSSPP 677
Cdd:cd07876  320 VWYDPAEAEAPPP 332
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
400-606 6.51e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 86.95  E-value: 6.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdLRepALGQGSFSVCRRCRQRQSGQEFAVKILsrRL-----EANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYL 474
Cdd:cd08219    1 QYNV-LR--VVGEGSFGRALLVQHVNSDQKYAMKEI--RLpksssAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRH--FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRp 552
Cdd:cd08219   76 VMEYCDGGDLMQKIKLQRGklFPEDTILQWFVQMCLGVQHIHEKR-VLHRDIKSKNIFL---TQNGKVKLGDFGSARLL- 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 553 QSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd08219  151 TSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANS 204
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
38-284 6.96e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 86.96  E-value: 6.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFlvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14148    1 IIGVGGFGKVY-----KGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQH-PNIIALRGVCLNPPHLCLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRvYGGEIVLALEHLHK---LGIIYRDLKLENVLL--DSEGH------IVLTDFGLSKEF 186
Cdd:cd14148   75 ARGGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNeaiVPIIHRDLKSSNILIlePIENDdlsgktLKITDFGLAREW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 lteEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPFtlegeRNTQA-EVSRRIL--KCSPPFPP 263
Cdd:cd14148  154 ---HKTTKMSAAGTYAWMAPEVIRLSL-FSKSSDVWSFGVLLWELLTGEVPY-----REIDAlAVAYGVAmnKLTLPIPS 224
                        250       260
                 ....*....|....*....|.
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14148  225 TCPEPFARLLEECWDPDPHGR 245
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
113-238 7.20e-19

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 87.71  E-value: 7.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-SEGHIV--LTDFGLSKEF 186
Cdd:cd14038   75 LAMEYCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqGEQRLIhkIIDLGYAKEL 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 187 ltEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14038  155 --DQGSLCTSFVGTLQYLAPELLEQQK-YTVTVDYWSFGTLAFECITGFRPF 203
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
29-302 7.58e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 88.19  E-value: 7.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMK--------------VLRKAALVQRAKtqeHTrterSVLELVR- 93
Cdd:cd07845    5 SVTEFEKLNRIGEGTYGIVY---RARDTTSGEIVALKkvrmdnerdgipisSLREITLLLNLR---HP----NIVELKEv 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  94 ------QAPFLVtLHYAFQTDAKLhliLDYVSggemfthlyqrQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENV 167
Cdd:cd07845   75 vvgkhlDSIFLV-MEYCEQDLASL---LDNMP-----------TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 168 LLDSEGHIVLTDFGLSKEFLTEEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERN-- 245
Cdd:cd07845  140 LLTDKGCLKIADFGLARTYGLPAKPMTPKVV-TLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEql 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 246 --------TQAE-----------VSRRILKCSP-----PFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07845  219 dliiqllgTPNEsiwpgfsdlplVGKFTLPKQPynnlkHKFPWLSEAGLRLLNFLLMYDPKKRA-----TAEEALESSYF 293

                 .
gi 663856869 302 Q 302
Cdd:cd07845  294 K 294
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
381-656 7.86e-19

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 88.73  E-value: 7.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 381 APGAGDRPGRAAVARSAMMQYELDlREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsH 456
Cdd:PLN00034  54 SSSSSSSSASGSAPSAAKSLSELE-RVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRrqicREIEILRDVN-H 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 457 PNVVNLHEVH-HDQLHTYLVLELLRGGELLEHIRKkrhfsESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddT 535
Cdd:PLN00034 132 PNVVKCHDMFdHNGEIQVLLEFMDGGSLEGTHIAD-----EQFLADVARQILSGIAYLHRRH-IVHRDIKPSNLLI---N 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 536 PGAPVKIIDFGFARLRPQSPGvPMQTPCFTLQYAAPEL----LAQQGYDE-SCDLWSLGVILYMMLSGQVPFqgasGQGG 610
Cdd:PLN00034 203 SAKNVKIADFGVSRILAQTMD-PCNSSVGTIAYMSPERintdLNHGAYDGyAGDIWSLGVSILEFYLGRFPF----GVGR 277
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 611 QSQAAEIMCKIregRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:PLN00034 278 QGDWASLMCAI---CMSQPPEAPATASREFRHFISCCLQREPAKRW 320
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
29-301 8.94e-19

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 87.66  E-value: 8.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKvlrkaalvqRAKTQEHT--------RTERSVLELvrQAPFLVT 100
Cdd:cd07843    3 SVDEYEKLNRIEEGTYGVVY---RARDKKTGEIVALK---------KLKMEKEKegfpitslREINILLKL--QHPNIVT 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 101 LHYAF--QTDAKLHLILDYVS---GGEMFTHlyqRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHI 175
Cdd:cd07843   69 VKEVVvgSNLDKIYMVMEYVEhdlKSLMETM---KQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGIL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 176 VLTDFGLSKEFLTEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGE------------ 243
Cdd:cd07843  146 KICDFGLAREYGSPLKPYT-QLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEidqlnkifkllg 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 244 ---RNTQAEVSR--RILKCSPPFPP------RIGPVAQ-----DLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07843  225 tptEKIWPGFSElpGAKKKTFTKYPynqlrkKFPALSLsdngfDLLNRLLTYDPAKRI-----SAEDALKHPYF 293
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
410-606 9.99e-19

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 87.60  E-value: 9.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANTQREVAAL-RLCQSHP----NVVNLH-------------EVHHDQ 469
Cdd:cd14210   21 LGKGSFGQVVKCLDHKTGQLVAIKIIrnKKRFHQQALVEVKILkHLNDNDPddkhNIVRYKdsfifrghlcivfELLSIN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 470 LHTYLvlellrggellehirKKRHFS-------ESEASQILRSLvsavSFMHEEaGVVHRDLKPENILYADDTPGApVKI 542
Cdd:cd14210  101 LYELL---------------KSNNFQglslsliRKFAKQILQAL----QFLHKL-NIIHCDLKPENILLKQPSKSS-IKV 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 543 IDFGFArlrpqspgvpmqtpCFT-------LQ---YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14210  160 IDFGSS--------------CFEgekvytyIQsrfYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGEN 219
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
38-238 1.15e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 86.63  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14146    1 IIGVGGFGKVYR-----ATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRH-PNIIKLEGVCLEEPNLCLVMEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEV--RV-------YGGEIVLALEHLHK---LGIIYRDLKLENVLL------DSEGHIVL-- 177
Cdd:cd14146   75 ARGGTLNRALAAANAAPGPRRarRIpphilvnWAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehDDICNKTLki 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 178 TDFGLSKEFlteEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14146  155 TDFGLAREW---HRTTKMSAAGTYAWMAPEVIKSSL-FSKGSDIWSYGVLLWELLTGEVPY 211
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
392-655 1.21e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 89.93  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 392 AVARSAMMQYELDLrepALGQGSFSVCRRCRQRQSGQEFAVKILSrrLEANT-------QREVAALRLCqSHPNVVNLHE 464
Cdd:PTZ00283  25 ATAKEQAKKYWISR---VLGSGATGTVLCAKRVSDGEPFAVKVVD--MEGMSeadknraQAEVCCLLNC-DFFSIVKCHE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 465 --VHHDQ------LHTYLVLELLRGGELLEHIRKK----RHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYA 532
Cdd:PTZ00283  99 dfAKKDPrnpenvLMIALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKH-MIHRDIKSANILLC 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 533 DDtpgAPVKIIDFGFARLRPQS-PGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggq 611
Cdd:PTZ00283 178 SN---GLVKLGDFGFSKMYAATvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENME--- 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 612 sqaaEIMCKIREGRFS-LDGEawqgVSEEAKELVRGLLTVDPAKR 655
Cdd:PTZ00283 252 ----EVMHKTLAGRYDpLPPS----ISPEMQEIVTALLSSDPKRR 288
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
410-607 1.29e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 86.63  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKILSRRLE------ANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLE------ 477
Cdd:cd14146    2 IGVGGFGKVYRATWK--GQEVAVKAARQDPDedikatAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEfarggt 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 ---LLRGGELLEHIRKKR----HFSESEASQILRSLVsavsFMHEEAGV--VHRDLKPENILYA-----DDTPGAPVKII 543
Cdd:cd14146   80 lnrALAAANAAPGPRRARrippHILVNWAVQIARGML----YLHEEAVVpiLHRDLKSSNILLLekiehDDICNKTLKIT 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 544 DFGFARLRPQSPGVpmqTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14146  156 DFGLAREWHRTTKM---SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDG 216
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
410-655 1.35e-18

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 86.30  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS------RRLEANTQ--REVAAL-RLCqsHPNVVNLH--EVHHDQLHTYLvlEL 478
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVSlvdddkKSRESVKQleQEIALLsKLR--HPNIVQYYgtEREEDNLYIFL--EY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFAR-LRPQSPGV 557
Cdd:cd06632   84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSR-NTVHRDIKGANILV--DTNGV-VKLADFGMAKhVEAFSFAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQ-TPCftlqYAAPELLAQQ--GYDESCDLWSLGVILYMMLSGQVPFqgasgqgGQSQAAEIMCKIreGRFSLDGEAWQ 634
Cdd:cd06632  160 SFKgSPY----WMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPW-------SQYEGVAAIFKI--GNSGELPPIPD 226
                        250       260
                 ....*....|....*....|.
gi 663856869 635 GVSEEAKELVRGLLTVDPAKR 655
Cdd:cd06632  227 HLSPDAKDFIRLCLQRDPEDR 247
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
33-238 1.45e-18

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 87.08  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQAPFLVTLHYAF------Q 106
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHV---KTGQLAAIKVMDVTG-----DEEEEIKQEINMLKKYSHHRNIATYYGAFikknppG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMfTHLYQR---QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd06637   80 MDDQLWLVMEFCGAGSV-TDLIKNtkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 184 KEfLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDW----WSLGILLFELLTGASPF 238
Cdd:cd06637  159 AQ-LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFksdlWSLGITAIEMAEGAPPL 216
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
39-238 1.46e-18

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 86.56  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGhdagKLYAMKVLR---KAALVQRAktqehtRTERSVLELVRQAPFLVTLHYAFQTDAKLhLIL 115
Cdd:cd14066    1 IGSGGFGTVYKGVLENG----TVVAVKRLNemnCAASKKEF------LTELEMLGRLRHPNLVRLLGYCLESDEKL-LVY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFK----EAEVRVYGGeIVLALEHLH---KLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLT 188
Cdd:cd14066   70 EYMPNGSLEDRLHCHKGSPplpwPQRLKIAKG-IARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLAR-LIP 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 189 EEKE--RTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14066  148 PSESvsKTSAVKGTIGYLAPEYIRTGR-VSTKSDVYSFGVVLLELLTGKPAV 198
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
488-656 2.10e-18

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 86.31  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgAPVKIIDFGFAR--------LRPQ--SPGv 557
Cdd:cd13974  124 IREKR-LSEREALVIFYDVVRVVEALHKK-NIVHRDLKLGNMVLNKRT--RKITITNFCLGKhlvseddlLKDQrgSPA- 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 pmqtpcftlqYAAPELLAQQGY-DESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSL--DGEawq 634
Cdd:cd13974  199 ----------YISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQ-------ELFRKIKAAEYTIpeDGR--- 258
                        170       180
                 ....*....|....*....|..
gi 663856869 635 gVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd13974  259 -VSENTVCLIRKLLVLNPQKRL 279
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
410-655 2.26e-18

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 85.54  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKI-----LSRRLEANTQREVAAL-RLcqSHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd08529    8 LGKGSFGVVYKVVRKVDGRVYALKQidisrMSRKMREEAIDEARVLsKL--NSPYVIKYYDSFVDKGKLNIVMEYAENGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRK--KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENI-LYADDTpgapVKIIDFGFARLRPQSpGVPMQ 560
Cdd:cd08529   86 LHSLIKSqrGRPLPEDQIWKFFIQTLLGLSHLHSKK-ILHRDIKSMNIfLDKGDN----VKIGDLGVAKILSDT-TNFAQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqgGQSQAAEIMcKIREGRFSLDGeawQGVSEEA 640
Cdd:cd08529  160 TIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFE------AQNQGALIL-KIVRGKYPPIS---ASYSQDL 229
                        250
                 ....*....|....*
gi 663856869 641 KELVRGLLTVDPAKR 655
Cdd:cd08529  230 SQLIDSCLTKDYRQR 244
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
401-655 2.33e-18

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 85.79  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDLRepaLGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAAL-RLCqsHPNVVNLHE--VHHDQLh 471
Cdd:cd08224    2 YEIEKK---IGKGQFSVVYRARCLLDGRLVALKkvqifeMMDAKARQDCLKEIDLLqQLN--HPNIIKYLAsfIENNEL- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 tYLVLELLRGGELLEHIRK----KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpGApVKIIDFGF 547
Cdd:cd08224   76 -NIVLELADAGDLSRLIKHfkkqKRLIPERTIWKYFVQLCSALEHMHSKR-IMHRDIKPANVFITAN--GV-VKLGDLGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 548 ARLRpQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqGGQSQAAEIMC-KIREGRF 626
Cdd:cd08224  151 GRFF-SSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPF------YGEKMNLYSLCkKIEKCEY 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 627 S-LDGEAWqgvSEEAKELVRGLLTVDPAKR 655
Cdd:cd08224  224 PpLPADLY---SQELRDLVAACIQPDPEKR 250
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
122-300 2.96e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 85.02  E-value: 2.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-SEGHIVLTDFGlSKEFLteeKERTFS-FCG 199
Cdd:cd14100   92 DLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG-SGALL---KDTVYTdFDG 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegerntqaEVSRRILKCSPPFPPRIGPVAQDLLQRLLCK 279
Cdd:cd14100  168 TRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPF----------EHDEEIIRGQVFFRQRVSSECQHLIKWCLAL 237
                        170       180
                 ....*....|....*....|.
gi 663856869 280 DPKKRlgagpQGAQEVRNHPF 300
Cdd:cd14100  238 RPSDR-----PSFEDIQNHPW 253
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
405-602 3.75e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 85.17  E-value: 3.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQREVA-------ALRLCQSHPNVVNLHEVHHDQLHTYLVL 476
Cdd:cd06630    3 LKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFcRNSSSEQEEVVeaireeiRMMARLNHPNIVRMLGATQHKSHFNIFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGAPVKIIDFGFA-RLRPQSP 555
Cdd:cd06630   83 EWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQ-IIHRDLKGANLLV--DSTGQRLRIADFGAAaRLASKGT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 556 GV-PMQTPCF-TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06630  160 GAgEFQGQLLgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
410-604 4.45e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 85.22  E-value: 4.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPstaiREISLMKELK-HENIVRLHDVIHTENKLMLVFEYMDKDLKK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 eHIRKKRHFSESEASQI---LRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARlrpqSPGVPMQT- 561
Cdd:cd07836   87 -YMDTHGVRGALDPNTVksfTYQLLKGIAFCHEN-RVLHRDLKPQNLLINKR---GELKLADFGLAR----AFGIPVNTf 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 562 --PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07836  158 snEVVTLWYRAPDvLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPG 203
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
131-304 4.85e-18

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 86.27  E-value: 4.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 131 QYFkeaevrVYggEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK------EFLTEekertfsFCGTIEYM 204
Cdd:cd07858  111 QYF------LY--QLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARttsekgDFMTE-------YVVTRWYR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 205 APEIIRSKTGHGKAVDWWSLGILLFELLTGASPF-------------------TLEGERNTQAEVSRRILKCSPPFP--- 262
Cdd:cd07858  176 APELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFpgkdyvhqlklitellgspSEEDLGFIRNEKARRYIRSLPYTPrqs 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 263 -----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGL 304
Cdd:cd07858  256 farlfPHANPLAIDLLEKMLVFDPSKRI-----TVEEALAHPYLASL 297
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
410-627 5.59e-18

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 85.62  E-value: 5.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS-----RRLEANtQREVAALRLCqSHPNVVNLHEVHHDQL--HTYLVLEL---L 479
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNnlsfmRPLDVQ-MREFEVLKKL-NHKNIVKLFAIEEELTtrHKVLVMELcpcG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPV-KIIDFGFAR-LRPQSPGV 557
Cdd:cd13988   79 SLYTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLREN-GIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAAReLEDDEQFV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 558 PMQTpcfTLQYAAPELL--------AQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqGGQSQAAEIMCKIREGRFS 627
Cdd:cd13988  158 SLYG---TEEYLHPDMYeravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPFRPF---EGPRRNKEVMYKIITGKPS 229
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
39-287 6.01e-18

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 84.48  E-value: 6.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKA--GGHDAGKLYAMKVLRKAALVQRAktqehTRTERSVLEL---VRQAPFLVtlhyafqtdaklhL 113
Cdd:cd13991   14 IGRGSFGEVHRMEDKqtGFQCAVKKVRLEVFRAEELMACA-----GLTSPRVVPLygaVREGPWVN-------------I 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG-HIVLTDFGLSKEF----LT 188
Cdd:cd13991   76 FMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLdpdgLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGASPFTlegeRNTQAEVSRRILKCSPPF---PPRI 265
Cdd:cd13991  156 KSLFTGDYIPGTETHMAPEVVLGKPCDAK-VDVWSSCCMMLHMLNGCHPWT----QYYSGPLCLKIANEPPPLreiPPSC 230
                        250       260
                 ....*....|....*....|..
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd13991  231 APLTAQAIQAGLRKEPVHRASA 252
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
27-284 6.37e-18

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 84.64  E-value: 6.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVEnfellKVLGTGAYGKVFLVRkagGHDAGKLYAMKVLrkaaLVQRAKTQEHTRTERSVLELVRQAPFLVTL--HYA 104
Cdd:cd14037    4 HVTIE-----KYLAEGGFAHVYLVK---TSNGGNRAALKRV----YVNDEHDLNVCKREIEIMKRLSGHKNIVGYidSSA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLH---LILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLLDSEGHIVL 177
Cdd:cd14037   72 NRSGNGVYevlLLMEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFG-LSKEFLTEEKERTFSFC-------GTIEYMAPEII---RSKTGHGKAvDWWSLGILLFELLTGASPFtleGERNT 246
Cdd:cd14037  152 CDFGsATTKILPPQTKQGVTYVeedikkyTTLQYRAPEMIdlyRGKPITEKS-DIWALGCLLYKLCFYTTPF---EESGQ 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 247 QAevsrrILKCSPPFP--PRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14037  228 LA-----ILNGNFTFPdnSRYSKRLHKLIRYMLEEDPEKR 262
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
410-625 6.85e-18

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 84.03  E-value: 6.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKIL-SRRLEANTQREVAAL-RLCqsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIeSESEKKAFEVEVRQLsRVD--HPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 I---RKKRHFSESEASQILRSLVSAVSFMH--EEAGVVHRDLKPENILYADDtpGAPVKIIDFGFArlrpqspgVPMQTP 562
Cdd:cd14058   77 LhgkEPKPIYTAAHAMSWALQCAKGVAYLHsmKPKALIHRDLKPPNLLLTNG--GTVLKICDFGTA--------CDISTH 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 563 CF----TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGqggqsQAAEIMCKIREGR 625
Cdd:cd14058  147 MTnnkgSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGG-----PAFRIMWAVHNGE 208
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
489-655 7.21e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 87.38  E-value: 7.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 489 RKKRH--FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPMQTP-CFT 565
Cdd:PTZ00267 159 RLKEHlpFQEYEVGLLFYQIVLALDEVHSRK-MMHRDLKSANIFL---MPTGIIKLGDFGFSKQYSDSVSLDVASSfCGT 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSldgEAWQGVSEEAKELVR 645
Cdd:PTZ00267 235 PYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQR-------EIMQQVLYGKYD---PFPCPVSSGMKALLD 304
                        170
                 ....*....|
gi 663856869 646 GLLTVDPAKR 655
Cdd:PTZ00267 305 PLLSKNPALR 314
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
31-300 8.23e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 84.54  E-value: 8.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVlrkaalVQRAKTQEHTRTERSVLELVRQ--APFLVTLHYAFQTD 108
Cdd:cd06619    1 QDIQYQEILGHGNGGTVY---KAYHLLTRRILAVKV------IPLDITVELQKQIMSELEILYKcdSPYIIGFYGAFFVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMftHLYQRqyFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd06619   72 NRISICTEFMDGGSL--DVYRK--IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKErtfSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPFtLEGERNTQAEVSRRILKC----SPPFPP- 263
Cdd:cd06619  148 SIAK---TYVGTNAYMAPERI-SGEQYGIHSDVWSLGISFMELALGRFPY-PQIQKNQGSLMPLQLLQCivdeDPPVLPv 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 264 -RIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPF 300
Cdd:cd06619  223 gQFSEKFVHFITQCMRKQPKERP-----APENLMDHPF 255
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
410-657 9.29e-18

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 85.85  E-value: 9.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-----EAN---TQREVaaLRLCQShPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKKVlfklnEVNhvlTERDI--LTTTNS-PWLVKLLYAFQDPENVYLAMEYVPG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFA------------- 548
Cdd:cd05600   96 GDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQ-LGYIHRDLKPENFLI--DSSGH-IKLTDFGLAsgtlspkkiesmk 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 -RL-RPQSPGVPMQTPCFTLQ---------------------YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGA 605
Cdd:cd05600  172 iRLeEVKNTAFLELTAKERRNiyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGS 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 606 SgqggqsqAAEIMCKIREGRFSLDGEAWQG------VSEEAKELVRGLLTvDPAKRLK 657
Cdd:cd05600  252 T-------PNETWANLYHWKKTLQRPVYTDpdlefnLSDEAWDLITKLIT-DPQDRLQ 301
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
400-668 9.99e-18

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 84.25  E-value: 9.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdlrEPALGQGSFSVCRRCRQRQSGQEFAVKILSRR--------------------LEANTQ---------REVAAL 450
Cdd:cd14199    3 QYKL---KDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKklmrqagfprrppprgaraaPEGCTQprgpiervyQEIAIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 451 RLCqSHPNVVNLHEVHHD--QLHTYLVLELLRGGELLeHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPEN 528
Cdd:cd14199   80 KKL-DHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQK-IIHRDVKPSN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 529 ILYADDtpgAPVKIIDFGFARLRPQSPGV---PMQTPCFTlqyaAPELLAQQGYD---ESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14199  157 LLVGED---GHIKIADFGVSNEFEGSDALltnTVGTPAFM----APETLSETRKIfsgKALDVWAMGVTLYCFVFGQCPF 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 603 QGasgqggqsqaAEIMC---KIREGRFSLDGEAwqGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd14199  230 MD----------ERILSlhsKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
141-297 1.17e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 87.16  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 141 YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF----LTEekerTFSFCGTIEYMAPEIIRsktghG 216
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALssttMTQ----TNSVLGTVHYLSPEQAR-----G 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 217 KAV----DWWSLGILLFELLTGASPFTleGErnTQAEVSRRILKCSPPFP----PRIGPVAQDLLQRLLCKDPKKRlgag 288
Cdd:NF033483 183 GTVdarsDIYSLGIVLYEMLTGRPPFD--GD--SPVSVAYKHVQEDPPPPselnPGIPQSLDAVVLKATAKDPDDR---- 254

                 ....*....
gi 663856869 289 PQGAQEVRN 297
Cdd:NF033483 255 YQSAAEMRA 263
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
39-238 1.32e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 83.81  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPFL----VTLHYAFQTDAKLHLI 114
Cdd:cd14039    1 LGTGGFGNVCLYQN---QETGEKIAIKSCR---LELSVKNKDRWCHEIQIMKKLNHPNVVkacdVPEEMNFLVNDVPLLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL-DSEGHIV--LTDFGLSKEFlt 188
Cdd:cd14039   75 MEYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIVhkIIDLGYAKDL-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14039  153 DQGSLCTSFVGTLQYLAPELFENKS-YTVTVDYWSFGTMVFECIAGFRPF 201
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
410-656 1.43e-17

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 84.66  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRlEANTQREVAALrLCQ----------SHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKALKKG-DIIARDEVESL-MCEkrifetvnsaRHPFLVNLFACFQTPEHVCFVMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIrkkrH---FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFARlRPQSPG 556
Cdd:cd05589   85 AGGDLMMHI----HedvFSEPRAVFYAACVVLGLQFLHEH-KIVYRDLKLDNLLL--DTEGY-VKIADFGLCK-EGMGFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKI-----REGRFsldge 631
Cdd:cd05589  156 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEE-------EVFDSIvndevRYPRF----- 223
                        250       260
                 ....*....|....*....|....*
gi 663856869 632 awqgVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05589  224 ----LSTEAISIMRRLLRKNPERRL 244
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
410-655 1.44e-17

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 83.26  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEantQR------EVAALRLCQsHPNVVNLHEVH--HDQLhtYLVLELLRG 481
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQ---QRrellfnEVVIMRDYQ-HPNIVEMYSSYlvGDEL--WVVMEFLEG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLrpqSPGVPMQ 560
Cdd:cd06648   89 GALTDIVTHTR-MNEEQIATVCRAVLKALSFLHSQ-GVIHRDIKSDSILLTSD---GRVKLSDFGFcAQV---SKEVPRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 -----TPCFTlqyaAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqgGQSQAAEIMCKIREGRFSLDGEAWQg 635
Cdd:cd06648  161 kslvgTPYWM----APEVISRLPYGTEVDIWSLGIMVIEMVDGEPPY-------FNEPPLQAMKRIRDNEPPKLKNLHK- 228
                        250       260
                 ....*....|....*....|
gi 663856869 636 VSEEAKELVRGLLTVDPAKR 655
Cdd:cd06648  229 VSPRLRSFLDRMLVRDPAQR 248
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
411-607 1.45e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 82.70  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRQSGQEFAVKILsrrLEANTQREVAALRlcqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRK 490
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKL---LKIEKEAEILSVL---SHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 491 KRHfSESEASQIL---RSLVSAVSFMHEEA--GVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQTpcfT 565
Cdd:cd14060   76 NES-EEMDMDQIMtwaTDIAKGMHYLHMEApvKVIHRDLKSRNVVIAAD---GVLKICDFGASRFHSHTTHMSLVG---T 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14060  149 FPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEG 190
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
410-702 1.49e-17

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 85.83  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEA---NTQREVAALRLCQShpnVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05624   80 IGRGAFGEVAVVKMKNTERIYAMKILNKwemlkRAETacfREERNVLVNGDCQW---ITTLHYAFQDENYLYLVMDYYVG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRK-KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGVPMQ 560
Cdd:cd05624  157 GDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLH-YVHRDIKPDNVLL--DMNGH-IRLADFGSCLKMNDDGTVQSS 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTLQYAAPELLA--QQG---YDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKI--REGRFSLDGEAw 633
Cdd:cd05624  233 VAVGTPDYISPEILQamEDGmgkYGPECDWWSLGVCMYEMLYGETPFYAES-------LVETYGKImnHEERFQFPSHV- 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 634 QGVSEEAKELVRGLLtVDPAKRLKLEGL---------RGSSW----------LQDGSARSSPP--------LRTPDVLES 686
Cdd:cd05624  305 TDVSEEAKDLIQRLI-CSRERRLGQNGIedfkkhaffEGLNWenirnleapyIPDVSSPSDTSnfdvdddvLRNPEILPP 383
                        330
                 ....*....|....*.
gi 663856869 687 SGPAVRSGLNATFMAF 702
Cdd:cd05624  384 SSHTGFSGLHLPFVGF 399
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
39-260 1.72e-17

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 84.08  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQehtRTERSVLELVRQAPfLVTLhYAFQTDAKLH---LIL 115
Cdd:cd13988    1 LGQGATANVFRGRH---KKTGDLYAVKVFNNLSFMRPLDVQ---MREFEVLKKLNHKN-IVKL-FAIEEELTTRhkvLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQ--RQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL--LDSEGHIV--LTDFGLSKEFlt 188
Cdd:cd13988   73 ELCPCGSLYTVLEEpsNAYgLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFGAAREL-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGTIEYMAPEI-----IRSKTG--HGKAVDWWSLGILLFELLTGASPF-TLEGERNTQaEVSRRILKCSPP 260
Cdd:cd13988  151 EDDEQFVSLYGTEEYLHPDMyeravLRKDHQkkYGATVDLWSIGVTFYHAATGSLPFrPFEGPRRNK-EVMYKIITGKPS 229
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
410-606 1.80e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 83.54  E-value: 1.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA------VKILSRRLEANTQREVAALRLCQS--HPNVVNLHEV---------------- 465
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRFValkrvrVQTGEEGMPLSTIREVAVLRHLETfeHPNVVRLFDVctvsrtdretkltlvf 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 -HHDQ-LHTYLVLELLRGgellehirkkrhFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKII 543
Cdd:cd07862   89 eHVDQdLTTYLDKVPEPG------------VPTETIKDMMFQLLRGLDFLHSHR-VVHRDLKPQNILV---TSSGQIKLA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 544 DFGFARLrpQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07862  153 DFGLARI--YSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSS 213
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
410-656 1.92e-17

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 83.56  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRrCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCQShPNVVNLHEVHH--DQLHtyLVLELLR 480
Cdd:cd05605    8 LGKGGFgEVCA-CQVRATGKMYACKklekkrIKKRKGEAMALNEKQILEKVNS-RFVVSLAYAYEtkDALC--LVLTIMN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRK--KRHFSESE----ASQILRSLVSavsfMHEEaGVVHRDLKPENILYaDDTpgAPVKIIDFGFARLRPqs 554
Cdd:cd05605   84 GGDLKFHIYNmgNPGFEEERavfyAAEITCGLEH----LHSE-RIVYRDLKPENILL-DDH--GHVRISDLGLAVEIP-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREGRFSLDGEAwq 634
Cdd:cd05605  154 EGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFR---ARKEKVKREEVDRRVKEDQEEYSEKF-- 228
                        250       260
                 ....*....|....*....|..
gi 663856869 635 gvSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05605  229 --SEEAKSICSQLLQKDPKTRL 248
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
31-238 2.02e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 83.57  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAK 110
Cdd:cd06616    6 EDLKDLGEIGRGAFGTV---NKMLHKPSGTIMAVKRIR---STVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 -------LHLILDYVSggeMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHK-LGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd06616   80 cwicmelMDISLDKFY---KYVYEVLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILLDRNGNIKLCDFGI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 183 SKEfLTEEKERTFSfCGTIEYMAPEII---RSKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd06616  157 SGQ-LVDSIAKTRD-AGCRPYMAPERIdpsASRDGYDVRSDVWSLGITLYEVATGKFPY 213
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
410-604 2.03e-17

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 84.16  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK---------ILSRRleanTQREVAALRLCQsHPNVVNLHEVHHDQLH-TYLVLELL 479
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKkimkpfstpVLAKR----TYRELKLLKHLR-HENIISLSDIFISPLEdIYFVTELL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRK--KRHFSESEASQILRSLvsavSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLR-PQSPG 556
Cdd:cd07856   93 GTDLHRLLTSRplEKQFIQYFLYQILRGL----KYVHS-AGVIHRDLKPSNILVNEN---CDLKICDFGLARIQdPQMTG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 557 VpmqtpCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07856  165 Y-----VSTRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPG 208
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
410-667 2.34e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 83.31  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQLHT---------- 472
Cdd:cd07864   15 IGEGTYGQVYKAKDKDTGELVALKKV--RLDNEKEgfpitaiREIKILRQLN-HRSVVNLKEIVTDKQDAldfkkdkgaf 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 473 YLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRP 552
Cdd:cd07864   92 YLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKK-NFLHRDIKCSNILLNNK---GQIKLADFGLARLYN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSPGVPMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQgASGQGGQSQAAEIMC------------ 619
Cdd:cd07864  168 SEESRPYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQ-ANQELAQLELISRLCgspcpavwpdvi 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 620 ----------------KIREgRFSLdgeawqgVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd07864  247 klpyfntmkpkkqyrrRLRE-EFSF-------IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
410-602 2.41e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 83.09  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA-NTQREVAALRLCQ--SHPNVVNLHEVHHD--QLHTYLVLELLRGGEL 484
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPkNRERWCLEIQIMKrlNHPNVVAARDVPEGlqKLAPNDLPLLAMEYCQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRH-------FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQspGV 557
Cdd:cd14038   82 GGDLRKYLNqfenccgLREGAILTLLSDISSALRYLHENR-IIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQ--GS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 558 PMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14038  159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
410-602 2.53e-17

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 82.31  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRrCRQRQSGQEFAVKILSrrLEANTQ---REVAALRLCQShPNVVNLHEVHHDQLHTYLVLE--LLRGGE 483
Cdd:cd06612   11 LGEGSYgSVYK-AIHKETGQVVAIKVVP--VEEDLQeiiKEISILKQCDS-PYIVKYYGSYFKNTDLWIVMEycGAGSVS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFA-----RLRPQspGVP 558
Cdd:cd06612   87 DIMKITNKT-LTEEEIAAILYQTLKGLEYLHSN-KKIHRDIKAGNILLNEE---GQAKLADFGVSgqltdTMAKR--NTV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 663856869 559 MQTPCftlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06612  160 IGTPF----WMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
396-656 3.16e-17

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 83.13  E-value: 3.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 396 SAMMQYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN-----TQREVAALRLCQsHPNVVNLHE---VHH 467
Cdd:cd07866    5 SKLRDYEILGK---LGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfpitALREIKILKKLK-HPNVVPLIDmavERP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 468 DQLH-----TYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKI 542
Cdd:cd07866   81 DKSKrkrgsVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHE-NHILHRDIKAANILI--DNQGI-LKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 543 IDFGFARL------RPQSPGVPMQ---TPCF-TLQYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQGASgqgGQ 611
Cdd:cd07866  157 ADFGLARPydgpppNPKGGGGGGTrkyTNLVvTRWYRPPELLLGeRRYTTAVDIWGIGCVFAEMFTRRPILQGKS---DI 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 612 SQAAEImckiregrFSLDG----EAWQG--------------------------VSEEAKELVRGLLTVDPAKRL 656
Cdd:cd07866  234 DQLHLI--------FKLCGtpteETWPGwrslpgcegvhsftnyprtleerfgkLGPEGLDLLSKLLSLDPYKRL 300
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
38-284 3.83e-17

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 82.28  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLVRKAGGHDAGKLY------------AMKVLRKAALVQRAKTQEHTRTERSVLELVRQA---------- 95
Cdd:cd14000    1 LLGDGGFGSVYRASYKGEPVAVKIFnkhtssnfanvpADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPsivyllgigi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 -PFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEvrvyggeivlALEHLHKLGIIYRDLKLENVLL----- 169
Cdd:cd14000   81 hPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVAD----------GLRYLHSAMIIYRDLKSHNVLVwtlyp 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEFLteeKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtLEGErntQAE 249
Cdd:cd14000  151 NSAIIIKIADYGISRQCC---RMGAKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPM-VGHL---KFP 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 250 VSRRILKCSPP--------FPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:cd14000  224 NEFDIHGGLRPplkqyecaPWPEV----EVLMKKCWKENPQQR 262
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31-284 4.36e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 82.15  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKvlrkaalvqRAKTQeHTRTERSVLELVR-QAPFLVTLH------- 102
Cdd:cd14047    6 QDFKEIELIGSGGFGQVF---KAKHRIDGKTYAIK---------RVKLN-NEKAEREVKALAKlDHPNIVRYNgcwdgfd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAK---------LHLILDYVSGGEMFTHLYQRQYFK----EAEVRVYggEIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14047   73 YDPETSSSnssrsktkcLFIQMEFCEKGTLESWIEKRNGEKldkvLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEfLTEEKERTFSFcGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASpftlegERNTQAE 249
Cdd:cd14047  151 VDTGKVKIGDFGLVTS-LKNDGKRTKSK-GTLSYMSPEQISSQD-YGKEVDIYALGLILFELLHVCD------SAFEKSK 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 250 V--SRRILKCSPPFPPRIgPVAQDLLQRLLCKDPKKR 284
Cdd:cd14047  222 FwtDLRNGILPDIFDKRY-KIEKTIIKKMLSKKPEDR 257
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
35-287 4.89e-17

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 81.66  E-value: 4.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFlvrKAGGHdaGKLYAMKVLRKAAlVQRAKTQEhTRTERSVLEL-----VRqapfLVTLHYAFQTDA 109
Cdd:cd13979    7 LQEPLGSGGFGSVY---KATYK--GETVAVKIVRRRR-KNRASRQS-FWAELNAARLrheniVR----VLAAETGTDFAS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRV-YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF-- 186
Cdd:cd13979   76 LGLIIMEYCGNGTLQQLIYEGSEPLPLAHRIlISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLge 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPP-FPPRI 265
Cdd:cd13979  156 GNEVGTPRSHIGGTYTYRAPELLKGERVTPKA-DIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGlEDSEF 234
                        250       260
                 ....*....|....*....|..
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd13979  235 GQRLRSLISRCWSAQPAERPNA 256
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
398-606 5.04e-17

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 82.17  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 398 MMQYEldlREPALGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQL 470
Cdd:PLN00009   1 MDQYE---KVEKIGEGTYGVVYKARDRVTNETIALKKI--RLEQEDEgvpstaiREISLLKEMQ-HGNIVRLQDVVHSEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HTYLVLE-----LLRGGELLEHIRKKRHFSESEASQILRslvsAVSFMHEEAgVVHRDLKPENILYadDTPGAPVKIIDF 545
Cdd:PLN00009  75 RLYLVFEyldldLKKHMDSSPDFAKNPRLIKTYLYQILR----GIAYCHSHR-VLHRDLKPQNLLI--DRRTNALKLADF 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 546 GFARlrpqSPGVPMQT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:PLN00009 148 GLAR----AFGIPVRTfthEVVTLWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDS 208
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
395-661 5.46e-17

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 83.51  E-value: 5.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 395 RSAMMQYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEAN---TQREVAALrlcQSHPNVVNLHEVH 466
Cdd:cd05621   45 RELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemikRSDSAffwEERDIMAF---ANSPWVVQLFCAF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLHTYLVLELLRGGELLeHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFG 546
Cdd:cd05621  122 QDDKYLYMVMEYMPGGDLV-NLMSNYDVPEKWAKFYTAEVVLALDAIHS-MGLIHRDVKPDNMLL--DKYGH-LKLADFG 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 547 FARLRPQSPGVPMQTPCFTLQYAAPELLAQQG----YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSqaaeimcKIR 622
Cdd:cd05621  197 TCMKMDETGMVHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYS-------KIM 269
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 623 EGRFSLDGEAWQGVSEEAKELVRGLLTvDPAKRLKLEGL 661
Cdd:cd05621  270 DHKNSLNFPDDVEISKHAKNLICAFLT-DREVRLGRNGV 307
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
427-604 5.46e-17

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 82.85  E-value: 5.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 427 GQEFAVKILSRRLEANTQ-----REVAALRLCqSHPNVVNLHEVHHDQ------LHTYLVLELLRGGELLEHIRKKRHfs 495
Cdd:cd07850   25 GQNVAIKKLSRPFQNVTHakrayRELVLMKLV-NHKNIIGLLNVFTPQksleefQDVYLVMELMDANLCQVIQMDLDH-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 496 eSEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPgvpMQTP-CFTLQYAAPELL 574
Cdd:cd07850  102 -ERMSYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSD---CTLKILDFGLARTAGTSF---MMTPyVVTRYYRAPEVI 173
                        170       180       190
                 ....*....|....*....|....*....|
gi 663856869 575 AQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07850  174 LGMGYKENVDIWSVGCIMGEMIRGTVLFPG 203
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
121-301 5.54e-17

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 81.25  E-value: 5.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 121 GEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFS-FCG 199
Cdd:cd14023   69 GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDALSdKHG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSK-TGHGKAVDWWSLGILLFELLTGASPFTlEGERNTQAEVSRRILKCsppFPPRIGPVAQDLLQRLLC 278
Cdd:cd14023  149 CPAYVSPEILNTTgTYSGKSADVWSLGVMLYTLLVGRYPFH-DSDPSALFSKIRRGQFC---IPDHVSPKARCLIRSLLR 224
                        170       180
                 ....*....|....*....|...
gi 663856869 279 KDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14023  225 REPSERL-----TAPEILLHPWF 242
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
403-682 6.34e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 81.85  E-value: 6.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 403 LDLRepALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQREVAALR---LCQSHPN-VVNLHEVHHDQLHTYLVLE 477
Cdd:cd05608    4 LDFR--VLGKGGFGEVSACQMRATGKLYACKKLNKkRLKKRKGYEGAMVEkriLAKVHSRfIVSLAYAFQTKTDLCLVMT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHI----RKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFA----R 549
Cdd:cd05608   82 IMNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRR-IIYRDLKPENVLLDDD---GNVRISDLGLAvelkD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 LRPQSPGVPmQTPCFTlqyaAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasGQGGQSQAAEIMCKIREGRFSLD 629
Cdd:cd05608  158 GQTKTKGYA-GTPGFM----APELLLGEEYDYSVDYFTLGVTLYEMIAARGPFR---ARGEKVENKELKQRILNDSVTYS 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 630 geawQGVSEEAKELVRGLLTVDPAKRLKLEG-----------LRGSSWLQDGSARSSPPLrTPD 682
Cdd:cd05608  230 ----EKFSPASKSICEALLAKDPEKRLGFRDgncdglrthpfFRDINWRKLEAGILPPPF-VPD 288
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
401-604 6.37e-17

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 83.03  E-value: 6.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 401 YELDLREPAL---GQGSF-SVCRRCRQRqSGQEFAVKILSRRLEAN--TQREVAALRLCQ--SHPNVVNLHEV------H 466
Cdd:cd07879   11 WELPERYTSLkqvGSGAYgSVCSAIDKR-TGEKVAIKKLSRPFQSEifAKRAYRELTLLKhmQHENVIGLLDVftsavsG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLHTYLVLELLRGgelleHIRKKR--HFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIID 544
Cdd:cd07879   90 DEFQDFYLVMPYMQT-----DLQKIMghPLSEDKVQYLVYQMLCGLKYIHS-AGIIHRDLKPGNLAVNED---CELKILD 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 545 FGFARlrpqSPGVPMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07879  161 FGLAR----HADAEMTGYVVTRWYRAPEvILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKG 217
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
410-681 6.46e-17

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 81.72  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR---------LEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKrikmkqgetLALNERIMLSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFG----FARLRPQ-SP 555
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNR-FIVYRDLKPANILL--DEHGH-VRISDLGlacdFSKKKPHaSV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GvpmqtpcfTLQYAAPELLAQ-QGYDESCDLWSLGVILYMMLSGQVPFqgasgqggQSQAAEIMCKIREGRFSLDGEAWQ 634
Cdd:cd05606  158 G--------THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPF--------RQHKTKDKHEIDRMTLTMNVELPD 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 635 GVSEEAKELVRGLLTVDPAKRLKLEG-----------LRGSSWLQDGSARSSPPLRTP 681
Cdd:cd05606  222 SFSPELKSLLEGLLQRDVSKRLGCLGrgatevkehpfFKGVDWQQVYLQKYPPPLIPP 279
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
410-602 6.64e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 81.89  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilSRRLEANTQREVaalRLCQ--------SHPNVVNLHEVHHDQLH-TYLVLELLR 480
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIK--SCRLELSVKNKD---RWCHeiqimkklNHPNVVKACDVPEEMNFlVNDVPLLAM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRH-------FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQ 553
Cdd:cd14039   76 EYCSGGDLRKLLNkpenccgLKESQVLSLLSDIGSGIQYLHENK-IIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQ 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 554 spGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14039  155 --GSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
31-304 7.78e-17

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 82.05  E-value: 7.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAK 110
Cdd:cd07869    5 DSYEKLEKLGEGSYATVY---KGKSKVNGKLVALKVIR---LQEEEGTPFTAIREASLLKGLKHAN-IVLLHDIIHTKET 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVsggemftHLYQRQYFKEA-------EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd07869   78 LTLVFEYV-------HTDLCQYMDKHpgglhpeNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEflTEEKERTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSRRILKCSPP-- 260
Cdd:cd07869  151 RA--KSVPSHTYSNeVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFP--GMKDIQDQLERIFLVLGTPne 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 261 --FP-----PRIGPV----------------------AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGL 304
Cdd:cd07869  227 dtWPgvhslPHFKPErftlyspknlrqawnklsyvnhAEDLASKLLQCFPKNRL-----SAQAALSHEYFSDL 294
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
406-668 7.81e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 81.05  E-value: 7.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSR-RLEANTQ--------REVAALRLCQS---HPNVVNLHEVHHDQLHTY 473
Cdd:cd14101    4 MGNLLGKGGFGTVYAGHRISDGLQVAIKQISRnRVQQWSKlpgvnpvpNEVALLQSVGGgpgHRGVIRLLDWFEIPEGFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELL-EHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGAPVKIIDFGFARLRP 552
Cdd:cd14101   84 LVLERPQHCQDLfDYITERGALDESLARRFFKQVVEAVQHCHSK-GVVHRDIKDENILV--DLRTGDIKLIDFGSGATLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSPGVPMQTpcfTLQYAAPELLAQQGYDE-SCDLWSLGVILYMMLSGQVPFQgasgQGGQSQAAEIMCKIRegrfsldge 631
Cdd:cd14101  161 DSMYTDFDG---TRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPFE----RDTDILKAKPSFNKR--------- 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 632 awqgVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQ 668
Cdd:cd14101  225 ----VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
410-607 7.94e-17

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 80.90  E-value: 7.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKILsrRLEANTQREVAALRLCQ--------SHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKAA--RQDPDEDISVTLENVRQearlfwmlRHPNIIALRGVCLQPPNLCLVMEYARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKR---HFSESEASQILRSLvsavSFMHEEAGV--VHRDLKPENILYA-----DDTPGAPVKIIDFGFAR-- 549
Cdd:cd14061   78 GALNRVLAGRKippHVLVDWAIQIARGM----NYLHNEAPVpiIHRDLKSSNILILeaienEDLENKTLKITDFGLARew 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 550 ---LRPQSPGvpmqtpcfTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14061  154 hktTRMSAAG--------TYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDG 206
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
410-655 7.95e-17

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 81.56  E-value: 7.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilsRRLEANTQ------REVAALRLCQSHPNVVNLHEVHH----DQLHTYLVLELL 479
Cdd:cd14037   11 LAEGGFAHVYLVKTSNGGNRAALK---RVYVNDEHdlnvckREIEIMKRLSGHKNIVGYIDSSAnrsgNGVYEVLLLMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKR---HFSESEASQILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDtpgAPVKIIDFG---FARLRP 552
Cdd:cd14037   88 CKGGGVIDLMNQRlqtGLTESEILKIFCDVCEAVAAMHYlKPPLIHRDLKVENVLISDS---GNYKLCDFGsatTKILPP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSP-GVPM-------QTpcfTLQYAAPE---LLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasGQGGQSqaaeimcKI 621
Cdd:cd14037  165 QTKqGVTYveedikkYT---TLQYRAPEmidLYRGKPITEKSDIWALGCLLYKLCFYTTPF----EESGQL-------AI 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 622 REGRFSL-DGEAWqgvSEEAKELVRGLLTVDPAKR 655
Cdd:cd14037  231 LNGNFTFpDNSRY---SKRLHKLIRYMLEEDPEKR 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
410-603 8.46e-17

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 81.11  E-value: 8.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRqRQSGQEFAVK--ILSRRLEANTQ---REVAALRLCQSHPNVVNL--HEVHHDQLHTYLVLELLRGG 482
Cdd:cd14131    9 LGKGGSSKVYKVL-NPKKKIYALKrvDLEGADEQTLQsykNEIELLKKLKGSDRIIQLydYEVTDEDDYLYMVMECGEID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELleHIRKKRH---FSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtpGApVKIIDFGFA-RLRPQSPGVP 558
Cdd:cd14131   88 LA--TILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEE-GIVHSDLKPANFLLVK---GR-LKLIDFGIAkAIQNDTTSIV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDE----------SCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14131  161 RDSQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQ 215
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
410-606 8.58e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 81.01  E-value: 8.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-----ILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYVIKeinisKMSPKEREESRKEVAVLSKMK-HPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEaSQILRSLVS---AVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSpgVPMQT 561
Cdd:cd08218   87 YKRINAQRGVLFPE-DQILDWFVQlclALKHVHDRK-ILHRDIKSQNIFL---TKDGIIKLGDFGIARVLNST--VELAR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 562 PCF-TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd08218  160 TCIgTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGN 205
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
33-299 8.67e-17

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 80.82  E-value: 8.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRKAALVQRAKTQEHTRTERsvLELVRQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRS---REDGKLYAVKRSRSRFRGEKDRKRKLEEVER--HEKLGEHPNCVRFIKAWEEKGILY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGgEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL----SKEFLT 188
Cdd:cd14050   78 IQTELCDT-SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLvvelDKEDIH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKErtfsfcGTIEYMAPEIIRsktGH-GKAVDWWSLGILLFELLTgaspfTLEGERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd14050  157 DAQE------GDPRYMAPELLQ---GSfTKAADIFSLGITILELAC-----NLELPSGGDGWHQLRQGYLPEEFTAGLSP 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 268 VAQDLLQRLLCKDPKKRlgagPQgAQEVRNHP 299
Cdd:cd14050  223 ELRSIIKLMMDPDPERR----PT-AEDLLALP 249
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31-284 9.05e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 81.23  E-value: 9.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLR-----KAALVQraktQEhtrtersvLELVRQAPFLVTLHY-- 103
Cdd:cd06646    9 HDYELIQRVGSGTYGDVYKARNL---HTGELAAVKIIKlepgdDFSLIQ----QE--------IFMVKECKHCNIVAYfg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd06646   74 SYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTEEKERTfSFCGTIEYMAPEI--IRSKTGHGKAVDWWSLGILLFELLTGASP-FTLEGER--------NTQAEVSR 252
Cdd:cd06646  154 AKITATIAKRK-SFIGTPYWMAPEVaaVEKNGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRalflmsksNFQPPKLK 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 663856869 253 RILKCSPPFpprigpvaQDLLQRLLCKDPKKR 284
Cdd:cd06646  233 DKTKWSSTF--------HNFVKISLTKNPKKR 256
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
410-606 9.12e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 81.58  E-value: 9.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL-----SRRLEANTQREVAALRLCQSHpNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd07848    9 VGEGAYGVVLKCRHKETKEIVAIKKFkdseeNEEVKETTLRELKMLRTLKQE-NIVELKEAFRRRGKLYLVFEYVEKNML 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCF 564
Cdd:cd07848   88 ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKND-IVHRDIKPENLLISHNDV---LKLCDFGFARNLSEGSNANYTEYVA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07848  164 TRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGES 205
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
410-659 1.14e-16

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 81.97  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS---RRLEA-NTQREVAALRLCQsHPNVVNLHEV----HHDQLH-TYLVLELLR 480
Cdd:cd07849   13 IGEGAYGMVCSAVHKPTGQKVAIKKISpfeHQTYClRTLREIKILLRFK-HENIIGILDIqrppTFESFKdVYIVQELME 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLehIRKKRHFSESEAS----QILRSLvsavSFMHEeAGVVHRDLKPENIL--YADDtpgapVKIIDFGFARLR-PQ 553
Cdd:cd07849   92 TDLYK--LIKTQHLSNDHIQyflyQILRGL----KYIHS-ANVLHRDLKPSNLLlnTNCD-----LKICDFGLARIAdPE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTP-CFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS---------GQGGQSQAAEIMC--- 619
Cdd:cd07849  160 HDHTGFLTEyVATRWYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDylhqlnlilGILGTPSQEDLNCiis 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 620 -KIREGRFSL---DGEAWQ----GVSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd07849  240 lKARNYIKSLpfkPKVPWNklfpNADPKALDLLDKMLTFNPHKRITVE 287
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
410-667 1.20e-16

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 80.65  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQR--QSGQEFAVKILSRRLEA-NTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLe 486
Cdd:cd14112   11 IFRGRFSVIVKAVDSttETDAHCAVKIFEVSDEAsEAVREFESLRTLQ-HENVQRLIAAFKPSNFAYLVMEKLQEDVFT- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdTPGAPVKIIDFGFARlrPQSPGVpMQTPCFTL 566
Cdd:cd14112   89 RFSSNDYYSEEQVATTVRQILDALHYLHFK-GIAHLDVQPDNIMFQS-VRSWQVKLVDFGRAQ--KVSKLG-KVPVDGDT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 567 QYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIregRFSLdgeAWQGVSEEAKELVR 645
Cdd:cd14112  164 DWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENVIFVKC---RPNL---IFVEATQEALRFAT 237
                        250       260
                 ....*....|....*....|..
gi 663856869 646 GLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14112  238 WALKKSPTRRMRTDEALEHRWL 259
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
122-284 1.35e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 80.38  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE-GHIVLTDFGlSKEFLteeKERTFS-FCG 199
Cdd:cd14102   91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLIDFG-SGALL---KDTVYTdFDG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFtlegerntqaEVSRRILKCSPPFPPRIGPVAQDLLQRLLCK 279
Cdd:cd14102  167 TRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPF----------EQDEEILRGRLYFRRRVSPECQQLIKWCLSL 236

                 ....*
gi 663856869 280 DPKKR 284
Cdd:cd14102  237 RPSDR 241
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
31-333 1.44e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 81.33  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLV--RKAGGHDAGKLYAMKVlrKAALVQRAktqehTRtERSVLELVRqAPFLVTLHYAFQTD 108
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVlhRPSGLIMARKLIHLEI--KPAIRNQI-----IR-ELKVLHECN-SPYIVGFYGAFYSD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMfthlyqRQYFKEAEvRV---YGGEIVLA----LEHLH-KLGIIYRDLKLENVLLDSEGHIVLTDF 180
Cdd:cd06615   72 GEISICMEHMDGGSL------DQVLKKAG-RIpenILGKISIAvlrgLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEFLTEEKErtfSFCGTIEYMAPEIIrskTGHGKAV--DWWSLGILLFELLTGASPF------TLEGERNTQ----- 247
Cdd:cd06615  145 GVSGQLIDSMAN---SFVGTRSYMSPERL---QGTHYTVqsDIWSLGLSLVEMAIGRYPIpppdakELEAMFGRPvsege 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 248 AEVSRRILKCSPP--------F----------PPRI-----GPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFFQgl 304
Cdd:cd06615  219 AKESHRPVSGHPPdsprpmaiFelldyivnepPPKLpsgafSDEFQDFVDKCLKKNPKERADLK-----ELTKHPFIK-- 291
                        330       340
                 ....*....|....*....|....*....
gi 663856869 305 dwvalaarkipapfrpqiRSELDVGNFAE 333
Cdd:cd06615  292 ------------------RAELEEVDFAG 302
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
410-644 1.46e-16

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 82.03  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsRRLEANTQREVAALR-----LCQSHPN-VVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05627   10 IGRGAFGEVRLVQKKDTGHIYAMKIL-RKADMLEKEQVAHIRaerdiLVEADGAwVVKMFYSFQDKRNLYLIMEFLPGGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYadDTPGApVKIIDFG------------FARLR 551
Cdd:cd05627   89 MMTLLMKKDTLSEEATQFYIAETVLAIDAIH-QLGFIHRDIKPDNLLL--DAKGH-VKLSDFGlctglkkahrteFYRNL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 552 PQSPGVPMQ----------------------TPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQg 609
Cdd:cd05627  165 THNPPSDFSfqnmnskrkaetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQ- 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 610 gqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd05627  244 ------ETYRKVMNWKETLVFPPEVPISEKAKDLI 272
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
410-603 1.67e-16

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 81.46  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL--------SRRLEANTQREVAalrlcQSHPN----VVNLHEV--HHDqlHTYLV 475
Cdd:cd14134   20 LGEGTFGKVLECWDRKRKRYVAVKIIrnvekyreAAKIEIDVLETLA-----EKDPNgkshCVQLRDWfdYRG--HMCIV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLehIRKKRH---FSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDT----------------P 536
Cdd:cd14134   93 FELLGPSLYD--FLKKNNygpFPLEHVQHIAKQLLEAVAFLHD-LKLTHTDLKPENILLVDSDyvkvynpkkkrqirvpK 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 537 GAPVKIIDFGFArlrpqspgvpmqtpCF----------TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14134  170 STDIKLIDFGSA--------------TFddeyhssivsTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQ 232
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
501-655 1.75e-16

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 80.14  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLvsavSFMHEEAgVVHRDLKPENILYadDTPGAPVKIIDFGFA-RLrpqsPGVPMQTPCF--TLQYAAPELLA-- 575
Cdd:cd06624  116 QILEGL----KYLHDNK-IVHRDIKGDNVLV--NTYSGVVKISDFGTSkRL----AGINPCTETFtgTLQYMAPEVIDkg 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 576 QQGYDESCDLWSLGVILYMMLSGQVPFQgasgQGGQSQAAeiMCKIreGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd06624  185 QRGYGPPADIWSLGCTIIEMATGKPPFI----ELGEPQAA--MFKV--GMFKIHPEIPESLSEEAKSFILRCFEPDPDKR 256
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
410-644 1.83e-16

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 82.01  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsRRLEANTQREVAALR-----LCQSHPN-VVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05628    9 IGRGAFGEVRLVQKKDTGHVYAMKIL-RKADMLEKEQVGHIRaerdiLVEADSLwVVKMFYSFQDKLNLYLIMEFLPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYadDTPGApVKIIDFG----------------- 546
Cdd:cd05628   88 MMTLLMKKDTLTEEETQFYIAETVLAIDSIH-QLGFIHRDIKPDNLLL--DSKGH-VKLSDFGlctglkkahrtefyrnl 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 547 ---------------------FARLRPQSPGVPMQTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGA 605
Cdd:cd05628  164 nhslpsdftfqnmnskrkaetWKRNRRQLAFSTVGTP----DYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 606 SGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:cd05628  240 TPQ-------ETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
33-301 1.87e-16

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 81.57  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAalVQRAktqEHT-RTERSvLELVR--QAPFLVTLHYAFQTDA 109
Cdd:cd07851   17 YQNLSPVGSGAYGQVCSAFDTKT---GRKVAIKKLSRP--FQSA---IHAkRTYRE-LRLLKhmKHENVIGLLDVFTPAS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILD-YVSGGEMFTHLYQ---RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd07851   88 SLEDFQDvYLVTHLMGADLNNivkCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 fltEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF-------------------TLEGERNT 246
Cdd:cd07851  168 ---TDDEMT-GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFpgsdhidqlkrimnlvgtpDEELLKKI 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 247 QAEVSRRILKCSPPFP--------PRIGPVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd07851  244 SSESARNYIQSLPQMPkkdfkevfSGANPLAIDLLEKMLVLDPDKRITAA-----EALAHPYL 301
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
431-677 2.11e-16

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 81.67  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 431 AVKILSRRLEANTQ-----REVAALRlCQSHPNVVNLHEVHHDQ------LHTYLVLELLRGGELLEhirKKRHFSESEA 499
Cdd:cd07874   46 AIKKLSRPFQNQTHakrayRELVLMK-CVNHKNIISLLNVFTPQksleefQDVYLVMELMDANLCQV---IQMELDHERM 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPgvpMQTP-CFTLQYAAPELLAQQG 578
Cdd:cd07874  122 SYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSD---CTLKILDFGLARTAGTSF---MMTPyVVTRYYRAPEVILGMG 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 579 YDESCDLWSLGVILYMMLSGQVPFQGAS---------GQGGqSQAAEIMCKIR-------EGR----------------F 626
Cdd:cd07874  195 YKENVDIWSVGCIMGEMVRHKILFPGRDyidqwnkviEQLG-TPCPEFMKKLQptvrnyvENRpkyagltfpklfpdslF 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 627 SLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRG----SSWLQDGSARSSPP 677
Cdd:cd07874  274 PADSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQhpyiNVWYDPAEVEAPPP 328
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
407-667 2.14e-16

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 79.31  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFsvcrRCRQRQSGQEFAVKILSRRLeanTQREVAALRLCQSHPNVVNLHEVHHDQLHTYlVLELLRGGELLE 486
Cdd:cd14022    2 EPLEGDHVF----RAVHLHSGEELVCKVFDIGC---YQESLAPCFCLPAHSNINQITEIILGETKAY-VFFERSYGDMHS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPgAPVKIIDFGFAR-LRPQSPGVPMQTPCFT 565
Cdd:cd14022   74 FVRTCKKLREEEAARLFYQIASAVAHCHD-GGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYiLRGHDDSLSDKHGCPA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 lqYAAPELLAQQGY--DESCDLWSLGVILYMMLSGQVPFQGAsgqggqsQAAEIMCKIREGRFSLDgeawQGVSEEAKEL 643
Cdd:cd14022  152 --YVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDI-------EPSSLFSKIRRGQFNIP----ETLSPKAKCL 218
                        250       260
                 ....*....|....*....|....
gi 663856869 644 VRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14022  219 IRSILRREPSERLTSQEILDHPWF 242
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
18-304 2.15e-16

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 81.15  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  18 EANLTGHEEKvsvENFELLKVLGTGAYGKV--FLVRKAGGHDAGK---------LYAMKVLRKAALVQraktqeHTRTEr 86
Cdd:cd07880    5 EVNKTIWEVP---DRYRDLKQVGSGAYGTVcsALDRRTGAKVAIKklyrpfqseLFAKRAYRELRLLK------HMKHE- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  87 SVLELVRqapflvtlhyAFQTDAKL------HLILDYVsgGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYR 160
Cdd:cd07880   75 NVIGLLD----------VFTPDLSLdrfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 161 DLKLENVLLDSEGHIVLTDFGLSKEfltEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF-- 238
Cdd:cd07880  143 DLKPGNLAVNEDCELKILDFGLARQ---TDSEMT-GYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFkg 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 239 -----------------TLEGERNTQAEVSRRILKCSPPFP--------PRIGPVAQDLLQRLLCKDPKKRLGAGpqgaq 293
Cdd:cd07880  219 hdhldqlmeimkvtgtpSKEFVQKLQSEDAKNYVKKLPRFRkkdfrsllPNANPLAVNVLEKMLVLDAESRITAA----- 293
                        330
                 ....*....|.
gi 663856869 294 EVRNHPFFQGL 304
Cdd:cd07880  294 EALAHPYFEEF 304
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
31-301 2.31e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 81.25  E-value: 2.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVflvrkagghdaGKLYAMKVLRKAALVQRAKTQE---HTRTERSVLELVRqapflvtlHYAFQT 107
Cdd:cd07878   15 ERYQNLTPVGSGAYGSV-----------CSAYDTRLRQKVAVKKLSRPFQsliHARRTYRELRLLK--------HMKHEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLY--------------QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd07878   76 VIGLLDVFTPATSIENFNEVYlvtnlmgadlnnivKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKEfltEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF--------------- 238
Cdd:cd07878  156 ELRILDFGLARQ---ADDEMT-GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFpgndyidqlkrimev 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 239 ----TLEGERNTQAEVSRRILKCSPPFPPR--------IGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07878  232 vgtpSPEVLKKISSEHARKYIQSLPHMPQQdlkkifrgANPLAIDLLEKMLVLDSDKRI-----SASEALAHPYF 301
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
410-659 2.39e-16

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 80.91  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-VCR-RCRQRQSGQEFAVK---------ILSRRleanTQREVAALRLCQSHPNVVNLHE---VHHDQLHTYLV 475
Cdd:cd07857    8 LGQGAYGiVCSaRNAETSEEETVAIKkitnvfskkILAKR----ALRELKLLRHFRGHKNITCLYDmdiVFPGNFNELYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYaddTPGAPVKIIDFGFARlrPQSP 555
Cdd:cd07857   84 YEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHS-ANVLHRDLKPGNLLV---NADCELKICDFGLAR--GFSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 556 GvPMQTPCF------TLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS--GQGGQ------SQAAEIMCK 620
Cdd:cd07857  158 N-PGENAGFmteyvaTRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDyvDQLNQilqvlgTPDEETLSR 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 621 IREGR-----FSLD-------GEAWQGVSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd07857  237 IGSPKaqnyiRSLPnipkkpfESIFPNANPLALDLLEKLLAFDPTKRISVE 287
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
431-682 2.40e-16

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 81.63  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 431 AVKILSRRLEANTQ-----REVAALRlCQSHPNVVNLHEVHHDQ------LHTYLVLELLRGGELLEhirKKRHFSESEA 499
Cdd:cd07875   53 AIKKLSRPFQNQTHakrayRELVLMK-CVNHKNIIGLLNVFTPQksleefQDVYIVMELMDANLCQV---IQMELDHERM 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpgVPMQTPCFTLQYAAPELLAQQGY 579
Cdd:cd07875  129 SYLLYQMLCGIKHLHS-AGIIHRDLKPSNIVVKSD---CTLKILDFGLARTAGTS--FMMTPYVVTRYYRAPEVILGMGY 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 580 DESCDLWSLGVILYMMLSGQVPFQGAS---------GQGGqSQAAEIMCKIR-------EGR----------------FS 627
Cdd:cd07875  203 KENVDIWSVGCIMGEMIKGGVLFPGTDhidqwnkviEQLG-TPCPEFMKKLQptvrtyvENRpkyagysfeklfpdvlFP 281
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 628 LDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQ---DGSARSSPPLRTPD 682
Cdd:cd07875  282 ADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINvwyDPSEAEAPPPKIPD 339
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
399-669 2.43e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 80.50  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 399 MQYELDLRE----PALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA-NTQREVAALR-LCQSH--PNVVNLHEVHHDQL 470
Cdd:cd06618    8 KKYKADLNDlenlGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKeENKRILMDLDvVLKSHdcPYIVKCYGYFITDS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFA-R 549
Cdd:cd06618   88 DVFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILLDES---GNVKLCDFGISgR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 L-----RPQSPGVPMqtpcftlqYAAPELLAQQG---YDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaAEIMCKI 621
Cdd:cd06618  165 LvdskaKTRSAGCAA--------YMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRNCKTE------FEVLTKI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 622 -REGRFSLDGEawQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQD 669
Cdd:cd06618  231 lNEEPPSLPPN--EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRR 277
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
38-301 2.44e-16

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 79.58  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFlvrKAGGHDAGKLYAMKV--LRKAALVQRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAKLHLIL 115
Cdd:cd13983    8 VLGRGSFKTVY---RAFDTEEGIEVAWNEikLRKLPKAERQRFKQEIEILKSL-----KHPNIIKFYDSWESKSKKEVIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 --DYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLLD-SEGHIVLTDFGLSKEfltEE 190
Cdd:cd13983   80 itELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATL---LR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKtgHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVSRRILKCSPP--FPPRIGPV 268
Cdd:cd13983  157 QSFAKSVIGTPEFMAPEMYEEH--YDEKVDIYAFGMCLLEMATGEYPY---SECTNAAQIYKKVTSGIKPesLSKVKDPE 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 269 AQDLLQRLLCKdPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd13983  232 LKDFIEKCLKP-PDERP-----SARELLEHPFF 258
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
39-284 2.76e-16

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 79.86  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAalvqRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14154    1 LGKGFFGQAI---KVTHRETGEVMVMKELIRF----DEEAQRNFLKEVKVMRSL-DHPNVLKFIGVLYKDKKLNLITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEM--FTHLYQRQYFKEAEVRvYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKERT-- 194
Cdd:cd14154   73 PGGTLkdVLKDMARPLPWAQRVR-FAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLAR-LIVEERLPSgn 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 ------------------FSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGAS------PFTLEGERNTQAEV 250
Cdd:cd14154  151 mspsetlrhlkspdrkkrYTVVGNPYWMAPEMLNGRS-YDEKVDIFSFGIVLCEIIGRVEadpdylPRTKDFGLNVDSFR 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 251 SRRILKCSPPFPPrIGPVAQDLlqrllckDPKKR 284
Cdd:cd14154  230 EKFCAGCPPPFFK-LAFLCCDL-------DPEKR 255
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
400-667 2.76e-16

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 79.99  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdlrEPALGQGSFSVCRRCRQRQSGQEFAVKILSRR------------------------------LEANTQrEVAA 449
Cdd:cd14200    1 QYKL---QSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKkllkqygfprrppprgskaaqgeqakplapLERVYQ-EIAI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 450 LRLCqSHPNVVNLHEVHHD--QLHTYLVLELLRGGELLeHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPE 527
Cdd:cd14200   77 LKKL-DHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQK-IVHRDIKPS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 528 NILYADDtpgAPVKIIDFGFARlrpQSPGVPMQ------TPCFTlqyaAPELLAQQGYD---ESCDLWSLGVILYMMLSG 598
Cdd:cd14200  154 NLLLGDD---GHVKIADFGVSN---QFEGNDALlsstagTPAFM----APETLSDSGQSfsgKALDVWAMGVTLYCFVYG 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 599 QVPFQgasgqggQSQAAEIMCKIREGRFSLDGEAwqGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14200  224 KCPFI-------DEFILALHNKIKNKPVEFPEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
410-624 2.83e-16

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 79.51  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEF---AVKILSRRLEANTQREVAA-LRLCQS--HPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd00192    3 LGEGAFGEVYKGKLKGGDGKTvdvAVKTLKEDASESERKDFLKeARVMKKlgHPNVVRLLGVCTEEEPLYLVMEYMEGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILrSLVSAVSFMHEEA---------GVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQS 554
Cdd:cd00192   83 LLDFLRKSRPVFPSPEPSTL-SLKDLLSFAIQIAkgmeylaskKFVHRDLAARNCLVGED---LVVKISDFGLSRDIYDD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 555 PGVPMQTPC-FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaaEIMCKIREG 624
Cdd:cd00192  159 DYYRKKTGGkLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNE-------EVLEYLRKG 223
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
36-301 3.04e-16

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 80.01  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLrkaalvqraktqeHTRTERSV-LELVRQAPFL--------VTLHYAFQ 106
Cdd:cd07870    5 LEKLGEGSYATVY---KGISRINGQLVALKVI-------------SMKTEEGVpFTAIREASLLkglkhaniVLLHDIIH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYvsggeMFTHL--YQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd07870   69 TKETLTFVFEY-----MHTDLaqYMIQHpggLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKEflTEEKERTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRIL----- 255
Cdd:cd07870  144 LARA--KSIPSQTYSSeVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIWTVLgvpte 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 256 --------------KCSPPFPPRI----------GPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07870  222 dtwpgvsklpnykpEWFLPCKPQQlrvvwkrlsrPPKAEDLASQMLMMFPKDRI-----SAQDALLHPYF 286
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
402-607 3.48e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 79.32  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPAL----GQGSFSvcRRCRQRQSGQEFAVKI--------LSRRLEanTQREVAALRLCQSHPNVVNLHEVHHDQ 469
Cdd:cd14145    2 EIDFSELVLeeiiGIGGFG--KVYRAIWIGDEVAVKAarhdpdedISQTIE--NVRQEAKLFAMLKHPNIIALRGVCLKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 470 LHTYLVLELLRGGELLEHIRKKR---HFSESEASQILRslvsAVSFMHEEA--GVVHRDLKPENILYA-----DDTPGAP 539
Cdd:cd14145   78 PNLCLVMEFARGGPLNRVLSGKRippDILVNWAVQIAR----GMNYLHCEAivPVIHRDLKSSNILILekvenGDLSNKI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 540 VKIIDFGFARLRPQSPGVpmqTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14145  154 LKITDFGLAREWHRTTKM---SAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDG 218
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
410-655 3.48e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 79.86  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-IL----SRRLEANTQREVAALRLCQsHPNVVNLHE--VHHDQLHTYLVLELLRGG 482
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKkILikkvTKRDCMKVLREVKVLAGLQ-HPNIVGYHTawMEHVQLMLYIQMQLCELS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESE-------------ASQILRSLVSAVSFMHEEaGVVHRDLKPENI-LYADDTPgapVKIIDFGFA 548
Cdd:cd14049   93 LWDWIVERNKRPCEEEfksapytpvdvdvTTKILQQLLEGVTYIHSM-GIVHRDLKPRNIfLHGSDIH---VRIGDFGLA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 -----------RLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLsgqVPFqgasgqGGQSQAAEI 617
Cdd:cd14049  169 cpdilqdgndsTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPF------GTEMERAEV 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 663856869 618 MCKIREGRF--SLDgEAWQgvseEAKELVRGLLTVDPAKR 655
Cdd:cd14049  240 LTQLRNGQIpkSLC-KRWP----VQAKYIKLLTSTEPSER 274
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
501-673 3.83e-16

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 80.94  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLvsavSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELL-AQQGY 579
Cdd:cd07853  111 QILRGL----KYLHS-AGILHRDIKPGNLLVNSN---CVLKICDFGLARVEEPDESKHMTQEVVTQYYRAPEILmGSRHY 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 580 DESCDLWSLGVILYMMLSGQVPFQGAS------------------GQGGQSQAAEIMC-------KIREGRFSLDGEAwq 634
Cdd:cd07853  183 TSAVDIWSVGCIFAELLGRRILFQAQSpiqqldlitdllgtpsleAMRSACEGARAHIlrgphkpPSLPVLYTLSSQA-- 260
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 663856869 635 gvSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSAR 673
Cdd:cd07853  261 --THEAVHLLCRMLVFDPDKRISAADALAHPYLDEGRLR 297
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
410-609 4.84e-16

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 80.10  E-value: 4.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK---------ILSRRleanTQREVAALRLCQsHPNVVNLHEV------HHDQLHTYL 474
Cdd:cd07855   13 IGSGAYGVVCSAIDTKSGQKVAIKkipnafdvvTTAKR----TLRELKILRHFK-HDNIIAIRDIlrpkvpYADFKDVYV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGElleH--IRKKRHFSESEAS----QILRSLvsavSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFA 548
Cdd:cd07855   88 VLDLMESDL---HhiIHSDQPLTLEHIRyflyQLLRGL----KYIHS-ANVIHRDLKPSNLLVNEN---CELKIGDFGMA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 549 RLRPQSP---GVPMQTPCFTLQYAAPEL-LAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQG 609
Cdd:cd07855  157 RGLCTSPeehKYFMTEYVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVH 221
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
30-301 4.87e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 79.28  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDA 109
Cdd:cd07871    4 LETYVKLDKLGEGTYATVF---KGRSKLTENLVALKEIR---LEHEEGAPCTAIREVSLLKNLKHAN-IVTLHDIIHTER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGemfthlyQRQYFKEA-------EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd07871   77 CLTLVFEYLDSD-------LKQYLDNCgnlmsmhNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKerTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF---TLEGERN------------- 245
Cdd:cd07871  150 ARAKSVPTK--TYSNeVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFpgsTVKEELHlifrllgtpteet 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 246 -----TQAEVSRRILKCSPPFP-----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07871  228 wpgvtSNEEFRSYLFPQYRAQPlinhaPRLDTDGIDLLSSLLLYETKSRI-----SAEAALRHSYF 288
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
410-603 5.57e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 78.49  E-value: 5.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKilSRRLEANTQREVAALRLCQS--------HPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14148    2 IGVGGFGKVYKGLWR--GEEVAVK--AARQDPDEDIAVTAENVRQEarlfwmlqHPNIIALRGVCLNPPHLCLVMEYARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKR---HFSESEASQILRSLvsavSFMHEEAGV--VHRDLKPENILYA-----DDTPGAPVKIIDFGFARLR 551
Cdd:cd14148   78 GALNRALAGKKvppHVLVNWAVQIARGM----NYLHNEAIVpiIHRDLKSSNILILepienDDLSGKTLKITDFGLAREW 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 552 PQSPGVpmqTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14148  154 HKTTKM---SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYR 202
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
488-656 5.83e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 78.74  E-value: 5.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHeEAGVVHRDLKPENILYadDTPGAPVKIIDFGFARlrpqspgvPMQTPCF--- 564
Cdd:PHA03390 100 LKKEGKLSEAEVKKIIRQLVEALNDLH-KHNIIHNDIKLENVLY--DRAKDRIYLCDYGLCK--------IIGTPSCydg 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELV 644
Cdd:PHA03390 169 TLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDE-------ELDLESLLKRQQKKLPFIKNVSKNANDFV 241
                        170
                 ....*....|..
gi 663856869 645 RGLLTVDPAKRL 656
Cdd:PHA03390 242 QSMLKYNINYRL 253
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
32-301 5.85e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 79.01  E-value: 5.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLR---------KAALvqraktqehtrTERSVLELVRQaPFLVTLH 102
Cdd:cd07839    1 KYEKLEKIGEGTYGTVF---KAKNRETHEIVALKRVRlddddegvpSSAL-----------REICLLKELKH-KNIVRLY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAKLHLILDYVS----------GGEMFTHLyqrqyfkeaeVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE 172
Cdd:cd07839   66 DVLHSDKKLTLVFEYCDqdlkkyfdscNGDIDPEI----------VKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GHIVLTDFGLSKEFLTeeKERTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASP-------------- 237
Cdd:cd07839  136 GELKLADFGLARAFGI--PVRCYSAeVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPlfpgndvddqlkri 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 238 FTLEGERNTQAEVSRRILKCSPPFP------------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07839  214 FRLLGTPTEESWPGVSKLPDYKPYPmypattslvnvvPKLNSTGRDLLQNLLVCNPVQRI-----SAEEALQHPYF 284
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
42-287 6.10e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 78.51  E-value: 6.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  42 GAYGKVFLV--RKAGGHDAGKLYAMKVLRKAALvqraKTQEHTRTERsvlelvrqapfLVTLHYAFQTDAKLHLILDYVS 119
Cdd:cd13995   15 GAFGKVYLAqdTKTKKRMACKLIPVEQFKPSDV----EIQACFRHEN-----------IAELYGALLWEETVHLFMEAGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 120 GGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSeGHIVLTDFGLSKEfLTEEKERTFSFCG 199
Cdd:cd13995   80 GGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS-TKAVLVDFGLSVQ-MTEDVYVPKDLRG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKtGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPF---PPRIGPVAQDLLQRL 276
Cdd:cd13995  158 TEIYMSPEVILCR-GHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLediAQDCSPAMRELLEAA 236
                        250
                 ....*....|.
gi 663856869 277 LCKDPKKRLGA 287
Cdd:cd13995  237 LERNPNHRSSA 247
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
410-606 6.66e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 79.01  E-value: 6.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE-------ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIVALKRV--RLDdddegvpSSALREICLLKELK-HKNIVRLYDVLHSDKKLTLVFEYCDQD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 EllehirkKRHFSESEAS---QILRS----LVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARlrpqSP 555
Cdd:cd07839   85 L-------KKYFDSCNGDidpEIVKSfmfqLLKGLAFCHSH-NVLHRDLKPQNLLINKN---GELKLADFGLAR----AF 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 556 GVPMQtpCF-----TLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVP-FQGAS 606
Cdd:cd07839  150 GIPVR--CYsaevvTLWYRPPDvLFGAKLYSTSIDMWSAGCIFAELANAGRPlFPGND 205
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
33-301 6.66e-16

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 78.96  E-value: 6.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAKLH 112
Cdd:cd07844    2 YKKLDKLGEGSYATVY---KGRSKLTGQLVALKEIR---LEHEEGAPFTAIREASLLKDLKHAN-IVTLHDIIHTKKTLT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSggemfTHLyqRQYFKE-------AEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL--S 183
Cdd:cd07844   75 LVFEYLD-----TDL--KQYMDDcggglsmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLarA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KEFLTeekeRTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSR--RIL----- 255
Cdd:cd07844  148 KSVPS----KTYSNeVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFP--GSTDVEDQLHKifRVLgtpte 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 256 -----------------KCSPPFP-----PRIGPV--AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07844  222 etwpgvssnpefkpysfPFYPPRPlinhaPRLDRIphGEELALKFLQYEPKKRI-----SAAEAMKHPYF 286
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
410-638 6.90e-16

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 78.85  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQ---------LHTYLVL 476
Cdd:cd07870    8 LGEGSYATVYKGISRINGQLVALKVISMKTEEGVPftaiREASLLKGLK-HANIVLLHDIIHTKetltfvfeyMHTDLAQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLeHIRKKRHFseseASQILRSLvsavSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARlrpqSPG 556
Cdd:cd07870   87 YMIQHPGGL-HPYNVRLF----MFQLLRGL----AYIHGQH-ILHRDLKPQNLLI---SYLGELKLADFGLAR----AKS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGRFSLDGEA 632
Cdd:cd07870  150 IPSQTyssEVVTLWYRPPDvLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGV------SDVFEQLEKIWTVLGVPTEDT 223

                 ....*.
gi 663856869 633 WQGVSE 638
Cdd:cd07870  224 WPGVSK 229
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
32-301 7.08e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 78.62  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRT-ERSVL-ELvrQAPFLVTLHYAFQTDA 109
Cdd:cd07861    1 DYTKIEKIGEGTYGVVY---KGRNKKTGQIVAMKKIR---LESEEEGVPSTAIrEISLLkEL--QHPNIVCLEDVLMQEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGG--EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd07861   73 RLYLVFEFLSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 TEEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSrRILKC---------- 257
Cdd:cd07861  153 IPVRVYTHEVV-TLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIF-RILGTptediwpgvt 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 258 -----SPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07861  231 slpdyKNTFPkwkkgslrtavKNLDEDGLDLLEKMLIYDPAKRI-----SAKKALVHPYF 285
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
33-301 7.58e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 78.85  E-value: 7.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQAPF-------LVTLHYAF 105
Cdd:cd07863    2 YEPVAEIGVGAYGTVY---KARDPHSGHFVALKSVR----VQTNEDGLPLSTVREVALLKRLEAFdhpnivrLMDVCATS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILdyvsggeMFTHLYQ--RQYFKEA--------EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHI 175
Cdd:cd07863   75 RTDRETKVTL-------VFEHVDQdlRTYLDKVpppglpaeTIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 176 VLTDFGLSkeflteekeRTFSF-------CGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFE------LLTGASP----- 237
Cdd:cd07863  148 KLADFGLA---------RIYSCqmaltpvVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEmfrrkpLFCGNSEadqlg 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 238 --FTL-----EGERNTQAEVSRRILKCSPPFP-----PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd07863  218 kiFDLiglppEDDWPRDVTLPRGAFSPRGPRPvqsvvPEIEESGAQLLLEMLTFNPHKRI-----SAFRALQHPFF 288
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
410-624 9.21e-16

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 77.77  E-value: 9.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRRCRQRQSGQEF--AVKILSRRLEANTQREV--AALRLCQ-SHPNVVNLHEV-HHDQLhtYLVLELLRGG 482
Cdd:cd05060    3 LGHGNFgSVRKGVYLMKSGKEVevAVKTLKQEHEKAGKKEFlrEASVMAQlDHPCIVRLIGVcKGEPL--MLVMELAPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEasqiLRSLVSAVSF-MH--EEAGVVHRDLKPENILYADDTPgapVKIIDFGFAR-LRPQSPGVP 558
Cdd:cd05060   81 PLLKYLKKRREIPVSD----LKELAHQVAMgMAylESKHFVHRDLAARNVLLVNRHQ---AKISDFGMSRaLGAGSDYYR 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 559 MQT----PcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGqggqsqaAEIMCKIREG 624
Cdd:cd05060  154 ATTagrwP---LKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKG-------PEVIAMLESG 214
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
410-604 9.28e-16

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 79.32  E-value: 9.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRRCRQRQSgQEFAVKILSRRLEA--NTQREVAALRLCQ--SHPNVVNLHEVH------HDQLHTYLVLEL 478
Cdd:cd07878   23 VGSGAYgSVCSAYDTRLR-QKVAVKKLSRPFQSliHARRTYRELRLLKhmKHENVIGLLDVFtpatsiENFNEVYLVTNL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELleHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpgvp 558
Cdd:cd07878  102 MGADLN--NIVKCQKLSDEHVQFLIYQLLRGLKYIHS-AGIIHRDLKPSNVAVNED---CELRILDFGLARQADDE---- 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 559 MQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07878  172 MTGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLKGKALFPG 218
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
148-304 9.75e-16

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 79.05  E-value: 9.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 148 ALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTF--SFCGTIEYMAPEIIRS-KTGHGKAVDWWSL 224
Cdd:cd07859  115 ALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFwtDYVATRWYRAPELCGSfFSKYTPAIDIWSI 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 225 GILLFELLTG----------------------ASPFTLEGERNTQAEVSRRILKCSPPFP-----PRIGPVAQDLLQRLL 277
Cdd:cd07859  195 GCIFAEVLTGkplfpgknvvhqldlitdllgtPSPETISRVRNEKARRYLSSMRKKQPVPfsqkfPNADPLALRLLERLL 274
                        170       180
                 ....*....|....*....|....*..
gi 663856869 278 CKDPKKRlgagpQGAQEVRNHPFFQGL 304
Cdd:cd07859  275 AFDPKDR-----PTAEEALADPYFKGL 296
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
410-606 9.79e-16

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 78.51  E-value: 9.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE------ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEI--RLEheegapCTAIREVSLLKNLK-HANIVTLHDIIHTERCLTLVFEYLDSDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRpqspGVPMQT-- 561
Cdd:cd07871   90 KQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRK-ILHRDLKPQNLLINEK---GELKLADFGLARAK----SVPTKTys 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 562 -PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07871  162 nEVVTLWYRPPDvLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGST 208
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
409-604 1.00e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 78.56  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEANTQR---EVAALRLCQSHPNVVN----------------LHEVHHD 468
Cdd:cd06616   13 EIGRGAFGTVNKMLHKPSGTIMAVKrIRSTVDEKEQKRllmDLDVVMRSSDCPYIVKfygalfregdcwicmeLMDISLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 469 QLHTYLvlellrggelleHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYadDTPGApVKIIDFGFA 548
Cdd:cd06616   93 KFYKYV------------YEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILL--DRNGN-IKLCDFGIS 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 RLRPQSPGVPMQTPCftLQYAAPELL----AQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd06616  158 GQLVDSIAKTRDAGC--RPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPK 215
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
410-661 1.19e-15

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 79.66  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEAN---TQREVAALrlcQSHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05622   81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAffwEERDIMAF---ANSPWVVQLFYAFQDDRYLYMVMEYMPG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLeHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGVPMQT 561
Cdd:cd05622  158 GDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHS-MGFIHRDVKPDNMLL--DKSGH-LKLADFGTCMKMNKEGMVRCDT 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQG----YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSqaaeimcKIREGRFSLDGEAWQGVS 637
Cdd:cd05622  233 AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYS-------KIMNHKNSLTFPDDNDIS 305
                        250       260
                 ....*....|....*....|....
gi 663856869 638 EEAKELVRGLLTvDPAKRLKLEGL 661
Cdd:cd05622  306 KEAKNLICAFLT-DREVRLGRNGV 328
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
389-655 1.31e-15

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 78.87  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 389 GRAAVARSAMMQYeldlrePALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEantqrevaalrlcqsHPNVVNLHEVHHD 468
Cdd:PTZ00426  44 GRVILATYKNEDF------PPVAIKRFEKSKIIKQKQVDHVFSERKILNYIN---------------HPFCVNLYGSFKD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 469 QLHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFA 548
Cdd:PTZ00426 103 ESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYL-QSLNIVYRDLKPENLLLDKD---GFIKMTDFGFA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 RLRPQSpgvpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGasgqggqSQAAEIMCKIREGRFSL 628
Cdd:PTZ00426 179 KVVDTR----TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYA-------NEPLLIYQKILEGIIYF 247
                        250       260
                 ....*....|....*....|....*..
gi 663856869 629 DgeawQGVSEEAKELVRGLLTVDPAKR 655
Cdd:PTZ00426 248 P----KFLDNNCKHLMKKLLSHDLTKR 270
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
410-626 1.39e-15

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 77.19  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   410 LGQGSFSVCRRCRQRQSG----QEFAVKILsrRLEANTQ------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:smart00219   7 LGEGAFGEVYKGKLKGKGgkkkVEVAVKTL--KEDASEQqieeflREARIMRKLD-HPNVVKLLGVCTEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   480 RGGELLEHIRKKRH-FSESE----ASQILRslvsAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQS 554
Cdd:smart00219  84 EGGDLLSYLRKNRPkLSLSDllsfALQIAR----GMEYLESK-NFIHRDLAARNCLVGENL---VVKISDFGLSRDLYDD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869   555 PGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaaEIMCKIREGRF 626
Cdd:smart00219 156 DYYRKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNE-------EVLEYLKNGYR 221
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
33-243 1.39e-15

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 79.41  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQRaKTQEHTRtersVLELVRQAPFLVTL-------HYAF 105
Cdd:cd14224   67 YEVLKVIGKGSFGQVV---KAYDHKTHQHVALKMVRNEKRFHR-QAAEEIR----ILEHLKKQDKDNTMnvihmleSFTF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTdaklHLILDYvsggEMFT-HLYQR------QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH--IV 176
Cdd:cd14224  139 RN----HICMTF----ELLSmNLYELikknkfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIK 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 177 LTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTLEGE 243
Cdd:cd14224  211 VIDFGSS----CYEHQRIYTYIQSRFYRAPEVILG-ARYGMPIDMWSFGCILAELLTGYPLFPGEDE 272
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
410-659 1.41e-15

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 77.26  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSV-------CRRCRQRQSGQEFAVK-ILSRRLEANTQREVAALRLCQSHPNVVNL-----HEVH---------H 467
Cdd:cd14019    9 IGEGTFSSvykaedkLHDLYDRNKGRLVALKhIYPTSSPSRILNELECLERLGGSNNVSGLitafrNEDQvvavlpyieH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 468 DQLHTYLvlellrggellehirkkRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDT-PGApvkIIDFG 546
Cdd:cd14019   89 DDFRDFY-----------------RKMSLTDIRIYLRNLFKALKHVHS-FGIIHRDVKPGNFLYNRETgKGV---LVDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 547 FARLRPQSPgvPMQTPCF-TLQYAAPELLAQQGyDESC--DLWSLGVILYMMLSGQVP-FQGASGQGGqsqAAEIMCkIR 622
Cdd:cd14019  148 LAQREEDRP--EQRAPRAgTRGFRAPEVLFKCP-HQTTaiDIWSAGVILLSILSGRFPfFFSSDDIDA---LAEIAT-IF 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 663856869 623 eGrfsldgeawqgvSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd14019  221 -G------------SDEAYDLLDKLLELDPSKRITAE 244
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
31-263 1.42e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 77.81  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVR-KAGGHDAGKLYAMKVLrkaalvQRAKTQEHTRTERSVLELVR--QAPFLVTLHYAFQT 107
Cdd:cd05038    4 RHLKFIKQLGEGHFGSVELCRyDPLGDNTGEQVAVKSL------QPSGEEQHMSDFKREIEILRtlDHEYIVKYKGVCES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAK--LHLILDYVSGGEmFTHLYQRQYFKEAEVRV--YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd05038   78 PGRrsLRLIMEYLPSGS-LRDYLQRHRDQIDLKRLllFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 KeFLTEEKE-------RTFSfcgtIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFT--------LEGERNTQA 248
Cdd:cd05038  157 K-VLPEDKEyyyvkepGESP----IFWYAPECLRESRFSSAS-DVWSFGVTLYELFTYGDPSQsppalflrMIGIAQGQM 230
                        250
                 ....*....|....*..
gi 663856869 249 EVSR--RILKCSPPFPP 263
Cdd:cd05038  231 IVTRllELLKSGERLPR 247
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
30-304 1.49e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 78.12  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDA 109
Cdd:cd07873    1 LETYIKLDKLGEGTYATVY---KGRSKLTDNLVALKEIR---LEHEEGAPCTAIREVSLLKDLKHAN-IVTLHDIIHTEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGemfthlyQRQYFKEA-------EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd07873   74 SLTLVFEYLDKD-------LKQYLDDCgnsinmhNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGAS-------------------------- 236
Cdd:cd07873  147 ARAKSIPTKTYSNEVV-TLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPlfpgstveeqlhfifrilgtpteetw 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 237 PFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGL 304
Cdd:cd07873  226 PGILSNEEFKSYNYPKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRI-----SAEEAMKHPYFHSL 288
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
31-301 1.83e-15

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 78.54  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVflvrkAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHY-----AF 105
Cdd:cd07877   17 ERYQNLSPVGSGAYGSV-----CAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVftparSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLIlDYVSGGEMfTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd07877   92 EEFNDVYLV-THLMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 fltEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF-----------------TLEGE--RNT 246
Cdd:cd07877  170 ---TDDEMT-GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFpgtdhidqlklilrlvgTPGAEllKKI 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 247 QAEVSRRILKCSPPFPPR------IG--PVAQDLLQRLLCKDPKKRLGAGpqgaqEVRNHPFF 301
Cdd:cd07877  246 SSESARNYIQSLTQMPKMnfanvfIGanPLAVDLLEKMLVLDSDKRITAA-----QALAHAYF 303
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
25-289 1.96e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.88  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  25 EEKVSVEN--FELLKVLGTGAYGKVFLvrkagghdagklyAMKVLRKAALVQRAKTQEHTRTERSVLELVRQaPFLVTLH 102
Cdd:PHA03212  84 EARAGIEKagFSILETFTPGAEGFAFA-------------CIDNKTCEHVVIKAGQRGGTATEAHILRAINH-PSIIQLK 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAKLHLILDYVSGgEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:PHA03212 150 GTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGA 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLTGASPF----TLEGERNTQAEVsRRILKCS 258
Cdd:PHA03212 229 ACFPVDINANKYYGWAGTIATNAPELL-ARDPYGPAVDIWSAGIVLFEMATCHDSLfekdGLDGDCDSDRQI-KLIIRRS 306
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 259 PPFPPRIGPVAQDLLQRL---LCKDPKKRLGAGP 289
Cdd:PHA03212 307 GTHPNEFPIDAQANLDEIyigLAKKSSRKPGSRP 340
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
410-606 2.00e-15

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 77.42  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQ------REVAALRLCQsHPNVVNLHEVHHDQ-------------L 470
Cdd:cd07844    8 LGEGSYATVYKGRSKLTGQLVALKEI--RLEHEEGapftaiREASLLKDLK-HANIVTLHDIIHTKktltlvfeyldtdL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HTYLvlellRGGELLEHIRKKRHFseseASQILRSLvsavSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARL 550
Cdd:cd07844   85 KQYM-----DDCGGGLSMHNVRLF----LFQLLRGL----AYCHQRR-VLHRDLKPQNLLISER---GELKLADFGLARA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RpqspGVPMQT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07844  148 K----SVPSKTysnEVVTLWYRPPDvLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGST 203
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
410-673 2.06e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 77.81  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPftaiREASLLKGLK-HANIVLLHDIIHTKETLTLVFEYVHTDLCQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRpQSPGVPMQTPCFT 565
Cdd:cd07869   92 YMDKHPGGLHPENVKLFLFQLLRGLSYIHQRY-ILHRDLKPQNLLISDT---GELKLADFGLARAK-SVPSHTYSNEVVT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQ---------------AAEIMCKIREGRFSLD 629
Cdd:cd07869  167 LWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLEriflvlgtpnedtwpGVHSLPHFKPERFTLY 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 630 G-----EAWQGVS--EEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSAR 673
Cdd:cd07869  247 SpknlrQAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFSDLPPR 297
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
400-618 2.15e-15

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 77.11  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT-QREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd14016    1 RYKLVKK---IGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQlEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFA---------R 549
Cdd:cd14016   78 LGPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSK-GYIHRDIKPENFLMGLGKNSNKVYLIDFGLAkkyrdprtgK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 550 LRPQSPGVPMqtpCFTLQYAApeLLAQQGYDES--CDLWSLG-VILYmMLSGQVPFQGASGQGGQSQAAEIM 618
Cdd:cd14016  157 HIPYREGKSL---TGTARYAS--INAHLGIEQSrrDDLESLGyVLIY-FLKGSLPWQGLKAQSKKEKYEKIG 222
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
409-647 2.32e-15

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 78.07  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN--TQREVAALRLCQ--SHPNVVNLHEVHH-----DQLHT-YLVLEL 478
Cdd:cd07880   22 QVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSElfAKRAYRELRLLKhmKHENVIGLLDVFTpdlslDRFHDfYLVMPF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLehIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpgvp 558
Cdd:cd07880  102 MGTDLGK--LMKHEKLSEDRIQFLVYQMLKGLKYIHA-AGIIHRDLKPGNLAVNED---CELKILDFGLARQTDSE---- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqgGQSQAAEIMcKIrEGRFSLDGEAwQGVS 637
Cdd:cd07880  172 MTGYVVTRWYRAPEvILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHD---HLDQLMEIM-KV-TGTPSKEFVQ-KLQS 245
                        250
                 ....*....|
gi 663856869 638 EEAKELVRGL 647
Cdd:cd07880  246 EDAKNYVKKL 255
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
39-284 2.54e-15

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 76.92  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAalvqrakTQEHTRTERSVLELVR--QAPFLVTLHYAFQTDAKLHLILD 116
Cdd:cd14221    1 LGKGCFGQAI---KVTHRETGEVMVMKELIRF-------DEETQRTFLKEVKVMRclEHPNVLKFIGVLYKDKRLNFITE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMfthlyqRQYFKEAEV------RV-YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK----- 184
Cdd:cd14221   71 YIKGGTL------RGIIKSMDShypwsqRVsFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARlmvde 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 --------EFLTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGAS------PFTLEGERNTQAEV 250
Cdd:cd14221  145 ktqpeglrSLKKPDRKKRYTVVGNPYWMAPEMINGRS-YDEKVDVFSFGIVLCEIIGRVNadpdylPRTMDFGLNVRGFL 223
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 251 SRRilkCSPPFPPRIGPVAQdllqrLLCK-DPKKR 284
Cdd:cd14221  224 DRY---CPPNCPPSFFPIAV-----LCCDlDPEKR 250
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
400-655 2.63e-15

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 76.58  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSrrLE-----ANTQREVAALRLCqSHPNVVNLHEVHH--DQLht 472
Cdd:cd06613    1 DYELIQR---IGSGTYGDVYKARNIATGELAAVKVIK--LEpgddfEIIQQEISMLKEC-RHPNIVAYFGSYLrrDKL-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 473 YLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRP 552
Cdd:cd06613   73 WIVMEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHST-GKIHRDIKGANILLTED---GDVKLADFGVSAQLT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 553 QSPGvPMQTPCFTLQYAAPELLAQQ---GYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAAEIMCKIREGRFSL- 628
Cdd:cd06613  149 ATIA-KRKSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFDLH----PMRALFLIPKSNFDPPKLk 223
                        250       260
                 ....*....|....*....|....*..
gi 663856869 629 DGEAWqgvSEEAKELVRGLLTVDPAKR 655
Cdd:cd06613  224 DKEKW---SPDFHDFIKKCLTKNPKKR 247
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
34-238 2.68e-15

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 76.62  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  34 ELLKVLGTGAYGKVFlvrKAGGHD--AGKLYAMKVLRKAALV---QRAKTQEHTRTERSVLelvrqapFLvtlhYAFQTD 108
Cdd:cd14063    3 EIKEVIGKGRFGRVH---RGRWHGdvAIKLLNIDYLNEEQLEafkEEVAAYKNTRHDNLVL-------FM----GACMDP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSeGHIVLTDFGLSK-EF 186
Cdd:cd14063   69 PHLAIVTSLCKGRTLYSLIHeRKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlSG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 187 LTEEKERTFSFC---GTIEYMAPEIIR---------SKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14063  148 LLQPGRREDTLVipnGWLCYLAPEIIRalspdldfeESLPFTKASDVYAFGTVWYELLAGRWPF 211
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
405-602 2.84e-15

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 76.96  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPA--------LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANT--QREVAALRLCQSHPNVVNL--------HEVH 466
Cdd:cd06608    1 LPDPAgifelvevIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEeiKLEINILRKFSNHPNIATFygafikkdPPGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLH-----------TYLVLELlrggellehIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddT 535
Cdd:cd06608   81 DDQLWlvmeycgggsvTDLVKGL---------RKKGKRLKEEWIAYILRETLRGLAYLHENK-VIHRDIKGQNILL---T 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 536 PGAPVKIIDFGFARL-------RPQSPGvpmqTPCftlqYAAPELLA-----QQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06608  148 EEAEVKLVDFGVSAQldstlgrRNTFIG----TPY----WMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPL 218
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
119-301 3.01e-15

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 76.23  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFS-F 197
Cdd:cd14022   67 SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSdK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 198 CGTIEYMAPEIIRSKTGH-GKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRL 276
Cdd:cd14022  147 HGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSI 222
                        170       180
                 ....*....|....*....|....*
gi 663856869 277 LCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14022  223 LRREPSERL-----TSQEILDHPWF 242
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
129-287 3.31e-15

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 76.52  E-value: 3.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 129 QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE-FLTEEKERTFSF---------C 198
Cdd:cd13980   90 TRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPtYLPEDNPADFSYffdtsrrrtC 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 199 gtieYMAPE-----------IIRSKTGHGKAVDWWSLGILLFELLT-GASPFTLEG---ERNTQAEVSRRILKCSPPFpp 263
Cdd:cd13980  170 ----YIAPErfvdaltldaeSERRDGELTPAMDIFSLGCVIAELFTeGRPLFDLSQllaYRKGEFSPEQVLEKIEDPN-- 243
                        170       180
                 ....*....|....*....|....
gi 663856869 264 rigpvAQDLLQRLLCKDPKKRLGA 287
Cdd:cd13980  244 -----IRELILHMIQRDPSKRLSA 262
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
410-602 3.50e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 76.95  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLCQsHPNVVNLHEvhhdqlhTYLVLELL------R 480
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRREllfNEVVIMRDYQ-HPNVVEMYK-------SYLVGEELwvlmeyL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLrpqSPGVPM 559
Cdd:cd06659  101 QGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQ-GVIHRDIKSDSILLTLD---GRVKLSDFGFcAQI---SKDVPK 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 663856869 560 QTPCFTLQY-AAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06659  174 RKSLVGTPYwMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPY 217
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
420-656 3.85e-15

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 75.85  E-value: 3.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 420 RCRQRQSGQEFAVKILSRRleaNTQREVAALRLCQSHPNVVNLHEVHHDQLHTYlVLELLRGGELLEHIRKKRHFSESEA 499
Cdd:cd14023   11 RALQLHSGAELQCKVFPLK---HYQDKIRPYIQLPSHRNITGIVEVILGDTKAY-VFFEKDFGDMHSYVRSCKRLREEEA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapvkiidfgfARLRPQS-----------------PGVPmqtp 562
Cdd:cd14023   87 ARLFKQIVSAVAHCHQSA-IVLGDLKLRKFVFSDEER-----------TQLRLESledthimkgeddalsdkHGCP---- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 cftlQYAAPELLAQQG-YD-ESCDLWSLGVILYMMLSGQVPFQgasgqggQSQAAEIMCKIREGRFSLDgeawQGVSEEA 640
Cdd:cd14023  151 ----AYVSPEILNTTGtYSgKSADVWSLGVMLYTLLVGRYPFH-------DSDPSALFSKIRRGQFCIP----DHVSPKA 215
                        250
                 ....*....|....*.
gi 663856869 641 KELVRGLLTVDPAKRL 656
Cdd:cd14023  216 RCLIRSLLRREPSERL 231
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
410-626 3.93e-15

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 76.05  E-value: 3.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   410 LGQGSFSVCRRCRQRQSG----QEFAVKILsrRLEANTQ------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGdgkeVEVAVKTL--KEDASEQqieeflREARIMRKLD-HPNIVKLLGVCTEEEPLMIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   480 RGGELLEHIRKKRH--FSESE----ASQILRslvsAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQ 553
Cdd:smart00221  84 PGGDLLDYLRKNRPkeLSLSDllsfALQIAR----GMEYLESK-NFIHRDLAARNCLVGENL---VVKISDFGLSRDLYD 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869   554 SPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASgqggqsqAAEIMCKIREGRF 626
Cdd:smart00221 156 DDYYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMS-------NAEVLEYLKKGYR 222
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
130-287 4.20e-15

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 76.76  E-value: 4.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 130 RQYFKEAEVRVYGGEIVLA--LE---HLHKLGIIYRDLKLENVLL--DSEG--HIVLTDFG---------LSKEFLTEEK 191
Cdd:cd14018  127 RQYLWVNTPSYRLARVMILqlLEgvdHLVRHGIAHRDLKSDNILLelDFDGcpWLVIADFGccladdsigLQLPFSSWYV 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 192 ERTfsfcGTIEYMAPEIIRSKTGHGKAVDW-----WSLGILLFELLTGASPF-TLEGERNTQAEVSRRILkcsPPFPPRI 265
Cdd:cd14018  207 DRG----GNACLMAPEVSTAVPGPGVVINYskadaWAVGAIAYEIFGLSNPFyGLGDTMLESRSYQESQL---PALPSAV 279
                        170       180
                 ....*....|....*....|..
gi 663856869 266 GPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd14018  280 PPDVRQVVKDLLQRDPNKRVSA 301
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
402-604 4.47e-15

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 75.88  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPaLGQGSFSVCRRCRQRqsGQEFAVKILSRRLEANTQR-----EVAALRLcqSHPNVVNL--HEVHHDQLHTYL 474
Cdd:cd13979    4 PLRLQEP-LGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRqsfwaELNAARL--RHENIVRVlaAETGTDFASLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHI--RKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpGAPvKIIDFGFARL-- 550
Cdd:cd13979   79 IIMEYCGNGTLQQLiyEGSEPLPLAHRILISLDIARALRFCHS-HGIVHLDVKPANILISEQ--GVC-KLCDFGCSVKlg 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 551 RPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd13979  155 EGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG 208
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
75-246 4.57e-15

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 75.71  E-value: 4.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  75 RAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAKLhLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHK 154
Cdd:cd14108   38 RAKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVV-IIVTELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQ 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 155 LGIIYRDLKLENVLL--DSEGHIVLTDFGLSKEFLTEEKErtfsFC--GTIEYMAPEIIrSKTGHGKAVDWWSLGILLFE 230
Cdd:cd14108  116 NDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQ----YCkyGTPEFVAPEIV-NQSPVSKVTDIWPVGVIAYL 190
                        170
                 ....*....|....*.
gi 663856869 231 LLTGASPFTLEGERNT 246
Cdd:cd14108  191 CLTGISPFVGENDRTT 206
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
506-669 4.62e-15

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 76.21  E-value: 4.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMHEEAGVVHRDLKPENILYadDTPGApVKIIDFGFARlrpQSPGVPMQTPCF-------------TLQYAAPE 572
Cdd:cd14011  123 ISEALSFLHNDVKLVHGNICPESVVI--NSNGE-WKLAGFDFCI---SSEQATDQFPYFreydpnlpplaqpNLNYLAPE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 573 LLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQGGQSQAAEIMCKIREGRFSLdgeawqgVSEEAKELVRGLLTVD 651
Cdd:cd14011  197 YILSKTCDPASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEK-------VPEELRDHVKTLLNVT 269
                        170
                 ....*....|....*...
gi 663856869 652 PAKRLKLEGLRGSSWLQD 669
Cdd:cd14011  270 PEVRPDAEQLSKIPFFDD 287
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
33-301 4.98e-15

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 76.83  E-value: 4.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRkagGHDAGKLYAMKVLRKaalVQRAKtqEHTRTERSVLELVRQ-----APFLVTLHYAFqt 107
Cdd:cd14134   14 YKILRLLGEGTFGKVLECW---DRKRKRYVAVKIIRN---VEKYR--EAAKIEIDVLETLAEkdpngKSHCVQLRDWF-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILdyVS---GGEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG--------- 173
Cdd:cd14134   84 DYRGHMCI--VFellGPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 ----------HIVLTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPF----- 238
Cdd:cd14134  162 krqirvpkstDIKLIDFGSA----TFDDEYHSSIVSTRHYRAPEVILG-LGWSYPCDVWSIGCILVELYTGELLFqthdn 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 239 ---------TLEG--------------------------ERNTQAEVSRRILKCSPPFPPRIGPVAQ---DLLQRLLCKD 280
Cdd:cd14134  237 lehlammerILGPlpkrmirrakkgakyfyfyhgrldwpEGSSSGRSIKRVCKPLKRLMLLVDPEHRllfDLIRKMLEYD 316
                        330       340
                 ....*....|....*....|.
gi 663856869 281 PKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14134  317 PSKRI-----TAKEALKHPFF 332
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
406-655 5.14e-15

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 75.42  E-value: 5.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVK-----ILSRRLEANTQREVAALRLCQSHPNVVNLH----EVHHDQLHTYLVl 476
Cdd:cd14050    5 ILSKLGEGSFGEVFKVRSREDGKLYAVKrsrsrFRGEKDRKRKLEEVERHEKLGEHPNCVRFIkaweEKGILYIQTELC- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ellrGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGF------ARL 550
Cdd:cd14050   84 ----DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDH-GLIHLDIKPANIFL---SKDGVCKLGDFGLvveldkEDI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RPQSPGVPMqtpcftlqYAAPELLaqQG-YDESCDLWSLGV-ILYMMLSGQVPFQGASGQggqsqaaeimcKIREGRfsL 628
Cdd:cd14050  156 HDAQEGDPR--------YMAPELL--QGsFTKAADIFSLGItILELACNLELPSGGDGWH-----------QLRQGY--L 212
                        250       260
                 ....*....|....*....|....*..
gi 663856869 629 DGEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd14050  213 PEEFTAGLSPELRSIIKLMMDPDPERR 239
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
31-304 5.67e-15

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 76.86  E-value: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKV--FLVRKAGGHDAGK---------LYAMKVLRKAALVQraktqeHTRTERSVLELVRQAPflV 99
Cdd:cd07879   15 ERYTSLKQVGSGAYGSVcsAIDKRTGEKVAIKklsrpfqseIFAKRAYRELTLLK------HMQHENVIGLLDVFTS--A 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQtdaKLHLILDYvsggeMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVL 177
Cdd:cd07879   87 VSGDEFQ---DFYLVMPY-----MQTDLQKimGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFGLSKEfltEEKERTfSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFT------------------ 239
Cdd:cd07879  159 LDFGLARH---ADAEMT-GYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKgkdyldqltqilkvtgvp 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 240 -LEGERNTQAEVSRRILKCSPPFP--------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGL 304
Cdd:cd07879  235 gPEFVQKLEDKAAKSYIKSLPKYPrkdfstlfPKASPQAVDLLEKMLELDVDKRL-----TATEALEHPYFDSF 303
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
39-263 6.02e-15

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 75.22  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaalvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14065    1 LGKGFFGEVYKVTH---RETGKVMVMKELK------RFDEQRSFLKEVKLMRRLSH-PNILRFIGVCVKDNKLNFITEYV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMfthlyqRQYFKEAE------VRVY-GGEIVLALEHLHKLGIIYRDLKLENVLL---DSEGHIVLTDFGLSKEFLT 188
Cdd:cd14065   71 NGGTL------EELLKSMDeqlpwsQRVSlAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 E-----EKERTFSFCGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLTGAS------PFTLEGERNTQAEVSRRILKC 257
Cdd:cd14065  145 EktkkpDRKKRLTVVGSPYWMAPEMLRGESYDEK-VDVFSFGIVLCEIIGRVPadpdylPRTMDFGLDVRAFRTLYVPDC 223

                 ....*.
gi 663856869 258 SPPFPP 263
Cdd:cd14065  224 PPSFLP 229
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
410-655 6.81e-15

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 75.68  E-value: 6.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK--ILSRRLEANTQ--REVAALRLCQsHPNVVNLH-----------EVHHDQLHTYL 474
Cdd:cd14048   14 LGRGGFGVVFEAKNKVDDCNYAVKriRLPNNELAREKvlREVRALAKLD-HPGIVRYFnawlerppegwQEKMDEVYLYI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRKKRHFSESEAS---QILRSLVSAVSFMHEEaGVVHRDLKPENILYA-DDTpgapVKIIDFGFARL 550
Cdd:cd14048   93 QMQLCRKENLKDWMNRRCTMESRELFvclNIFKQIASAVEYLHSK-GLIHRDLKPSNVFFSlDDV----VKVGDFGLVTA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RPQspGVPMQT-----PCF--------TLQYAAPELLAQQGYDESCDLWSLGVILYMMLsgqVPFqgasgqGGQSQAAEI 617
Cdd:cd14048  168 MDQ--GEPEQTvltpmPAYakhtgqvgTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSF------STQMERIRT 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 618 MCKIREGRFSLdgEAWQGVSEEAKeLVRGLLTVDPAKR 655
Cdd:cd14048  237 LTDVRKLKFPA--LFTNKYPEERD-MVQQMLSPSPSER 271
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
31-237 7.28e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 76.25  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd06650    5 DDFEKISELGAGNGGVVF---KVSHKPSGLVMARKLIH---LEIKPAIRNQIIRELQVLHEC-NSPYIVGFYGAFYSDGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHL-HKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:cd06650   78 ISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 190 EKErtfSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASP 237
Cdd:cd06650  158 MAN---SFVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
410-602 7.31e-15

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 76.04  E-value: 7.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHD-QLHTYLVLELLRGGELLEHI 488
Cdd:cd14132   26 IGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLRGGPNIVKLLDVVKDpQSKTPSLIFEYVNNTDFKTL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 489 RKKrhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGAPVKIIDFGFARLrpQSPGVPMQTPCFTLQY 568
Cdd:cd14132  106 YPT--LTDYDIRYYMYELLKALDYCHSK-GIMHRDVKPHNIMI--DHEKRKLRLIDWGLAEF--YHPGQEYNVRVASRYY 178
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 663856869 569 AAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14132  179 KGPELLvDYQYYDYSLDMWSLGCMLASMIFRKEPF 213
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
402-607 7.64e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 75.45  E-value: 7.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREpALGQGSFSVCRRCRQRqsGQEFAVKILSR------RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLV 475
Cdd:cd14147    4 ELRLEE-VIGIGGFGKVYRGSWR--GELVAVKAARQdpdediSVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 476 LELLRGGELLEHIRKKR---HFSESEASQILRSLVsavsFMHEEA--GVVHRDLKPENILYA-----DDTPGAPVKIIDF 545
Cdd:cd14147   81 MEYAAGGPLSRALAGRRvppHVLVNWAVQIARGMH----YLHCEAlvPVIHRDLKSNNILLLqpienDDMEHKTLKITDF 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 546 GFARLRPQSpgVPMQTPCfTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14147  157 GLAREWHKT--TQMSAAG-TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDC 215
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
37-302 7.86e-15

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 76.34  E-value: 7.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQRAKTQE--------HTRTERSvLELVRQA--PFLVTLHYAFQ 106
Cdd:PTZ00024  15 AHLGEGTYGKVE---KAYDTLTGKIVAIKKVKIIEISNDVTKDRqlvgmcgiHFTTLRE-LKIMNEIkhENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGgEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:PTZ00024  91 EGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 -------------LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGE---------- 243
Cdd:PTZ00024 170 gyppysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEidqlgrifel 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 244 RNTQAEVSRRILKCSP---PFPPR-------IGPVAQ----DLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:PTZ00024 250 LGTPNEDNWPQAKKLPlytEFTPRkpkdlktIFPNASddaiDLLQSLLKLNPLERI-----SAKEALKHEYFK 317
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
488-667 8.78e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 74.99  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVKIIDFGFARLRPQSPGVPMQTpcfTLQ 567
Cdd:cd14102   96 ITEKGALDEDTARGFFRQVLEAVRHCYS-CGVVHRDIKDENLLV--DLRTGELKLIDFGSGALLKDTVYTDFDG---TRV 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggqsQAAEIMckirEGRFSLDgeawQGVSEEAKELVRG 646
Cdd:cd14102  170 YSPPEWIRYHRYHgRSATVWSLGVLLYDMVCGDIPFE---------QDEEIL----RGRLYFR----RRVSPECQQLIKW 232
                        170       180
                 ....*....|....*....|.
gi 663856869 647 LLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14102  233 CLSLRPSDRPTLEQIFDHPWM 253
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
30-233 9.80e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 77.43  E-value: 9.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFL--VRKAGGHDAGKlyamkvlRKAALVQRAKTQEHTRTERSVLELVRQAPFL----VTLHY 103
Cdd:PHA03210 147 LAHFRVIDDLPAGAFGKIFIcaLRASTEEAEAR-------RGVNSTNQGKPKCERLIAKRVKAGSRAAIQLeneiLALGR 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDA-KLHLILDYVSGGEMFTHLYQRQYF----------KEA----EVRVYGGEIVLALEHLHKLGIIYRDLKLENVL 168
Cdd:PHA03210 220 LNHENIlKIEEILRSEANTYMITQKYDFDLYsfmydeafdwKDRpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIF 299
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 169 LDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLT 233
Cdd:PHA03210 300 LNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPEIL-AGDGYCEITDIWSCGLILLDMLS 363
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
410-648 1.03e-14

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 76.98  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR-----RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05623   80 IGRGAFGEVAVVKLKNADKVFAMKILNKwemlkRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRK-KRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGVPMQTPC 563
Cdd:cd05623  160 LTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQ-LHYVHRDIKPDNILM--DMNGH-IRLADFGSCLKLMEDGTVQSSVAV 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FTLQYAAPELL-AQQG----YDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKI--REGRFSLDGEAwQGV 636
Cdd:cd05623  236 GTPDYISPEILqAMEDgkgkYGPECDWWSLGVCMYEMLYGETPFYAES-------LVETYGKImnHKERFQFPTQV-TDV 307
                        250
                 ....*....|..
gi 663856869 637 SEEAKELVRGLL 648
Cdd:cd05623  308 SENAKDLIRRLI 319
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
28-284 1.07e-14

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 74.63  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKAAlvqrakTQEHTRTERSVLELVRQAPFLVTLHYAFQT 107
Cdd:cd05082    3 LNMKELKLLQTIGKGEFGDVML-----GDYRGNKVAVKCIKNDA------TAQAFLAEASVMTQLRHSNLVQLLGVIVEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQRQYfkeaevRVYGGEIVL--------ALEHLHKLGIIYRDLKLENVLLDSEGHIVLTD 179
Cdd:cd05082   72 KGGLYIVTEYMAKGSLVDYLRSRGR------SVLGGDCLLkfsldvceAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 180 FGLSKEFLTEEKERTFSfcgtIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTlegeRNTQAEVSRRILKC- 257
Cdd:cd05082  146 FGLTKEASSTQDTGKLP----VKWTAPEALREKKFSTKS-DVWSFGILLWEIYSfGRVPYP----RIPLKDVVPRVEKGy 216
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 258 ---SPPFPPrigPVAQDLLQRLLCKDPKKR 284
Cdd:cd05082  217 kmdAPDGCP---PAVYDVMKNCWHLDAAMR 243
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
2-252 1.12e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.45  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   2 GDEDDDESCAVELRITEAnltgheEKVSVENFELLKVLGTGAYGKVFLVRKAGGHDAGKL-YAMK--VLRKAALVQRAKt 78
Cdd:PHA03209  43 ESDDDDDDGLIPTKQKAR------EVVASLGYTVIKTLTPGSEGRVFVATKPGQPDPVVLkIGQKgtTLIEAMLLQNVN- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  79 qeHTRTERSVLELVR-QAPFLVTLHYAfqtdaklhlildyvsgGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLG 156
Cdd:PHA03209 116 --HPSVIRMKDTLVSgAITCMVLPHYS----------------SDLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQR 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 157 IIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKErtFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLtgAS 236
Cdd:PHA03209 178 IIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAF--LGLAGTVETNAPEVL-ARDKYNSKADIWSAGIVLFEML--AY 252
                        250
                 ....*....|....*..
gi 663856869 237 PFTL-EGERNTQAEVSR 252
Cdd:PHA03209 253 PSTIfEDPPSTPEEYVK 269
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
427-655 1.17e-14

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 75.00  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 427 GQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTY----LVLELLRGGELLEHIRKKRHFSESEASQI 502
Cdd:cd13982   25 GRPVAVKRLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYialeLCAASLQDLVESPRESKLFLRPGLEPVRL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 503 LRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPG--APVKIIDFGFA-RL-RPQSPGVPMQTPCFTLQYAAPELLAQQG 578
Cdd:cd13982  105 LRQIASGLAHLHS-LNIVHRDLKPQNILISTPNAHgnVRAMISDFGLCkKLdVGRSSFSRRSGVAGTSGWIAPEMLSGST 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 579 YDE---SCDLWSLGVILYMMLS-GQVPFqgasGQGGQSQAaeimcKIREGRFSLDGEAWQGV-SEEAKELVRGLLTVDPA 653
Cdd:cd13982  184 KRRqtrAVDIFSLGCVFYYVLSgGSHPF----GDKLEREA-----NILKGKYSLDKLLSLGEhGPEAQDLIERMIDFDPE 254

                 ..
gi 663856869 654 KR 655
Cdd:cd13982  255 KR 256
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
121-288 1.18e-14

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 74.14  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 121 GEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF-LTEEKERTFSFCG 199
Cdd:cd14024   69 GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCpLNGDDDSLTDKHG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKTGH-GKAVDWWSLGILLFELLTGASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLC 278
Cdd:cd14024  149 CPAYVGPEILSSRRSYsGKAADVWSLGVCLYTMLLGRYPF----QDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLR 224
                        170
                 ....*....|
gi 663856869 279 KDPKKRLGAG 288
Cdd:cd14024  225 RSPAERLKAS 234
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
410-604 1.63e-14

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 75.46  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRRCRQRqSGQEFAVKILSRRLEA--NTQREVAALRLCQ--SHPNVVNLHEVH------HDQLHTYLVLEL 478
Cdd:cd07877   25 VGSGAYgSVCAAFDTK-TGLRVAVKKLSRPFQSiiHAKRTYRELRLLKhmKHENVIGLLDVFtparslEEFNDVYLVTHL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELleHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpgvp 558
Cdd:cd07877  104 MGADLN--NIVKCQKLTDDHVQFLIYQILRGLKYIHS-ADIIHRDLKPSNLAVNED---CELKILDFGLARHTDDE---- 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 559 MQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd07877  174 MTGYVATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPG 220
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
410-662 1.63e-14

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 75.69  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL------SRRLEANTQREVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVkkadmiNKNMVHQVQAERDALALSKS-PFIVHLYYSLQSANNVYLVMEYLIGGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARL------------- 550
Cdd:cd05610   91 VKSLLHIYGYFDEEMAVKYISEVALALDYLHRH-GIIHRDLKPDNMLISNE---GHIKLTDFGLSKVtlnrelnmmdilt 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 -----RP-----QSPG--------------VPMQTP---------------CFTLQYAAPELLAQQGYDESCDLWSLGVI 591
Cdd:cd05610  167 tpsmaKPkndysRTPGqvlslisslgfntpTPYRTPksvrrgaarvegeriLGTPDYLAPELLLGKPHGPAVDWWALGVC 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 592 LYMMLSGQVPFQGASGQggqsqaaeimcKIREGRFSLD---GEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLR 662
Cdd:cd05610  247 LFEFLTGIPPFNDETPQ-----------QVFQNILNRDipwPEGEEELSVNAQNAIEILLTMDPTKRAGLKELK 309
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
39-284 1.85e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 74.07  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRkaggHDAGKLYAMKVLRKAAlvQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd14027    1 LDSGGFGKVSLCF----HRTQGLVVLKTVYTGP--NCIEHNEALLEEGKMMNRLRHSR-VVKLLGVILEEGKYSLVMEYM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQrqyfKEAEVRVYGG---EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG---------LSKEF 186
Cdd:cd14027   74 EKGNLMHVLKK----VSVPLSVKGRiilEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSF---CGTIEYMAPEIIRSKtgHGKAV---DWWSLGILLFELLTGASPFtlEGERNTQaEVSRRILKCSPP 260
Cdd:cd14027  150 HNEQREVDGTAkknAGTLYYMAPEHLNDV--NAKPTeksDVYSFAIVLWAIFANKEPY--ENAINED-QIIMCIKSGNRP 224
                        250       260
                 ....*....|....*....|....*...
gi 663856869 261 ----FPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14027  225 dvddITEYCPREIIDLMKLCWEANPEAR 252
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
410-625 2.01e-14

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 74.07  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  410 LGQGSF-SVCR---RCRQRQSGQEFAVKILsrrLEANTQREVAALR-----LCQ-SHPNVVNLHEV--HHDQ-------- 469
Cdd:pfam07714   7 LGEGAFgEVYKgtlKGEGENTKIKVAVKTL---KEGADEEEREDFLeeasiMKKlDHPNIVKLLGVctQGEPlyivteym 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  470 ----LHTYLVlellrggellehiRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPgapVKIIDF 545
Cdd:pfam07714  84 pggdLLDFLR-------------KHKRKLTLKDLLSMALQIAKGMEYLESK-NFVHRDLAARNCLVSENLV---VKISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  546 GFARLRPQSPGVPMQTPCFT-LQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaaEIMCKIRE 623
Cdd:pfam07714 147 GLSRDIYDDDYYRKRGGGKLpIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNE-------EVLEFLED 219

                  ..
gi 663856869  624 GR 625
Cdd:pfam07714 220 GY 221
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
410-602 2.09e-14

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 73.81  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLcQSHPNVVNLhevhhdqLHTYLVLELL------R 480
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKEliiNEILVMRE-NKNPNIVNY-------LDSYLVGDELwvvmeyL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRP-QSPGVP 558
Cdd:cd06647   87 AGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSN-QVIHRDIKSDNILLGMD---GSVKLTDFGFcAQITPeQSKRST 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 559 M-QTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06647  163 MvGTP----YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 203
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
410-655 2.15e-14

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 74.11  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK--ILS----------RRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKqvELPsvsaenkdrkKSMLDALQREIALLRELQ-HENIVQYLGSSSDANHLNIFLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFAR---LRPQS 554
Cdd:cd06628   87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNR-GIIHRDIKGANILV--DNKGG-IKISDFGISKkleANSLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQTPCF--TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggQSQAaeiMCKIREgrfSLDGEA 632
Cdd:cd06628  163 TKNNGARPSLqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCT----QMQA---IFKIGE---NASPTI 232
                        250       260
                 ....*....|....*....|...
gi 663856869 633 WQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd06628  233 PSNISSEARDFLEKTFEIDHNKR 255
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
409-655 2.17e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 73.84  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILS------RRLEAnTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd08225    7 KIGEGSFGKIYLAKAKSDSEHCVIKEIDltkmpvKEKEA-SKKEVILLAKMK-HPNIVTFFASFQENGRLFIVMEYCDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEaSQILRSLVS-AVSFMH-EEAGVVHRDLKPENILYADDtpGAPVKIIDFGFARLRPQSPGVPmQ 560
Cdd:cd08225   85 DLMKRINRQRGVLFSE-DQILSWFVQiSLGLKHiHDRKILHRDIKSQNIFLSKN--GMVAKLGDFGIARQLNDSMELA-Y 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaaEIMCKIREGRFSldgEAWQGVSEEA 640
Cdd:cd08225  161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLH-------QLVLKICQGYFA---PISPNFSRDL 230
                        250
                 ....*....|....*
gi 663856869 641 KELVRGLLTVDPAKR 655
Cdd:cd08225  231 RSLISQLFKVSPRDR 245
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
121-301 2.24e-14

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 73.62  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 121 GEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFS-FCG 199
Cdd:cd13976   69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGEDDSLSdKHG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSK-TGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKcsppFPPRIGPVAQDLLQRLLC 278
Cdd:cd13976  149 CPAYVSPEILNSGaTYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFA----IPETLSPRARCLIRSLLR 224
                        170       180
                 ....*....|....*....|...
gi 663856869 279 KDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd13976  225 REPSERL-----TAEDILLHPWL 242
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
410-681 2.37e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 75.10  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAAL--RLCQSH------PNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd05633   13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALneRIMLSLvstgdcPFIVCMTYAFHTPDKLCFILDLMNG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFG----FARLRPQSPgv 557
Cdd:cd05633   93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF-VVYRDLKPANILLDEH---GHVRISDLGlacdFSKKKPHAS-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 pmqtpCFTLQYAAPELLaQQG--YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQsqaaeimcKIREGRFSLDGEAWQG 635
Cdd:cd05633  167 -----VGTHGYMAPEVL-QKGtaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH--------EIDRMTLTVNVELPDS 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEG-----------LRGSSWLQDGSARSSPPLRTP 681
Cdd:cd05633  233 FSPELKSLLEGLLQRDVSKRLGCHGrgaqevkehsfFKGIDWQQVYLQKYPPPLIPP 289
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
410-666 2.41e-14

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 73.54  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEANTQREVAALR----LCQS--HPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKqVEIDPINTEASKEVKALEceiqLLKNlqHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFA-RLRPQSPGVPMQT 561
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNM-IVHRDIKGANILR--DSNGN-VKLGDFGASkRLQTICSSTGMKS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgqgGQSQAAEIMCKI--REGRFSLDgeawQGVSEE 639
Cdd:cd06625  164 VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW-------AEFEPMAAIFKIatQPTNPQLP----PHVSED 232
                        250       260
                 ....*....|....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSW 666
Cdd:cd06625  233 ARDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
488-667 2.46e-14

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 73.47  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGAPVKIIDFGFARLRPQSPGVPMQTpcfTLQ 567
Cdd:cd14100   97 ITERGALPEELARSFFRQVLEAVRHCHN-CGVLHRDIKDENILI--DLNTGELKLIDFGSGALLKDTVYTDFDG---TRV 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 568 YAAPELLAQQGYD-ESCDLWSLGVILYMMLSGQVPFQgasgqggqsQAAEImckiregrfsLDGEAW--QGVSEEAKELV 644
Cdd:cd14100  171 YSPPEWIRFHRYHgRSAAVWSLGILLYDMVCGDIPFE---------HDEEI----------IRGQVFfrQRVSSECQHLI 231
                        170       180
                 ....*....|....*....|...
gi 663856869 645 RGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14100  232 KWCLALRPSDRPSFEDIQNHPWM 254
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
39-263 2.58e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 73.82  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRkaggHDA-GKLYAMKVLRKAalvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQtDAKLHLILDY 117
Cdd:cd14222    1 LGKGFFGQAIKVT----HKAtGKVMVMKELIRC----DEETQKTFLTEVKVMRSLDHPNVLKFIGVLYK-DKRLNLLTEF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEE------- 190
Cdd:cd14222   72 IEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKkkpppdk 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 ---KERTF---------SFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGAS------PFTLEGERNTQAEVSR 252
Cdd:cd14222  152 pttKKRTLrkndrkkryTVVGNPYWMAPEMLNGKS-YDEKVDIFSFGIVLCEIIGQVYadpdclPRTLDFGLNVRLFWEK 230
                        250
                 ....*....|..
gi 663856869 253 RILK-CSPPFPP 263
Cdd:cd14222  231 FVPKdCPPAFFP 242
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
39-242 3.33e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 73.68  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrkAGGHDAGKLYAMKVLRKaalvQRAKTQEHT-RTERSVLELVRQAPFLVTLHYAFQTDAKLhLILDY 117
Cdd:cd14664    1 IGRGGAGTVY----KGVMPNGTLVAVKRLKG----EGTQGGDHGfQAEIQTLGMIRHRNIVRLRGYCSNPTTNL-LVYEY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQR-------QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEE 190
Cdd:cd14664   72 MPNGSLGELLHSRpesqpplDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 191 KERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFTLEG 242
Cdd:cd14664  152 SHVMSSVAGSYGYIAPEYAYTGKVSEKS-DVYSYGVVLLELITGKRPFDEAF 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
409-656 3.39e-14

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 73.70  E-value: 3.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVK-ILSRRLEANTQ--REVAALRLCQSHPNVVN------LHEVHHDQLHT-YLVLEL 478
Cdd:cd14036    7 VIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAiiQEINFMKKLSGHPNIVQfcsaasIGKEESDQGQAeYLLLTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILR---SLVSAVSFMHEEA-GVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQS 554
Cdd:cd14036   87 LCKGQLVDFVKKVEAPGPFSPDTVLKifyQTCRAVQHMHKQSpPIIHRDLKIENLLIGNQ---GQIKLCDFGSATTEAHY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQ-----------TPCFTLQYAAPELL---AQQGYDESCDLWSLGVILYMMLSGQVPFQgasgQGGQSQaaeimck 620
Cdd:cd14036  164 PDYSWSaqkrslvedeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFE----DGAKLR------- 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 663856869 621 IREGRFSL--DGEAWQGVSeeakELVRGLLTVDPAKRL 656
Cdd:cd14036  233 IINAKYTIppNDTQYTVFH----DLIRSTLKVNPEERL 266
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
31-301 3.72e-14

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 73.94  E-value: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKV--LRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:cd14040    6 ERYLLLHLLGRGGFSEVY---KAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLH-LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLL---DSEGHIVLTDFGL 182
Cdd:cd14040   83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SK-----EFLTEEKERTFSFCGTIEYMAPE---IIRSKTGHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVSRR- 253
Cdd:cd14040  163 SKimdddSYGVDGMDLTSQGAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQEn 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 254 -ILKCSP---PFPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14040  240 tILKATEvqfPVKPVVSNEAKAFIRRCLAYRKEDRF-----DVHQLASDPYL 286
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
407-655 3.83e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 73.14  E-value: 3.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCqSHPNVVNLHE--VHHDQLHTYL-VLE 477
Cdd:cd08228    7 EKKIGRGQFSEVYRATCLLDRKPVALKkvqifeMMDAKARQDCVKEIDLLKQL-NHPNVIKYLDsfIEDNELNIVLeLAD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHF-SESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRpQSPG 556
Cdd:cd08228   86 AGDLSQMIKYFKKQKRLiPERTVWKYFVQLCSAVEHMHSRR-VMHRDIKPANVFI---TATGVVKLGDLGLGRFF-SSKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgQGGQSQAAEIMCKIREGRF-SLDGEAWqg 635
Cdd:cd08228  161 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF-----YGDKMNLFSLCQKIEQCDYpPLPTEHY-- 233
                        250       260
                 ....*....|....*....|
gi 663856869 636 vSEEAKELVRGLLTVDPAKR 655
Cdd:cd08228  234 -SEKLRELVSMCIYPDPDQR 252
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
33-243 4.03e-14

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 74.35  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalvQRAKTQEHTRTERSVLELVRQApflvtlhyafQTDAKLH 112
Cdd:cd14225   45 YEILEVIGKGSFGQVV---KALDHKTNEHVAIKIIR-----NKKRFHHQALVEVKILDALRRK----------DRDNSHN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LI--LDY--------VSGGEMFTHLYQR------QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH-- 174
Cdd:cd14225  107 VIhmKEYfyfrnhlcITFELLGMNLYELikknnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQss 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 175 IVLTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIrskTGH--GKAVDWWSLGILLFELLTGASPFTLEGE 243
Cdd:cd14225  187 IKVIDFGSS----CYEHQRVYTYIQSRFYRSPEVI---LGLpySMAIDMWSLGCILAELYTGYPLFPGENE 250
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
410-592 4.03e-14

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 73.22  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQ-SGQEFAVKILS----------RRLEantqrEVAALRLCQS--HPNVVNLHEV--HHDQLH--T 472
Cdd:cd14052    8 IGSGEFSQVYKVSERVpTGKVYAVKKLKpnyagakdrlRRLE-----EVSILRELTLdgHDNIVQLIDSweYHGHLYiqT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 473 YLVLELLRGGELLEHIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRP 552
Cdd:cd14052   83 ELCENGSLDVFLSELGLLGR-LDEFRVWKILVELSLGLRFIHDH-HFVHLDLKPANVLI---TFEGTLKIGDFGMATVWP 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663856869 553 QSPGVPMQTPCftlQYAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd14052  158 LIRGIEREGDR---EYIAPEILSEHMYDKPADIFSLGLIL 194
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
456-675 4.15e-14

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 73.94  E-value: 4.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 456 HPNVVNLHEVHHDQLHTY-LVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHE-EAGVVHRDLKPENILYAD 533
Cdd:cd14040   69 HPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLVD 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 534 DTPGAPVKIIDFGFAR-------------LRPQSPGVPMQTP--CFTLQYAAPELlaqqgyDESCDLWSLGVILYMMLSG 598
Cdd:cd14040  149 GTACGEIKITDFGLSKimdddsygvdgmdLTSQGAGTYWYLPpeCFVVGKEPPKI------SNKVDVWSVGVIFFQCLYG 222
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 599 QVPFQGASGQGGQSQAAEIMcKIREGRFSLDgeawQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSS 675
Cdd:cd14040  223 RKPFGHNQSQQDILQENTIL-KATEVQFPVK----PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSN 294
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
31-285 4.26e-14

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 73.94  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAALVQRAKTQEH----TRTERSVLELvrQAPFLVTLHYAFQ 106
Cdd:cd14041    6 DRYLLLHLLGRGGFSEVY---KAFDLTEQRYVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKEL--DHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDA-KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENVLL---DSEGHIVLTDF 180
Cdd:cd14041   81 LDTdSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLSKEF------LTEEKERTFSFCGTIEYMAPE---IIRSKTGHGKAVDWWSLGILLFELLTGASPFtleGERNTQAEVS 251
Cdd:cd14041  161 GLSKIMdddsynSVDGMELTSQGAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFYQCLYGRKPF---GHNQSQQDIL 237
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 252 RR--ILKCSP-PFPPR--IGPVAQDLLQRLLCKDPKKRL 285
Cdd:cd14041  238 QEntILKATEvQFPPKpvVTPEAKAFIRRCLAYRKEDRI 276
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
410-655 5.43e-14

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 73.08  E-value: 5.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRqRQSGQEFAVKILS----RRLEANTQREVAALRLCQsHPNVVNL-------HE-------VHHDQLH 471
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGTVVAVKRLNemncAASKKEFLTELEMLGRLR-HPNLVRLlgyclesDEkllvyeyMPNGSLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 TYLvLELLRGGELLEHIRKKrhfseseasqILRSLVSAVSFMHEEAG--VVHRDLKPENILYADD-TPgapvKIIDFGFA 548
Cdd:cd14066   79 DRL-HCHKGSPPLPWPQRLK----------IAKGIARGLEYLHEECPppIIHGDIKSSNILLDEDfEP----KLTDFGLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 RLRPQSPGVPMQTP-CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFS 627
Cdd:cd14066  144 RLIPPSESVSKTSAvKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVESKGKEELE 223
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 628 --LDGEAWQGVS---EEAKELVR-GLLTV--DPAKR 655
Cdd:cd14066  224 diLDKRLVDDDGveeEEVEALLRlALLCTrsDPSLR 259
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
31-267 5.54e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 73.93  E-value: 5.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVrQAPFLVTLHYAFQTDAK 110
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQH---KPSGLIMARKLIH---LEIKPAIRNQIIRELQVLHEC-NSPYIVGFYGAFYSDGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHL-HKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE 189
Cdd:cd06649   78 ISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 190 EKErtfSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd06649  158 MAN---SFVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISP 231
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
410-655 5.75e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 72.91  E-value: 5.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilsrRLEANT---QREVAAL-RLcqSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14047   14 IGSGGFGQVFKAKHRIDGKTYAIK----RVKLNNekaEREVKALaKL--DHPNIVRYNGCWDGFDYDPETSSSNSSRSKT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSES------------------EASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF 547
Cdd:cd14047   88 KCLFIQMEFCEKgtleswiekrngekldkvLALEIFEQITKGVEYIHSK-KLIHRDLKPSNIFLVDT---GKVKIGDFGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 548 arLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVpfqgasgqgGQSQAAEIMCKIREGRFS 627
Cdd:cd14047  164 --VTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCD---------SAFEKSKFWTDLRNGILP 232
                        250       260
                 ....*....|....*....|....*...
gi 663856869 628 lDGEAWQGVSEEAkeLVRGLLTVDPAKR 655
Cdd:cd14047  233 -DIFDKRYKIEKT--IIKKMLSKKPEDR 257
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
30-304 6.33e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 73.49  E-value: 6.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRTERSVLELVRQAPfLVTLHYAFQTDA 109
Cdd:cd07872    5 METYIKLEKLGEGTYATVF---KGRSKLTENLVALKEIR---LEHEEGAPCTAIREVSLLKDLKHAN-IVTLHDIVHTDK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGemfthlyQRQYFKEA-------EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd07872   78 SLTLVFEYLDKD-------LKQYMDDCgnimsmhNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFLTEEKERTFSFCgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF---TLEGE------------RNTQ 247
Cdd:cd07872  151 ARAKSVPTKTYSNEVV-TLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFpgsTVEDElhlifrllgtptEETW 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 248 AEVSRRILKCSPPFP-----------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQGL 304
Cdd:cd07872  230 PGISSNDEFKNYNFPkykpqplinhaPRLDTEGIELLTKFLQYESKKRI-----SAEEAMKHAYFRSL 292
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
410-656 6.45e-14

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 73.01  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIL-SRRLEANTQREVAALR---LCQSH-PNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05607   10 LGKGGFGEVCAVQVKNTGQMYACKKLdKKRLKKKSGEKMALLEkeiLEKVNsPFIVSLAYAFETKTHLCLVMSLMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHI----------RKKRHFSESEASQILRslvsavsfMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQs 554
Cdd:cd05607   90 KYHIynvgergiemERVIFYSAQITCGILH--------LHS-LKIVYRDMKPENVLLDDN---GNCRLSDLGLAVEVKE- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 pGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgasgqggqsQAAEIMCKIREGRFSLDGEA-- 632
Cdd:cd05607  157 -GKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFR---------DHKEKVSKEELKRRTLEDEVkf 226
                        250       260
                 ....*....|....*....|....*
gi 663856869 633 -WQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd05607  227 eHQNFTEEAKDICRLFLAKKPENRL 251
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
406-602 7.03e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 73.22  E-value: 7.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLcQSHPNVVNLhevhhdqLHTYLV------L 476
Cdd:cd06654   24 RFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEliiNEILVMRE-NKNPNIVNY-------LDSYLVgdelwvV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRPQSP 555
Cdd:cd06654   96 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQ-VIHRDIKSDNILLGMD---GSVKLTDFGFcAQITPEQS 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 556 gvPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06654  172 --KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
410-656 7.75e-14

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 73.73  E-value: 7.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsRRLEANTQREVAALR-----LCQSH-PNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05629    9 IGKGAFGEVRLVQKKDTGKIYAMKTL-LKSEMFKKDQLAHVKaerdvLAESDsPWVVSLYYSFQDAQYLYLIMEFLPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYadDTPGApVKIIDFG-------------FARL 550
Cdd:cd05629   88 LMTMLIKYDTFSEDVTRFYMAECVLAIEAVHK-LGFIHRDIKPDNILI--DRGGH-IKLSDFGlstgfhkqhdsayYQKL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 551 RPQSPGVP----------------------MQT-----------PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS 597
Cdd:cd05629  164 LQGKSNKNridnrnsvavdsinltmsskdqIATwkknrrlmaysTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLI 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 598 GQVPFQGASGQggqsqaaEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTvDPAKRL 656
Cdd:cd05629  244 GWPPFCSENSH-------ETYRKIINWRETLYFPDDIHLSVEAEDLIRRLIT-NAENRL 294
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
29-301 8.60e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 73.12  E-value: 8.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLrkaaLVQRAKTQEHTRTER--SVLELVRQAPFLVTLHYAFQ 106
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVY---KARQIKTGRVVALKKI----LMHNEKDGFPITALReiKILKKLKHPNVVPLIDMAVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILdyvsgGEMFTHL-Y-----------QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH 174
Cdd:cd07866   79 RPDKSKRKR-----GSVYMVTpYmdhdlsgllenPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 175 IVLTDFGLSKEF----------LTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGER 244
Cdd:cd07866  154 LKIADFGLARPYdgpppnpkggGGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 245 NtQAEVsrrILK-CSPP----FP-----------------PRI--------GPVAQDLLQRLLCKDPKKRLgagpqGAQE 294
Cdd:cd07866  234 D-QLHL---IFKlCGTPteetWPgwrslpgcegvhsftnyPRTleerfgklGPEGLDLLSKLLSLDPYKRL-----TASD 304

                 ....*..
gi 663856869 295 VRNHPFF 301
Cdd:cd07866  305 ALEHPYF 311
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
410-602 8.84e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 72.74  E-value: 8.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS--RRLEANTQREVAALRLCQSHPNVVNLHEVHH-------DQLHTYL--VLEL 478
Cdd:cd06638   26 IGKGTYGKVFKVLNKKNGSKAAVKILDpiHDIDEEIEAEYNILKALSDHPNVVKFYGMYYkkdvkngDQLWLVLelCNGG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFA------RLRP 552
Cdd:cd06638  106 SVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNK-TIHRDVKGNNILL---TTEGGVKLVDFGVSaqltstRLRR 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 553 Q-SPGVPMqtpcftlqYAAPELLA--QQ---GYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06638  182 NtSVGTPF--------WMAPEVIAceQQldsTYDARCDVWSLGITAIELGDGDPPL 229
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
410-602 9.85e-14

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 72.46  E-value: 9.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREV-----AALRL--CqshPNVVNLH-------------EVHHDQ 469
Cdd:cd06617    9 LGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLlmdldISMRSvdC---PYTVTFYgalfregdvwicmEVMDTS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 470 LHTYLVLEllrggellehIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYadDTPGApVKIIDFGFAR 549
Cdd:cd06617   86 LDKFYKKV----------YDKGLTIPEDILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLI--NRNGQ-VKLCDFGISG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 550 LRPQSPGVPMQTPCftLQYAAPEL----LAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06617  153 YLVDSVAKTIDAGC--KPYMAPERinpeLNQKGYDVKSDVWSLGITMIELATGRFPY 207
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
410-606 1.06e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 72.34  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE------ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEI--RLEheegapCTAIREVSLLKDLK-HANIVTLHDIIHTEKSLTLVFEYLDKDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRpqspGVPMQT-- 561
Cdd:cd07873   87 KQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRK-VLHRDLKPQNLLINER---GELKLADFGLARAK----SIPTKTys 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 562 -PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07873  159 nEVVTLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGST 205
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
406-602 1.09e-13

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 72.45  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLcQSHPNVVNLhevhhdqLHTYLV------L 476
Cdd:cd06656   23 RFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEliiNEILVMRE-NKNPNIVNY-------LDSYLVgdelwvV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRPQSP 555
Cdd:cd06656   95 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ-VIHRDIKSDNILLGMD---GSVKLTDFGFcAQITPEQS 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 556 gvPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06656  171 --KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
410-667 1.16e-13

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 72.40  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKIlsRRLEAN---TQREVAALRLCQS--------HPNVVNLHEVHHDQLHTY-LVLE 477
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVKI--HQLNKNwrdEKKENYHKHACREyrihkeldHPRIVKLYDYFSLDTDSFcTVLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDTPGAPVKIIDFGFAR------- 549
Cdd:cd14041   92 YCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEiKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKimdddsy 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 550 -------LRPQSPGVPMQTP--CFTLQYAAPELlaqqgyDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMcK 620
Cdd:cd14041  172 nsvdgmeLTSQGAGTYWYLPpeCFVVGKEPPKI------SNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTIL-K 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 621 IREGRFSLDgeawQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd14041  245 ATEVQFPPK----PVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
138-303 1.25e-13

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 73.24  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 138 VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS-KEFLTEEKERTFSFCgTIEYMAPEIIRSKTGHG 216
Cdd:cd07853  105 VKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLArVEEPDESKHMTQEVV-TQYYRAPEILMGSRHYT 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 217 KAVDWWSLGILLFELLTG------ASPFT-------------LEGERNTQAEVSRRILKcSPPFPPRIGPV--------- 268
Cdd:cd07853  184 SAVDIWSVGCIFAELLGRrilfqaQSPIQqldlitdllgtpsLEAMRSACEGARAHILR-GPHKPPSLPVLytlssqath 262
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663856869 269 -AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQG 303
Cdd:cd07853  263 eAVHLLCRMLVFDPDKRI-----SAADALAHPYLDE 293
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
34-245 1.36e-13

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 71.59  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  34 ELLKVLGTGAYGKVFLVRKAGGhdagklYAMKVLRKAAlvQRAKTQEHTRTERSVLELVRQAPFLvtLHYAFQTDAKLHL 113
Cdd:cd14150    3 SMLKRIGTGSFGTVFRGKWHGD------VAVKILKVTE--PTPEQLQAFKNEMQVLRKTRHVNIL--LFMGFMTRPNFAI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL----SKEFLT 188
Cdd:cd14150   73 ITQWCEGSSLYRHLHvTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLatvkTRWSGS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 189 EEKERTfsfCGTIEYMAPEIIRSKTGHGKAV--DWWSLGILLFELLTGASPFTLEGERN 245
Cdd:cd14150  153 QQVEQP---SGSILWMAPEVIRMQDTNPYSFqsDVYAYGVVLYELMSGTLPYSNINNRD 208
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
31-254 1.38e-13

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 71.45  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAGGHDAgklyAMKVLRKAAL-----VQRAKTQEHTRTERsvlelvrqapfLVTLHYAF 105
Cdd:cd05113    4 KDLTFLKELGTGQFGVVKYGKWRGQYDV----AIKMIKEGSMsedefIEEAKVMMNLSHEK-----------LVQLYGVC 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd05113   69 TKQRPIFIITEYMANGCLLNYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 185 EFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRI 254
Cdd:cd05113  149 YVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKS-DVWAFGVLMWEVYSlGKMPY----ERFTNSETVEHV 214
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
501-607 1.53e-13

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 72.22  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHEEAGVVHRDLKPENILYADDTPGapVKIIDFGFArlrpqspgvpmqtpCF----------TLQYAA 570
Cdd:cd14136  123 KIARQVLQGLDYLHTKCGIIHTDIKPENVLLCISKIE--VKIADLGNA--------------CWtdkhftediqTRQYRS 186
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663856869 571 PELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd14136  187 PEVILGAGYGTPADIWSTACMAFELATGDYLFDPHSG 223
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
410-602 1.61e-13

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 71.10  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA---VKiLSRRLEANTQR---EVAALRLCQsHPNVVNLHEVHHDQLHTY--LVLELLRG 481
Cdd:cd13983    9 LGRGSFKTVYRAFDTEEGIEVAwneIK-LRKLPKAERQRfkqEIEILKSLK-HPNIIKFYDSWESKSKKEviFITELMTS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSE----SEASQILRSLVsavsFMH-EEAGVVHRDLKPENILYadDTPGAPVKIIDFGFARLRPQSPG 556
Cdd:cd13983   87 GTLKQYLKRFKRLKLkvikSWCRQILEGLN----YLHtRDPPIIHRDLKCDNIFI--NGNTGEVKIGDLGLATLLRQSFA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 557 VP-MQTPcftlQYAAPELLaQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd13983  161 KSvIGTP----EFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPY 202
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
410-603 1.80e-13

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 72.02  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQR--QSGQEFAVK-ILSRRLEANTQREVAALRLCQsHPNVVNLHEV--HHDQLHTYLVLELLRGGEL 484
Cdd:cd07867   10 VGRGTYGHVYKAKRKdgKDEKEYALKqIEGTGISMSACREIALLRELK-HPNVIALQKVflSHSDRKVWLLFDYAEHDLW 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 leHI----------RKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPG-APVKIIDFGFARL--R 551
Cdd:cd07867   89 --HIikfhraskanKKPMQLPRSMVKSLLYQILDGIHYLHAN-WVLHRDLKPANILVMGEGPErGRVKIADMGFARLfnS 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 552 PQSPGVPMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd07867  166 PLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFH 218
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
144-284 1.89e-13

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 71.37  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLG--IIYRDLKLENVLLDSEGHIVLTDFGLSK--EFLTEEKERTFSFCGTIEYMAPEIIRSKT-GHGKA 218
Cdd:cd14025  100 ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwnGLSHSHDLSRDGLRGTIAYLPPERFKEKNrCPDTK 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 219 VDWWSLGILLFELLTGASPFTleGERNtqaeVSRRILKCSPPFPPRIGPVAQ----------DLLQRLLCKDPKKR 284
Cdd:cd14025  180 HDVYSFAIVIWGILTQKKPFA--GENN----ILHIMVKVVKGHRPSLSPIPRqrpsecqqmiCLMKRCWDQDPRKR 249
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
122-284 2.32e-13

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 70.64  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV--LTDFGLSKEFlteEKERTFSFCG 199
Cdd:cd14112   85 DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQvkLVDFGRAQKV---SKLGKVPVDG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTleGERNTQAEVSRRIL--KCSPPF-PPRIGPVAQDLLQRL 276
Cdd:cd14112  162 DTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFT--SEYDDEEETKENVIfvKCRPNLiFVEATQEALRFATWA 239

                 ....*...
gi 663856869 277 LCKDPKKR 284
Cdd:cd14112  240 LKKSPTRR 247
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
28-284 2.44e-13

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 70.84  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKaalVQRAKTQehTRTERSVLELVRQaPFLVTLHYAFQT 107
Cdd:cd05039    3 INKKDLKLGELIGKGEFGDVML-----GDYRGQKVAVKCLKD---DSTAAQA--FLAEASVMTTLRH-PNLVQLLGVVLE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05039   72 GNGLYIVTEYMAKGSLVDYLRSRgrAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSfcgtIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTlegeRNTQAEVSRRILK-----CSP 259
Cdd:cd05039  152 ASSNQDGGKLP----IKWTAPEALREKKFSTKS-DVWSFGILLWEIYSfGRVPYP----RIPLKDVVPHVEKgyrmeAPE 222
                        250       260
                 ....*....|....*....|....*
gi 663856869 260 PFPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:cd05039  223 GCPPEV----YKVMKNCWELDPAKR 243
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
410-661 2.74e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 70.80  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA-VKILSRRL-EANTQR---EVAALRlCQSHPNVVNLHE----VHHDQLHTYLVLELLR 480
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAwCELQTRKLsKGERQRfseEVEMLK-GLQHPNIVRFYDswksTVRGHKCIILVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG-VVHRDLKPENILYADdtPGAPVKIIDFGFARLRPQSpgvPM 559
Cdd:cd14033   88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCPpILHRDLKCDNIFITG--PTGSVKIGDLGLATLKRAS---FA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPCFTLQYAAPELLAQQgYDESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGRFSldGEAWQGVSEE 639
Cdd:cd14033  163 KSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSEC------QNAAQIYRKVTSGIKP--DSFYKVKVPE 233
                        250       260
                 ....*....|....*....|..
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGL 661
Cdd:cd14033  234 LKEIIEGCIRTDKDERFTIQDL 255
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
410-655 2.95e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 70.54  E-value: 2.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSG-----QEFAVKILSRRLEANTQREVAALRLCQsHPNVVNL--HEVHHDQLHTYLVLELLRGG 482
Cdd:cd08221    8 LGRGAFGEAVLYRKTEDNslvvwKEVNLSRLSEKERRDALNEIDILSLLN-HDNIITYynHFLDGESLFIEMEYCNGGNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYaddTPGAPVKIIDFGFAR-LRPQSPgvpMQT 561
Cdd:cd08221   87 HDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHK-AGILHRDIKTLNIFL---TKADLVKLGDFGISKvLDSESS---MAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCF-TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQgASGQggqsqaAEIMCKIREGRFSLDGEAWqgvSEEA 640
Cdd:cd08221  160 SIVgTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFD-ATNP------LRLAVKIVQGEYEDIDEQY---SEEI 229
                        250
                 ....*....|....*
gi 663856869 641 KELVRGLLTVDPAKR 655
Cdd:cd08221  230 IQLVHDCLHQDPEDR 244
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
410-606 3.11e-13

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 71.51  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR--EVAALRLC------QSHPNVVNL--HEVHHDqlHTYLVLELL 479
Cdd:cd14212    7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAmlEIAILTLLntkydpEDKHHIVRLldHFMHHG--HLCIVFELL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEhIRKKRH--FSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGApVKIIDFGFArlrpqspgv 557
Cdd:cd14212   85 GVNLYEL-LKQNQFrgLSLQLIRKFLQQLLDALSVLKD-ARIIHCDLKPENILLVNLDSPE-IKLIDFGSA--------- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 558 pmqtpCFTLQ----------YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14212  153 -----CFENYtlytyiqsrfYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNS 206
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
4-239 3.84e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 72.38  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   4 EDDDESCAVELRITEAnltgheekvSVENFELLKVLGTGAYGKVFlvrkagghdagKLYAMKVLRKAALVQRAKTQEHTR 83
Cdd:PTZ00036  48 EDEDEEKMIDNDINRS---------PNKSYKLGNIIGNGSFGVVY-----------EAICIDTSEKVAIKKVLQDPQYKN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  84 TERSVLELVRQAP--FLVTLHY--AFQTDAK---LHLILDYVSggeMFTHLYQRQYFKEAE------VRVYGGEIVLALE 150
Cdd:PTZ00036 108 RELLIMKNLNHINiiFLKDYYYteCFKKNEKnifLNVVMEFIP---QTVHKYMKHYARNNHalplflVKLYSYQLCRALA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 151 HLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSKEFLTeeKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLF 229
Cdd:PTZ00036 185 YIHSKFICHRDLKPQNLLIDPNTHTLkLCDFGSAKNLLA--GQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIA 262
                        250
                 ....*....|
gi 663856869 230 ELLTGASPFT 239
Cdd:PTZ00036 263 EMILGYPIFS 272
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
39-284 4.00e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 70.16  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAAlvqraktqehtrtERSVLELVR-QAPFLVTLHYAFQTDAKLHLILDY 117
Cdd:cd14058    1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAF-------------EVEVRQLSRvDHPNIIKLYGACSNQKPVCLVMEY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLYQRQ---YFKEAEVRVYGGEIVLALEHLHKLG---IIYRDLKLENVLLdSEGHIVLT--DFGLSKEF--- 186
Cdd:cd14058   68 AEGGSLYNVLHGKEpkpIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLL-TNGGTVLKicDFGTACDIsth 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKertfsfcGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLTGASPFT-LEGERntqaevSRRILKCS----PPF 261
Cdd:cd14058  147 MTNNK-------GSAAWMAPEVFEGSKYSEKC-DVFSWGIILWEVITRRKPFDhIGGPA------FRIMWAVHngerPPL 212
                        250       260
                 ....*....|....*....|...
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14058  213 IKNCPKPIESLMTRCWSKDPEKR 235
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
410-606 4.69e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 70.94  E-value: 4.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ--REVAAL-RLCQSHP---NVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14211    7 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqIEVSILsRLSQENAdefNFVRAYECFQHKNHTCLVFEMLEQNL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LleHIRKKRHFSESEASQI---LRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgAP--VKIIDFGfarlrpqSPGVP 558
Cdd:cd14211   87 Y--DFLKQNKFSPLPLKYIrpiLQQVLTALLKL-KSLGLIHADLKPENIMLVDPVR-QPyrVKVIDFG-------SASHV 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 559 MQTPCFT-LQ---YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14211  156 SKAVCSTyLQsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSS 207
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
39-239 5.56e-13

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 70.09  E-value: 5.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGhdagklYAMKVLRKAAlvQRAKTQEHTRTERSVLELVRQAPFLVTLHYAfqTDAKLHLILDYV 118
Cdd:cd14151   16 IGSGSFGTVYKGKWHGD------VAVKMLNVTA--PTPQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVTQWC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQY-FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTF-S 196
Cdd:cd14151   86 EGSSLYHHLHIIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFeQ 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 197 FCGTIEYMAPEIIR--SKTGHGKAVDWWSLGILLFELLTGASPFT 239
Cdd:cd14151  166 LSGSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPYS 210
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
33-301 5.64e-13

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 70.39  E-value: 5.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL-VRKAGghDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVL-ELvrQAPFLVTLHYAF--QTD 108
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKaKRKNG--KDGKEYAIKKFKGDKEQYTGISQSACR-EIALLrEL--KHENVVSLVEVFleHAD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSG--GEMFTHLYQ--RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH----IVLTDF 180
Cdd:cd07842   77 KSVYLLFDYAEHdlWQIIKFHRQakRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 181 GLS-------KEFLTEEKERTfsfcgTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNT-----QA 248
Cdd:cd07842  157 GLArlfnaplKPLADLDPVVV-----TIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKIKksnpfQR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 249 EVSRRILKC--------------------------SPPFPPRI-----------GPVAQDLLQRLLCKDPKKRLgagpqG 291
Cdd:cd07842  232 DQLERIFEVlgtptekdwpdikkmpeydtlksdtkASTYPNSLlakwmhkhkkpDSQGFDLLRKLLEYDPTKRI-----T 306
                        330
                 ....*....|
gi 663856869 292 AQEVRNHPFF 301
Cdd:cd07842  307 AEEALEHPYF 316
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
32-284 5.76e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 69.90  E-value: 5.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEhtRTERSVLELVR-QAPFLVTLHYAFQTD-- 108
Cdd:cd14048    7 DFEPIQCLGRGGFGVVF---EAKNKVDDCNYAVKRIR---LPNNELARE--KVLREVRALAKlDHPGIVRYFNAWLERpp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVsggemftHLY-QRQYFKEAEVRVYGG------------------EIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14048   79 EGWQEKMDEV-------YLYiQMQLCRKENLKDWMNrrctmesrelfvclnifkQIASAVEYLHSKGLIHRDLKPSNVFF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEFLTEEKERTF-----------SFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTgasPF 238
Cdd:cd14048  152 SLDDVVKVGDFGLVTAMDQGEPEQTVltpmpayakhtGQVGTRLYMSPEQIHGNQ-YSEKVDIFALGLILFELIY---SF 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 239 TLEGER-NTQAEVsrRILKCSPPFPPRIgPVAQDLLQRLLCKDPKKR 284
Cdd:cd14048  228 STQMERiRTLTDV--RKLKFPALFTNKY-PEERDMVQQMLSPSPSER 271
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
36-233 5.83e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 69.92  E-value: 5.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVR-KAGGHDAGKLYAMKvlrkaalvqraKTQEHTRTErsVLELVRQAPFLVTLHYAFQTDAK---- 110
Cdd:cd05081    9 ISQLGKGNFGSVELCRyDPLGDNTGALVAVK-----------QLQHSGPDQ--QRDFQREIQILKALHSDFIVKYRgvsy 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 ------LHLILDYVSGGEMFTHLYQRQYFKEA-EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd05081   76 gpgrrsLRLVMEYLPSGCLRDFLQRHRARLDAsRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLA 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 184 K-------EFLTEEKERTFSFcgtieYMAPEIIrSKTGHGKAVDWWSLGILLFELLT 233
Cdd:cd05081  156 KllpldkdYYVVREPGQSPIF-----WYAPESL-SDNIFSRQSDVWSFGVVLYELFT 206
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
39-238 5.89e-13

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 69.34  E-value: 5.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrKAGGHDAgklYAMKVLRkaaLVQRAKTQEHT-RTERSVLELVRQAPFLvtLHYAFQTDAKLHLILDY 117
Cdd:cd14062    1 IGSGSFGTVY---KGRWHGD---VAVKKLN---VTDPTPSQLQAfKNEVAVLRKTRHVNIL--LFMGYMTKPQLAIVTQW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS---KEFLTEEKER 193
Cdd:cd14062   70 CEGSSLYKHLHvLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkTRWSGSQQFE 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 194 TFSfcGTIEYMAPEIIRSKTGHGKAV--DWWSLGILLFELLTGASPF 238
Cdd:cd14062  150 QPT--GSILWMAPEVIRMQDENPYSFqsDVYAFGIVLYELLTGQLPY 194
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
398-606 5.93e-13

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 70.81  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 398 MMQYELDlrePALGQGSFSVCRRCRQRQSGQEFAVKILSRRLE--ANTQREVAALRLCQSHPNVVNLHEV---HHDQLHT 472
Cdd:cd14226   12 MDRYEID---SLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAflNQAQIEVRLLELMNKHDTENKYYIVrlkRHFMFRN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 473 YLVLELLRGGELLEHIRKKRHF---SESEASQILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDTPGApVKIIDFGfa 548
Cdd:cd14226   89 HLCLVFELLSYNLYDLLRNTNFrgvSLNLTRKFAQQLCTALLFLSTpELSIIHCDLKPENILLCNPKRSA-IKIIDFG-- 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 549 rlrpqspgvpmqTPCFTLQ----------YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14226  166 ------------SSCQLGQriyqyiqsrfYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGAN 221
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
410-602 7.18e-13

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 69.76  E-value: 7.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQShPNVVNLHEVHHDQLHTYL-VLELLRGGEL 484
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQkqilRELEINKSCAS-PYIVKYYGAFLDEQDSSIgIAMEYCEGGS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKK-----RHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGvpm 559
Cdd:cd06621   88 LDSIYKKvkkkgGRIGEKVLGKIAESVLKGLSYLHSRK-IIHRDIKPSNILL--TRKGQ-VKLCDFGVSGELVNSLA--- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06621  161 GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF 203
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
131-287 7.29e-13

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 70.29  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 131 QYFkeaevrVYggEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeflTEEKERTfSFCGTIEYMAPEIIR 210
Cdd:cd07856  111 QYF------LY--QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR---IQDPQMT-GYVSTRYYRAPEIML 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 211 SKTGHGKAVDWWSLGILLFELLTGASPF-------------TLEGE------RNTQAEVSRRILKCSP-----PFP---P 263
Cdd:cd07856  179 TWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitELLGTppddviNTICSENTLRFVQSLPkrervPFSekfK 258
                        170       180
                 ....*....|....*....|....
gi 663856869 264 RIGPVAQDLLQRLLCKDPKKRLGA 287
Cdd:cd07856  259 NADPDAIDLLEKMLVFDPKKRISA 282
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
33-238 7.58e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 69.54  E-value: 7.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHD-AGKLYAMKVLRkaalvqRAKTQEHTRTERSVLELVRQAPFLVTLHY----AFQT 107
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYDPTNDgTGEMVAVKALK------ADCGPQHRSGWKQEIDILKTLYHENIVKYkgccSEQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGEMFTHLyQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd05080   80 GKSLQLIMEYVPLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVP 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 188 TEEKERTFSFCGT--IEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd05080  159 EGHEYYRVREDGDspVFWYAPECLK-EYKFYYASDVWSFGVTLYELLTHCDSS 210
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
407-655 7.86e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 69.67  E-value: 7.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEFAVK------ILSRRLEANTQREVAALRLCqSHPNVVNLHE--VHHDQLHTYL-VLE 477
Cdd:cd08229   29 EKKIGRGQFSEVYRATCLLDGVPVALKkvqifdLMDAKARADCIKEIDLLKQL-NHPNVIKYYAsfIEDNELNIVLeLAD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRK-KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFARLRpQSPG 556
Cdd:cd08229  108 AGDLSRMIKHFKKqKRLIPEKTVWKYFVQLCSALEHMHSRR-VMHRDIKPANVFI---TATGVVKLGDLGLGRFF-SSKT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFqgasgQGGQSQAAEIMCKIREGRF-SLDGEAWqg 635
Cdd:cd08229  183 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF-----YGDKMNLYSLCKKIEQCDYpPLPSDHY-- 255
                        250       260
                 ....*....|....*....|
gi 663856869 636 vSEEAKELVRGLLTVDPAKR 655
Cdd:cd08229  256 -SEELRQLVNMCINPDPEKR 274
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
410-682 8.05e-13

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 70.08  E-value: 8.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAAL--RLCQSH------PNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd14223    8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALneRIMLSLvstgdcPFIVCMSYAFHTPDKLSFILDLMNG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFG----FARLRPQSPgv 557
Cdd:cd14223   88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRF-VVYRDLKPANILLDEF---GHVRISDLGlacdFSKKKPHAS-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 pmqtpCFTLQYAAPELLaQQG--YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQsqaaeimcKIREGRFSLDGEAWQG 635
Cdd:cd14223  162 -----VGTHGYMAPEVL-QKGvaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH--------EIDRMTLTMAVELPDS 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGlRGSSwlqdgSARSSPPLRTPD 682
Cdd:cd14223  228 FSPELRSLLEGLLQRDVNRRLGCMG-RGAQ-----EVKEEPFFRGLD 268
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
32-233 8.60e-13

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 69.66  E-value: 8.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGHD-AGKLYAMKVLRKAalvqrakTQEHTRTERSVLELVR--QAPFLVTLHYAFQTD 108
Cdd:cd14205    5 HLKFLQQLGKGNFGSVEMCRYDPLQDnTGEVVAVKKLQHS-------TEEHLRDFEREIEILKslQHDNIVKYKGVCYSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AK--LHLILDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd14205   78 GRrnLRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSFCGT--IEYMAPEIIrSKTGHGKAVDWWSLGILLFELLT 233
Cdd:cd14205  158 LPQDKEYYKVKEPGEspIFWYAPESL-TESKFSVASDVWSFGVVLYELFT 206
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
35-245 8.97e-13

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 69.67  E-value: 8.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLVRKAGGhdagklYAMKVLRkaaLVQRAKTQ-EHTRTERSVLELVRQAPFLVTLHYafQTDAKLHL 113
Cdd:cd14149   16 LSTRIGSGSFGTVYKGKWHGD------VAVKILK---VVDPTPEQfQAFRNEVAVLRKTRHVNILLFMGY--MTKDNLAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK-EFLTEEK 191
Cdd:cd14149   85 VTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGS 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKAV--DWWSLGILLFELLTGASPFTLEGERN 245
Cdd:cd14149  165 QQVEQPTGSILWMAPEVIRMQDNNPFSFqsDVYSYGIVLYELMTGELPYSHINNRD 220
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
410-602 8.99e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 69.30  E-value: 8.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA-NTQREVAALRlCQ-------SHPNVVNLHEVHHDQLHTYLVLELLRG 481
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVQFDPESpETSKEVNALE-CEiqllknlLHERIVQYYGCLRDPQERTLSIFMEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRH--FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILyaDDTPGApVKIIDFGFARlRPQS---PG 556
Cdd:cd06652   89 PGGSIKDQLKSYgaLTENVTRKYTRQILEGVHYLHSNM-IVHRDIKGANIL--RDSVGN-VKLGDFGASK-RLQTiclSG 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06652  164 TGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
33-238 1.04e-12

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 69.37  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL-VRKAGGHDAGKLYAMKVLRKAAlvQRAKTQEHTRtERSVLELVrQAPFLVTLhYAFQTDAKL 111
Cdd:cd05057    9 LEKGKVLGSGAFGTVYKgVWIPEGEKVKIPVAIKVLREET--GPKANEEILD-EAYVMASV-DHPHLVRL-LGICLSSQV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQRQyfkeAEVRVY-----GGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKef 186
Cdd:cd05057   84 QLITQLMPLGCLLDYVRNHR----DNIGSQlllnwCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK-- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 187 LTEEKERTFSFCG---TIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05057  158 LLDVDEKEYHAEGgkvPIKWMALESIQYRIYTHKS-DVWSYGVTVWELMTfGAKPY 212
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
488-667 1.09e-12

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 68.95  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGApVKIIDFGFAR----LRPQSPGVPMQTPC 563
Cdd:cd06629   99 LRKYGKFEEDLVRFFTRQILDGLAYLHSK-GILHRDLKADNILV--DLEGI-CKISDFGISKksddIYGNNGATSMQGSV 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 564 FtlqYAAPELL--AQQGYDESCDLWSLGVILYMMLSGQVP------FQGASGQGGQSQAAEIMCKIRegrfsldgeawqg 635
Cdd:cd06629  175 F---WMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPwsddeaIAAMFKLGNKRSAPPVPEDVN------------- 238
                        170       180       190
                 ....*....|....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd06629  239 LSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
410-605 1.10e-12

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 69.79  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA---VKILSRRLEANTQREV--------AALRLCQ-----SHPNVVNLHEVHHDQLHTY 473
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLvgmcgihfTTLRELKimneiKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVLELLRGGELLEHIRKKRhFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQ 553
Cdd:PTZ00024  97 LVMDIMASDLKKVVDRKIR-LTESQVKCILLQILNGLNVLHKWY-FMHRDLSPANIFI--NSKGI-CKIADFGLARRYGY 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 554 SPGVP-------------MQTPCFTLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQGA 605
Cdd:PTZ00024 172 PPYSDtlskdetmqrreeMTSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGE 237
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
410-601 1.11e-12

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 68.67  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ-REVAALRlCQSHPNVVNLHEV--HHDQLHtYLVLELLRGGELLE 486
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFlKEVKLMR-RLSHPNILRFIGVcvKDNKLN-FITEYVNGGTLEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGV-PMQTPCFT 565
Cdd:cd14065   79 LKSMDEQLPWSQRVSLAKDIASGMAYLHSK-NIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKkPDRKKRLT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663856869 566 L----QYAAPELLAQQGYDESCDLWSLGVILYMMLsGQVP 601
Cdd:cd14065  158 VvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP 196
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
501-645 1.14e-12

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 68.63  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHEEA-GVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPGVPMQ--TPCF--TLQYAAPELL- 574
Cdd:cd13978   97 RIIHEIALGMNFLHNMDpPLLHHDLKPENILLDNHF---HVKISDFGLSKLGMKSISANRRrgTENLggTPIYMAPEAFd 173
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 575 -AQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQggqsqaAEIMCKIREG-RFSLDGEAWQGVSEEAKELVR 645
Cdd:cd13978  174 dFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINP------LLIMQIVSKGdRPSLDDIGRLKQIENVQELIS 240
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
39-284 1.22e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 69.19  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVR-KAGGHDAGKLYAMKVLRKAAlvqrakTQEHTRTERSVLELVRQAPFLVTLHYAF----QTDAKLHL 113
Cdd:cd05079   12 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES------GGNHIADLKKEIEILRNLYHENIVKYKGicteDGGNGIKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHL-YQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKE 192
Cdd:cd05079   86 IMEFLPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 193 RTFS--FCGTIEYMAPE-IIRSKtgHGKAVDWWSLGILLFELLT----GASPFT----LEGERNTQAEVSR--RILKCSP 259
Cdd:cd05079  166 YTVKddLDSPVFWYAPEcLIQSK--FYIASDVWSFGVTLYELLTycdsESSPMTlflkMIGPTHGQMTVTRlvRVLEEGK 243
                        250       260
                 ....*....|....*....|....*..
gi 663856869 260 --PFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd05079  244 rlPRPPNCPEEVYQLMRKCWEFQPSKR 270
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
410-656 1.26e-12

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 69.09  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKilSRRLEANTQ-------REVAALRLCQSHPNVVNLHEVHH----DQLHTYLVLEL 478
Cdd:cd07837    9 IGEGTYGKVYKARDKNTGKLVALK--KTRLEMEEEgvpstalREVSLLQMLSQSIYIVRLLDVEHveenGKPLLYLVFEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRS----LVSAVSFMHEEaGVVHRDLKPENILyADDTPGApVKIIDFGFARlrpqS 554
Cdd:cd07837   87 LDTDLKKFIDSYGRGPHNPLPAKTIQSfmyqLCKGVAHCHSH-GVMHRDLKPQNLL-VDKQKGL-LKIADLGLGR----A 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 PGVPMQT---PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIregrFSLDG 630
Cdd:cd07837  160 FTIPIKSythEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDS-------ELQQLLHI----FRLLG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 631 ----EAWQGVSE------------------------EAKELVRGLLTVDPAKRL 656
Cdd:cd07837  229 tpneEVWPGVSKlrdwheypqwkpqdlsravpdlepEGVDLLTKMLAYDPAKRI 282
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
410-601 1.38e-12

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 69.00  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR---EVAALRLCQsHPNVVNLHEVH-HDQLHTYLVLELLRGGELL 485
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDfmvEIDILSECK-HPNIVGLYEAYfYENKLWILIEFCDGGALDS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRP--QSPGVPMQTP 562
Cdd:cd06611   92 IMLELERGLTEPQIRYVCRQMLEALNFLHSHK-VIHRDLKAGNILLTLD---GDVKLADFGVsAKNKStlQKRDTFIGTP 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 663856869 563 cftlQYAAPELLA-----QQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06611  168 ----YWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPP 207
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
410-602 1.56e-12

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 68.87  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILS--RRLEANTQREVAALRLCQSHPNVVNLHEVHH--DQL---HTYLVLEL---- 478
Cdd:cd06639   30 IGKGTYGKVYKVTNKKDGSLAAVKILDpiSDVDEEIEAEYNILRSLPNHPNVVKFYGMFYkaDQYvggQLWLVLELcngg 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGF------ARLRP 552
Cdd:cd06639  110 SVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNR-IIHRDVKGNNILL---TTEGGVKLVDFGVsaqltsARLRR 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 553 Q-SPGVPMqtpcftlqYAAPELLA--QQ---GYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06639  186 NtSVGTPF--------WMAPEVIAceQQydySYDARCDVWSLGITAIELADGDPPL 233
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
406-602 1.57e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 68.98  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLCQShPNVVNLHEVH--HDQLhtyLVLELLR 480
Cdd:cd06655   23 RYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEliiNEILVMKELKN-PNIVNFLDSFlvGDEL---FVVMEYL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRPQSPgvPM 559
Cdd:cd06655   99 AGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQ-VIHRDIKSDNVLLGMD---GSVKLTDFGFcAQITPEQS--KR 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06655  173 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
410-602 1.93e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 68.53  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREllfNEVVIMRDYH-HENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRPQSPgvPMQTPCFT 565
Cdd:cd06658  109 IVTHTR-MNEEQIATVCLSVLRALSYLHNQ-GVIHRDIKSDSILLTSD---GRIKLSDFGFcAQVSKEVP--KRKSLVGT 181
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06658  182 PYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPY 218
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
32-237 1.95e-12

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 68.05  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKAGGhdaGKLYAMKVLRKAALVQRAKTqehtrtERSVLELVRQAPFLVTLHYAFQTDAKL 111
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVD---GEEVAMKVESKSQPKQVLKM------EVAVLKKLQGKPHFCRLIGCGRTERYN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYV--SGGEMFTHLYQRQYFKEAEVRVyGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH----IVLTDFGLSKE 185
Cdd:cd14017   72 YIVMTLLgpNLAELRRSQPRGKFSVSTTLRL-GIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQ 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 186 FLTEEKER------TFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLTGASP 237
Cdd:cd14017  151 YTNKDGEVerpprnAAGFRGTVRYASVNAHRNKE-QGRRDDLWSWFYMLIEFVTGQLP 207
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
410-603 2.02e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 68.93  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQR--QSGQEFAVK-ILSRRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd07868   25 VGRGTYGHVYKAKRKdgKDDKDYALKqIEGTGISMSACREIALLRELK-HPNVISLQKVFLSHADRKVWLLFDYAEHDLW 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESE----------ASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPG-APVKIIDFGFARL--RPQ 553
Cdd:cd07868  104 HIIKFHRASKANkkpvqlprgmVKSLLYQILDGIHYLHAN-WVLHRDLKPANILVMGEGPErGRVKIADMGFARLfnSPL 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 554 SPGVPMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd07868  183 KPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFH 233
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
502-618 2.06e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 69.49  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 502 ILRSLVSAVSFMHEEaGVVHRDLKPENILYadDTPGAPVkIIDFGFARLRPQSPGVPMqtpCF----TLQYAAPELLAQQ 577
Cdd:PHA03207 190 IQRRLLEALAYLHGR-GIIHRDVKTENIFL--DEPENAV-LGDFGAACKLDAHPDTPQ---CYgwsgTLETNSPELLALD 262
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663856869 578 GYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIM 618
Cdd:PHA03207 263 PYCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSSSSQLRSII 303
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
113-284 2.07e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 67.67  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHK---LGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFl 187
Cdd:cd14060   59 IVTEYASYGSLFDYLNSNesEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASRFH- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 188 teEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTGASPFT-LEGERNTQAEVSrrilKCSPPFPPRIG 266
Cdd:cd14060  138 --SHTTHMSLVGTFPWMAPEVIQS-LPVSETCDTYSYGVVLWEMLTREVPFKgLEGLQVAWLVVE----KNERPTIPSSC 210
                        170
                 ....*....|....*....
gi 663856869 267 PVA-QDLLQRLLCKDPKKR 284
Cdd:cd14060  211 PRSfAELMRRCWEADVKER 229
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
28-265 2.10e-12

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 68.17  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVF---LVRKAGGHDAGKLyAMKVLRKAALVqraKTQEHTRTERSVLELVRQaPFLVTLHYA 104
Cdd:cd05048    2 IPLSAVRFLEELGEGAFGKVYkgeLLGPSSEESAISV-AIKTLKENASP---KTQQDFRREAELMSDLQH-PNIVCLLGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGI----------------IYRDLKLENVL 168
Cdd:cd05048   77 CTKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIaiqiaagmeylsshhyVHRDLAARNCL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 169 LDSEGHIVLTDFGLSKEFLTEEKERTFSFCG-TIEYMAPEIIRSktghGK---AVDWWSLGILLFELLT-GASPFTleGE 243
Cdd:cd05048  157 VGDGLTVKISDFGLSRDIYSSDYYRVQSKSLlPVRWMPPEAILY----GKfttESDVWSFGVVLWEIFSyGLQPYY--GY 230
                        250       260
                 ....*....|....*....|....*..
gi 663856869 244 RNTqaEV-----SRRILKCSPPFPPRI 265
Cdd:cd05048  231 SNQ--EViemirSRQLLPCPEDCPARV 255
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
400-596 2.14e-12

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 68.74  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 400 QYELdLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLCQS-HPNVVNLHEV---------- 465
Cdd:cd13977    1 KYSL-IRE--VGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVElalREFWALSSIQRqHPNVIQLEECvlqrdglaqr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 --HHD---QLHTYLVLELLRGGELL---------------------EHIRKKRHFSESEASQILRsLVSAVSFMHEEAgV 519
Cdd:cd13977   78 msHGSsksDLYLLLVETSLKGERCFdprsacylwfvmefcdggdmnEYLLSRRPDRQTNTSFMLQ-LSSALAFLHRNQ-I 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPGAPVKIIDFGFAR------LRPQSPGVPMQ----TPCFTLQYAAPELLaQQGYDESCDLWSLG 589
Cdd:cd13977  156 VHRDLKPDNILISHKRGEPILKVADFGLSKvcsgsgLNPEEPANVNKhflsSACGSDFYMAPEVW-EGHYTAKADIFALG 234

                 ....*..
gi 663856869 590 VILYMML 596
Cdd:cd13977  235 IIIWAMV 241
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
428-613 2.37e-12

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 67.72  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 428 QEFAVKILSrrlEANTQREVaalrlcqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRhfSESEASQILRSLV 507
Cdd:cd05085   34 QELKIKFLS---EARILKQY-------DHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKK--DELKTKQLVKFSL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 508 SAVSFMH--EEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRP----QSPGVPmQTPcftLQYAAPELLAQQGYDE 581
Cdd:cd05085  102 DAAAGMAylESKNCIHRDLAARNCLVGENN---ALKISDFGMSRQEDdgvySSSGLK-QIP---IKWTAPEALNYGRYSS 174
                        170       180       190
                 ....*....|....*....|....*....|...
gi 663856869 582 SCDLWSLGVILYMMLS-GQVPFQGASGQGGQSQ 613
Cdd:cd05085  175 ESDVWSFGILLWETFSlGVCPYPGMTNQQAREQ 207
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
388-655 2.57e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 70.54  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  388 PGRAAVARSAMMQYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILSRR-----------LEANTQREVaalrlcqSH 456
Cdd:PTZ00266    2 PGKYDDGESRLNEYEVIKK---IGNGRFGEVFLVKHKRTQEFFCWKAISYRglkereksqlvIEVNVMREL-------KH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  457 PNVVNLHE--VHHDQLHTYLVLELLRGGELLEHIRK-KRHFSESEASQIL---RSLVSAVSFMHEEAG------VVHRDL 524
Cdd:PTZ00266   72 KNIVRYIDrfLNKANQKLYILMEFCDAGDLSRNIQKcYKMFGKIEEHAIVditRQLLHALAYCHNLKDgpngerVLHRDL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  525 KPENILY-------------ADDTPGAPV-KIIDFGFARlrpqSPGV-PMQTPCF-TLQYAAPELLAQQ--GYDESCDLW 586
Cdd:PTZ00266  152 KPQNIFLstgirhigkitaqANNLNGRPIaKIGDFGLSK----NIGIeSMAHSCVgTPYYWSPELLLHEtkSYDDKSDMW 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869  587 SLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGrfslDGEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:PTZ00266  228 ALGCIIYELCSGKTPFHKA------NNFSQLISELKRG----PDLPIKGKSKELNILIKNLLNLSAKER 286
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
30-301 2.92e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 68.16  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMK--------------VLRKAALVQRAKTQEHTRtersVLELVRQA 95
Cdd:cd07865   11 VSKYEKLAKIGQGTFGEVF---KARHRKTGQIVALKkvlmenekegfpitALREIKILQLLKHENVVN----LIEICRTK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 PflvTLHYAFQtdAKLHLILDYVSggemftH----LYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd07865   84 A---TPYNRYK--GSIYLVFEFCE------HdlagLLSNKNvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 170 DSEGHIVLTDFGLSKEFLTEEKERTFSFCG---TIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTgASPFtLEG--ER 244
Cdd:cd07865  153 TKDGVLKLADFGLARAFSLAKNSQPNRYTNrvvTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWT-RSPI-MQGntEQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 245 NTQAEVSRRILKCSPPFPPRI----------------------------GPVAQDLLQRLLCKDPKKRLgagpqGAQEVR 296
Cdd:cd07865  231 HQLTLISQLCGSITPEVWPGVdklelfkkmelpqgqkrkvkerlkpyvkDPYALDLIDKLLVLDPAKRI-----DADTAL 305

                 ....*
gi 663856869 297 NHPFF 301
Cdd:cd07865  306 NHDFF 310
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
410-597 2.99e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 68.12  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCR----QRQSGQEFAVKILSRRLEA---NTQREVAALRLCQsHPNVVNLHEVHHD--QLHTYLVLELLR 480
Cdd:cd14205   12 LGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEhlrDFEREIEILKSLQ-HDNIVKYKGVCYSagRRNLRLIMEYLP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRK-KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGV-- 557
Cdd:cd14205   91 YGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKR-YIHRDLATRNILVENENR---VKIGDFGLTKVLPQDKEYyk 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 663856869 558 ---PMQTPCFtlqYAAPELLAQQGYDESCDLWSLGVILYMMLS 597
Cdd:cd14205  167 vkePGESPIF---WYAPESLTESKFSVASDVWSFGVVLYELFT 206
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
372-611 3.49e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 69.34  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 372 NAVMTDGLEAPGAGDRPGRAAVAR-----SAMMQYEL--DLREPALGQGSFSVCRRC-----RQRQSGQEFAVKILSRRL 439
Cdd:PHA03210 116 DASHLDFDEAPPDAAGPVPLAQAKlkhddEFLAHFRVidDLPAGAFGKIFICALRASteeaeARRGVNSTNQGKPKCERL 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 440 EA----NTQR-------EVAALRLcQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSES----EASQILR 504
Cdd:PHA03210 196 IAkrvkAGSRaaiqlenEILALGR-LNHENILKIEEILRSEANTYMITQKYDFDLYSFMYDEAFDWKDRpllkQTRAIMK 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 505 SLVSAVSFMHEEAgVVHRDLKPENILYADDtpGAPVkIIDFGFArLRPQSPGVPMQTPCF-TLQYAAPELLAQQGYDESC 583
Cdd:PHA03210 275 QLLCAVEYIHDKK-LIHRDIKLENIFLNCD--GKIV-LGDFGTA-MPFEKEREAFDYGWVgTVATNSPEILAGDGYCEIT 349
                        250       260
                 ....*....|....*....|....*....
gi 663856869 584 DLWSLGVILYMMLSGQ-VPFQGASGQGGQ 611
Cdd:PHA03210 350 DIWSCGLILLDMLSHDfCPIGDGGGKPGK 378
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
30-304 3.51e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 67.92  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaaLVQRAKTQEHTRT-ERSVLELVRQAPfLVTLHYAFQTD 108
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVY---KARDRVTNETIALKKIR---LEQEDEGVPSTAIrEISLLKEMQHGN-IVRLQDVVHSE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGgEMFTHLYQRQYFKEAE--VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSKE 185
Cdd:PLN00009  74 KRLYLVFEYLDL-DLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALkLADFGLARA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTeeKERTFSF-CGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERN----------TQAEVSRRI 254
Cdd:PLN00009 153 FGI--PVRTFTHeVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDelfkifrilgTPNEETWPG 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 255 LKCSP----PFP-----------PRIGPVAQDLLQRLLCKDPKKRLGAgpQGAQEvrnHPFFQGL 304
Cdd:PLN00009 231 VTSLPdyksAFPkwppkdlatvvPTLEPAGVDLLSKMLRLDPSKRITA--RAALE---HEYFKDL 290
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
33-257 3.60e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 68.72  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghDAGKlyaMKVLRKAalVQRAKTQEhtrTERSVLELVRQAPFLVTLHyAFQTDAKLH 112
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVCTKHG--DEQR---KKVIVKA--VTGGKTPG---REIDILKTISHRAIINLIH-AYRWKSTVC 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGgEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS-KEFLTEEK 191
Cdd:PHA03207 163 MVMPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAcKLDAHPDT 241
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 192 ERTFSFCGTIEYMAPEIIRSKTGHGKaVDWWSLGILLFELLtgASPFTLEGERN-TQAEVSRRILKC 257
Cdd:PHA03207 242 PQCYGWSGTLETNSPELLALDPYCAK-TDIWSAGLVLFEMS--VKNVTLFGKQVkSSSSQLRSIIRC 305
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
410-606 3.74e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 68.09  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILsrRLE------ANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALKEI--RLEheegapCTAIREVSLLKDLK-HANIVTLHDIVHTDKSLTLVFEYLDKDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARLRpqspGVPMQT-- 561
Cdd:cd07872   91 KQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRK-VLHRDLKPQNLLINER---GELKLADFGLARAK----SVPTKTys 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 562 -PCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07872  163 nEVVTLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGST 209
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
410-660 4.74e-12

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 68.53  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAALRLCQSHPN---VVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd05625    9 LGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADnewVVRLYYSFQDKDNLYFVMDYIPGGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFA---------------- 548
Cdd:cd05625   89 MSLLIRMGVFPEDLARFYIAELTCAVESVHK-MGFIHRDIKPDNILIDRD---GHIKLTDFGLCtgfrwthdskyyqsgd 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 -----------------------RLRP-QSPGVPMQTPCF------TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSG 598
Cdd:cd05625  165 hlrqdsmdfsnewgdpencrcgdRLKPlERRAARQHQRCLahslvgTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 599 QVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTvDPAKRLKLEG 660
Cdd:cd05625  245 QPPFLAQT-------PLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRLGKNG 298
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
410-602 4.79e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 68.50  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSF-SVCRRCRQrQSGQEFAVKILSRR--LEANTQREVAALRLCQSHPN---VVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05626    9 LGIGAFgEVCLACKV-DTHALYAMKTLRKKdvLNRNQVAHVKAERDILAEADnewVVKLYYSFQDKDNLYFVMDYIPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFA--------------- 548
Cdd:cd05626   88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHK-MGFIHRDIKPDNILIDLD---GHIKLTDFGLCtgfrwthnskyyqkg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 -------------------------------RLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS 597
Cdd:cd05626  164 shirqdsmepsdlwddvsncrcgdrlktleqRATKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243

                 ....*
gi 663856869 598 GQVPF 602
Cdd:cd05626  244 GQPPF 248
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
33-234 5.07e-12

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 67.66  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLR-KAALVQRAktqehtRTERSVLELVRQApflvtlhyaFQTDAKL 111
Cdd:cd14212    1 YLVLDLLGQGTFGQVV---KCQDLKTNKLVAVKVLKnKPAYFRQA------MLEIAILTLLNTK---------YDPEDKH 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLI--LDYvsggemFTH--------------LY----QRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14212   63 HIVrlLDH------FMHhghlcivfellgvnLYellkQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILL 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 170 DS--EGHIVLTDFGlSKEFlteEKERTFSFCGTIEYMAPEIIrskTGH--GKAVDWWSLGILLFELLTG 234
Cdd:cd14212  137 VNldSPEIKLIDFG-SACF---ENYTLYTYIQSRFYRSPEVL---LGLpySTAIDMWSLGCIAAELFLG 198
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
410-606 6.43e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 67.50  E-value: 6.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLE-----ANTQREVAALRLCQsHPNVVnlhEVHHDQL--------HTYLVL 476
Cdd:cd07859    8 IGKGSYGVVCSAIDTHTGEKVAIKKINDVFEhvsdaTRILREIKLLRLLR-HPDIV---EIKHIMLppsrrefkDIYVVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEhIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLR-PQSP 555
Cdd:cd07859   84 ELMESDLHQV-IKANDDLTPEHHQFFLYQLLRALKYIHT-ANVFHRDLKPKNILANAD---CKLKICDFGLARVAfNDTP 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 556 GVPMQTP-CFTLQYAAPELLAQ--QGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd07859  159 TAIFWTDyVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKN 212
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
32-279 6.81e-12

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 66.91  E-value: 6.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVflVRKAGGHDAGK----LYAMKVLRKAAlvqrakTQEHTRTERSVLELVRQA--PFLVTLHYAF 105
Cdd:cd05045    1 NLVLGKTLGEGEFGKV--VKATAFRLKGRagytTVAVKMLKENA------SSSELRDLLSEFNLLKQVnhPHVIKLYGAC 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGG------------------------EIVLALEHLHKLGIIYRD 161
Cdd:cd05045   73 SQDGPLLLIVEYAKYGSLRSFLRESRKVGPSYLGSDGNrnssyldnpderaltmgdlisfawQISRGMQYLAEMKLVHRD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 162 LKLENVLLdSEGHIV-LTDFGLSKE------FLTEEKERTfsfcgTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT- 233
Cdd:cd05045  153 LAARNVLV-AEGRKMkISDFGLSRDvyeedsYVKRSKGRI-----PVKWMAIESLFDHIYTTQS-DVWSFGVLLWEIVTl 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 234 GASPFT----------------LEGERNTQAEVSRRILKC---SPPFPPRIGPVAQDlLQRLLCK 279
Cdd:cd05045  226 GGNPYPgiaperlfnllktgyrMERPENCSEEMYNLMLTCwkqEPDKRPTFADISKE-LEKMMVK 289
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
410-623 7.42e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 66.64  E-value: 7.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCR----QRQSGQEFAVKILSRRLEANT----QREVAALRLCQsHPNVVNLHEVHHDQ--LHTYLVLELL 479
Cdd:cd05038   12 LGEGHFGSVELCRydplGDNTGEQVAVKSLQPSGEEQHmsdfKREIEILRTLD-HEYIVKYKGVCESPgrRSLRLIMEYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESE-----ASQILRSLvsavSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQS 554
Cdd:cd05038   91 PSGSLRDYLQRHRDQIDLKrlllfASQICKGM----EYLGSQ-RYIHRDLAARNILVESE---DLVKISDFGLAKVLPED 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 555 PGV-----PMQTPCFtlqYAAPELLAQQGYDESCDLWSLGVILYMMLS----GQVPFQGASGQGGQSQAAEIMCKIRE 623
Cdd:cd05038  163 KEYyyvkePGESPIF---WYAPECLRESRFSSASDVWSFGVTLYELFTygdpSQSPPALFLRMIGIAQGQMIVTRLLE 237
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
402-608 8.23e-12

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 66.30  E-value: 8.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREpALGQGSFSVCRRCRQRQSGQeFAVKILSRRLEANT---QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd05148    7 EFTLER-KLGSGYFGEVWEGLWKNRVR-VAIKILKSDDLLKQqdfQKEVQALKRLR-HKHLISLFAVCSVGEPVYIITEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 lrggellehIRKK--RHFSESEASQILRS---------LVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGF 547
Cdd:cd05148   84 ---------MEKGslLAFLRSPEGQVLPVaslidmacqVAEGMAYL-EEQNSIHRDLAARNILVGEDLV---CKVADFGL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 548 ARLRPQSPGVPMQTPcFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05148  151 ARLIKEDVYLSSDKK-IPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNH 211
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
31-289 8.24e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 66.59  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAggHDAGKLYAMK--------------VLRKAALVQRAKTQEHTRTERsvlelvrqap 96
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKARDL--KNGGRFVALKrvrvqtgeegmplsTIREVAVLRHLETFEHPNVVR---------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 fLVTLHYAFQTD--AKLHLILDYVSGgEMFTHLYQ-------RQYFKEAEVRVYGGeivlaLEHLHKLGIIYRDLKLENV 167
Cdd:cd07862   69 -LFDVCTVSRTDreTKLTLVFEHVDQ-DLTTYLDKvpepgvpTETIKDMMFQLLRG-----LDFLHSHRVVHRDLKPQNI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 168 LLDSEGHIVLTDFGLSKefLTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFT-------- 239
Cdd:cd07862  142 LVTSSGQIKLADFGLAR--IYSFQMALTSVVVTLWYRAPEVLL-QSSYATPVDLWSVGCIFAEMFRRKPLFRgssdvdql 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 240 --------LEGERNTQAEVS--RRILKCSPPFP-----PRIGPVAQDLLQRLLCKDPKKRLGAGP 289
Cdd:cd07862  219 gkildvigLPGEEDWPRDVAlpRQAFHSKSAQPiekfvTDIDELGKDLLLKCLTFNPAKRISAYS 283
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
409-655 9.92e-12

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 65.92  E-value: 9.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVA---ALRLCQ-SHPNVVNLH---EVHHDQLHTYLVLELLRG 481
Cdd:cd08223    7 VIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAeqeAKLLSKlKHPNIVSYKesfEGEDGFLYIVMGFCEGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPmQT 561
Cdd:cd08223   87 LYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHER-NILHRDLKTQNIFL---TKSNIIKVGDLGIARVLESSSDMA-TT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 562 PCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASgqggqsqAAEIMCKIREGRFSLDGEAWqgvSEEAK 641
Cdd:cd08223  162 LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKD-------MNSLVYKILEGKLPPMPKQY---SPELG 231
                        250
                 ....*....|....
gi 663856869 642 ELVRGLLTVDPAKR 655
Cdd:cd08223  232 ELIKAMLHQDPEKR 245
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
33-285 1.03e-11

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 66.58  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFL-VRKAGGHDAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAkL 111
Cdd:cd05108    9 FKKIKVLGSGAFGTVYKgLWIPEGEKVKIPVAIKELREAT---SPKANKEILDEAYVMASVDN-PHVCRLLGICLTST-V 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFthlyqrQYFKEAEVRVYGG-------EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd05108   84 QLITQLMPFGCLL------DYVREHKDNIGSQyllnwcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 EFLTEEKErtFSFCG---TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF----------TLE-GERNTQA- 248
Cdd:cd05108  158 LLGAEEKE--YHAEGgkvPIKWMALESILHRI-YTHQSDVWSYGVTVWELMTfGSKPYdgipaseissILEkGERLPQPp 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 249 ----EVSRRILKC---SPPFPPRIGPVAQDLLQrlLCKDPKKRL 285
Cdd:cd05108  235 ictiDVYMIMVKCwmiDADSRPKFRELIIEFSK--MARDPQRYL 276
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
410-659 1.06e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 67.01  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR----RLEA-NTQREVAALRLCQsHPNVVNLHEV----HHDQLH-TYLVLELL 479
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIANafdnRIDAkRTLREIKLLRHLD-HENVIAIKDImpppHREAFNdVYIVYELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGElleH--IRKKRHFSESEAS----QILRSLvsavSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQ 553
Cdd:cd07858   92 DTDL---HqiIRSSQTLSDDHCQyflyQLLRGL----KYIHS-ANVLHRDLKPSNLLLNAN---CDLKICDFGLARTTSE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVpMQTPCFTLQYAAPE-LLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS------------GqggqSQAAEIMCK 620
Cdd:cd07858  161 KGDF-MTEYVVTRWYRAPElLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDyvhqlklitellG----SPSEEDLGF 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 621 IRE-------------GRFSLdGEAWQGVSEEAKELVRGLLTVDPAKRLKLE 659
Cdd:cd07858  236 IRNekarryirslpytPRQSF-ARLFPHANPLAIDLLEKMLVFDPSKRITVE 286
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
410-661 1.38e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 65.90  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFA-VKILSRRL-EANTQR--EVAALRLCQSHPNVVNLHEVHHDQLH----TYLVLELLRG 481
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAwCELQDRKLtKAEQQRfkEEAEMLKGLQHPNIVRFYDSWESVLKgkkcIVLVTELMTS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG-VVHRDLKPENILYADdtPGAPVKIIDFGFARL-RPQSPGVPM 559
Cdd:cd14031   98 GTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPpIIHRDLKCDNIFITG--PTGSVKIGDLGLATLmRTSFAKSVI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPcftlQYAAPELLaQQGYDESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGrfsLDGEAWQGVSE- 638
Cdd:cd14031  176 GTP----EFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSEC------QNAAQIYRKVTSG---IKPASFNKVTDp 241
                        250       260
                 ....*....|....*....|...
gi 663856869 639 EAKELVRGLLTVDPAKRLKLEGL 661
Cdd:cd14031  242 EVKEIIEGCIRQNKSERLSIKDL 264
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
410-601 1.38e-11

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 65.82  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR---EVAALRLCqSHPNVVNLHEVHHDQLHTY-LVLELLRGGELL 485
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDymvEIDILASC-DHPNIVKLLDAFYYENNLWiLIEFCAGGAVDA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFA-------RLRPQSPGVP 558
Cdd:cd06643   92 VMLELERPLTEPQIRVVCKQTLEALVYLHENK-IIHRDLKAGNILFTLD---GDIKLADFGVSakntrtlQRRDSFIGTP 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 559 MqtpcftlqYAAPELL-----AQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06643  168 Y--------WMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPP 207
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
410-605 1.44e-11

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 66.59  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAAL-RLCQSHP---NVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14229    8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHpsYARQGQIEVGILaRLSNENAdefNFVRAYECFQHRNHTCLVFEMLEQNL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LleHIRKKRHFSESEAS---QILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgAP--VKIIDFGfarlrpqSPGVP 558
Cdd:cd14229   88 Y--DFLKQNKFSPLPLKvirPILQQVATALKKL-KSLGLIHADLKPENIMLVDPVR-QPyrVKVIDFG-------SASHV 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 559 MQTPCFT-LQ---YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGA 605
Cdd:cd14229  157 SKTVCSTyLQsryYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGA 207
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
35-255 1.52e-11

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 65.16  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLVRKAGGHDAgklyAMKVLRKAALvqraktQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLI 114
Cdd:cd05059    8 FLKELGSGQFGVVHLGKWRGKIDV----AIKMIKEGSM------SEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQyfkeaevRVYGGEIVL--------ALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF 186
Cdd:cd05059   78 TEYMANGCLLNYLRERR-------GKFQTEQLLemckdvceAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 187 LTEEKERTFSFCGTIEYMAPEIIrSKTGHGKAVDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRIL 255
Cdd:cd05059  151 LDDEYTSSVGTKFPVKWSPPEVF-MYSKFSSKSDVWSFGVLMWEVFSeGKMPY----ERFSNSEVVEHIS 215
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
408-601 1.58e-11

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 65.36  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 408 PALGQGSFSVCRRCRQRQSGQEFAVKIlsRRLEANTQR---EVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL-RGGE 483
Cdd:cd14017    6 KKIGGGGFGEIYKVRDVVDGEEVAMKV--ESKSQPKQVlkmEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLgPNLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENilYADDTPGA---PVKIIDFGFAR---------LR 551
Cdd:cd14017   84 ELRRSQPRGKFSVSTTLRLGIQILKAIEDIHE-VGFLHRDVKPSN--FAIGRGPSderTVYILDFGLARqytnkdgevER 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 552 PqspgvPMQTPCF--TLQYAAPEllAQQGYDESC--DLWSLgviLYMML---SGQVP 601
Cdd:cd14017  161 P-----PRNAAGFrgTVRYASVN--AHRNKEQGRrdDLWSW---FYMLIefvTGQLP 207
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
134-231 1.59e-11

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 65.16  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 134 KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEEKertfSFCGTIEYMAPEIIRS-K 212
Cdd:cd06607   99 QEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVCPAN----SFVGTPYWMAPEVILAmD 173
                         90       100
                 ....*....|....*....|.
gi 663856869 213 TGH--GKaVDWWSLGILLFEL 231
Cdd:cd06607  174 EGQydGK-VDVWSLGITCIEL 193
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
405-602 1.86e-11

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 65.41  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPA--------LGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANTQREVAALRLCQSHPNVVNLHEV--------H 466
Cdd:cd06636   11 LRDPAgifelvevVGNGTYGQVYKGRHVKTGQLAAIKVMdvTEDEEEEIKLEINMLKKYSHHRNIATYYGAfikksppgH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLhtYLVLELLRGGELLEHIRKKR--HFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIID 544
Cdd:cd06636   91 DDQL--WLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHK-VIHRDIKGQNVLL---TENAEVKLVD 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 545 FGFARLRPQSPGvPMQTPCFTLQYAAPELLA-----QQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06636  165 FGVSAQLDRTVG-RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
501-685 1.98e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 66.34  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLvsavSFMHEeAGVVHRDLKPENILYADDTpgAPVKIIDFGFARLRPQ--------SPGVpmqtpcFTLQYAAPE 572
Cdd:cd07854  122 QLLRGL----KYIHS-ANVLHRDLKPANVFINTED--LVLKIGDFGLARIVDPhyshkgylSEGL------VTKWYRSPR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 573 LLAQ-QGYDESCDLWSLGVILYMMLSGQVPFQGASgQGGQSQ-------------AAEIMCKIR--------EGRFSLDg 630
Cdd:cd07854  189 LLLSpNNYTKAIDMWAAGCIFAEMLTGKPLFAGAH-ELEQMQlilesvpvvreedRNELLNVIPsfvrndggEPRRPLR- 266
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 631 EAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGS-----ARSSPPLRTPDVLE 685
Cdd:cd07854  267 DLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYScpfdePVSLHPFHIEDELD 326
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
132-302 2.30e-11

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 65.42  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 132 YFKEAEVRVYG-GEIVLALEHLH-KLGIIYRDLKLENVLLDSEGHIVLTDFGLS---------KEFLTEEKERTFSFCG- 199
Cdd:cd14011  109 YKLYDVEIKYGlLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqatdqFPYFREYDPNLPPLAQp 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 200 TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELL-TGASPFTLEG-----ERNTQAEVSRRI-LKCSPPFPPRigpvaqDL 272
Cdd:cd14011  189 NLNYLAPEYILSKT-CDPASDMFSLGVLIYAIYnKGKPLFDCVNnllsyKKNSNQLRQLSLsLLEKVPEELR------DH 261
                        170       180       190
                 ....*....|....*....|....*....|
gi 663856869 273 LQRLLCKDPKKRlgagPQGAQEVRnHPFFQ 302
Cdd:cd14011  262 VKTLLNVTPEVR----PDAEQLSK-IPFFD 286
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
32-204 2.37e-11

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 64.79  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  32 NFELLKVLGTGAYGKVFLVRKaggHDAGKLYAMKVlrkaalvqraktqEHTRTERSVLElvrqapflvtlhyafqtdaKL 111
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGID---LKTGEEVAIKI-------------EKKDSKHPQLE-------------------YE 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 112 HLILDYVSGGEMFTHLYQrqYFKEAEVRVY----------------------------GGEIVLALEHLHKLGIIYRDLK 163
Cdd:cd14016   46 AKVYKLLQGGPGIPRLYW--FGQEGDYNVMvmdllgpsledlfnkcgrkfslktvlmlADQMISRLEYLHSKGYIHRDIK 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 164 LENVLLDSEGH---IVLTDFGLSKEFLT-------EEKERTfSFCGTIEYM 204
Cdd:cd14016  124 PENFLMGLGKNsnkVYLIDFGLAKKYRDprtgkhiPYREGK-SLTGTARYA 173
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
410-606 2.42e-11

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 64.78  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQeFAVKILSR-RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHI 488
Cdd:cd05059   12 LGSGQFGVVHLGKWRGKID-VAIKMIKEgSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 489 RKKRHfseSEASQILRSLVSAV-SFMH--EEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPGVPMQTPCFT 565
Cdd:cd05059   91 RERRG---KFQTEQLLEMCKDVcEAMEylESNGFIHRDLAARNCLVGEQN---VVKVSDFGLARYVLDDEYTSSVGTKFP 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGAS 606
Cdd:cd05059  165 VKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFS 206
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
145-284 2.57e-11

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 64.72  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 145 IVLALEHLHKLGIIYR-DLKLENVLLDSEGHIVLTDFGLsKEFLTEEKERTFSfcGTIE-----YMAPEIIRSKTGHGKA 218
Cdd:cd13992  106 IVKGMNYLHSSSIGYHgRLKSSNCLVDSRWVVKLTDFGL-RNLLEEQTNHQLD--EDAQhkkllWTAPELLRGSLLEVRG 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 219 V---DWWSLGILLFELLTGASPFTLEGERntqaEVSRRILKC-SPPFPP-------RIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd13992  183 TqkgDVYSFAIILYEILFRSDPFALEREV----AIVEKVISGgNKPFRPelavlldEFPPRLVLLVKQCWAENPEKR 255
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
39-293 2.65e-11

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 64.99  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHD-AGKLYAMKVLRKAALVQRAKTQEHTRTE---RSVLELVRQAPFL-------------VTL 101
Cdd:cd14067    1 LGQGGSGTVIYRARYQGQPvAVKRFHIKKCKKRTDGSADTMLKHLRAAdamKNFSEFRQEASMLhslqhpcivyligISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 H---YAFQTD--AKLHLILDYVSGGEMFTHLYQRQYFKEAEvrvyggEIVLALEHLHKLGIIYRDLKLENVL---LDSEG 173
Cdd:cd14067   81 HplcFALELAplGSLNTVLEENHKGSSFMPLGHMLTFKIAY------QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HI--VLTDFGLSKEFLteeKERTFSFCGTIEYMAPEIiRSKTGHGKAVDWWSLGILLFELLTGASPFTlegeRNTQAEVS 251
Cdd:cd14067  155 HIniKLSDYGISRQSF---HEGALGVEGTPGYQAPEI-RPRIVYDEKVDMFSYGMVLYELLSGQRPSL----GHHQLQIA 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 252 RRILKCSPPFPPRIGPVAQDLLQRLL--CKD--PKKRLGAGPQGAQ 293
Cdd:cd14067  227 KKLSKGIRPVLGQPEEVQFFRLQALMmeCWDtkPEKRPLACSVVEQ 272
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
410-602 2.67e-11

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 64.66  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEAN-TQREVAALRlCQ-------SHPNVVNLHEV--HHDQLHTYLVLELL 479
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQeTSKEVNALE-CEiqllknlRHDRIVQYYGClrDPEEKKLSIFVEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILyaDDTPGApVKIIDFGfARLRPQS---PG 556
Cdd:cd06653   89 PGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNM-IVHRDIKGANIL--RDSAGN-VKLGDFG-ASKRIQTicmSG 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06653  164 TGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
31-238 2.94e-11

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 65.20  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAG-GH-DAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:cd05055   35 NNLSFGKTLGAGAFGKVVEATAYGlSKsDAVMKVAVKMLKPTA---HSSEREALMSELKIMSHLGNHENIVNLLGACTIG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLY-QRQYFKEAE-VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLdSEGHIV-LTDFGLSKE 185
Cdd:cd05055  112 GPILVITEYCCYGDLLNFLRrKRESFLTLEdLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKIVkICDFGLARD 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 186 FLTEE----KERTFSfcgTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05055  191 IMNDSnyvvKGNARL---PVKWMAPESIFNCVYTFES-DVWSYGILLWEIFSlGSNPY 244
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
37-284 3.06e-11

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 64.17  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEhtrteRSVLELVRQAPfLVTLhYAFQTDAKLHLILD 116
Cdd:cd14203    1 VKLGQGCFGEVWM----GTWNGTTKVAIKTLKPGTMSPEAFLEE-----AQIMKKLRHDK-LVQL-YAVVSEEPIYIVTE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 117 YVSGGEMFTHLY--QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefLTEEKERT 194
Cdd:cd14203   70 FMSKGSLLDFLKdgEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR--LIEDNEYT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 195 FSFCGT--IEYMAPE-------IIRSktghgkavDWWSLGILLFELLT-GASPFTLEGERNTQAEVSRRI-LKCSPPFPP 263
Cdd:cd14203  148 ARQGAKfpIKWTAPEaalygrfTIKS--------DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGYrMPCPPGCPE 219
                        250       260
                 ....*....|....*....|.
gi 663856869 264 RIgpvaQDLLQRLLCKDPKKR 284
Cdd:cd14203  220 SL----HELMCQCWRKDPEER 236
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
410-658 3.07e-11

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 65.42  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCR-QRQSGQEFAVKIL--------SRRLEANTQRevaalRLCQSHPNVVNLHEVHHD--QLHTYLVLEL 478
Cdd:cd14215   20 LGEGTFGRVVQCIdHRRGGARVALKIIknvekykeAARLEINVLE-----KINEKDPENKNLCVQMFDwfDYHGHMCISF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILR---SLVSAVSFMHEEAgVVHRDLKPENILYADD----------------TPGAP 539
Cdd:cd14215   95 ELLGLSTFDFLKENNYLPYPIHQVRHmafQVCQAVKFLHDNK-LTHTDLKPENILFVNSdyeltynlekkrdersVKSTA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 540 VKIIDFGFARLRPQSpgvpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMC 619
Cdd:cd14215  174 IRVVDFGSATFDHEH----HSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILG 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 620 KI--------------REGRFSLDGEAWQG-------------VSEEAKE------LVRGLLTVDPAKRLKL 658
Cdd:cd14215  250 PIpsrmirktrkqkyfYHGRLDWDENTSAGryvrenckplrryLTSEAEEhhqlfdLIESMLEYEPSKRLTL 321
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
31-238 3.15e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 65.06  E-value: 3.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd06633   21 EIFVDLHEIGHGSFGAVYFATNS---HTNEVVAIKKMSYSGKQTNEKWQDIIK-EVKFLQQLKH-PNTIEYKGCYLKDHT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEE 190
Cdd:cd06633   96 AWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SASIASPA 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KertfSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd06633  175 N----SFVGTPYWMAPEVILAmdEGQYDGKVDIWSLGITCIELAERKPPL 220
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
303-363 3.26e-11

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 59.30  E-value: 3.26e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869   303 GLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVY--SPPGSPPPGDPRIFQGYSFVA 363
Cdd:smart00133   2 GIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLtpVDSPLSGGIQQEPFRGFSYVF 64
pknD PRK13184
serine/threonine-protein kinase PknD;
145-311 3.27e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 67.10  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 145 IVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFS-----------------FCGTIEYMAPE 207
Cdd:PRK13184 122 ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEEDLLDIdvdernicyssmtipgkIVGTPDYMAPE 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 208 IIRsktGH--GKAVDWWSLGILLFELLTGASPFTLEGERntQAEVSRRILKCSPPFPPR-IGPVAQDLLQRLLCKDPKKR 284
Cdd:PRK13184 202 RLL---GVpaSESTDIYALGVILYQMLTLSFPYRRKKGR--KISYRDVILSPIEVAPYReIPPFLSQIAMKALAVDPAER 276
                        170       180
                 ....*....|....*....|....*...
gi 663856869 285 LGAGPQGAQEVRNHpfFQGL-DWVALAA 311
Cdd:PRK13184 277 YSSVQELKQDLEPH--LQGSpEWTVKAT 302
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
37-232 3.35e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 64.60  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLvrkagGHDAGKLYAMKVLrkaalvqraktqeHTRTERSVLE--LVRQapfLVTLH------------ 102
Cdd:cd14056    1 KTIGKGRYGEVWL-----GKYRGEKVAVKIF-------------SSRDEDSWFRetEIYQ---TVMLRhenilgfiaadi 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAKLHLILDYVSGGEMFTHLyQRQYFKEAEVRVYGGEIVLALEHLH--------KLGIIYRDLKLENVLLDSEGH 174
Cdd:cd14056   60 KSTGSWTQLWLITEYHEHGSLYDYL-QRNTLDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNILVKRDGT 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 175 IVLTDFGLSKEF---LTEEKERTFSFCGTIEYMAPEIIRSKTG-----HGKAVDWWSLGILLFELL 232
Cdd:cd14056  139 CCIADLGLAVRYdsdTNTIDIPPNPRVGTKRYMAPEVLDDSINpksfeSFKMADIYSFGLVLWEIA 204
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
446-606 3.86e-11

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 64.20  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 446 EVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDL 524
Cdd:cd05112   48 EEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYL-EEASVIHRDL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 525 KPENILYADDTpgaPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQ 603
Cdd:cd05112  127 AARNCLVGENQ---VVKVSDFGMTRFVLDDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYE 203

                 ...
gi 663856869 604 GAS 606
Cdd:cd05112  204 NRS 206
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
36-283 3.95e-11

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 64.66  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFL-VRKAGGHDAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVrQAPFLVTLhYAFQTDAKLHLI 114
Cdd:cd05109   12 VKVLGSGAFGTVYKgIWIPDGENVKIPVAIKVLRENT---SPKANKEILDEAYVMAGV-GSPYVCRL-LGICLTSTVQLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQ-RQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKEr 193
Cdd:cd05109   87 TQLMPYGCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETE- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 194 tFSFCG---TIEYMAPE-IIRSKTGHGKavDWWSLGILLFELLT-GASPFT----------LE-GERNTQA-----EVSR 252
Cdd:cd05109  166 -YHADGgkvPIKWMALEsILHRRFTHQS--DVWSYGVTVWELMTfGAKPYDgipareipdlLEkGERLPQPpictiDVYM 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 253 RILKC---SPPFPPRIGPVAQDLLQrlLCKDPKK 283
Cdd:cd05109  243 IMVKCwmiDSECRPRFRELVDEFSR--MARDPSR 274
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
36-238 4.25e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 64.55  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKtQEHTRTERSVLELVRQAPFLVTLHYAFQTDAkLHLIL 115
Cdd:cd14026    2 LRYLSRGAFGTVSRARHA---DWRVTVAIKCLKLDSPVGDSE-RNCLLKEAEILHKARFSYILPILGICNEPEF-LGIVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 116 DYVSGGEMFTHLYQRQYFKEA----EVRVYGgEIVLALEHLHKLG--IIYRDLKLENVLLDSEGHIVLTDFGLSK----E 185
Cdd:cd14026   77 EYMTNGSLNELLHEKDIYPDVawplRLRILY-EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwrqlS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 186 FLTEEKERTFSFCGTIEYMAPE------IIRSKTGHgkavDWWSLGILLFELLTGASPF 238
Cdd:cd14026  156 ISQSRSSKSAPEGGTIIYMPPEeyepsqKRRASVKH----DIYSYAIIMWEVLSRKIPF 210
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
410-592 4.28e-11

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 64.03  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKI-LSRRLEANTQREVAAL-RLcqSHPNVVNLHEV--HHDQLHTylVLELLRGGELL 485
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMnTLSSNRANMLREVQLMnRL--SHPNILRFMGVcvHQGQLHA--LTEYINGGNLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVPMQTPCFT 565
Cdd:cd14155   77 QLLDSNEPLSWTVRVKLALDIARGLSYLHS-KGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIPDYSDGKEKLAVVG 155
                        170       180
                 ....*....|....*....|....*...
gi 663856869 566 LQY-AAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd14155  156 SPYwMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
492-608 4.54e-11

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 63.95  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 492 RHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPGVP-MQTPCFTLQYAA 570
Cdd:cd14062   84 TKFEMLQLIDIARQTAQGMDYLHAK-NIIHRDLKSNNIFLHEDL---TVKIGDFGLATVKTRWSGSQqFEQPTGSILWMA 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663856869 571 PELLAQQG---YDESCDLWSLGVILYMMLSGQVPFQGASGQ 608
Cdd:cd14062  160 PEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNR 200
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
144-234 4.54e-11

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 64.05  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlskeFLTEEKERTFSFCGTIEYMAPEIIRSKtgHGKAVDWWS 223
Cdd:cd13975  110 DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLG----FCKPEAMMSGSIVGTPIHMAPELFSGK--YDNSVDVYA 183
                         90
                 ....*....|.
gi 663856869 224 LGILLFELLTG 234
Cdd:cd13975  184 FGILFWYLCAG 194
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
39-287 4.78e-11

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 64.19  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHDAGKlYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTL------HYAFQTDAKLH 112
Cdd:cd14020    8 LGQGSSASVYRVSSGRGADQPT-SALKEFQLDHQGSQESGDYGFAKERAALEQLQGHRNIVTLygvftnHYSANVPSRCL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LI--LDyVSGGEMFTHlYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIV-LTDFGLSkeflTE 189
Cdd:cd14020   87 LLelLD-VSVSELLLR-SSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFkLIDFGLS----FK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCGTIEYMAPEI----------IRSKTGHGKAVDWWSLGILLFELLTGA----SPFTLEGERNTQAEVSrRIL 255
Cdd:cd14020  161 EGNQDVKYIQTDGYRAPEAelqnclaqagLQSETECTSAVDLWSLGIVLLEMFSGMklkhTVRSQEWKDNSSAIID-HIF 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 256 KCSPPFPPRIgPV--AQDLLQRLLCKDPKKRLGA 287
Cdd:cd14020  240 ASNAVVNPAI-PAyhLRDLIKSMLHNDPGKRATA 272
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
410-602 5.30e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 64.27  E-value: 5.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ---REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF-ARLRPQSPgvPMQTPCFT 565
Cdd:cd06657  107 IVTHTR-MNEEQIAAVCLAVLKALSVLHAQ-GVIHRDIKSDSILLTHD---GRVKLSDFGFcAQVSKEVP--RRKSLVGT 179
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06657  180 PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPY 216
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
410-592 5.36e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 63.82  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRrLEANTQR----EVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIR-FDEETQRtflkEVKVMR-CLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRK-KRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQ---- 560
Cdd:cd14221   79 GIIKSmDSHYPWSQRVSFAKDIASGMAYLHS-MNIIHRDLNSHNCLVREN---KSVVVADFGLARLMVDEKTQPEGlrsl 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 663856869 561 ---------TPCFTLQYAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd14221  155 kkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
27-238 6.27e-11

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 63.91  E-value: 6.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEHTrtersvLELVRQAPFLVTLHYAFQ 106
Cdd:cd05072    3 EIPRESIKLVKKLGAGQFGEVWM----GYYNNSTKVAVKTLKPGTMSVQAFLEEAN------LMKTLQHDKLVRLYAVVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRV--YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd05072   73 KEEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLidFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLAR 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 185 efLTEEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05072  153 --VIEDNEYTAREGAKfpIKWTAPEAINFGSFTIKS-DVWSFGILLYEIVTyGKIPY 206
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
406-602 7.24e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 63.56  E-value: 7.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEA-NTQREVAALRlCQ-------SHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd06651   11 RGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpETSKEVSALE-CEiqllknlQHERIVQYYGCLRDRAEKTLTIF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRH--FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILyaDDTPGApVKIIDFGFARlRPQS- 554
Cdd:cd06651   90 MEYMPGGSVKDQLKAYgaLTESVTRKYTRQILEGMSYLHSNM-IVHRDIKGANIL--RDSAGN-VKLGDFGASK-RLQTi 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 555 --PGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06651  165 cmSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
410-592 7.26e-11

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 63.68  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSR---RLEANTQREVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRfdeEAQRNFLKEVKVMR-SLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIR-KKRHFSESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYADDTPgapVKIIDFGFARL----RPQSPGVPMQT 561
Cdd:cd14154   80 VLKdMARPLPWAQRVRFAKDIASGMAYLHS-MNIIHRDLNSHNCLVREDKT---VVVADFGLARLiveeRLPSGNMSPSE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 562 PCFTLQ---------------YAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd14154  156 TLRHLKspdrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVL 201
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
144-234 7.30e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 64.13  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLH-KLGIIYRDLKLENVLLDSEGHIV-LTDFG----LSKEFlTEEKErtfsfcgTIEYMAPEIIRsKTGHGK 217
Cdd:cd14136  127 QVLQGLDYLHtKCGIIHTDIKPENVLLCISKIEVkIADLGnacwTDKHF-TEDIQ-------TRQYRSPEVIL-GAGYGT 197
                         90
                 ....*....|....*..
gi 663856869 218 AVDWWSLGILLFELLTG 234
Cdd:cd14136  198 PADIWSTACMAFELATG 214
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
410-608 7.38e-11

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 63.23  E-value: 7.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREV---AALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKFlqeARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRhfSESEASQILRSLVSAVSFMH--EEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQ-----SPGVPm 559
Cdd:cd05041   83 FLRKKG--ARLTVKQLLQMCLDAAAGMEylESKNCIHRDLAARNCLVGENN---VLKISDFGMSREEEDgeytvSDGLK- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 560 QTPcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05041  157 QIP---IKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQ 203
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
138-265 7.56e-11

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 64.17  E-value: 7.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 138 VRVYGGEIVLALEHLHKLGIIYRDLKLENVLLdSEGHIVL--TDFGLSkeFLTEEKERT------FsfcgtieYMAPEII 209
Cdd:cd14135  107 VRSYAQQLFLALKHLKKCNILHADIKPDNILV-NEKKNTLklCDFGSA--SDIGENEITpylvsrF-------YRAPEII 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 210 rskTGHG--KAVDWWSLGILLFELLTGASPFTleGERNTQaeVSRRILKCSPPFPPRI 265
Cdd:cd14135  177 ---LGLPydYPIDMWSVGCTLYELYTGKILFP--GKTNNH--MLKLMMDLKGKFPKKM 227
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
425-606 8.78e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 65.64  E-value: 8.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   425 QSGQEFAVKILsRRLEANTQREVAALR----LCQ--SHPNVVNL---HEVHHDQLHTylVLELLRGGELLEHIRKKRHFS 495
Cdd:TIGR03903    1 MTGHEVAIKLL-RTDAPEEEHQRARFRretaLCArlYHPNIVALldsGEAPPGLLFA--VFEYVPGRTLREVLAADGALP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   496 ESEASQILRSLVSAVSFMHEeAGVVHRDLKPENILYA--DDTPGApvKIIDFGFARLRPQSPGVPMQTPCFTL------Q 567
Cdd:TIGR03903   78 AGETGRLMLQVLDALACAHN-QGIVHRDLKPQNIMVSqtGVRPHA--KVLDFGIGTLLPGVRDADVATLTRTTevlgtpT 154
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 663856869   568 YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:TIGR03903  155 YCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGAS 193
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
28-238 1.05e-10

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 63.24  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFlvrkagghdAGKLYAMKVLRKAALVQRAKTQ----EHTR--TERSVLELVRQAPFLVTL 101
Cdd:cd05043    3 VSRERVTLSDLLQEGTFGRIF---------HGILRDEKGKEEEVLVKTVKDHaseiQVTMllQESSLLYGLSHQNLLPIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRV--------YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd05043   74 HVCIEDGEKPMVLYPYMNWGNLKLFLQQCRLSEANNPQAlstqqlvhMALQIACGMSYLHRRGVIHKDIAARNCVIDDEL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 174 HIVLTDFGLSKEF-------LTEEKERtfsfcgTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05043  154 QVKITDNALSRDLfpmdyhcLGDNENR------PIKWMSLESLVNKE-YSSASDVWSFGVLLWELMTlGQTPY 219
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
39-181 1.07e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 60.15  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFlvrKAGGHDAGKLYAMKVLRkaalVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAF-QTDAKLHLILDY 117
Cdd:cd13968    1 MGEGASAKVF---WAEGECTTIGVAVKIGD----DVNNEEGEDLESEMDILRRLKGLELNIPKVLVTeDVDGPNILLMEL 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 118 VSGGEMFTHLyQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd13968   74 VKGGTLIAYT-QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
38-293 1.17e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 62.66  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVFLvrkagGHDAGKLYAMKVLRKAAlvqrakTQEHTRTERSVLELVRQaPFLVTLhYAFQTDAKLhLILDY 117
Cdd:cd14068    1 LLGDGGFGSVYR-----AVYRGEDVAVKIFNKHT------SFRLLRQELVVLSHLHH-PSLVAL-LAAGTAPRM-LVMEL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 118 VSGGEMfTHLYQRQyfKEAEVRVYGGEIVL----ALEHLHKLGIIYRDLKLENVLL-----DSEGHIVLTDFGLSkEFLT 188
Cdd:cd14068   67 APKGSL-DALLQQD--NASLTRTLQHRIALhvadGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA-QYCC 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFsfCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTlEG----ERNTQAEVSRRI------LKCS 258
Cdd:cd14068  143 RMGIKTS--EGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCGERIV-EGlkfpNEFDELAIQGKLpdpvkeYGCA 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 259 PpfppriGPVAQDLLQRLLCKDPKKRlgagPQGAQ 293
Cdd:cd14068  220 P------WPGVEALIKDCLKENPQCR----PTSAQ 244
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
79-301 1.24e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 62.82  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  79 QEHTRTERSVLELVrQAPFLVTLHYAFQTDAK----LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHK 154
Cdd:cd14031   53 QQRFKEEAEMLKGL-QHPNIVRFYDSWESVLKgkkcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 155 LG--IIYRDLKLENVLLDS-EGHIVLTDFGLSKEFLTEEKErtfSFCGTIEYMAPEIIRSKtgHGKAVDWWSLGILLFEL 231
Cdd:cd14031  132 RTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLMRTSFAK---SVIGTPEFMAPEMYEEH--YDESVDVYAFGMCMLEM 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 232 LTGASPFTlegERNTQAEVSRRILKCSPP--FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFF 301
Cdd:cd14031  207 ATSEYPYS---ECQNAAQIYRKVTSGIKPasFNKVTDPEVKEIIEGCIRQNKSERL-----SIKDLLNHAFF 270
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
35-267 1.25e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 62.57  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALvqraktQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLI 114
Cdd:cd05114    8 FMKELGSGLFGVVRL----GKWRAQYKVAIKAIREGAM------SEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQRQ-YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKER 193
Cdd:cd05114   78 TEFMENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 194 TFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRILKCSPPFPPRIGP 267
Cdd:cd05114  158 SSGAKFPVKWSPPEVFNYSKFSSKS-DVWSFGVLMWEVFTeGKMPF----ESKSNYEVVEMVSRGHRLYRPKLAS 227
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
144-317 1.26e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 63.89  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFcgTIEYMAPEIIRSkTGHGKAVDWWS 223
Cdd:cd07876  131 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVV--TRYYRAPEVILG-MGYKENVDIWS 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 224 LGILLFELLTGASPF-----------------TLEGE-RNTQAEVSRRILKCSPP---------FPPRIGPV-------- 268
Cdd:cd07876  208 VGCIMGELVKGSVIFqgtdhidqwnkvieqlgTPSAEfMNRLQPTVRNYVENRPQypgisfeelFPDWIFPSeserdklk 287
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 269 ---AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQglDWVALAARKIPAP 317
Cdd:cd07876  288 tsqARDLLSKMLVIDPDKRI-----SVDEALRHPYIT--VWYDPAEAEAPPP 332
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
33-238 1.29e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 65.14  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869   33 FELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAALVQRAKTQehTRTERSVLELVRQAPFLVTL-HYAFQTDAKL 111
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQE---FFCWKAISYRGLKEREKSQ--LVIEVNVMRELKHKNIVRYIdRFLNKANQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  112 HLILDYVSGGEMFTHLyQRQY-----FKEAEVRVYGGEIVLALEHLHKLG-------IIYRDLKLENVLLDSE----GHI 175
Cdd:PTZ00266   90 YILMEFCDAGDLSRNI-QKCYkmfgkIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGirhiGKI 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869  176 V-------------LTDFGLSKEFLTEEKERtfSFCGTIEYMAPEIIRSKT-GHGKAVDWWSLGILLFELLTGASPF 238
Cdd:PTZ00266  169 TaqannlngrpiakIGDFGLSKNIGIESMAH--SCVGTPYYWSPELLLHETkSYDDKSDMWALGCIIYELCSGKTPF 243
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
111-284 1.29e-10

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 62.64  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefltE 189
Cdd:cd05084   69 IYIVMELVQGGDFLTFLRtEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR----E 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 190 EKERTFSFCG-----TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPFTLEGERNTQAEVSR--RILkcsppf 261
Cdd:cd05084  145 EEDGVYAATGgmkqiPVKWTAPEALNYGR-YSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQgvRLP------ 217
                        170       180
                 ....*....|....*....|....*..
gi 663856869 262 PPRIGPvaqDLLQRLLCK----DPKKR 284
Cdd:cd05084  218 CPENCP---DEVYRLMEQcweyDPRKR 241
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
410-606 1.29e-10

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 62.75  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFS-----VCRRCRQRQSGQEFAVKILSRRlEANTQR-----EVAALRLCQSHpNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05032   14 LGQGSFGmvyegLAKGVVKGEPETRVAIKTVNEN-ASMRERieflnEASVMKEFNCH-HVVRLLGVVSTGQPTLVVMELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRhfSESE---------ASQILR---SLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGF 547
Cdd:cd05032   92 AKGDLKSYLRSRR--PEAEnnpglgpptLQKFIQmaaEIADGMAYLAAKK-FVHRDLAARNCMVAEDLT---VKIGDFGM 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 548 ARL-------RPQSPGVpmqtpcFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGAS 606
Cdd:cd05032  166 TRDiyetdyyRKGGKGL------LPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLS 226
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
504-659 1.36e-10

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 63.03  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 504 RSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGapVKIIDFGFARLRPQSPGVPMQTPcftlQYAAPEL-----LAQQG 578
Cdd:cd14020  117 RDVLEALAFLHHE-GYVHADLKPRNILWSAEDEC--FKLIDFGLSFKEGNQDVKYIQTD----GYRAPEAelqncLAQAG 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 579 Y--DESC----DLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIregrFSLDGEAWQGV-SEEAKELVRGLLTVD 651
Cdd:cd14020  190 LqsETECtsavDLWSLGIVLLEMFSGMKLKHTVRSQEWKDNSSAIIDHI----FASNAVVNPAIpAYHLRDLIKSMLHND 265

                 ....*...
gi 663856869 652 PAKRLKLE 659
Cdd:cd14020  266 PGKRATAE 273
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
108-284 1.48e-10

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 62.54  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 DAKLHLILDYVSGGeMFTHLYQRQYFKEA--EVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHI---VLTDFGL 182
Cdd:cd14156   60 DEKLHPILEYVSGG-CLEELLAREELPLSwrEKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGreaVVTDFGL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEFL---TEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT--GASPFTLEGERNTQAEVSRRILKC 257
Cdd:cd14156  139 AREVGempANDPERKLSLVGSAFWMAPEMLRGEP-YDRKVDVFSFGIVLCEILAriPADPEVLPRTGDFGLDVQAFKEMV 217
                        170       180
                 ....*....|....*....|....*..
gi 663856869 258 sPPFPPRIGPVAQDLLQRllckDPKKR 284
Cdd:cd14156  218 -PGCPEPFLDLAASCCRM----DAFKR 239
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
25-238 1.63e-10

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 62.60  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  25 EEKVSVENFELLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERsvlelvRQAPFLVTLHyA 104
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEVWM----GYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQ------LQHQRLVRLY-A 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRV--YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd05067   70 VVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLldMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 183 SKefLTEEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05067  150 AR--LIEDNEYTAREGAKfpIKWTAPEAINYGTFTIKS-DVWSFGILLTEIVThGRIPY 205
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
501-661 1.68e-10

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 62.45  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRslvsAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIIDFGFAR-----LRPQSPGVPMQTPCFTLQYAAPELLA 575
Cdd:cd06631  111 QILE----GVAYLHNNN-VIHRDIKGNNIML---MPNGVIKLIDFGCAKrlcinLSSGSQSQLLKSMRGTPYWMAPEVIN 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 576 QQGYDESCDLWSLGVILYMMLSGQVP----------FQGASGQGGQSQAAEimckiregRFsldgeawqgvSEEAKELVR 645
Cdd:cd06631  183 ETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSGRKPVPRLPD--------KF----------SPEARDFVH 244
                        170
                 ....*....|....*.
gi 663856869 646 GLLTVDPAKRLKLEGL 661
Cdd:cd06631  245 ACLTRDQDERPSAEQL 260
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
77-260 2.24e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 61.94  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  77 KTQEHTRTERS----VLELVR--QAPFLVTLHYAFQTDAKLH----LILDYVSGGEMFTHLyqrQYFKEAEVRV---YGG 143
Cdd:cd14033   35 QTRKLSKGERQrfseEVEMLKglQHPNIVRFYDSWKSTVRGHkciiLVTELMTSGTLKTYL---KRFREMKLKLlqrWSR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLG--IIYRDLKLENVLLDS-EGHIVLTDFGLSKEflteeKERTF--SFCGTIEYMAPEIIRSKtgHGKA 218
Cdd:cd14033  112 QILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLATL-----KRASFakSVIGTPEFMAPEMYEEK--YDEA 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 219 VDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILKCSPP 260
Cdd:cd14033  185 VDVYAFGMCILEMATSEYPYS---ECQNAAQIYRKVTSGIKP 223
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
405-602 2.29e-10

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 62.43  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 405 LREPA--------LGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANTQREVAALRLCQSHPNVVNLHEVH-------- 466
Cdd:cd06637    1 LRDPAgifelvelVGNGTYGQVYKGRHVKTGQLAAIKVMdvTGDEEEEIKQEINMLKKYSHHRNIATYYGAFikknppgm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLhtYLVLELLRGGELLEHIR--KKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaddTPGAPVKIID 544
Cdd:cd06637   81 DDQL--WLVMEFCGAGSVTDLIKntKGNTLKEEWIAYICREILRGLSHLHQHK-VIHRDIKGQNVLL---TENAEVKLVD 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 545 FGFARLRPQSPGvPMQTPCFTLQYAAPELLA-----QQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06637  155 FGVSAQLDRTVG-RRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
455-597 2.30e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 455 SHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYAD- 533
Cdd:PHA03209 115 NHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQR-IIHRDVKTENIFINDv 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 534 DTpgapVKIIDFGFARLrpqspgvPMQTPCF-----TLQYAAPELLAQQGYDESCDLWSLGVILYMMLS 597
Cdd:PHA03209 194 DQ----VCIGDLGAAQF-------PVVAPAFlglagTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
127-302 2.76e-10

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 62.49  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 127 LYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEgHIVLT--DFGLS---------KEFLTEEKERTF 195
Cdd:cd07854  105 VLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTE-DLVLKigDFGLArivdphyshKGYLSEGLVTKW 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 196 sfcgtieYMAPEIIRSKTGHGKAVDWWSLGILLFELLTG------------------ASPFTLEGERNTQAEVSRRILKC 257
Cdd:cd07854  184 -------YRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGkplfagaheleqmqlileSVPVVREEDRNELLNVIPSFVRN 256
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 258 SPPFP--------PRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd07854  257 DGGEPrrplrdllPGVNPEALDFLEQILTFNPMDRL-----TAEEALMHPYMS 304
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
499-669 3.16e-10

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 61.47  E-value: 3.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 499 ASQIlrslVSAVSFMhEEAGVVHRDLKPENILYADdtpGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQG 578
Cdd:cd14203   97 AAQI----ASGMAYI-ERMNYIHRDLRAANILVGD---NLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 579 YDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaaEIMCKIREGrfsLDGEAWQGVSEEAKELVRGLLTVDPAKRLK 657
Cdd:cd14203  169 FTIKSDVWSFGILLTELVTkGRVPYPGMNNR-------EVLEQVERG---YRMPCPPGCPESLHELMCQCWRKDPEERPT 238
                        170
                 ....*....|..
gi 663856869 658 LEGLRgsSWLQD 669
Cdd:cd14203  239 FEYLQ--SFLED 248
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
107-284 3.54e-10

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 61.28  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRV-YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKe 185
Cdd:cd05056   77 TENPVWIVMELAPLGELRSYLQVNKYSLDLASLIlYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSR- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 FLTEEKERTFSFCG-TIEYMAPEII--RSKTghgKAVDWWSLGILLFELLT-GASPFtlEGERNTqaEVSRRILKCS-PP 260
Cdd:cd05056  156 YMEDESYYKASKGKlPIKWMAPESInfRRFT---SASDVWMFGVCMWEILMlGVKPF--QGVKNN--DVIGRIENGErLP 228
                        170       180
                 ....*....|....*....|....
gi 663856869 261 FPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd05056  229 MPPNCPPTLYSLMTKCWAYDPSKR 252
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
39-286 3.75e-10

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 61.13  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVflvrKAGghdagkLYAMKVLRKAALVQRAKTQEHTRTERSvlELVRQA--------PFLVTLHYAFQTDAk 110
Cdd:cd05116    3 LGSGNFGTV----KKG------YYQMKKVVKTVAVKILKNEANDPALKD--ELLREAnvmqqldnPYIVRMIGICEAES- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEE 190
Cdd:cd05116   70 WMLVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 191 KERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFT-LEGERNTQAEVSRRILKCsppfPPRIG 266
Cdd:cd05116  150 NYYKAQTHGKwpVKWYAPECMNYYKFSSKS-DVWSFGVLMWEAFSyGQKPYKgMKGNEVTQMIEKGERMEC----PAGCP 224
                        250       260
                 ....*....|....*....|
gi 663856869 267 PVAQDLLQRLLCKDPKKRLG 286
Cdd:cd05116  225 PEMYDLMKLCWTYDVDERPG 244
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
33-238 4.38e-10

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 61.60  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAgghDAGKLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDV---RTSEVVAIKKMSYSGKQSNEKWQDIIK-EVKFLQRIKH-PNSIEYKGCYLREHTAW 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEEKe 192
Cdd:cd06635  102 LVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SASIASPAN- 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 193 rtfSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd06635  180 ---SFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKPPL 224
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
35-238 4.40e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 61.57  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLVrKAGGHDAGK-----LYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDA 109
Cdd:cd05098   17 LGKPLGEGCFGQVVLA-EAIGLDKDKpnrvtKVAVKMLKSDA---TEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQ------------------YFKEAEVRVYggEIVLALEHLHKLGIIYRDLKLENVLLDS 171
Cdd:cd05098   93 PLYVIVEYASKGNLREYLQARRppgmeycynpshnpeeqlSSKDLVSCAY--QVARGMEYLASKKCIHRDLAARNVLVTE 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663856869 172 EGHIVLTDFGLSKEF-LTEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05098  171 DNVMKIADFGLARDIhHIDYYKKTTNGRLPVKWMAPEALFDRI-YTHQSDVWSFGVLLWEIFTlGGSPY 238
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
410-606 5.19e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 62.03  E-value: 5.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAAL-RLCQSHP---NVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14228   23 LGRGTFGQVAKCWKRSTKEIVAIKILKNHpsYARQGQIEVSILsRLSSENAdeyNFVRSYECFQHKNHTCLVFEMLEQNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LleHIRKKRHFSE---SEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQSPgvpM 559
Cdd:cd14228  103 Y--DFLKQNKFSPlplKYIRPILQQVATALMKL-KSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSKAV---C 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14228  177 STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGAS 223
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
68-301 5.36e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 60.86  E-value: 5.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  68 RKAALVQRAKTQEHTRTERSVlelvrQAPFLVTLHYAFQTDAK----LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGG 143
Cdd:cd14032   37 RKLTKVERQRFKEEAEMLKGL-----QHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLG--IIYRDLKLENVLLDS-EGHIVLTDFGLSKeflteEKERTF--SFCGTIEYMAPEIIRSKtgHGKA 218
Cdd:cd14032  112 QILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT-----LKRASFakSVIGTPEFMAPEMYEEH--YDES 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 219 VDWWSLGILLFELLTGASPFTlegERNTQAEVSRRILKCSPP--FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVR 296
Cdd:cd14032  185 VDVYAFGMCMLEMATSEYPYS---ECQNAAQIYRKVTCGIKPasFEKVTDPEIKEIIGECICKNKEERY-----EIKDLL 256

                 ....*
gi 663856869 297 NHPFF 301
Cdd:cd14032  257 SHAFF 261
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
407-608 5.57e-10

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 61.04  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQE---FAVKILSRRLEANTQREV---AALRLCQSHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd05065    9 EEVIGAGEFGEVCRGRLKLPGKReifVAIKTLKSGYTEKQRRDFlseASIMGQFDHPNIIHLEGVVTKSRPVMIITEFME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPM 559
Cdd:cd05065   89 NGALDSFLRQNDgQFTVIQLVGMLRGIAAGMKYL-SEMNYVHRDLAARNILVNSNLV---CKVSDFGLSRFLEDDTSDPT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 560 QTPCF----TLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05065  165 YTSSLggkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQ 218
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
487-602 5.68e-10

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 60.80  E-value: 5.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtpGAPVKIIDFGFARLRPQSPGV-PMQTPCFT 565
Cdd:cd14150   87 HVTETR-FDTMQLIDVARQTAQGMDYLHAK-NIIHRDLKSNNIFLHE---GLTVKIGDFGLATVKTRWSGSqQVEQPSGS 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663856869 566 LQYAAPELLAQQG---YDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14150  162 ILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
63-284 6.06e-10

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 60.44  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  63 AMKVLRKAALVQRAKtqehtrtersvlELVRQA--------PFLVTLHYAFQTDAkLHLILDYVSGGEMFTHLYQRQYFK 134
Cdd:cd05060   27 AVKTLKQEHEKAGKK------------EFLREAsvmaqldhPCIVRLIGVCKGEP-LMLVMELAPLGPLLKYLKKRREIP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 135 EAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGT--IEYMAPEIIRSK 212
Cdd:cd05060   94 VSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAGRwpLKWYAPECINYG 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 213 TGHGKAvDWWSLGILLFELLT-GASPFtleGERnTQAEVSRRILKCSP-PFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd05060  174 KFSSKS-DVWSYGVTLWEAFSyGAKPY---GEM-KGPEVIAMLESGERlPRPEECPQEIYSIMLSCWKYRPEDR 242
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
97-231 6.07e-10

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 60.92  E-value: 6.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 FLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVyGGEIVLALEHLH---------KLGIIYRDLKLENV 167
Cdd:cd13998   54 FIAADERDTALRTELWLVTAFHPNGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHseipgctqgKPAIAHRDLKSKNI 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 168 LLDSEGHIVLTDFGLSKEF---LTEEKERTFSFCGTIEYMAPEIIRSKTGHG-----KAVDWWSLGILLFEL 231
Cdd:cd13998  133 LVKNDGTCCIADFGLAVRLspsTGEEDNANNGQVGTKRYMAPEVLEGAINLRdfesfKRVDIYAMGLVLWEM 204
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
402-601 6.10e-10

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 60.86  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRlEA-----NTQREVAALRLCQShPNVVNLHEVHHDQLHTYLVL 476
Cdd:cd06641    4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLE-EAedeieDIQQEITVLSQCDS-PYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLeHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVvHRDLKPENILYADDtpgAPVKIIDFGFArlrPQSPG 556
Cdd:cd06641   82 EYLGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKI-HRDIKAANVLLSEH---GEVKLADFGVA---GQLTD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 557 VPMQTPCF--TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06641  154 TQIKRN*FvgTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
29-238 7.29e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 61.18  E-value: 7.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  29 SVENFELLKVLGTGAYGKVFLVrKAGGHDAGK-----LYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHY 103
Cdd:cd05101   22 PRDKLTLGKPLGEGCFGQVVMA-EAVGIDKDKpkeavTVAVKMLKDDA---TEKDLSDLVSEMEMMKMIGKHKNIINLLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGEMFTHLYQRQ------------------YFKEAEVRVYggEIVLALEHLHKLGIIYRDLKLE 165
Cdd:cd05101   98 ACTQDGPLYVIVEYASKGNLREYLRARRppgmeysydinrvpeeqmTFKDLVSCTY--QLARGMEYLASQKCIHRDLAAR 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 166 NVLLDSEGHIVLTDFGLSKEFLT-EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05101  176 NVLVTENNVMKIADFGLARDINNiDYYKKTTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVLMWEIFTlGGSPY 249
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
410-606 7.59e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 60.26  E-value: 7.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIR 489
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYKVAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 490 KKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQTPCFTLQY 568
Cdd:cd05114   92 QRRgKLSRDMLLSMCQDVCEGMEYL-ERNNFIHRDLAARNCLVNDT---GVVKVSDFGMTRYVLDDQYTSSSGAKFPVKW 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 663856869 569 AAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGAS 606
Cdd:cd05114  168 SPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKS 206
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
410-546 7.80e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 57.45  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR---LEANTQREVAALRLCQSH-PNVVN-LHEVHHDQLHtYLVLELLRGGEL 484
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVnneEGEDLESEMDILRRLKGLeLNIPKvLVTEDVDGPN-ILLMELVKGGTL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 485 LEHIrKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFG 546
Cdd:cd13968   80 IAYT-QEEELDEKDVESIMYQLAECMRLLHSFH-LIHRDLNNDNILLSED---GNVKLIDFG 136
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
402-655 7.85e-10

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 60.44  E-value: 7.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPaLGQGSFSVCRRCRQRQsgqEFAVKILS------RRLEANTQrEVAALRLCQsHPNVV-------NLHEV--- 465
Cdd:cd14063    1 ELEIKEV-IGKGRFGRVHRGRWHG---DVAIKLLNidylneEQLEAFKE-EVAAYKNTR-HDNLVlfmgacmDPPHLaiv 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 ----HHDQLHTYLvlellrggelleHIRKKRhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYAddtpGAPVK 541
Cdd:cd14063   75 tslcKGRTLYSLI------------HERKEK-FDFNKTVQIAQQICQGMGYLHAK-GIIHKDLKSKNIFLE----NGRVV 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 542 IIDFGFARL-----RPQSPGVPMqTPCFTLQYAAPELL----------AQQGYDESCDLWSLGVILYMMLSGQVPFQgas 606
Cdd:cd14063  137 ITDFGLFSLsgllqPGRREDTLV-IPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFK--- 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 607 GQGGQSQAAEIMCKIREGRFSLDGeawqgvSEEAKELVRGLLTVDPAKR 655
Cdd:cd14063  213 EQPAESIIWQVGCGKKQSLSQLDI------GREVKDILMQCWAYDPEKR 255
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
410-601 7.86e-10

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 60.82  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR---EVAALRLCqSHPNVVNL-HEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDymvEIEILATC-NHPYIVKLlGAFYWDGKLWIMIEFCPGGAVDA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFA-------RLRPQSPGVP 558
Cdd:cd06644   99 IMLELDRGLTEPQIQVICRQMLEALQYLHSMK-IIHRDLKAGNVLLTLD---GDIKLADFGVSaknvktlQRRDSFIGTP 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 559 MqtpcftlqYAAPEL-----LAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06644  175 Y--------WMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPP 214
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
34-251 8.18e-10

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 60.37  E-value: 8.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  34 ELLKVLGTGAYGKVFLVRKAG----------GHDAGKLyamKVLRKAALVQRaktqeHTRTERSVLEL--VRQAPFLVTL 101
Cdd:cd14152    3 ELGELIGQGRWGKVHRGRWHGevairlleidGNNQDHL---KLFKKEVMNYR-----QTRHENVVLFMgaCMHPPHLAII 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 H--------YAFQTDAKLHLILDyvsggemfthlyqrqyfkeaEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSeG 173
Cdd:cd14152   75 TsfckgrtlYSFVRDPKTSLDIN--------------------KTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-G 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGL---SKEFLTEEKERTFSFC-GTIEYMAPEIIRSKT-GHG-------KAVDWWSLGILLFELLTGASPFtle 241
Cdd:cd14152  134 KVVITDFGLfgiSGVVQEGRRENELKLPhDWLCYLAPEIVREMTpGKDedclpfsKAADVYAFGTIWYELQARDWPL--- 210
                        250
                 ....*....|
gi 663856869 242 geRNTQAEVS 251
Cdd:cd14152  211 --KNQPAEAL 218
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
407-655 8.33e-10

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 60.78  E-value: 8.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEF--AVKILSRRLEANTQREVAALR--LCQ--SHPNVVNLHEVHHDQLHTYLVLELLR 480
Cdd:cd05089    7 EDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFAGELevLCKlgHHPNIINLLGACENRGYLYIAIEYAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKR-----------HFSESEAS--QILRSLVSAVSFMH--EEAGVVHRDLKPENILYADDTPGapvKIIDF 545
Cdd:cd05089   87 YGNLLDFLRKSRvletdpafakeHGTASTLTsqQLLQFASDVAKGMQylSEKQFIHRDLAARNVLVGENLVS---KIADF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 546 GFArlRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASgqggqsqAAEIMCKIREG 624
Cdd:cd05089  164 GLS--RGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMT-------CAELYEKLPQG 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 663856869 625 rFSLdgEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd05089  235 -YRM--EKPRNCDDEVYELMRQCWRDRPYER 262
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
410-606 8.54e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 61.26  E-value: 8.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR--LEANTQREVAAL-RLCQSHP---NVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd14227   23 LGRGTFGQVVKCWKRGTNEIVAIKILKNHpsYARQGQIEVSILaRLSTESAddyNFVRAYECFQHKNHTCLVFEMLEQNL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LleHIRKKRHFSESEASQI---LRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPGA-PVKIIDFGFARLRPQSPgvpM 559
Cdd:cd14227  103 Y--DFLKQNKFSPLPLKYIrpiLQQVATALMKL-KSLGLIHADLKPENIMLVDPSRQPyRVKVIDFGSASHVSKAV---C 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14227  177 STYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGAS 223
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
406-608 9.47e-10

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 60.08  E-value: 9.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSF-SVCRRCRQRQSGQEF--AVKILSRRLEANTQREV--AALRLCQ-SHPNVVNLHEV-------------- 465
Cdd:cd05033    8 IEKVIGGGEFgEVCSGSLKLPGKKEIdvAIKTLKSGYSDKQRLDFltEASIMGQfDHPNVIRLEGVvtksrpvmivteym 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 HHDQLHTYLvlellrggellehiRKKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIID 544
Cdd:cd05033   88 ENGSLDKFL--------------RENDgKFTVTQLVGMLRGIASGMKYL-SEMNYVHRDLAARNILVNSDLV---CKVSD 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 545 FGFAR-LRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05033  150 FGLSRrLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQ 215
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
33-238 9.74e-10

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 60.81  E-value: 9.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAALVQRAKTQEHTRtERSVLELVRQaPFLVTLHYAFQTDAKLH 112
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNE---VVAIKKMSYSGKQSNEKWQDIIK-EVKFLQKLRH-PNTIEYRGCYLREHTAW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEEKe 192
Cdd:cd06634   92 LVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG-SASIMAPAN- 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 193 rtfSFCGTIEYMAPEIIRS--KTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd06634  170 ---SFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKPPL 214
pknD PRK13184
serine/threonine-protein kinase PknD;
502-608 1.06e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 62.10  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 502 ILRSLVSAVSFMHEEaGVVHRDLKPENIL---YADdtpgapVKIIDFGFARLRPQ------SPGVPMQTPCF-------- 564
Cdd:PRK13184 118 IFHKICATIEYVHSK-GVLHRDLKPDNILlglFGE------VVILDWGAAIFKKLeeedllDIDVDERNICYssmtipgk 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 565 ---TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQ 608
Cdd:PRK13184 191 ivgTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
410-604 1.21e-09

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 59.94  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKILSRRLEANTQREVAALRL------------CQSHPNVVNLHEVHHDQLhTYLVLE 477
Cdd:cd14000    2 LGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTMLrhlratdamknfRLLRQELTVLSHLHHPSI-VYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKK-------RHFSESEAS-------QILRSLVSAVSFMHEeAGVVHRDLKPENIL-YADDTPGA-PVK 541
Cdd:cd14000   79 GIHPLMLVLELAPLgsldhllQQDSRSFASlgrtlqqRIALQVADGLRYLHS-AMIIYRDLKSHNVLvWTLYPNSAiIIK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 542 IIDFGFARlrpQSPGVPMQTPCFTLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd14000  158 IADYGISR---QCCRMGAKGSEGTPGFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGGAPMVG 218
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
31-257 1.22e-09

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 60.12  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVrKAGGHDAGKLYAMKVLRKAaLVQRAKTQEHTR--TERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:cd05053   12 DRLTLGKPLGEGAFGQVVKA-EAVGLDNKPNEVVTVAVKM-LKDDATEKDLSDlvSEMEMMKMIGKHKNIINLLGACTQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQR----QYFKEAEVRVYGGEIVL------------ALEHLHKLGIIYRDLKLENVLLdSE 172
Cdd:cd05053   90 GPLYVVVEYASKGNLREFLRARrppgEEASPDDPRVPEEQLTQkdlvsfayqvarGMEYLASKKCIHRDLAARNVLV-TE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GHIV-LTDFGLSKEFLTEEKERTfsfCGT----IEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASP--------- 237
Cdd:cd05053  169 DNVMkIADFGLARDIHHIDYYRK---TTNgrlpVKWMAPEALFDRV-YTHQSDVWSFGVLLWEIFTlGGSPypgipveel 244
                        250       260
                 ....*....|....*....|....*..
gi 663856869 238 FTL--EGER-----NTQAEVSRRILKC 257
Cdd:cd05053  245 FKLlkEGHRmekpqNCTQELYMLMRDC 271
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
441-593 1.23e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.45  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 441 ANTQREVAALRLCqSHPNVVNLHEVH-------------HDQLHTYLVlellrggellehiRKKRHFSESEASQILRSLV 507
Cdd:PHA03211 205 ASSVHEARLLRRL-SHPAVLALLDVRvvggltclvlpkyRSDLYTYLG-------------ARLRPLGLAQVTAVARQLL 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 508 SAVSFMHEEaGVVHRDLKPENILYadDTPgAPVKIIDFG---FARLRPQSP---GVPMqtpcfTLQYAAPELLAQQGYDE 581
Cdd:PHA03211 271 SAIDYIHGE-GIIHRDIKTENVLV--NGP-EDICLGDFGaacFARGSWSTPfhyGIAG-----TVDTNAPEVLAGDPYTP 341
                        170
                 ....*....|..
gi 663856869 582 SCDLWSLGVILY 593
Cdd:PHA03211 342 SVDIWSAGLVIF 353
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
410-655 1.35e-09

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 59.67  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEF--AVKILSRRLEANTQREVAALR--LCQ--SHPNVVNLHEVHHDQLHTYLVLELLRGGE 483
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELevLCKlgHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 LLEHIRKKRHFSESEA-------------SQILRSLVSAVSFMH--EEAGVVHRDLKPENILYADDTPGapvKIIDFGFA 548
Cdd:cd05047   83 LLDFLRKSRVLETDPAfaianstastlssQQLLHFAADVARGMDylSQKQFIHRDLAARNILVGENYVA---KIADFGLS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 549 rlRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASgqggqsqAAEIMCKIREGrFS 627
Cdd:cd05047  160 --RGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMT-------CAELYEKLPQG-YR 229
                        250       260
                 ....*....|....*....|....*...
gi 663856869 628 LdgEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd05047  230 L--EKPLNCDDEVYDLMRQCWREKPYER 255
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
503-656 1.40e-09

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 59.30  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 503 LRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPElLAQQG--YD 580
Cdd:cd14012  110 TLQLLEALEYLHRN-GVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPE-LAQGSksPT 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 581 ESCDLWSLGVILYMMLSGQVPFQGASGqggqsqaaeimckIREGRFSLDgeawqgVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd14012  188 RKTDVWDLGLLFLQMLFGLDVLEKYTS-------------PNPVLVSLD------LSASLQDFLSKCLSLDPKKRP 244
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
515-624 1.51e-09

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 59.67  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05072  121 ERKNYIHRDLRAANVLVSESLM---CKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYE 197
                         90       100       110
                 ....*....|....*....|....*....|.
gi 663856869 595 MLS-GQVPFQGASGqggqsqaAEIMCKIREG 624
Cdd:cd05072  198 IVTyGKIPYPGMSN-------SDVMSALQRG 221
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
409-606 1.69e-09

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 59.93  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCRQRQ-SGQEFAVKILsRRLEA---NTQREVAALR-LCQSHPNvvnlhevhhDQLHTylvlellrgge 483
Cdd:cd14135    7 YLGKGVFSNVVRARDLArGNQEVAIKII-RNNELmhkAGLKELEILKkLNDADPD---------DKKHC----------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 484 llehIRKKRHFS---------ESEASQiLRSL-----------VSAV---------SFMH-EEAGVVHRDLKPENILYAD 533
Cdd:cd14135   66 ----IRLLRHFEhknhlclvfESLSMN-LREVlkkygknvglnIKAVrsyaqqlflALKHlKKCNILHADIKPDNILVNE 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 534 DTpgAPVKIIDFGFARLRPQSPGVPMQTPCFtlqYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGAS 606
Cdd:cd14135  141 KK--NTLKLCDFGSASDIGENEITPYLVSRF---YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKT 208
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
410-597 1.83e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 59.52  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVaalRLCQSHPNVvnLHEVHHDQLHTY-------------LVL 476
Cdd:cd05081   12 LGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQ---RDFQREIQI--LKALHSDFIVKYrgvsygpgrrslrLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESE-----ASQILRSLVSAVSfmheeAGVVHRDLKPENILYADDTPgapVKIIDFGFARLR 551
Cdd:cd05081   87 EYLPSGCLRDFLQRHRARLDASrlllySSQICKGMEYLGS-----RRCVHRDLAARNILVESEAH---VKIADFGLAKLL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 552 PQSPGV-----PMQTPCFtlqYAAPELLAQQGYDESCDLWSLGVILYMMLS 597
Cdd:cd05081  159 PLDKDYyvvrePGQSPIF---WYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
402-601 1.92e-09

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 59.30  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRlEA-----NTQREVAALRLCQShPNVVNLHEVHHDQLHTYLVL 476
Cdd:cd06640    4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLE-EAedeieDIQQEITVLSQCDS-PYVTKYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRhFSESEASQILRSLVSAVSFMHEEAGVvHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPg 556
Cdd:cd06640   82 EYLGGGSALDLLRAGP-FDEFQIATMLKEILKGLDYLHSEKKI-HRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQ- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 557 VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06640  156 IKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
410-608 2.05e-09

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 58.89  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQE---FAVKILSRrlEANTQ--------REVAALRLCQsHPNVVNLHEVHHDQlHTYLVLEL 478
Cdd:cd05040    3 LGDGSFGVVRRGEWTTPSGKviqVAVKCLKS--DVLSQpnamddflKEVNAMHSLD-HPNLIRLYGVVLSS-PLMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRK-KRHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGFARlrpqspGV 557
Cdd:cd05040   79 APLGSLLDRLRKdQGHFLISTLCDYAVQIANGMAYL-ESKRFIHRDLAARNILLASKDK---VKIGDFGLMR------AL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 558 PMQTPCFTLQ--------YAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05040  149 PQNEDHYVMQehrkvpfaWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGS 208
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
506-656 2.08e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 60.43  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMHEEAgVVHRDLKPENILYADDTpgAPVKIIDFGFAR-LRPQSPGVPMQTPCFtlqYAAPEL-LAQQGYDESC 583
Cdd:PTZ00036 179 LCRALAYIHSKF-ICHRDLKPQNLLIDPNT--HTLKLCDFGSAKnLLAGQRSVSYICSRF---YRAPELmLGATNYTTHI 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 584 DLWSLGVILYMMLSGQVPFQGAS------------GQGGQSQAAEIMCKIREGRF------SLDGEAWQGVSEEAKELVR 645
Cdd:PTZ00036 253 DLWSLGCIIAEMILGYPIFSGQSsvdqlvriiqvlGTPTEDQLKEMNPNYADIKFpdvkpkDLKKVFPKGTPDDAINFIS 332
                        170
                 ....*....|.
gi 663856869 646 GLLTVDPAKRL 656
Cdd:PTZ00036 333 QFLKYEPLKRL 343
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
410-603 2.11e-09

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 59.12  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQ-EFAVKILSR-RLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEH 487
Cdd:cd05113   12 LGTGQFGVVKYGKWR--GQyDVAIKMIKEgSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRK-KRHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGVPMQTPCFTL 566
Cdd:cd05113   90 LREmRKRFQTQQLLEMCKDVCEAMEYL-ESKQFLHRDLAARNCLVNDQ---GVVKVSDFGLSRYVLDDEYTSSVGSKFPV 165
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663856869 567 QYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQ 603
Cdd:cd05113  166 RWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYE 203
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
31-284 2.15e-09

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 59.01  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVrKAGGHDAGKLYAMkVLRKAAlvqraktqEHTRTERSVLELVRQAPFLVTLHYAFQT--- 107
Cdd:cd05046    5 SNLQEITTLGRGEFGEVFLA-KAKGIEEEGGETL-VLVKAL--------QKTKDENLQSEFRRELDMFRKLSHKNVVrll 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 ----DAKLH-LILDYVSGGEMfthlyqRQYFKEAEVRVYGG---------------EIVLALEHLHKLGIIYRDLKLENV 167
Cdd:cd05046   75 glcrEAEPHyMILEYTDLGDL------KQFLRATKSKDEKLkppplstkqkvalctQIALGMDHLSNARFVHRDLAARNC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 168 LLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFtlegERNT 246
Cdd:cd05046  149 LVSSQREVKVSLLSLSKDVYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKS-DVWSFGVLMWEVFTqGELPF----YGLS 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 247 QAEVSRRI----LKCSPP--FPPRIgpvaQDLLQRLLCKDPKKR 284
Cdd:cd05046  224 DEEVLNRLqagkLELPVPegCPSRL----YKLMTRCWAVNPKDR 263
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
36-238 2.28e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 59.20  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFL------------VRKAGGHDAGKLYAMKVLRKAalvQRAKTQEHTRTERSVLELVRQAPFLVTLHY 103
Cdd:cd14206    2 LQEIGNGWFGKVILgeifsdytpaqvVVKELRVSAGPLEQRKFISEA---QPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 104 AFQTDAKLHLILDYVSGGeMFTHLYQRQYfkeAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd14206   79 CQLGDLKRYLRAQRKADG-MTPDLPTRDL---RTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 184 ----KE--FLTEEKertfsFCGTIEYMAPEIIRSKTGHGKAVDW------WSLGILLFELLT-GASPF 238
Cdd:cd14206  155 hnnyKEdyYLTPDR-----LWIPLRWVAPELLDELHGNLIVVDQskesnvWSLGVTIWELFEfGAQPY 217
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
410-600 2.28e-09

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 59.19  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRrLEANTQR----EVAALRlCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIR-CDEETQKtfltEVKVMR-SLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpgAPVKIIDFGFARL----RPQSPGVPMQT 561
Cdd:cd14222   79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMS-IIHRDLNSHNCLIKLD---KTVVVADFGLSRLiveeKKKPPPDKPTT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 562 PCFTLQ---------------YAAPELLAQQGYDESCDLWSLGVILYMMLsGQV 600
Cdd:cd14222  155 KKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEII-GQV 207
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
20-265 2.37e-09

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 59.65  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  20 NLTGHEEKVSVENFELLKVLGTGAYGKVFLV---RKAGGHdagklYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQAP 96
Cdd:cd14215    1 HLIYRSGDWLQERYEIVSTLGEGTFGRVVQCidhRRGGAR-----VALKIIKNVE-----KYKEAARLEINVLEKINEKD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 -----FLVTLHYAFqtDAKLHLILDY-VSGGEMFTHLYQRQYFKEA--EVRVYGGEIVLALEHLHKLGIIYRDLKLENVL 168
Cdd:cd14215   71 penknLCVQMFDWF--DYHGHMCISFeLLGLSTFDFLKENNYLPYPihQVRHMAFQVCQAVKFLHDNKLTHTDLKPENIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 169 LDSEGH-------------------IVLTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLF 229
Cdd:cd14215  149 FVNSDYeltynlekkrdersvkstaIRVVDFGSA----TFDHEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIF 223
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 663856869 230 ELLTGASPFTLEGERNTQAeVSRRILKcspPFPPRI 265
Cdd:cd14215  224 EYYVGFTLFQTHDNREHLA-MMERILG---PIPSRM 255
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
410-602 2.48e-09

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 58.92  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRlEA-----NTQREVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGEL 484
Cdd:cd06642   12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLE-EAedeieDIQQEITVLSQCDS-PYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 485 LeHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVvHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPgVPMQTPCF 564
Cdd:cd06642   90 L-DLLKPGPLEETYIATILREILKGLDYLHSERKI-HRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQ-IKRNTFVG 163
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663856869 565 TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd06642  164 TPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
35-282 2.54e-09

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 59.25  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFlvrkaGGH------DAGKLYAMKVLRKAAlvqraKTQEHT--RTERSVL-ELvrQAPFLVTLHYAF 105
Cdd:cd05090    9 FMEELGECAFGKIY-----KGHlylpgmDHAQLVAIKTLKDYN-----NPQQWNefQQEASLMtEL--HHPNIVCLLGVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLILDYVSGGEMFTHLYQRQyfKEAEVRVYGGE-------------------IVLALEHLHKLGIIYRDLKLEN 166
Cdd:cd05090   77 TQEQPVCMLFEFMNQGDLHEFLIMRS--PHSDVGCSSDEdgtvkssldhgdflhiaiqIAAGMEYLSSHFFVHKDLAARN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 167 VLLDSEGHIVLTDFGLSKEFLTEEKERTFS-FCGTIEYMAPEIIRsktgHGKAV---DWWSLGILLFELLT-GASP-FTL 240
Cdd:cd05090  155 ILVGEQLHVKISDLGLSREIYSSDYYRVQNkSLLPIRWMPPEAIM----YGKFSsdsDIWSFGVVLWEIFSfGLQPyYGF 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 663856869 241 EGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPK 282
Cdd:cd05090  231 SNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPR 272
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
422-604 2.71e-09

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 58.27  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 422 RQRQSGQEFAVKilsrRLEANTQREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQ 501
Cdd:cd14059   11 LGKFRGEEVAVK----KVRDEKETDIKHLRKLN-HPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 502 ILRSLVSAVSFMHEEAgVVHRDLKPENILYA-DDTpgapVKIIDFGFAR-LRPQSPGVPMQTpcfTLQYAAPELLAQQGY 579
Cdd:cd14059   86 WSKQIASGMNYLHLHK-IIHRDLKSPNVLVTyNDV----LKISDFGTSKeLSEKSTKMSFAG---TVAWMAPEVIRNEPC 157
                        170       180
                 ....*....|....*....|....*
gi 663856869 580 DESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd14059  158 SEKVDIWSFGVVLWELLTGEIPYKD 182
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
487-599 2.85e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 59.62  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYadDTPGaPVKIIDFGFArlrpqspgvpmqtpCF-- 564
Cdd:PHA03212 172 YLAAKRNIAICDILAIERSVLRAIQYLHENR-IIHRDIKAENIFI--NHPG-DVCLGDFGAA--------------CFpv 233
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 663856869 565 ------------TLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQ 599
Cdd:PHA03212 234 dinankyygwagTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
410-626 2.91e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 58.55  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRR----LEANTQREVAALRLCQSHPNVVNLHEVHHDQLH----TYLVLELLRG 481
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRkltkVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG-VVHRDLKPENILYADdtPGAPVKIIDFGFARLRPQSPGvpmQ 560
Cdd:cd14032   89 GTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPpIIHRDLKCDNIFITG--PTGSVKIGDLGLATLKRASFA---K 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 561 TPCFTLQYAAPELLaQQGYDESCDLWSLGVILYMMLSGQVPFqgASGQGGQSQAAEIMCKIREGRF 626
Cdd:cd14032  164 SVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPY--SECQNAAQIYRKVTCGIKPASF 226
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
506-603 2.92e-09

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 59.25  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMHEEAgVVHRDLKPENILYAD---DT-------------PGAPVKIIDFGFARLRPQSpgvpMQTPCFTLQYA 569
Cdd:cd14214  126 LCHALKFLHENQ-LTHTDLKPENILFVNsefDTlynesksceeksvKNTSIRVADFGSATFDHEH----HTTIVATRHYR 200
                         90       100       110
                 ....*....|....*....|....*....|....
gi 663856869 570 APELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14214  201 PPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQ 234
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
489-607 3.05e-09

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 58.99  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 489 RKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGvpmQTPCFTLQY 568
Cdd:cd06620   96 KKKGPFPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILV---NSKGQIKLCDFGVSGELINSIA---DTFVGTSTY 169
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663856869 569 AAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASG 607
Cdd:cd06620  170 MSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSND 208
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
395-590 3.31e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 58.52  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 395 RSAMMQYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILsrRLE-----ANTQREVAALRLCQsHPNVVNL--HEVHH 467
Cdd:cd06645    7 RNPQEDFELIQR---IGSGTYGDVYKARNVNTGELAAIKVI--KLEpgedfAVVQQEIIMMKDCK-HSNIVAYfgSYLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 468 DQLHTYLVLELLRGGELLEHIRKKrhFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGF 547
Cdd:cd06645   81 DKLWICMEFCGGGSLQDIYHVTGP--LSESQIAYVSRETLQGLYYLHSK-GKMHRDIKGANILLTDN---GHVKLADFGV 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 548 ArlrPQSPGVPMQTPCF--TLQYAAPELLAQQ---GYDESCDLWSLGV 590
Cdd:cd06645  155 S---AQITATIAKRKSFigTPYWMAPEVAAVErkgGYNQLCDIWAVGI 199
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
515-676 3.50e-09

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 58.54  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05069  125 ERMNYIHRDLRAANILVGDNLV---CKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTE 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 595 MLS-GQVPFQGASGQggqsqaaEIMCKIREG-RFSLDgeawQGVSEEAKELVRGLLTVDPAKRLKLEGLRgsSWLQDGSA 672
Cdd:cd05069  202 LVTkGRVPYPGMVNR-------EVLEQVERGyRMPCP----QGCPESLHELMKLCWKKDPDERPTFEYIQ--SFLEDYFT 268

                 ....
gi 663856869 673 RSSP 676
Cdd:cd05069  269 ATEP 272
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
113-287 4.00e-09

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 58.53  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMFTHLYQRQYFKEAEVRVyGGEIVLALEHLH---------KLGIIYRDLKLENVLLDSEGHIVLTDFGL- 182
Cdd:cd14054   71 LVLEYAPKGSLCSYLRENTLDWMSSCRM-ALSLTRGLAYLHtdlrrgdqyKPAIAHRDLNSRNVLVKADGSCVICDFGLa 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 -----SKEFLTEEKE---RTFSFCGTIEYMAPEI------IRSKTGHGKAVDWWSLGILLFELLTGAS------------ 236
Cdd:cd14054  150 mvlrgSSLVRGRPGAaenASISEVGTLRYMAPEVlegavnLRDCESALKQVDVYALGLVLWEIAMRCSdlypgesvppyq 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 237 -PFTLEGERNT-----QAEVSRRilKCSPPFPP--RIGPVAQDLLQRLL--C--KDPKKRLGA 287
Cdd:cd14054  230 mPYEAELGNHPtfedmQLLVSRE--KARPKFPDawKENSLAVRSLKETIedCwdQDAEARLTA 290
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
403-590 4.36e-09

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 58.51  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 403 LDLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR------EVAALRLCQsHPNVVNLHEVHHDQLHTYLVL 476
Cdd:cd06633   24 VDLHE--IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqdiikEVKFLQQLK-HPNTIEYKGCYLKDHTAWLVM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 477 ELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADdtPGApVKIIDFGFArlrpqSPG 556
Cdd:cd06633  101 EYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHN-MIHRDIKAGNILLTE--PGQ-VKLADFGSA-----SIA 171
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 663856869 557 VPMQTPCFTLQYAAPE--LLAQQG-YDESCDLWSLGV 590
Cdd:cd06633  172 SPANSFVGTPYWMAPEviLAMDEGqYDGKVDIWSLGI 208
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
94-302 4.90e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 58.46  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  94 QAPFLVTLHYAFQTDAKLHLILDYVSGGEMfTHLYQRQY---FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD 170
Cdd:cd08216   57 QHPNILPYVTSFVVDNDLYVVTPLMAYGSC-RDLLKTHFpegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILIS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 171 SEGHIVLTDFGLSKEFLTEEKERTFSFCGTIE------YMAPEIIR-SKTGHGKAVDWWSLGILLFELLTGASPFT---- 239
Cdd:cd08216  136 GDGKVVLSGLRYAYSMVKHGKRQRVVHDFPKSseknlpWLSPEVLQqNLLGYNEKSDIYSVGITACELANGVVPFSdmpa 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 240 ----LEGERNTQAEvsrrILKCS--PPF-----PPRIGPVA--------QDLLQRL----------LC--KDPKKRlgag 288
Cdd:cd08216  216 tqmlLEKVRGTTPQ----LLDCStyPLEedsmsQSEDSSTEhpnnrdtrDIPYQRTfseafhqfveLClqRDPELR---- 287
                        250
                 ....*....|....
gi 663856869 289 PqGAQEVRNHPFFQ 302
Cdd:cd08216  288 P-SASQLLAHSFFK 300
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
94-302 5.01e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 58.14  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  94 QAPFLVTLHYAFQTDAK----LHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLG--IIYRDLKLENV 167
Cdd:cd14030   82 QHPNIVRFYDSWESTVKgkkcIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNI 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 168 LLDS-EGHIVLTDFGLSKEflteeKERTF--SFCGTIEYMAPEIIRSKtgHGKAVDWWSLGILLFELLTGASPFTlegER 244
Cdd:cd14030  162 FITGpTGSVKIGDLGLATL-----KRASFakSVIGTPEFMAPEMYEEK--YDESVDVYAFGMCMLEMATSEYPYS---EC 231
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 245 NTQAEVSRRILKCSPP--FPPRIGPVAQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQ 302
Cdd:cd14030  232 QNAAQIYRRVTSGVKPasFDKVAIPEVKEIIEGCIRQNKDERY-----AIKDLLNHAFFQ 286
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
491-600 5.16e-09

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 57.89  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 491 KRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGapvKIIDFGFARLRPQSPGVPMQTPCftlqYAA 570
Cdd:cd13975   96 KAGLSLEERLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKKNRA---KITDLGFCKPEAMMSGSIVGTPI----HMA 167
                         90       100       110
                 ....*....|....*....|....*....|
gi 663856869 571 PELLAQQgYDESCDLWSLGVILYMMLSGQV 600
Cdd:cd13975  168 PELFSGK-YDNSVDVYAFGILFWYLCAGHV 196
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
153-299 5.23e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 58.11  E-value: 5.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 153 HKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT-EEKERTFSFCGTIEYMAPEI----IRSKTGHGKAVDWWSLGIL 227
Cdd:cd14053  119 HKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPgKSCGDTHGQVGTRRYMAPEVlegaINFTRDAFLRIDMYAMGLV 198
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 228 LFELLTGASpftlegerNTQAEVSRRILkcspPFPPRIGPVAQ-DLLQRLLCKDpKKRlgagPQGAQEVRNHP 299
Cdd:cd14053  199 LWELLSRCS--------VHDGPVDEYQL----PFEEEVGQHPTlEDMQECVVHK-KLR----PQIRDEWRKHP 254
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
515-607 5.70e-09

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 57.68  E-value: 5.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADdtpGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILY- 593
Cdd:cd05034  109 ESRNYIHRDLAARNILVGE---NNVCKVADFGLARLIEDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYe 185
                         90
                 ....*....|....
gi 663856869 594 MMLSGQVPFQGASG 607
Cdd:cd05034  186 IVTYGRVPYPGMTN 199
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
404-590 6.06e-09

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 57.46  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpaLGQGSFSVCRRCRQRQSGQEFAVKILS---RRLEANTQ---REVAALRLCqSHPNVVN-----LHEvhhdqlHT 472
Cdd:cd06607    5 DLRE--IGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQdiiKEVKFLRQL-RHPNTIEykgcyLRE------HT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 473 -YLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFARLR 551
Cdd:cd06607   76 aWLVMEYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSH-NRIHRDVKAGNILLTEP---GTVKLADFGSASLV 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 552 pqspgVPMQTPCFTLQYAAPE--LLAQQG-YDESCDLWSLGV 590
Cdd:cd06607  152 -----CPANSFVGTPYWMAPEviLAMDEGqYDGKVDVWSLGI 188
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
501-626 6.40e-09

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 58.95  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHEeAGVVHRDLKPENILYADDtpgAPVKIID---F---GFARLRPQSPGVPMQTPcftlqyaaPELL 574
Cdd:COG4248  125 RTARNLAAAVAALHA-AGYVHGDVNPSNILVSDT---ALVTLIDtdsFqvrDPGKVYRCVVGTPEFTP--------PELQ 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 575 AQQ--GYD--ESCDLWSLGVILYMML-SGQVPFQGasGQGGQSQAAEIMCKIREGRF 626
Cdd:COG4248  193 GKSfaRVDrtEEHDRFGLAVLIFQLLmEGRHPFSG--VYQGDGDDPTLEERIAMGHF 247
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
487-603 6.75e-09

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 58.32  E-value: 6.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKrhfseseASQILRSlvsaVSFMHEEAgVVHRDLKPENILYADDT----------------PGAPVKIIDFGFARL 550
Cdd:cd14213  117 HIRNM-------AYQICKS----VNFLHHNK-LTHTDLKPENILFVQSDyvvkynpkmkrdertlKNPDIKVVDFGSATY 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 551 RPQSpgvpMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14213  185 DDEH----HSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQ 233
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
402-602 6.90e-09

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 57.36  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREpALGQGSFSVCRRCRQRqsGQEFAVKILSRRLEANTQ--REvAALRLCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd05039    7 DLKLGE-LIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQAflAE-ASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQIL--RSLVSAVSFMhEEAGVVHRDLKPENILYADDTPGapvKIIDFGFARLRPQSpgv 557
Cdd:cd05039   83 AKGSLVDYLRSRGRAVITRKDQLGfaLDVCEGMEYL-ESKKFVHRDLAARNVLVSEDNVA---KVSDFGLAKEASSN--- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 558 pMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPF 602
Cdd:cd05039  156 -QDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
111-248 7.03e-09

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 57.45  E-value: 7.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQrqyfKEAEVRV-----YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05041   68 IMIVMELVPGGSLLTFLRK----KGARLTVkqllqMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRE 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 186 flTEEKERTFSfCGT----IEYMAPEIIRsktgHGK---AVDWWSLGILLFELLT-GASPFTleGERNTQA 248
Cdd:cd05041  144 --EEDGEYTVS-DGLkqipIKWTAPEALN----YGRytsESDVWSFGILLWEIFSlGATPYP--GMSNQQT 205
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
113-266 8.44e-09

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 57.77  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEMftHLYQRQYFKE-AEVRVYGGEIVLALEHLH---------KLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd14055   76 LITAYHENGSL--QDYLTRHILSwEDLCKMAGSLARGLAHLHsdrtpcgrpKIPIAHRDLKSSNILVKNDGTCVLADFGL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 SKEF---LTEEKERTFSFCGTIEYMAPEIIRSKTG-----HGKAVDWWSLGILLFELLtgaspftlegernTQAEVSRRI 254
Cdd:cd14055  154 ALRLdpsLSVDELANSGQVGTARYMAPEALESRVNledleSFKQIDVYSMALVLWEMA-------------SRCEASGEV 220
                        170
                 ....*....|..
gi 663856869 255 LKCSPPFPPRIG 266
Cdd:cd14055  221 KPYELPFGSKVR 232
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
27-284 8.90e-09

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 57.39  E-value: 8.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALvqrakTQEHTRTERSVLELVRQAPfLVTLhYAFQ 106
Cdd:cd05070    5 EIPRESLQLIKRLGNGQFGEVWM----GTWNGNTKVAIKTLKPGTM-----SPESFLEEAQIMKKLKHDK-LVQL-YAVV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLY--QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK 184
Cdd:cd05070   74 SEEPIYIVTEYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 185 efLTEEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTLEGERNTQAEVSRRI-LKCspp 260
Cdd:cd05070  154 --LIEDNEYTARQGAKfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGYrMPC--- 227
                        250       260
                 ....*....|....*....|....*
gi 663856869 261 fpPRIGPVA-QDLLQRLLCKDPKKR 284
Cdd:cd05070  228 --PQDCPISlHELMIHCWKKDPEER 250
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
27-238 9.18e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 57.72  E-value: 9.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  27 KVSVENFELLKVLGTGAYGKVFLVrKAGGHDAGK-----LYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTL 101
Cdd:cd05100    8 ELSRTRLTLGKPLGEGCFGQVVMA-EAIGIDKDKpnkpvTVAVKMLKDDA---TDKDLSDLVSEMEMMKMIGKHKNIINL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFQTDAKLHLILDYVSGGEMFTHLYQRQ------------------YFKEAEVRVYggEIVLALEHLHKLGIIYRDLK 163
Cdd:cd05100   84 LGACTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdtcklpeeqlTFKDLVSCAY--QVARGMEYLASQKCIHRDLA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 164 LENVLLDSEGHIVLTDFGLSKEFLT-EEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05100  162 ARNVLVTEDNVMKIADFGLARDVHNiDYYKKTTNGRLPVKWMAPEALFDRV-YTHQSDVWSFGVLLWEIFTlGGSPY 237
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
427-602 9.47e-09

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 56.81  E-value: 9.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 427 GQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEV-HHDQLhtYLVLELLRGGELLEHIRKKRHFSESEAsQILRS 505
Cdd:cd05083   29 GQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGViLHNGL--YIVMELMSKGNLVNFLRSRGRALVPVI-QLLQF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMH--EEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSpgvpMQTPCFTLQYAAPELLAQQGYDESC 583
Cdd:cd05083  106 SLDVAEGMEylESKKLVHRDLAARNILVSED---GVAKISDFGLAKVGSMG----VDNSRLPVKWTAPEALKNKKFSSKS 178
                        170       180
                 ....*....|....*....|
gi 663856869 584 DLWSLGVILYMMLS-GQVPF 602
Cdd:cd05083  179 DVWSYGVLLWEVFSyGRAPY 198
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
31-284 9.90e-09

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 57.39  E-value: 9.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEhtrteRSVLELVRQAPfLVTLhYAFQTDAK 110
Cdd:cd05071    9 ESLRLEVKLGQGCFGEVWM----GTWNGTTRVAIKTLKPGTMSPEAFLQE-----AQVMKKLRHEK-LVQL-YAVVSEEP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefLT 188
Cdd:cd05071   78 IYIVTEYMSKGSLLDFLKGEmgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLAR--LI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTLEGERNTQAEVSRRIlkcSPPFPPRI 265
Cdd:cd05071  156 EDNEYTARQGAKfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGY---RMPCPPEC 231
                        250
                 ....*....|....*....
gi 663856869 266 GPVAQDLLQRLLCKDPKKR 284
Cdd:cd05071  232 PESLHDLMCQCWRKEPEER 250
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
404-590 1.08e-08

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 57.37  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpaLGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR------EVAALRLCQsHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd06635   29 DLRE--IGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqdiikEVKFLQRIK-HPNSIEYKGCYLREHTAWLVME 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtPGApVKIIDFGFArlrpqSPGV 557
Cdd:cd06635  106 YCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSH-NMIHRDIKAGNILLTE--PGQ-VKLADFGSA-----SIAS 176
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663856869 558 PMQTPCFTLQYAAPEL---LAQQGYDESCDLWSLGV 590
Cdd:cd06635  177 PANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGI 212
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
399-604 1.13e-08

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 57.79  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 399 MQYELDLREpALGQGSFSVCRRCRQRQSGQEFAVKIL--SRRLEANTQREV---AALRlcQSHPNvvNLHEVHHDQLHTY 473
Cdd:cd14225   41 IAYRYEILE-VIGKGSFGQVVKALDHKTNEHVAIKIIrnKKRFHHQALVEVkilDALR--RKDRD--NSHNVIHMKEYFY 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 ----LVLELLRGGELLEHIRKKRHFSESEASQILR---SLVSAVSFMHEEAgVVHRDLKPENILYADDTPGApVKIIDFG 546
Cdd:cd14225  116 frnhLCITFELLGMNLYELIKKNNFQGFSLSLIRRfaiSLLQCLRLLYRER-IIHCDLKPENILLRQRGQSS-IKVIDFG 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 547 farlrpqspgvpmqTPCFTLQ----------YAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd14225  194 --------------SSCYEHQrvytyiqsrfYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPG 247
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
410-608 1.28e-08

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 56.48  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVK----ILSRRLEANTQREVAALRLcQSHPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKscreTLPPDLKAKFLQEARILKQ-YSHPNIVRLIGVCTQKQPIYIVMELVQGGDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKK-RHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQ----SPGVPMQ 560
Cdd:cd05084   83 TFLRTEgPRLKVKELIRMVENAAAGMEYL-ESKHCIHRDLAARNCLVTEKN---VLKISDFGMSREEEDgvyaATGGMKQ 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 561 TPcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05084  159 IP---VKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQ 204
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
110-232 1.28e-08

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 56.72  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMfTHLYQRQYFKEAEVRVY-GGEIVLALEHLHKLGIIYRDLKLENVLLDSEGH---IVLTDFGLSKE 185
Cdd:cd14155   62 QLHALTEYINGGNL-EQLLDSNEPLSWTVRVKlALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAEK 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 186 F--LTEEKERtFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELL 232
Cdd:cd14155  141 IpdYSDGKEK-LAVVGSPYWMAPEVLRGEPYNEKA-DVFSYGIILCEII 187
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
31-284 1.39e-08

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 56.62  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEhtrteRSVLELVRQAPfLVTLhYAFQTDAK 110
Cdd:cd05069   12 ESLRLDVKLGQGCFGEVWM----GTWNGTTKVAIKTLKPGTMMPEAFLQE-----AQIMKKLRHDK-LVPL-YAVVSEEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefLT 188
Cdd:cd05069   81 IYIVTEFMGKGSLLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR--LI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTLEGERNTQAEVSRRI-LKCSPPFPPR 264
Cdd:cd05069  159 EDNEYTARQGAKfpIKWTAPEAALYGRFTIKS-DVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGYrMPCPQGCPES 237
                        250       260
                 ....*....|....*....|
gi 663856869 265 IgpvaQDLLQRLLCKDPKKR 284
Cdd:cd05069  238 L----HELMKLCWKKDPDER 253
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
39-243 1.68e-08

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 57.00  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGGHDAgKLYAMKVLRKAALVQRAKTQehtrtersvLELVRQA--PFLVTLHYAF--QTDAKLHLI 114
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKDE-KEYALKQIEGTGISMSACRE---------IALLRELkhPNVIALQKVFlsHSDRKVWLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 115 LDYVSGGEMFTHLYQR--------QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGL 182
Cdd:cd07867   80 FDYAEHDLWHIIKFHRaskankkpMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpergRVKIADMGF 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 183 SKEFLTEEKERTF--SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGE 243
Cdd:cd07867  160 ARLFNSPLKPLADldPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQE 222
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
24-238 1.81e-08

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 56.35  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  24 HEEKVSVENFELLKV------LGTGAYGKVFLvrkagGHDAGKLYAMKVLrkAALVQrAKTQEHTR---TERSVLELVRQ 94
Cdd:cd14158    2 HELKNMTNNFDERPIsvggnkLGEGGFGVVFK-----GYINDKNVAVKKL--AAMVD-ISTEDLTKqfeQEIQVMAKCQH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  95 APFLVTLHYAFQTDaKLHLILDYVSGGEMFTHLYQRQYFKEAEVR-----VYGGeiVLALEHLHKLGIIYRDLKLENVLL 169
Cdd:cd14158   74 ENLVELLGYSCDGP-QLCLVYTYMPNGSLLDRLACLNDTPPLSWHmrckiAQGT--ANGINYLHENNHIHRDIKSANILL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 170 DSEGHIVLTDFGLS----KEFLTEEKERtfsFCGTIEYMAPEIIRSKTghGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd14158  151 DETFVPKISDFGLAraseKFSQTIMTER---IVGTTAYMAPEALRGEI--TPKSDIFSFGVVLLEIITGLPPV 218
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
520-624 1.90e-08

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 56.91  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPG-VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSg 598
Cdd:cd05103  201 IHRDLAARNILLSENNV---VKICDFGLARDIYKDPDyVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFS- 276
                         90       100
                 ....*....|....*....|....*.
gi 663856869 599 qvpfQGASGQGGQSQAAEIMCKIREG 624
Cdd:cd05103  277 ----LGASPYPGVKIDEEFCRRLKEG 298
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
515-669 1.93e-08

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 56.14  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADDTPGapvKIIDFGFARlrpqSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05082  119 EGNNFVHRDLAARNVLVSEDNVA---KVSDFGLTK----EASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWE 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 595 MLS-GQVPFQgasgqggQSQAAEIMCKIREGrFSLDgeAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRgsSWLQD 669
Cdd:cd05082  192 IYSfGRVPYP-------RIPLKDVVPRVEKG-YKMD--APDGCPPAVYDVMKNCWHLDAAMRPSFLQLR--EQLEH 255
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
408-604 2.01e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 56.51  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 408 PALGQGSFSVCRRCRQRqsGQEFAVKILSRRLEANTQREVAALRLCQ-SHPNVVNL--------------------HEvh 466
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSWFRETEIYQTVMlRHENILGFiaadikstgswtqlwliteyHE-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLHTYLvlellrggellehirKKRHFSESEASQILRSLVSAVSFMHEE-------AGVVHRDLKPENILYADDTPGAp 539
Cdd:cd14056   77 HGSLYDYL---------------QRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkPAIAHRDLKSKNILVKRDGTCC- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 540 vkIIDFGFArLRPQSPGVPMQTP----CFTLQYAAPELLAQQGYDES------CDLWSLGVILYMML----------SGQ 599
Cdd:cd14056  141 --IADLGLA-VRYDSDTNTIDIPpnprVGTKRYMAPEVLDDSINPKSfesfkmADIYSFGLVLWEIArrceiggiaeEYQ 217

                 ....*
gi 663856869 600 VPFQG 604
Cdd:cd14056  218 LPYFG 222
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
426-656 2.02e-08

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 56.02  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 426 SGQEFAVKILSRRLEANTQREVAALRlcqSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKkrHFSESEASQILRS 505
Cdd:cd05576   23 TQETFILKGLRKSSEYSRERKTIIPR---CVPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSK--FLNDKEIHQLFAD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 L------------------------VSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFG-FARLRPQSPGVPMQ 560
Cdd:cd05576   98 LderlaaasrfyipeeciqrwaaemVVALDALHRE-GIVCRDLNPNNILLNDR---GHIQLTYFSrWSEVEDSCDSDAIE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TpcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQG-ASGQGGQSQaaeimckiregrfsLDGEAWqgVSEE 639
Cdd:cd05576  174 N-----MYCAPEVGGISEETEACDWWSLGALLFELLTGKALVEChPAGINTHTT--------------LNIPEW--VSEE 232
                        250
                 ....*....|....*..
gi 663856869 640 AKELVRGLLTVDPAKRL 656
Cdd:cd05576  233 ARSLLQQLLQFNPTERL 249
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
37-277 2.12e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 56.06  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRKAGGHDAGKLyAMKVLRKAALVQRAKT----------QEHTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd05042    1 QEIGNGWFGKVLLGEIYSGTSVAQV-VVKELKASANPKEQDTflkegqpyriLQHPNILQCLGQCVEAIPYLLVMEFCDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVS-GGEMFTHLYQRQyfkeaevrvyGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS-- 183
Cdd:cd05042   80 GDLKAYLRSEREHeRGDSDTRTLQRM----------ACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhs 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 184 --KE--FLTEEKERTfsfcgTIEYMAPEIIRSKTGHGKAVDW------WSLGILLFELLT-GASPFTLEGERNTQAEVSR 252
Cdd:cd05042  150 ryKEdyIETDDKLWF-----PLRWTAPELVTEFHDRLLVVDQtkysniWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVR 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 663856869 253 -RILKCSPP------------------FPPRIGPVAQDlLQRLL 277
Cdd:cd05042  225 eQDTKLPKPqlelpysdrwyevlqfcwLSPEQRPAAED-VHLLL 267
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
406-624 2.12e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 56.14  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 406 REPALGQGSFSVCRRCRQRQSGQ-EFAVKIlsRRLEA---NTQRE----VAALRLCQSHPNVVNLHEVHHDQLHTYLVLE 477
Cdd:cd05063    9 KQKVIGAGEFGEVFRGILKMPGRkEVAVAI--KTLKPgytEKQRQdflsEASIMGQFSHHNIIRLEGVVTKFKPAMIITE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 478 LLRGGELLEHIRKKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPG 556
Cdd:cd05063   87 YMENGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYL-SDMNYVHRDLAARNILVNSNLE---CKVSDFGLSRVLEDDPE 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 557 VPMQTPC--FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaaEIMCKIREG 624
Cdd:cd05063  163 GTYTTSGgkIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNH-------EVMKAINDG 226
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
31-238 2.39e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 56.51  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRKAG----GHDAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQ 106
Cdd:cd05099   12 DRLVLGKPLGEGCFGQVVRAEAYGidksRPDQTVTVAVKMLKDNA---TDKDLADLISEMELMKLIGKHKNIINLLGVCT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLILDYVSGGEMFTHLYQRQ------------------YFKEAEVRVYggEIVLALEHLHKLGIIYRDLKLENVL 168
Cdd:cd05099   89 QEGPLYVIVEYAAKGNLREFLRARRppgpdytfditkvpeeqlSFKDLVSCAY--QVARGMEYLESRRCIHRDLAARNVL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 169 LDSEGHIVLTDFGLSKEFL-TEEKERTFSFCGTIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05099  167 VTEDNVMKIADFGLARGVHdIDYYKKTSNGRLPVKWMAPEALFDRV-YTHQSDVWSFGILMWEIFTlGGSPY 237
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
395-601 2.45e-08

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 55.81  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 395 RSAMMQYELDLRepaLGQGSFSVCRRCRQRQSGQEFAVKILsrRLEAN-----TQREVAALRLCQsHPNVVNLHEVHHDQ 469
Cdd:cd06646    5 RNPQHDYELIQR---VGSGTYGDVYKARNLHTGELAAVKII--KLEPGddfslIQQEIFMVKECK-HCNIVAYFGSYLSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 470 LHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDtpgAPVKIIDFGFAR 549
Cdd:cd06646   79 EKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSK-GKMHRDIKGANILLTDN---GDVKLADFGVAA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 550 lRPQSPGVPMQTPCFTLQYAAPELLAQQ---GYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06646  155 -KITATIAKRKSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPP 208
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
148-285 2.58e-08

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 55.98  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 148 ALEHLHK--LGIIYRDLKLENVLLDSEGHIVLTDFGLSKeflTEEKERTFSFCG--------------TIEYMAPEIIR- 210
Cdd:cd14036  120 AVQHMHKqsPPIIHRDLKIENLLIGNQGQIKLCDFGSAT---TEAHYPDYSWSAqkrslvedeitrntTPMYRTPEMIDl 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 211 -SKTGHGKAVDWWSLGILLFELLTGASPFTlEGERntqaevsRRIL--KCSPPFPPRIGPVAQDLLQRLLCKDPKKRL 285
Cdd:cd14036  197 ySNYPIGEKQDIWALGCILYLLCFRKHPFE-DGAK-------LRIInaKYTIPPNDTQYTVFHDLIRSTLKVNPEERL 266
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
520-624 2.63e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 56.55  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPG-VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS- 597
Cdd:cd14207  202 IHRDLAARNILLSENNV---VKICDFGLARDIYKNPDyVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSl 278
                         90       100
                 ....*....|....*....|....*...
gi 663856869 598 GQVPFQGAsgqggqsQAAEIMC-KIREG 624
Cdd:cd14207  279 GASPYPGV-------QIDEDFCsKLKEG 299
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
407-608 2.67e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 55.64  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSF-SVCRRCRQRQSGQEFAVKIlsRRLEANTQREVAALRLCQS-------HPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd05066    9 EKVIGAGEFgEVCSGRLKLPGKREIPVAI--KTLKAGYTEKQRRDFLSEAsimgqfdHPNIIHLEGVVTRSKPVMIVTEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKR-HFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGV 557
Cdd:cd05066   87 MENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYL-SDMGYVHRDLAARNILVNSNLV---CKVSDFGLSRVLEDDPEA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 558 PMQTPC--FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05066  163 AYTTRGgkIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSNQ 216
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
404-692 2.72e-08

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 56.18  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 404 DLREpaLGQGSFSVCRRCRQRQSGQEFAVKILS---RRLEANTQREVAALRLCQS--HPNVVNLHEVHHDQLHTYLVLEL 478
Cdd:cd06634   19 DLRE--IGHGSFGAVYFARDVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKlrHPNTIEYRGCYLREHTAWLVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 479 LRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtPGApVKIIDFGFARLRpqspgVP 558
Cdd:cd06634   97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSH-NMIHRDVKAGNILLTE--PGL-VKLGDFGSASIM-----AP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 559 MQTPCFTLQYAAPEL---LAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIregrfsLDGEAWqg 635
Cdd:cd06634  168 ANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPA------LQSGHW-- 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 636 vSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQdgsaRSSPPLRTPDVLESSGPAVR 692
Cdd:cd06634  240 -SEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLL----RERPPTVIMDLIQRTKDAVR 291
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
122-230 2.89e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 56.82  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 122 EMFTHLYQR-QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGlSKEFLTEEKERTFSF--C 198
Cdd:PHA03211 245 DLYTYLGARlRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFG-AACFARGSWSTPFHYgiA 323
                         90       100       110
                 ....*....|....*....|....*....|..
gi 663856869 199 GTIEYMAPEIIRSKTgHGKAVDWWSLGILLFE 230
Cdd:PHA03211 324 GTVDTNAPEVLAGDP-YTPSVDIWSAGLVIFE 354
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
28-238 2.99e-08

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 55.26  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVFlvrkaGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQapFLVTLHYAfqt 107
Cdd:cd05083    3 LNLQKLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRL--LGVILHNG--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 108 dakLHLILDYVSGGEMFTHLYQRQYF--KEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKE 185
Cdd:cd05083   73 ---LYIVMELMSKGNLVNFLRSRGRAlvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 186 FLTEEKERTFSfcgtIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05083  150 GSMGVDNSRLP----VKWTAPEALKNKKFSSKS-DVWSYGVLLWEVFSyGRAPY 198
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
109-250 3.03e-08

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 55.73  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFKEAEVRV-YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFL 187
Cdd:cd05111   81 ASLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLnWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLY 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 188 TEEKERTFSFCGT-IEYMAPE-IIRSKTGHGKavDWWSLGILLFELLT-GASPFT----------LE-GERNTQAEV 250
Cdd:cd05111  161 PDDKKYFYSEAKTpIKWMALEsIHFGKYTHQS--DVWSYGVTVWEMMTfGAEPYAgmrlaevpdlLEkGERLAQPQI 235
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
36-260 3.05e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 55.76  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  36 LKVLGTGAYGKVFLVRKAGGHDAGKLyAMKVLRKAALVQRA----------KTQEHTRTERSVLELVRQAPFLVTLHYAF 105
Cdd:cd05087    2 LKEIGHGWFGKVFLGEVNSGLSSTQV-VVKELKASASVQDQmqfleeaqpyRALQHTNLLQCLAQCAEVTPYLLVMEFCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAKLHLilDYVSGGEMFT---HLYQRQyfkeaevrvyGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGL 182
Cdd:cd05087   81 LGDLKGYL--RSCRAAESMApdpLTLQRM----------ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 183 S----KE--FLTEEKERTfsfcgTIEYMAPEIIRSKTGH------GKAVDWWSLGILLFELLT-GASPFTLEGERNTQA- 248
Cdd:cd05087  149 ShckyKEdyFVTADQLWV-----PLRWIAPELVDEVHGNllvvdqTKQSNVWSLGVTIWELFElGNQPYRHYSDRQVLTy 223
                        250
                 ....*....|..
gi 663856869 249 EVSRRILKCSPP 260
Cdd:cd05087  224 TVREQQLKLPKP 235
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
410-669 3.89e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 55.44  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQR----EVAALRLCQSHPNVVNLHEVHHDQLH----TYLVLELLRG 481
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERqrfkEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG-VVHRDLKPENILYADdtPGAPVKIIDFGFARLRPQSPGvpmQ 560
Cdd:cd14030  113 GTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPpIIHRDLKCDNIFITG--PTGSVKIGDLGLATLKRASFA---K 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 561 TPCFTLQYAAPELLAQQgYDESCDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGrfsLDGEAWQGVS-EE 639
Cdd:cd14030  188 SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSEC------QNAAQIYRRVTSG---VKPASFDKVAiPE 257
                        250       260       270
                 ....*....|....*....|....*....|
gi 663856869 640 AKELVRGLLTVDPAKRLKLEGLRGSSWLQD 669
Cdd:cd14030  258 VKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
33-232 3.99e-08

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 55.64  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVF--LVRKAGGHDAGK----------------LYAMK---------------VLRKAALVQRakTQ 79
Cdd:cd13977    2 YSLIREVGRGSYGVVYeaVVRRTGARVAVKkircnapenvelalreFWALSsiqrqhpnviqleecVLQRDGLAQR--MS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  80 EHTRTERSVLELVrQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEvRVYGGEIVLALEHLHKLGIIY 159
Cdd:cd13977   80 HGSSKSDLYLLLV-ETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTN-TSFMLQLSSALAFLHRNQIVH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 160 RDLKLENVLL-DSEGHIVL--TDFGLSK----------EFLTEEKERTFSFCGTIEYMAPEIIRsktGHGKA-VDWWSLG 225
Cdd:cd13977  158 RDLKPDNILIsHKRGEPILkvADFGLSKvcsgsglnpeEPANVNKHFLSSACGSDFYMAPEVWE---GHYTAkADIFALG 234

                 ....*..
gi 663856869 226 ILLFELL 232
Cdd:cd13977  235 IIIWAMV 241
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
144-317 4.37e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.86  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFcgTIEYMAPEIIRSkTGHGKAVDWWS 223
Cdd:cd07874  127 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVV--TRYYRAPEVILG-MGYKENVDIWS 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 224 LGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPV----------------------------------- 268
Cdd:cd07874  204 VGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTvrnyvenrpkyagltfpklfpdslfpadsehnklk 283
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 269 ---AQDLLQRLLCKDPKKRLgagpqGAQEVRNHPFFQglDWVALAARKIPAP 317
Cdd:cd07874  284 asqARDLLSKMLVIDPAKRI-----SVDEALQHPYIN--VWYDPAEVEAPPP 328
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
39-285 4.64e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 55.36  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAG--GHDAGKLYAMKVLRKAalvqraktqehtrTERSVLELVRQAPFLVTLH-------YAFQTDA 109
Cdd:cd05092   13 LGEGAFGKVFLAECHNllPEQDKMLVAVKALKEA-------------TESARQDFQREAELLTVLQhqhivrfYGVCTEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 K-LHLILDYVSGGEM----FTHLYQRQYFKEAEVRVYG-----------GEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd05092   80 EpLIMVFEYMRHGDLnrflRSHGPDAKILDGGEGQAPGqltlgqmlqiaSQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKEFLTEEKERTFSFCG-TIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF-----TLEGERNT 246
Cdd:cd05092  160 VVKIGDFGMSRDIYSTDYYRVGGRTMlPIRWMPPESILYRKFTTES-DIWSFGVVLWEIFTyGKQPWyqlsnTEAIECIT 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 663856869 247 QAEVSRRILKCsppfPPRIGPVAQDLLQRllckDPKKRL 285
Cdd:cd05092  239 QGRELERPRTC----PPEVYAIMQGCWQR----EPQQRH 269
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
144-238 4.97e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 55.82  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK----EFLTEekertfSFCGTIEYMAPEIIRSkTGHGKAV 219
Cdd:cd07875  134 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtagtSFMMT------PYVVTRYYRAPEVILG-MGYKENV 206
                         90
                 ....*....|....*....
gi 663856869 220 DWWSLGILLFELLTGASPF 238
Cdd:cd07875  207 DIWSVGCIMGEMIKGGVLF 225
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
141-262 5.02e-08

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 54.79  E-value: 5.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 141 YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGT---IEYMAPEIIRSKTGHGK 217
Cdd:cd05058  103 FGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNHTGAklpVKWMALESLQTQKFTTK 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 218 AvDWWSLGILLFELLT-GASP-----------FTLEGERNTQAE-----VSRRILKCSPPFP 262
Cdd:cd05058  183 S-DVWSFGVLLWELMTrGAPPypdvdsfditvYLLQGRRLLQPEycpdpLYEVMLSCWHPKP 243
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
105-238 5.96e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 55.39  E-value: 5.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHlilDYVSGGEMFTHLYQRQYFKEaEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLdSEGHIV-LTDFGLS 183
Cdd:cd14207  153 FQEDKSLS---DVEEEEEDSGDFYKRPLTME-DLISYSFQVARGMEFLSSRKCIHRDLAARNILL-SENNVVkICDFGLA 227
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 184 KE-FLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd14207  228 RDiYKNPDYVRKGDARLPLKWMAPESIFDKIYSTKS-DVWSYGVLLWEIFSlGASPY 283
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
39-265 6.40e-08

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 54.57  E-value: 6.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVflvrKAGghdagkLYAMKVLRKAALVQRAKTQEhtrtERSVL-ELVRQA--------PFLVTLHYAFQTDA 109
Cdd:cd05115   12 LGSGNFGCV----KKG------VYKMRKKQIDVAIKVLKQGN----EKAVRdEMMREAqimhqldnPYIVRMIGVCEAEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 kLHLILDYVSGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLT 188
Cdd:cd05115   78 -LMLVMEMASGGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 189 EE---KERTFSFCgTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF-TLEG-ERNTQAEVSRRiLKCSPPFP 262
Cdd:cd05115  157 DDsyyKARSAGKW-PLKWYAPECINFRKFSSRS-DVWSYGVTMWEAFSyGQKPYkKMKGpEVMSFIEQGKR-MDCPAECP 233

                 ...
gi 663856869 263 PRI 265
Cdd:cd05115  234 PEM 236
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
410-601 6.72e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 55.06  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd06650   13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRnqiiRELQVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGvpmQTPCFT 565
Cdd:cd06650   92 QVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILV---NSRGEIKLCDFGVSGQLIDSMA---NSFVGT 165
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06650  166 RSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
21-234 6.73e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 55.48  E-value: 6.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  21 LTGHEEKVSVEN-FELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFlV 99
Cdd:cd14227    4 LVQHEVLCSMTNtYEVLEFLGRGTFGQVVKCWKRGTNE---IVAIKILKNHPSYARQGQIEVSILARLSTESADDYNF-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQTDAKLHLILDYVSGgEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG---- 173
Cdd:cd14227   80 RAYECFQHKNHTCLVFEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpy 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 174 HIVLTDFGLSKEFlteEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTG 234
Cdd:cd14227  159 RVKVIDFGSASHV---SKAVCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLG 215
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
410-598 6.76e-08

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 54.19  E-value: 6.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKILSRRleantqrevAALRLCQSHpnVVNLHEVHHDQLhTYLVLELLRGGELLEHIR 489
Cdd:cd14068    2 LGDGGFGSVYRAVYR--GEDVAVKIFNKH---------TSFRLLRQE--LVVLSHLHHPSL-VALLAAGTAPRMLVMELA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 490 KK---RHFSESEASQILRSL--------VSAVSFMHEeAGVVHRDLKPENILYADDTPGAPV--KIIDFGFARlrpQSPG 556
Cdd:cd14068   68 PKgslDALLQQDNASLTRTLqhrialhvADGLRYLHS-AMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQ---YCCR 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 663856869 557 VPMQTPCFTLQYAAPELL-AQQGYDESCDLWSLGVILYMMLSG 598
Cdd:cd14068  144 MGIKTSEGTPGFRAPEVArGNVIYNQQADVYSFGLLLYDILTC 186
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
502-602 7.15e-08

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 54.65  E-value: 7.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 502 ILRSLVSAVSFMHEEaGVVHRDLKPENILYADdtpGAPVKIIDFGFARLRPQSPGV-PMQTPCFTLQYAAPELLAQQG-- 578
Cdd:cd14149  113 IARQTAQGMDYLHAK-NIIHRDMKSNNIFLHE---GLTVKIGDFGLATVKSRWSGSqQVEQPTGSILWMAPEVIRMQDnn 188
                         90       100
                 ....*....|....*....|....*
gi 663856869 579 -YDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14149  189 pFSFQSDVYSYGIVLYELMTGELPY 213
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
18-238 7.29e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 55.06  E-value: 7.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  18 EANLTGHEEKVS-VENFELLKVlGTGAYGKVFLVRKAGGHDaGKLYAMKVLRKAALVQRAKTQehtrtersvLELVRQA- 95
Cdd:cd07868    4 KVKLTGERERVEdLFEYEGCKV-GRGTYGHVYKAKRKDGKD-DKDYALKQIEGTGISMSACRE---------IALLRELk 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  96 -PFLVTLHYAF--QTDAKLHLILDYVSGGEMFTHLYQRQ--------YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKL 164
Cdd:cd07868   73 hPNVISLQKVFlsHADRKVWLLFDYAEHDLWHIIKFHRAskankkpvQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 165 ENVLLDSEG----HIVLTDFGLSKEFLTEEKERTF--SFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPF 238
Cdd:cd07868  153 ANILVMGEGpergRVKIADMGFARLFNSPLKPLADldPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIF 232
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
110-231 7.78e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 54.40  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 110 KLHLILDYVSGGEMFTHLYQRQYFKEAEVRVyGGEIVLALEHLH--------KLGIIYRDLKLENVLLDSEGHIVLTDFG 181
Cdd:cd14144   67 QLYLITDYHENGSLYDFLRGNTLDTQSMLKL-AYSAACGLAHLHteifgtqgKPAIAHRDIKSKNILVKKNGTCCIADLG 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 182 LSKEFLTEEKERTF---SFCGTIEYMAPEIIRSKTGHG-----KAVDWWSLGILLFEL 231
Cdd:cd14144  146 LAVKFISETNEVDLppnTRVGTKRYMAPEVLDESLNRNhfdayKMADMYSFGLVLWEI 203
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
492-657 7.80e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 54.81  E-value: 7.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 492 RHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKII-DFGFArLRPQSPGvpMQTPcFTLQYA- 569
Cdd:cd14018  133 NTPSYRLARVMILQLLEGVDHLVRH-GIAHRDLKSDNILLELDFDGCPWLVIaDFGCC-LADDSIG--LQLP-FSSWYVd 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 570 --------APELL-AQQGYD-----ESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAaeimckIREGRFSLDGEAwqg 635
Cdd:cd14018  208 rggnaclmAPEVStAVPGPGvvinySKADAWAVGAIAYEIFGLSNPFYGLGDTMLESRS------YQESQLPALPSA--- 278
                        170       180
                 ....*....|....*....|..
gi 663856869 636 VSEEAKELVRGLLTVDPAKRLK 657
Cdd:cd14018  279 VPPDVRQVVKDLLQRDPNKRVS 300
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
39-269 8.38e-08

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 54.19  E-value: 8.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLvrkaGGHDAGKLYAMKVLRKAALvqrakTQEHTRTERSVLELVRQaPFLVTLHYAFQTDAKLHLILDYV 118
Cdd:cd05112   12 IGSGQFGLVHL----GYWLNKDKVAIKTIREGAM-----SEEDFIEEAEVMMKLSH-PKLVQLYGVCLEQAPICLVFEFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLY-QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSF 197
Cdd:cd05112   82 EHGCLSDYLRtQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGT 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 198 CGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFtlegERNTQAEVSRRILKCSPPFPPRIGPVA 269
Cdd:cd05112  162 KFPVKWSSPEVFSFSRYSSKS-DVWSFGVLMWEVFSeGKIPY----ENRSNSEVVEDINAGFRLYKPRLASTH 229
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
30-234 8.41e-08

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 55.02  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  30 VENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLR-KAALVQRAKTqehtrtERSVLELVRQAP-----FLVTL-- 101
Cdd:cd14226   12 MDRYEIDSLIGKGSFGQVV---KAYDHVEQEWVAIKIIKnKKAFLNQAQI------EVRLLELMNKHDtenkyYIVRLkr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 102 HYAFqtdaKLHLILDYvsggEMFTH-LYQ---RQYFKEAE---VRVYGGEIVLALEHLHK--LGIIYRDLKLENVLLDS- 171
Cdd:cd14226   83 HFMF----RNHLCLVF----ELLSYnLYDllrNTNFRGVSlnlTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNp 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 172 -EGHIVLTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTG 234
Cdd:cd14226  155 kRSAIKIIDFGSS----CQLGQRIYQYIQSRFYRSPEVLLG-LPYDLAIDMWSLGCILVEMHTG 213
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
515-608 8.59e-08

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 54.30  E-value: 8.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADdtpGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05070  122 ERMNYIHRDLRSANILVGN---GLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTE 198
                         90
                 ....*....|....*
gi 663856869 595 MLS-GQVPFQGASGQ 608
Cdd:cd05070  199 LVTkGRVPYPGMNNR 213
PTZ00284 PTZ00284
protein kinase; Provisional
23-234 8.89e-08

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 55.36  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  23 GHEEKVSVENFELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQA------P 96
Cdd:PTZ00284 121 GEDIDVSTQRFKILSLLGEGTFGKVV---EAWDRKRKEYCAVKIVRNVP-----KYTRDAKIEIQFMEKVRQAdpadrfP 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 FLVTLHYaFQTDAKlHL----------ILDYVSGGEMFTHLYQRQYFKEAEVrvyggeivlALEHLH-KLGIIYRDLKLE 165
Cdd:PTZ00284 193 LMKIQRY-FQNETG-HMcivmpkygpcLLDWIMKHGPFSHRHLAQIIFQTGV---------ALDYFHtELHLMHTDLKPE 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 166 NVLLDSEGHIV--LTDFGLSKE-----------FLTEEKERTfSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELL 232
Cdd:PTZ00284 262 NILMETSDTVVdpVTNRALPPDpcrvricdlggCCDERHSRT-AIVSTRHYRSPEVVLG-LGWMYSTDMWSMGCIIYELY 339

                 ..
gi 663856869 233 TG 234
Cdd:PTZ00284 340 TG 341
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
502-602 8.96e-08

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 54.30  E-value: 8.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 502 ILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGV-PMQTPCFTLQYAAPELLAQQG-- 578
Cdd:cd14151  109 IARQTAQGMDYLHAKS-IIHRDLKSNNIFLHEDLT---VKIGDFGLATVKSRWSGShQFEQLSGSILWMAPEVIRMQDkn 184
                         90       100
                 ....*....|....*....|....*
gi 663856869 579 -YDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14151  185 pYSFQSDVYAFGIVLYELMTGQLPY 209
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
410-655 9.19e-08

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 54.20  E-value: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRR--CRQRQSGQEFAVKILSRR-----------LEANTQRE------VAALRLCQSHPNVVNLHEVHHDQL 470
Cdd:cd05116    3 LGSGNFGTVKKgyYQMKKVVKTVAVKILKNEandpalkdellREANVMQQldnpyiVRMIGICEAESWMLVMEMAELGPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 471 HTYLvlellrggellehiRKKRHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENIL-----YAddtpgapvKIIDF 545
Cdd:cd05116   83 NKFL--------------QKNRHVTEKNITELVHQVSMGMKYL-EESNFVHRDLAARNVLlvtqhYA--------KISDF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 546 GFAR-LRPQSPGVPMQTPC-FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGqggqsqaAEIMCKIR 622
Cdd:cd05116  140 GLSKaLRADENYYKAQTHGkWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKG-------NEVTQMIE 212
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 623 EGRFSldgEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd05116  213 KGERM---ECPAGCPPEMYDLMKLCWTYDVDER 242
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
148-238 1.03e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 54.73  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 148 ALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSK----EFLTEEkertfsFCGTIEYMAPEIIRSkTGHGKAVDWWS 223
Cdd:cd07850  114 GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtagtSFMMTP------YVVTRYYRAPEVILG-MGYKENVDIWS 186
                         90
                 ....*....|....*
gi 663856869 224 LGILLFELLTGASPF 238
Cdd:cd07850  187 VGCIMGEMIRGTVLF 201
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
141-274 1.05e-07

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 54.60  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 141 YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE-EKERTFSFCGTIEYMAPEIIRSKTgHGKAV 219
Cdd:cd05102  177 YSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGSARLPLKWMAPESIFDKV-YTTQS 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 220 DWWSLGILLFELLT-GASPFT------------LEGER-----NTQAEVSRRILKC-------SPPFPPRIgPVAQDLLQ 274
Cdd:cd05102  256 DVWSFGVLLWEIFSlGASPYPgvqineefcqrlKDGTRmrapeYATPEIYRIMLSCwhgdpkeRPTFSDLV-EILGDLLQ 334
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
31-244 1.06e-07

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 54.63  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrKAGGHDAGK-LYAMKVLRKAAlvqraKTQEHTRTERSVLELVRQA----PFLVTLHYAF 105
Cdd:cd14214   13 ERYEIVGDLGEGTFGKVV---ECLDHARGKsQVALKIIRNVG-----KYREAARLEINVLKKIKEKdkenKFLCVLMSDW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 qTDAKLHLILDY-VSGGEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVL-LDSE--------- 172
Cdd:cd14214   85 -FNFHGHMCIAFeLLGKNTFEFLKENNFqpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILfVNSEfdtlynesk 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 ---------GHIVLTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRsKTGHGKAVDWWSLGILLFELLTGASPFTLEGE 243
Cdd:cd14214  164 sceeksvknTSIRVADFGSA----TFDHEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHEN 238

                 .
gi 663856869 244 R 244
Cdd:cd14214  239 R 239
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
410-601 1.09e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 54.36  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKI--LSRRLEANTQ--REVAALRLCQShPNVVNLH-------EV-----HHDQLHTY 473
Cdd:cd06615    9 LGAGNGGVVTKVLHRPSGLIMARKLihLEIKPAIRNQiiRELKVLHECNS-PYIVGFYgafysdgEIsicmeHMDGGSLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 474 LVlellrggellehIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDtpgAPVKIIDFGFARLRPQ 553
Cdd:cd06615   88 QV------------LKKAGRIPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLID 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 554 SpgvpM-QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06615  153 S----MaNSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYP 197
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
145-238 1.14e-07

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 53.82  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 145 IVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKERTFSFCG---TIEYMAPEIIrSKTGHGKAVDW 221
Cdd:cd05063  116 IAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSR-VLEDDPEGTYTTSGgkiPIRWTAPEAI-AYRKFTSASDV 193
                         90
                 ....*....|....*...
gi 663856869 222 WSLGILLFELLT-GASPF 238
Cdd:cd05063  194 WSFGIVMWEVMSfGERPY 211
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
515-606 1.14e-07

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 53.88  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05073  124 EQRNYIHRDLRAANILV---SASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLME 200
                         90
                 ....*....|...
gi 663856869 595 MLS-GQVPFQGAS 606
Cdd:cd05073  201 IVTyGRIPYPGMS 213
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
111-248 1.32e-07

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 53.47  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQ-YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefltE 189
Cdd:cd05085   68 IYIVMELVPGGDFLSFLRKKKdELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR----Q 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663856869 190 EKERTFSFCG----TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPFTleGERNTQA 248
Cdd:cd05085  144 EDDGVYSSSGlkqiPIKWTAPEALNYGR-YSSESDVWSFGILLWETFSlGVCPYP--GMTNQQA 204
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
515-604 1.35e-07

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 53.74  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05067  120 EERNYIHRDLRAANILVSDTLS---CKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTE 196
                         90
                 ....*....|.
gi 663856869 595 MLS-GQVPFQG 604
Cdd:cd05067  197 IVThGRIPYPG 207
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
31-238 1.41e-07

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 53.49  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFLVRkaggHDAGKLYAMKVLRKAALVQRAKTQEHTrtersvLELVRQAPFLVTLHyAFQTDAK 110
Cdd:cd05073   11 ESLKLEKKLGAGQFGEVWMAT----YNKHTKVAVKTMKPGSMSVEAFLAEAN------VMKTLQHDKLVKLH-AVVTKEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLYQRQYFKEAEVRV--YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKefLT 188
Cdd:cd05073   80 IYIITEFMAKGSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR--VI 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 189 EEKERTFSFCGT--IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPF 238
Cdd:cd05073  158 EDNEYTAREGAKfpIKWTAPEAINFGSFTIKS-DVWSFGILLMEIVTyGRIPY 209
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
26-276 1.42e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 53.87  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  26 EKVSVENFELLKVLGTGAYGKVF---LVRKAGGHDAgKLYAMKVLRKAALVQRAKTQEHTRTERSVLelvrQAPFLVTLH 102
Cdd:cd05091    1 KEINLSAVRFMEELGEDRFGKVYkghLFGTAPGEQT-QAVAIKTLKDKAEGPLREEFRHEAMLRSRL----QHPNIVCLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 103 YAFQTDAKLHLILDYVSGGEMFTHLYQRQ----------------YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLEN 166
Cdd:cd05091   76 GVVTKEQPMSMIFSYCSHGDLHEFLVMRSphsdvgstdddktvksTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 167 VLLDSEGHIVLTDFGLSKEFLTEEkerTFSFCGT----IEYMAPEIIRsktgHGKA---VDWWSLGILLFELLT-GASPF 238
Cdd:cd05091  156 VLVFDKLNVKISDLGLFREVYAAD---YYKLMGNsllpIRWMSPEAIM----YGKFsidSDIWSYGVVLWEVFSyGLQPY 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 239 -------TLEGERNTQ---------AEVSRRILKCSPPFPPRiGPVAQDLLQRL 276
Cdd:cd05091  229 cgysnqdVIEMIRNRQvlpcpddcpAWVYTLMLECWNEFPSR-RPRFKDIHSRL 281
PTZ00284 PTZ00284
protein kinase; Provisional
488-600 1.55e-07

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 54.59  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 488 IRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILY-ADDT----------PGAP--VKIIDFGFARLRPQS 554
Cdd:PTZ00284 222 IMKHGPFSHRHLAQIIFQTGVALDYFHTELHLMHTDLKPENILMeTSDTvvdpvtnralPPDPcrVRICDLGGCCDERHS 301
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663856869 555 PGVPMQTPcftlQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQV 600
Cdd:PTZ00284 302 RTAIVSTR----HYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKL 343
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
410-655 1.57e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 53.49  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRL-----EANTQREVAALRLCQSHPNVVNLH----EVHHDQLHTYLVLELLR 480
Cdd:cd14138   13 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagsvdEQNALREVYAHAVLGQHSHVVRYYsawaEDDHMLIQNEYCNGGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 481 GGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYA-------------DDTPGAP---VKIID 544
Cdd:cd14138   93 ADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMS-LVHMDIKPSNIFISrtsipnaaseegdEDEWASNkviFKIGD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 545 FGFARlRPQSPGVPMQTPcftlQYAAPELLaQQGYDE--SCDLWSLGVILYMMlSGQVPFqgaSGQGGQSQaaeimcKIR 622
Cdd:cd14138  172 LGHVT-RVSSPQVEEGDS----RFLANEVL-QENYTHlpKADIFALALTVVCA-AGAEPL---PTNGDQWH------EIR 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 663856869 623 EGRFSldgEAWQGVSEEAKELVRGLLTVDPAKR 655
Cdd:cd14138  236 QGKLP---RIPQVLSQEFLDLLKVMIHPDPERR 265
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
31-238 2.03e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 53.26  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKV-----FLVRKAgghDAGKLYAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAF 105
Cdd:cd05054    7 DRLKLGKPLGRGAFGKViqasaFGIDKS---ATCRTVAVKMLKEGA---TASEHKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 106 QTDAK-LHLILDYVSGGEMFTHL----------------------YQRQYFKE----AEVRVYGGEIVLALEHLHKLGII 158
Cdd:cd05054   81 TKPGGpLMVIVEFCKFGNLSNYLrskreefvpyrdkgardveeeeDDDELYKEpltlEDLICYSFQVARGMEFLASRKCI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 159 YRDLKLENVLLdSEGHIV-LTDFGLSKEFLTE-EKERTFSFCGTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GA 235
Cdd:cd05054  161 HRDLAARNILL-SENNVVkICDFGLARDIYKDpDYVRKGDARLPLKWMAPESIFDKVYTTQS-DVWSFGVLLWEIFSlGA 238

                 ...
gi 663856869 236 SPF 238
Cdd:cd05054  239 SPY 241
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
410-603 2.04e-07

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 53.29  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSgqEFAVKilsrRLEANTQREVAALR----------LCQSHPNVVNLHEVHHDQLHTYLVLELL 479
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVK----RLKEDSELDWSVVKnsflteveklSRFRHPNIVDLAGYSAQQGNYCLIYVYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 480 RGGELLEHIRKKRHFSESEASQ---ILRSLVSAVSFMHEEA-GVVHRDLKPENILYADD-TPgapvKIIDFGFARL--RP 552
Cdd:cd14159   75 PNGSLEDRLHCQVSCPCLSWSQrlhVLLGTARAIQYLHSDSpSLIHGDVKSSNILLDAAlNP----KLGDFGLARFsrRP 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 553 QSPGVP-----MQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd14159  151 KQPGMSstlarTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAME 206
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
37-237 2.23e-07

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 52.73  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGkvfLVRKAGGHD-AGKLY--AMKVLRKAALVQRAKTQEHTRTERSVLELvrQAPFLVTLhYAFQTDAKLHL 113
Cdd:cd05040    1 EKLGDGSFG---VVRRGEWTTpSGKVIqvAVKCLKSDVLSQPNAMDDFLKEVNAMHSL--DHPNLIRL-YGVVLSSPLMM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQ-YFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEF------ 186
Cdd:cd05040   75 VTELAPLGSLLDRLRKDQgHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALpqnedh 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663856869 187 --LTEEKERTFSFCgtieymAPEIIRSKT-GHgkAVDWWSLGILLFELLT-GASP 237
Cdd:cd05040  155 yvMQEHRKVPFAWC------APESLKTRKfSH--ASDVWMFGVTLWEMFTyGEEP 201
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
495-604 2.32e-07

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 53.87  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 495 SESEASQILR-------SLVSAVSFMHEEA---------GVVHRDLKPENILYADdtpGAPVKIIDFGFAR-LRPQSPGV 557
Cdd:cd05105  218 NDSEVKNLLSddgseglTTLDLLSFTYQVArgmeflaskNCVHRDLAARNVLLAQ---GKIVKICDFGLARdIMHDSNYV 294
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 558 PMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQG 604
Cdd:cd05105  295 SKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSlGGTPYPG 342
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
35-238 2.59e-07

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 52.76  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  35 LLKVLGTGAYGKVFLVRkagghdagklyaMKVLRKAALVQRAKTQEHTRTERSVLELVRQA--------PFLVTLhYAFQ 106
Cdd:cd05033    8 IEKVIGGGEFGEVCSGS------------LKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEAsimgqfdhPNVIRL-EGVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 107 TDAKLHLIL-DYVSGGEMFTHLYQ-RQYFKEAE-VRVYGGeIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS 183
Cdd:cd05033   75 TKSRPVMIVtEYMENGSLDKFLREnDGKFTVTQlVGMLRG-IASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 184 KEflTEEKERTFSFCG---TIEYMAPEIIrsktGHGK---AVDWWSLGILLFELLT-GASPF 238
Cdd:cd05033  154 RR--LEDSEATYTTKGgkiPIRWTAPEAI----AYRKftsASDVWSFGIVMWEVMSyGERPY 209
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
410-601 2.61e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 53.13  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ----REVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGELL 485
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRnqiiRELQVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 486 EHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYaddTPGAPVKIIDFGFARLRPQSPGvpmQTPCFT 565
Cdd:cd06649   92 QVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILV---NSRGEIKLCDFGVSGQLIDSMA---NSFVGT 165
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663856869 566 LQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVP 601
Cdd:cd06649  166 RSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
428-608 3.26e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 52.71  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 428 QEFAVKILSRRLEANTQREV---AALRLCQSHPNVVNLHEV--------------HHDQLHTYLVLELLRGGELLEHIRK 490
Cdd:cd05091   37 QAVAIKTLKDKAEGPLREEFrheAMLRSRLQHPNIVCLLGVvtkeqpmsmifsycSHGDLHEFLVMRSPHSDVGSTDDDK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 491 --KRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFG-FARLRPQSPGVPMQTPCFTLQ 567
Cdd:cd05091  117 tvKSTLEPADFLHIVTQIAAGMEYLSSHH-VVHKDLATRNVLVFDKLN---VKISDLGlFREVYAADYYKLMGNSLLPIR 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 663856869 568 YAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05091  193 WMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQ 234
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
410-602 3.30e-07

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 52.50  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRcrQRQSGQEFAVKILSRRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGG 482
Cdd:cd14158   23 LGEGGFGVVFK--GYINDKNVAVKKLAAMVDISTEdltkqfeQEIQVMAKCQ-HENLVELLGYSCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 483 ELLEHIRKKRH---FSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYaDDTPGApvKIIDFGFARLRPQ-SPGVP 558
Cdd:cd14158  100 SLLDRLACLNDtppLSWHMRCKIAQGTANGINYLHENN-HIHRDIKSANILL-DETFVP--KISDFGLARASEKfSQTIM 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 663856869 559 MQTPCFTLQYAAPELLAQQGYDEScDLWSLGVILYMMLSGQVPF 602
Cdd:cd14158  176 TERIVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPV 218
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
501-625 3.33e-07

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 52.50  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPG--VPMQTPCFTLQYAAPELLAQQ 577
Cdd:cd14025   96 RIIHETAVGMNFLHCmKPPLLHLDLKPANILLDAHY---HVKISDFGLAKWNGLSHShdLSRDGLRGTIAYLPPERFKEK 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 578 G--YDESCDLWSLGVILYMMLSGQVPFQgasgqgGQSQAAEIMCKIREGR 625
Cdd:cd14025  173 NrcPDTKHDVYSFAIVIWGILTQKKPFA------GENNILHIMVKVVKGH 216
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
520-624 4.15e-07

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 52.67  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPG-VPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS- 597
Cdd:cd05102  194 IHRDLAARNILLSENNV---VKICDFGLARDIYKDPDyVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSl 270
                         90       100
                 ....*....|....*....|....*...
gi 663856869 598 GQVPFQGAsgqggqsQAAEIMCK-IREG 624
Cdd:cd05102  271 GASPYPGV-------QINEEFCQrLKDG 291
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
33-234 4.19e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 52.72  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGGHDagkLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFlVTLHYAFQTDAKLH 112
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNE---IVAVKILKNHPSYARQGQIEVGILARLSNENADEFNF-VRAYECFQHRNHTC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGgEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEGHIVLTDFGLSKEF 186
Cdd:cd14229   78 LVFEMLEQ-NLYDFLKQNKFspLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHV 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 187 lteEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTG 234
Cdd:cd14229  157 ---SKTVCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLG 200
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
39-246 4.66e-07

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 52.14  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  39 LGTGAYGKVFLVRKAGghdagKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQtDAKLHLILDYV 118
Cdd:cd14159    1 IGEGGFGCVYQAVMRN-----TEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQ-QGNYCLIYVYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 119 SGGEMFTHLYQRQYFK----EAEVRVYGGEiVLALEHLHKL--GIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKE 192
Cdd:cd14159   75 PNGSLEDRLHCQVSCPclswSQRLHVLLGT-ARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLAR-FSRRPKQ 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663856869 193 --------RTFSFCGTIEYMAPEIIrsKTGH-GKAVDWWSLGILLFELLTGASPFTLEGERNT 246
Cdd:cd14159  153 pgmsstlaRTQTVRGTLAYLPEEYV--KTGTlSVEIDVYSFGVVLLELLTGRRAMEVDSCSPT 213
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
31-284 4.96e-07

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 51.67  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVFlvrkAGGHDAGKLYAMKVLRKAALVQraktQEHTRTERSVLELVRQaPFLVTLHYAFQTDAK 110
Cdd:cd05148    6 EEFTLERKLGSGYFGEVW----EGLWKNRVRVAIKILKSDDLLK----QQDFQKEVQALKRLRH-KHLISLFAVCSVGEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFTHLY--QRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLS---KE 185
Cdd:cd05148   77 VYIITELMEKGSLLAFLRspEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 186 --FLTEEKERTFsfcgtiEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFtlEGeRNTQaEVSRRILK-CSPPF 261
Cdd:cd05148  157 dvYLSSDKKIPY------KWTAPEAASHGTFSTKS-DVWSFGILLYEMFTyGQVPY--PG-MNNH-EVYDQITAgYRMPC 225
                        250       260
                 ....*....|....*....|...
gi 663856869 262 PPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd05148  226 PAKCPQEIYKIMLECWAAEPEDR 248
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
403-647 5.19e-07

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 52.27  E-value: 5.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 403 LDLREPaLGQGSFSVCRRC------RQRQS-GQEFAVKIL----SRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLH 471
Cdd:cd05099   14 LVLGKP-LGEGCFGQVVRAeaygidKSRPDqTVTVAVKMLkdnaTDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 472 TYLVLELLRGGELLEHIRKKR------HFSESEASQILRSLVSAVSFMHEEA---------GVVHRDLKPENILYADDTp 536
Cdd:cd05099   93 LYVIVEYAAKGNLREFLRARRppgpdyTFDITKVPEEQLSFKDLVSCAYQVArgmeylesrRCIHRDLAARNVLVTEDN- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 537 gaPVKIIDFGFAR-------LRPQSPGvpmQTPcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQ 608
Cdd:cd05099  172 --VMKIADFGLARgvhdidyYKKTSNG---RLP---VKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVE 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 609 ggqsqaaEIMCKIREGR------------FSLDGEAWQGVSEEA---KELVRGL 647
Cdd:cd05099  244 -------ELFKLLREGHrmdkpsncthelYMLMRECWHAVPTQRptfKQLVEAL 290
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
501-604 5.39e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 51.89  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHEEAgVVHRDLKPENILY--ADDTPGAPVKIIDFGFARLRPQSPGVPMQ-TPcftlQYAAPELLAQQ 577
Cdd:cd14067  118 KIAYQIAAGLAYLHKKN-IIFCDLKSDNILVwsLDVQEHINIKLSDYGISRQSFHEGALGVEgTP----GYQAPEIRPRI 192
                         90       100
                 ....*....|....*....|....*..
gi 663856869 578 GYDESCDLWSLGVILYMMLSGQVPFQG 604
Cdd:cd14067  193 VYDEKVDMFSYGMVLYELLSGQRPSLG 219
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
496-667 6.05e-07

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 51.77  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 496 ESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYadDTPGApVKIIDFGFARLRPQSPGvpmQTPCFTLQYAAPELLA 575
Cdd:cd06622  101 EDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLV--NGNGQ-VKLCDFGVSGNLVASLA---KTNIGCQSYMAPERIK 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 576 QQG------YDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEImckiregrfsLDGEAWQ---GVSEEAKELVRG 646
Cdd:cd06622  175 SGGpnqnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAI----------VDGDPPTlpsGYSDDAQDFVAK 244
                        170       180
                 ....*....|....*....|.
gi 663856869 647 LLTVDPAKRLKLEGLRGSSWL 667
Cdd:cd06622  245 CLNKIPNRRPTYAQLLEHPWL 265
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
444-603 6.88e-07

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 51.91  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 444 QREVAALRLCQsHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIrkKRHFS----ESEASQILRSLVSAVSFMHEEaGV 519
Cdd:cd08216   47 QQEILTSRQLQ-HPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLL--KTHFPeglpELAIAFILRDVLNALEYIHSK-GY 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYaddTPGAPVKIIDFGFAR------LRPQSPGVPMQTPCFTLQYAAPELLAQ--QGYDESCDLWSLGVI 591
Cdd:cd08216  123 IHRSVKASHILI---SGDGKVVLSGLRYAYsmvkhgKRQRVVHDFPKSSEKNLPWLSPEVLQQnlLGYNEKSDIYSVGIT 199
                        170
                 ....*....|..
gi 663856869 592 LYMMLSGQVPFQ 603
Cdd:cd08216  200 ACELANGVVPFS 211
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
499-604 6.92e-07

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 51.61  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 499 ASQIlrslVSAVSFMhEEAGVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQG 578
Cdd:cd05071  111 AAQI----ASGMAYV-ERMNYVHRDLRAANILVGENLV---CKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGR 182
                         90       100
                 ....*....|....*....|....*..
gi 663856869 579 YDESCDLWSLGVILYMMLS-GQVPFQG 604
Cdd:cd05071  183 FTIKSDVWSFGILLTELTTkGRVPYPG 209
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
516-608 7.66e-07

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 51.50  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 516 EAGVVHRDLKPENILYADdtpGAPVKIIDFGFAR-LRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05045  145 EMKLVHRDLAARNVLVAE---GRKMKISDFGLSRdVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWE 221
                         90
                 ....*....|....*
gi 663856869 595 MLS-GQVPFQGASGQ 608
Cdd:cd05045  222 IVTlGGNPYPGIAPE 236
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
487-605 8.07e-07

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 51.35  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPGVPMQT----- 561
Cdd:cd14027   80 HVLKKVSVPLSVKGRIILEIIEGMAYLHGK-GVIHKDLKPENILVDNDF---HIKIADLGLASFKMWSKLTKEEHneqre 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663856869 562 -------PCFTLQYAAPELLAQQGYD--ESCDLWSLGVILYMMLSGQVPFQGA 605
Cdd:cd14027  156 vdgtakkNAGTLYYMAPEHLNDVNAKptEKSDVYSFAIVLWAIFANKEPYENA 208
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
37-238 8.10e-07

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 51.41  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFLVRkagghdagklyaMKVLRKAALVQRAKTQEHTRTERSVLELVRQA--------PFLVTLHYAFQTD 108
Cdd:cd05066   10 KVIGAGEFGEVCSGR------------LKLPGKREIPVAIKTLKAGYTEKQRRDFLSEAsimgqfdhPNIIHLEGVVTRS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQR--QYFKEAEVRVYGGeIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeF 186
Cdd:cd05066   78 KPVMIVTEYMENGSLDAFLRKHdgQFTVIQLVGMLRG-IASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSR-V 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663856869 187 LTEEKERTFSFCG---TIEYMAPEIIRSKTgHGKAVDWWSLGILLFELLT-GASPF 238
Cdd:cd05066  156 LEDDPEAAYTTRGgkiPIRWTAPEAIAYRK-FTSASDVWSYGIVMWEVMSyGERPY 210
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
21-234 8.11e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 52.01  E-value: 8.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  21 LTGHEEKVSVEN-FELLKVLGTGAYGKVflvRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFlV 99
Cdd:cd14228    4 LVQHEILCSMTNsYEVLEFLGRGTFGQV---AKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNF-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 100 TLHYAFQTDAKLHLILDYVSGgEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLL----DSEG 173
Cdd:cd14228   80 RSYECFQHKNHTCLVFEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPY 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663856869 174 HIVLTDFGLSKEFlteEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTG 234
Cdd:cd14228  159 RVKVIDFGSASHV---SKAVCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLG 215
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
410-593 8.12e-07

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 51.59  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCrrCRQRQSGQEFAVKILSRRLEAN--TQREVAALRLCQsHPN---------------------VVNLHEvh 466
Cdd:cd14054    3 IGQGRYGTV--WKGSLDERPVAVKVFPARHRQNfqNEKDIYELPLME-HSNilrfigaderptadgrmeyllVLEYAP-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 467 HDQLHTYLvlellrggellehirkKRHFSESEASQIL-RSLVSAVSFMHEEA--------GVVHRDLKPENILYADDtpG 537
Cdd:cd14054   78 KGSLCSYL----------------RENTLDWMSSCRMaLSLTRGLAYLHTDLrrgdqykpAIAHRDLNSRNVLVKAD--G 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663856869 538 APVkIIDFGFARLRPQSPGVPMQTP---------CFTLQYAAPELLA-------QQGYDESCDLWSLGVILY 593
Cdd:cd14054  140 SCV-ICDFGLAMVLRGSSLVRGRPGaaenasiseVGTLRYMAPEVLEgavnlrdCESALKQVDVYALGLVLW 210
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
141-238 8.43e-07

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 51.91  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 141 YGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTE-EKERTFSFCGTIEYMAPEIIRSKTgHGKAV 219
Cdd:cd05103  184 YSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGDARLPLKWMAPETIFDRV-YTIQS 262
                         90       100
                 ....*....|....*....|
gi 663856869 220 DWWSLGILLFELLT-GASPF 238
Cdd:cd05103  263 DVWSFGVLLWEIFSlGASPY 282
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
407-602 8.52e-07

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 51.36  E-value: 8.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 407 EPALGQGSFSVCRRCRQRQSGQEFAVKILsrRLEANTQREVAALRLCQShPNVVNLHEVHHDQLHTYLVLELLRGGELLE 486
Cdd:cd13991   11 QLRIGRGSFGEVHRMEDKQTGFQCAVKKV--RLEVFRAEELMACAGLTS-PRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEAgVVHRDLKPENILYADDtpGAPVKIIDFGFA-RLRPQSPGVPMQT---P 562
Cdd:cd13991   88 LIKEQGCLPEDRALHYLGQALEGLEYLHSRK-ILHGDVKADNVLLSSD--GSDAFLCDFGHAeCLDPDGLGKSLFTgdyI 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd13991  165 PGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
409-623 1.23e-06

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 50.84  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 409 ALGQGSFSVCRRCR-----QRQSGQEFAVKILSRRLEANTQ----REVAALRLCQsHPNVVNLHEV-------------- 465
Cdd:cd05048   12 ELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASPKTQqdfrREAELMSDLQ-HPNIVCLLGVctkeqpqcmlfeym 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 466 HHDQLHTYLVLELLRGGELLEHIRKKRHfSESEASQILRSLVSAVSFMHEEAG--VVHRDLKPENILYADdtpGAPVKII 543
Cdd:cd05048   91 AHGDLHEFLVRHSPHSDVGVSSDDDGTA-SSLDQSDFLHIAIQIAAGMEYLSShhYVHRDLAARNCLVGD---GLTVKIS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 544 DFGFARL-------RPQSPGVpmqtpcFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGQggqsqaa 615
Cdd:cd05048  167 DFGLSRDiyssdyyRVQSKSL------LPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQ------- 233

                 ....*...
gi 663856869 616 EIMCKIRE 623
Cdd:cd05048  234 EVIEMIRS 241
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
37-284 1.46e-06

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 50.36  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  37 KVLGTGAYGKVFlvrkAGGHDAGKLYAMKVLR-----KAALVQRAKTQEHTRTERsvlelvrqapfLVTLhYAFQTDAK- 110
Cdd:cd05034    1 KKLGAGQFGEVW----MGVWNGTTKVAVKTLKpgtmsPEAFLQEAQIMKKLRHDK-----------LVQL-YAVCSDEEp 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 111 LHLILDYVSGGEMFthlyqrQYFKEAEVRV--------YGGEIVLALEHLHKLGIIYRDLKLENVLLdSEGHIV-LTDFG 181
Cdd:cd05034   65 IYIVTELMSKGSLL------DYLRTGEGRAlrlpqlidMAAQIASGMAYLESRNYIHRDLAARNILV-GENNVCkVADFG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 182 LSKefLTEEKERTfSFCGT---IEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASPFTLEGERNTQAEVSR--RIl 255
Cdd:cd05034  138 LAR--LIEDDEYT-AREGAkfpIKWTAPEAALYGRFTIKS-DVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERgyRM- 212
                        250       260
                 ....*....|....*....|....*....
gi 663856869 256 kcspPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd05034  213 ----PKPPGCPDELYDIMLQCWKKEPEER 237
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
520-604 1.46e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 50.57  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPC-FTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS- 597
Cdd:cd05054  160 IHRDLAARNILLSENNV---VKICDFGLARDIYKDPDYVRKGDArLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSl 236

                 ....*..
gi 663856869 598 GQVPFQG 604
Cdd:cd05054  237 GASPYPG 243
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
33-284 1.53e-06

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 50.41  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFlvrKAGGHDAGKLYAMKVLRKAaLVQRAKTQEHTRtERSVLELVRQAPFLVTLHYAFQTDAKLH 112
Cdd:cd14138    7 FHELEKIGSGEFGSVF---KCVKRLDGCIYAIKRSKKP-LAGSVDEQNALR-EVYAHAVLGQHSHVVRYYSAWAEDDHML 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 113 LILDYVSGGEM---FTHLYQR-QYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLD-----------------S 171
Cdd:cd14138   82 IQNEYCNGGSLadaISENYRImSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegdedewA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 172 EGHIV--LTDFGLSKEFLTEEKERtfsfcGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFElLTGASPFTLEGERntQAE 249
Cdd:cd14138  162 SNKVIfkIGDLGHVTRVSSPQVEE-----GDSRFLANEVLQENYTHLPKADIFALALTVVC-AAGAEPLPTNGDQ--WHE 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 663856869 250 VSRRILkcsPPFPPRIGPVAQDLLQRLLCKDPKKR 284
Cdd:cd14138  234 IRQGKL---PRIPQVLSQEFLDLLKVMIHPDPERR 265
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
28-238 1.68e-06

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 50.42  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  28 VSVENFELLKVLGTGAYGKVF--LVRKAGGHDAGKLYAMKVLRKAA-LVQRAktqeHTRTERSVLELVrQAPFLVTLHYA 104
Cdd:cd05032    3 LPREKITLIRELGQGSFGMVYegLAKGVVKGEPETRVAIKTVNENAsMRERI----EFLNEASVMKEF-NCHHVVRLLGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 105 FQTDAKLHLILDYVSGGEMFTHLYQRQYfKEAEVRVYG-----------GEIVLALEHLHKLGIIYRDLKLENVLLDSEG 173
Cdd:cd05032   78 VSTGQPTLVVMELMAKGDLKSYLRSRRP-EAENNPGLGpptlqkfiqmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 174 HIVLTDFGLSKE-FLTEEKERTFSFCGTIEYMAPEIIRSktghGK---AVDWWSLGILLFELLT-GASPF 238
Cdd:cd05032  157 TVKIGDFGMTRDiYETDYYRKGGKGLLPVRWMAPESLKD----GVfttKSDVWSFGVVLWEMATlAEQPY 222
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
519-602 2.41e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 49.88  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 519 VVHRDLKPENILYadDTPGApVKIIDFGFARlrpQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSG 598
Cdd:cd06619  116 ILHRDVKPSNMLV--NTRGQ-VKLCDFGVST---QLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALG 189

                 ....
gi 663856869 599 QVPF 602
Cdd:cd06619  190 RFPY 193
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
402-608 2.69e-06

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 49.97  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 402 ELDLREPaLGQGSFSvcRRCRQRQSGqEFAVKILsrRLEANTQ-------REVAALRLCQsHPNVVNLHEVHHDQLHTYL 474
Cdd:cd14152    1 QIELGEL-IGQGRWG--KVHRGRWHG-EVAIRLL--EIDGNNQdhlklfkKEVMNYRQTR-HENVVLFMGACMHPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEHIRK-KRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTpgapVKIIDFGF----AR 549
Cdd:cd14152   74 ITSFCKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAK-GIVHKDLKSKNVFYDNGK----VVITDFGLfgisGV 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 550 LRPQSPGVPMQTPCFTLQYAAPELLAQQ--GYDESC-------DLWSLGVILYMMLSGQVPFQGASGQ 608
Cdd:cd14152  149 VQEGRRENELKLPHDWLCYLAPEIVREMtpGKDEDClpfskaaDVYAFGTIWYELQARDWPLKNQPAE 216
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
410-610 3.08e-06

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 49.42  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQrQSGQEFAVKILSRRLEANT----QREVAALRLCQsHPNVVNL---HEVHHDQLHTY-LVLELLRG 481
Cdd:cd14664    1 IGRGGAGTVYKGVM-PNGTLVAVKRLKGEGTQGGdhgfQAEIQTLGMIR-HRNIVRLrgyCSNPTTNLLVYeYMPNGSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAG--VVHRDLKPENILYaDDTPGAPVKiiDFGFARLRPQSPGVPM 559
Cdd:cd14664   79 ELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDCSplIIHRDVKSNNILL-DEEFEAHVA--DFGLAKLMDDKDSHVM 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663856869 560 QTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGG 610
Cdd:cd14664  156 SSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDG 206
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
515-604 3.46e-06

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 49.34  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYadDTPGApVKIIDFGFARL--------RPQSPGVPmqtpcftLQYAAPELLAQQGYDESCDLW 586
Cdd:cd05057  126 EEKRLVHRDLAARNVLV--KTPNH-VKITDFGLAKLldvdekeyHAEGGKVP-------IKWMALESIQYRIYTHKSDVW 195
                         90
                 ....*....|....*....
gi 663856869 587 SLGVILY-MMLSGQVPFQG 604
Cdd:cd05057  196 SYGVTVWeLMTFGAKPYEG 214
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
500-659 3.51e-06

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 49.31  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQILRSLVSAVSFMHEEAGVVHRDLKPENILyADDTpgAPVKIIDFGFARLRPQSPGVPMQTPCFTLQ--YAAPELL--- 574
Cdd:cd13992  100 SSFIKDIVKGMNYLHSSSIGYHGRLKSSNCL-VDSR--WVVKLTDFGLRNLLEEQTNHQLDEDAQHKKllWTAPELLrgs 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 575 --AQQGyDESCDLWSLGVILYMMLSGQVPFqgASGQGGQSQAAEIMCKIREGRFSLDGEAWQgVSEEAKELVRGLLTVDP 652
Cdd:cd13992  177 llEVRG-TQKGDVYSFAIILYEILFRSDPF--ALEREVAIVEKVISGGNKPFRPELAVLLDE-FPPRLVLLVKQCWAENP 252

                 ....*..
gi 663856869 653 AKRLKLE 659
Cdd:cd13992  253 EKRPSFK 259
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
144-238 3.56e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 50.02  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 144 EIVLALEHLHKLGIIYRDLKLENVLLdSEGHIV-LTDFGLSKEFLTE----EKERTFSfcgTIEYMAPEIIRSKTgHGKA 218
Cdd:cd05105  245 QVARGMEFLASKNCVHRDLAARNVLL-AQGKIVkICDFGLARDIMHDsnyvSKGSTFL---PVKWMAPESIFDNL-YTTL 319
                         90       100
                 ....*....|....*....|.
gi 663856869 219 VDWWSLGILLFELLT-GASPF 238
Cdd:cd05105  320 SDVWSYGILLWEIFSlGGTPY 340
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
506-656 4.20e-06

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 49.17  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMHEeAGVVHRDLKPENIL-----------YA--------DDTPGapvkiiDFGF----ARLRpqspgvpmqtP 562
Cdd:cd13980  106 LLHALNQCHK-RGVCHGDIKTENVLvtswnwvyltdFAsfkptylpEDNPA------DFSYffdtSRRR----------T 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CftlqYAAPE-LLAQQGYDE-----------SCDLWSLG-VILYMMLSGQVPFQgasgqggQSQaaeiMCKIREGRFSLD 629
Cdd:cd13980  169 C----YIAPErFVDALTLDAeserrdgeltpAMDIFSLGcVIAELFTEGRPLFD-------LSQ----LLAYRKGEFSPE 233
                        170       180
                 ....*....|....*....|....*..
gi 663856869 630 GEAWQGVSEEAKELVRGLLTVDPAKRL 656
Cdd:cd13980  234 QVLEKIEDPNIRELILHMIQRDPSKRL 260
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
519-604 4.57e-06

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 49.74  E-value: 4.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 519 VVHRDLKPENILYADDTPGApVKIIDFGfarlrpqspgvpmqTPCFTLQ----------YAAPELLAQQGYDESCDLWSL 588
Cdd:cd14224  189 IIHCDLKPENILLKQQGRSG-IKVIDFG--------------SSCYEHQriytyiqsrfYRAPEVILGARYGMPIDMWSF 253
                         90
                 ....*....|....*.
gi 663856869 589 GVILYMMLSGQVPFQG 604
Cdd:cd14224  254 GCILAELLTGYPLFPG 269
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
411-597 4.82e-06

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 48.97  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 411 GQGSFSVCRRCRQRqsGQEFAVKILSRRLEANTQRE-----VAALRlcqsHPNVVNL----HEVHHDQLHTYLVLELLRG 481
Cdd:cd13998    4 GKGRFGEVWKASLK--NEPVAVKIFSSRDKQSWFREkeiyrTPMLK----HENILQFiaadERDTALRTELWLVTAFHPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 482 GELLEHIRkkRHFSESEAS-QILRSLVSAVSFMHEE--------AGVVHRDLKPENILYADDTPGApvkIIDFGFARLRP 552
Cdd:cd13998   78 GSL*DYLS--LHTIDWVSLcRLALSVARGLAHLHSEipgctqgkPAIAHRDLKSKNILVKNDGTCC---IADFGLAVRLS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663856869 553 QSPGVP---MQTPCFTLQYAAPELL---AQQGYDESC---DLWSLGVILYMMLS 597
Cdd:cd13998  153 PSTGEEdnaNNGQVGTKRYMAPEVLegaINLRDFESFkrvDIYAMGLVLWEMAS 206
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
410-602 5.30e-06

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 48.68  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRqsGQEFAVKilsrRLEANTQ----------REVAALrLCQSHPNVVN-----LHEVHHDQLHTYL 474
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIK----RYRANTYcsksdvdmfcREVSIL-CRLNHPCVIQfvgacLDDPSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 475 VLELLRGGELLEhirKKRHFSESEASQILRSLVSAVSFMHEEAG-VVHRDLKPENILYADDtpGAPVkIIDFGFARLRPQ 553
Cdd:cd14064   74 VSGGSLFSLLHE---QKRVIDLQSKLIIAVDVAKGMEYLHNLTQpIIHRDLNSHNILLYED--GHAV-VADFGESRFLQS 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663856869 554 SPGVPMQTPCFTLQYAAPELLAQQG-YDESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd14064  148 LDEDNMTKQPGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
501-602 9.27e-06

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 48.08  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLvsavSFMHEEAgVVHRDLKPENILYADdtpgAPVKIIDFGFARLRPQSPGVPMQTPCfTLQYAAPELLAQQGYD 580
Cdd:cd13995  104 HVLKGL----DFLHSKN-IIHHDIKPSNIVFMS----TKAVLVDFGLSVQMTEDVYVPKDLRG-TEIYMSPEVILCRGHN 173
                         90       100
                 ....*....|....*....|..
gi 663856869 581 ESCDLWSLGVILYMMLSGQVPF 602
Cdd:cd13995  174 TKADIYSLGATIIHMQTGSPPW 195
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
455-604 1.45e-05

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 47.87  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 455 SHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRH-FSESE-----ASQILRSLvsavSFMhEEAGVVHRDLKPEN 528
Cdd:cd05055   97 NHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKREsFLTLEdllsfSYQVAKGM----AFL-ASKNCIHRDLAARN 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663856869 529 ILYaddTPGAPVKIIDFGFAR-LRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQG 604
Cdd:cd05055  172 VLL---THGKIVKICDFGLARdIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPG 246
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
499-602 1.47e-05

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 47.45  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 499 ASQIlrslVSAVSFMHEEaGVVHRDLKPENILYADDTPgapVKIIDFGFARlrpqsPGVPMQTPCF------TLQYAAPE 572
Cdd:cd05043  122 ALQI----ACGMSYLHRR-GVIHKDIAARNCVIDDELQ---VKITDNALSR-----DLFPMDYHCLgdnenrPIKWMSLE 188
                         90       100       110
                 ....*....|....*....|....*....|.
gi 663856869 573 LLAQQGYDESCDLWSLGVILY-MMLSGQVPF 602
Cdd:cd05043  189 SLVNKEYSSASDVWSFGVLLWeLMTLGQTPY 219
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
501-682 1.76e-05

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 47.22  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 501 QILRSLVSAVSFMHE-EAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLR----PQSPGVPMQTPCFTLQYAAPElla 575
Cdd:cd14026  104 RILYEIALGVNYLHNmSPPLLHHDLKTQNILLDGEF---HVKIADFGLSKWRqlsiSQSRSSKSAPEGGTIIYMPPE--- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 576 qqGYDES--------CDLWSLGVILYMMLSGQVPFQGAsgqggqSQAAEIMCKIREGrfsldgeAWQGVSEEAkelvrgl 647
Cdd:cd14026  178 --EYEPSqkrrasvkHDIYSYAIIMWEVLSRKIPFEEV------TNPLQIMYSVSQG-------HRPDTGEDS------- 235
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 663856869 648 LTVDPAKRLKLEGLRGSSWLQDGSARSS---------PPLRTPD 682
Cdd:cd14026  236 LPVDIPHRATLINLIESGWAQNPDERPSflkclielePVLRTFD 279
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
520-604 2.95e-05

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 46.94  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFAR-------LRPQSPGvpmQTPcftLQYAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd05100  156 IHRDLAARNVLVTEDNV---MKIADFGLARdvhnidyYKKTTNG---RLP---VKWMAPEALFDRVYTHQSDVWSFGVLL 226
                         90
                 ....*....|...
gi 663856869 593 YMMLS-GQVPFQG 604
Cdd:cd05100  227 WEIFTlGGSPYPG 239
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
515-604 3.40e-05

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 46.55  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYadDTPGApVKIIDFGFARL--------RPQSPGVPmqtpcftLQYAAPELLAQQGYDESCDLW 586
Cdd:cd05108  126 EDRRLVHRDLAARNVLV--KTPQH-VKITDFGLAKLlgaeekeyHAEGGKVP-------IKWMALESILHRIYTHQSDVW 195
                         90
                 ....*....|....*....
gi 663856869 587 SLGVILY-MMLSGQVPFQG 604
Cdd:cd05108  196 SYGVTVWeLMTFGSKPYDG 214
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
520-604 4.83e-05

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 46.16  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFAR-------LRPQSPGvpmQTPcftLQYAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd05098  157 IHRDLAARNVLVTEDNV---MKIADFGLARdihhidyYKKTTNG---RLP---VKWMAPEALFDRIYTHQSDVWSFGVLL 227
                         90
                 ....*....|...
gi 663856869 593 YMMLS-GQVPFQG 604
Cdd:cd05098  228 WEIFTlGGSPYPG 240
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
410-655 4.85e-05

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 45.59  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 410 LGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQ-REVAALRLCqSHPNVVNLHE--VHHDQLHTYLvLELLRGGELLE 486
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIvREISLLQKL-SHPNIVRYLGicVKDEKLHPIL-EYVSGGCLEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRHFSESEASQILRSLVSAVSFMHEEaGVVHRDLKPENILYADDTPGAPVKIIDFGFAR----LRPQSPGVPMQTp 562
Cdd:cd14156   79 LAREELPLSWREKVELACDISRGMVYLHSK-NIYHRDLNSKNCLIRVTPRGREAVVTDFGLARevgeMPANDPERKLSL- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 563 CFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLsGQVPfqgasgqggqsqaAEIMCKIREGRFSLDGEAWQ----GVSE 638
Cdd:cd14156  157 VGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP-------------ADPEVLPRTGDFGLDVQAFKemvpGCPE 222
                        250
                 ....*....|....*..
gi 663856869 639 EAKELVRGLLTVDPAKR 655
Cdd:cd14156  223 PFLDLAASCCRMDAFKR 239
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
424-608 5.02e-05

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 45.78  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 424 RQSGQEFAVKILSRRLEANTQREVAALRLCQ-SHPNVVNLH--EVHHDQLHT-YLVLELLRGGELLEHIRKKRHFSESEA 499
Cdd:cd14053   15 QYLNRLVAVKIFPLQEKQSWLTEREIYSLPGmKHENILQFIgaEKHGESLEAeYWLITEFHERGSLCDYLKGNVISWNEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQILRSLVSAVSFMHEE---------AGVVHRDLKPENILYADDTPGApvkIIDFGFARLRpqSPGVPMQTPCF---TLQ 567
Cdd:cd14053   95 CKIAESMARGLAYLHEDipatngghkPSIAHRDFKSKNVLLKSDLTAC---IADFGLALKF--EPGKSCGDTHGqvgTRR 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663856869 568 YAAPELL--AQQGYDES---CDLWSLGVILYMMLSG-----------QVPFQGASGQ 608
Cdd:cd14053  170 YMAPEVLegAINFTRDAflrIDMYAMGLVLWELLSRcsvhdgpvdeyQLPFEEEVGQ 226
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
20-275 5.27e-05

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 46.00  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  20 NLTGHEEKVSVENFELLKVLGTGAYGKVFlvrKAGGHDA-GKLYAMKVLRKaalVQRAKtqEHTRTERSVLE-LVRQAP- 96
Cdd:cd14213    1 HLICQSGDVLRARYEIVDTLGEGAFGKVV---ECIDHKMgGMHVAVKIVKN---VDRYR--EAARSEIQVLEhLNTTDPn 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  97 ---FLVTLHYAFQTDAKLHLILDYVsGGEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDS 171
Cdd:cd14213   73 stfRCVQMLEWFDHHGHVCIVFELL-GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 172 EGHIV-------------------LTDFGLSkeflTEEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELL 232
Cdd:cd14213  152 SDYVVkynpkmkrdertlknpdikVVDFGSA----TYDDEHHSTLVSTRHYRAPEVILA-LGWSQPCDVWSIGCILIEYY 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 663856869 233 TGASPFTLEGERNTQAeVSRRILkcsppfppriGPVAQDLLQR 275
Cdd:cd14213  227 LGFTVFQTHDSKEHLA-MMERIL----------GPLPKHMIQK 258
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
515-604 5.66e-05

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 45.79  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 515 EEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARL--------RPQSPGVPmqtpcftLQYAAPELLAQQGYDESCDLW 586
Cdd:cd05109  126 EEVRLVHRDLAARNVLVKSPN---HVKITDFGLARLldideteyHADGGKVP-------IKWMALESILHRRFTHQSDVW 195
                         90
                 ....*....|....*....
gi 663856869 587 SLGVILY-MMLSGQVPFQG 604
Cdd:cd05109  196 SYGVTVWeLMTFGAKPYDG 214
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
403-625 5.70e-05

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 45.71  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 403 LDLREPALGQGSFSVCRR--CRQRQSGQEFAVKILSRRLEANTQRE----------------VAALRLCQSHPNVVNLHE 464
Cdd:cd05115    5 LLIDEVELGSGNFGCVKKgvYKMRKKQIDVAIKVLKQGNEKAVRDEmmreaqimhqldnpyiVRMIGVCEAEALMLVMEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 465 VHHDQLHTYLVLellrggellehirKKRHFSESEASQILRSLVSAVSFMhEEAGVVHRDLKPENILYADDTPGapvKIID 544
Cdd:cd05115   85 ASGGPLNKFLSG-------------KKDEITVSNVVELMHQVSMGMKYL-EEKNFVHRDLAARNVLLVNQHYA---KISD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 545 FGFAR--------LRPQSPGVpmqtpcFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQGASGqggqsqaA 615
Cdd:cd05115  148 FGLSKalgaddsyYKARSAGK------WPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKG-------P 214
                        250
                 ....*....|
gi 663856869 616 EIMCKIREGR 625
Cdd:cd05115  215 EVMSFIEQGK 224
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
33-234 6.02e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 45.90  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  33 FELLKVLGTGAYGKVFLVRKAGghdAGKLYAMKVLRKAALVQRaktqeHTRTERSVLELVRQAPF----LVTLHYAFQTD 108
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRG---TNEIVAIKILKNHPSYAR-----QGQIEVSILSRLSQENAdefnFVRAYECFQHK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGgEMFTHLYQRQY--FKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEG----HIVLTDFGL 182
Cdd:cd14211   73 NHTCLVFEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663856869 183 SKEFlteEKERTFSFCGTIEYMAPEIIRSkTGHGKAVDWWSLGILLFELLTG 234
Cdd:cd14211  152 ASHV---SKAVCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLG 199
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
145-238 6.69e-05

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 45.25  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 145 IVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKeFLTEEKER---TFSFCGTI--EYMAPEIIRSKTgHGKAV 219
Cdd:cd05065  115 IAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSR-FLEDDTSDptyTSSLGGKIpiRWTAPEAIAYRK-FTSAS 192
                         90       100
                 ....*....|....*....|
gi 663856869 220 DWWSLGILLFELLT-GASPF 238
Cdd:cd05065  193 DVWSYGIVMWEVMSyGERPY 212
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
31-283 7.18e-05

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 45.38  E-value: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  31 ENFELLKVLGTGAYGKVF--LVRKAGGHDAGklyAMKVLRKAAlvqRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTD 108
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIkaMIKKDGLKMNA---AIKMLKEFA---SENDHRDFAGELEVLCKLGHHPNIINLLGACENR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 109 AKLHLILDYVSGGEMFTHLYQRQYFK----------------EAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSE 172
Cdd:cd05089   76 GYLYIAIEYAPYGNLLDFLRKSRVLEtdpafakehgtastltSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGEN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 173 GHIVLTDFGLSKEFLTEEKERTFSFcgTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASP-------------- 237
Cdd:cd05089  156 LVSKIADFGLSRGEEVYVKKTMGRL--PVRWMAIESLNYSVYTTKS-DVWSFGVLLWEIVSlGGTPycgmtcaelyeklp 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663856869 238 --FTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKK 283
Cdd:cd05089  233 qgYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARK 280
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
520-634 8.25e-05

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 45.39  E-value: 8.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPMQTPCF-TLQYAAPELLAQQGYDESCDLWSLGVILYMMLS- 597
Cdd:cd05090  146 VHKDLAARNILVGEQLH---VKISDLGLSREIYSSDYYRVQNKSLlPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSf 222
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 663856869 598 GQVPFQGASGQggqsqaaEIMCKIREGR------------FSLDGEAWQ 634
Cdd:cd05090  223 GLQPYYGFSNQ-------EVIEMVRKRQllpcsedcpprmYSLMTECWQ 264
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
487-604 1.11e-04

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 44.95  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 487 HIRKKRhfSESEASQILRSLVSAVSFMH--EEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRP----QSPGVPMQ 560
Cdd:cd05111   98 HVRQHR--GSLGPQLLLNWCVQIAKGMYylEEHRMVHRNLAARNVLLKSPS---QVQVADFGVADLLYpddkKYFYSEAK 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 663856869 561 TPcftLQYAAPELLAQQGYDESCDLWSLGVILYMMLS-GQVPFQG 604
Cdd:cd05111  173 TP---IKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAG 214
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
446-604 1.38e-04

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 44.72  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 446 EVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQILR------SLVSAVSFMHEEA-- 517
Cdd:cd05053   66 EMEMMKMIGKHKNIINLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRvpeeqlTQKDLVSFAYQVArg 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 518 -------GVVHRDLKPENILYADDTPgapVKIIDFGFAR-------LRPQSPG-VPmqtpcftLQYAAPELLAQQGYDES 582
Cdd:cd05053  146 meylaskKCIHRDLAARNVLVTEDNV---MKIADFGLARdihhidyYRKTTNGrLP-------VKWMAPEALFDRVYTHQ 215
                        170       180
                 ....*....|....*....|...
gi 663856869 583 CDLWSLGVILY-MMLSGQVPFQG 604
Cdd:cd05053  216 SDVWSFGVLLWeIFTLGGSPYPG 238
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
38-274 1.41e-04

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 44.26  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869  38 VLGTGAYGKVF--LVRKAGGHDAGKLYAMKvlrkaalvQRAKTQEHT--RTERSVLELVRQAPFLVTLHYAFQTDAKLHL 113
Cdd:cd05047    2 VIGEGNFGQVLkaRIKKDGLRMDAAIKRMK--------EYASKDDHRdfAGELEVLCKLGHHPNIINLLGACEHRGYLYL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 114 ILDYVSGGEMFTHLYQRQYFK----------------EAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVL 177
Cdd:cd05047   74 AIEYAPHGNLLDFLRKSRVLEtdpafaianstastlsSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 178 TDFGLSKEFLTEEKERTFSFcgTIEYMAPEIIRSKTGHGKAvDWWSLGILLFELLT-GASP----------------FTL 240
Cdd:cd05047  154 ADFGLSRGQEVYVKKTMGRL--PVRWMAIESLNYSVYTTNS-DVWSYGVLLWEIVSlGGTPycgmtcaelyeklpqgYRL 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 663856869 241 EGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQ 274
Cdd:cd05047  231 EKPLNCDDEVYDLMRQCWREKPYERPSFAQILVS 264
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
520-597 2.42e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 43.76  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDtpgAPVKIIDFGFARLRPQSPGV-----PMQTPCFtlqYAAPELLAQQGYDESCDLWSLGVILYM 594
Cdd:cd05079  131 VHRDLAARNVLVESE---HQVKIGDFGLTKAIETDKEYytvkdDLDSPVF---WYAPECLIQSKFYIASDVWSFGVTLYE 204

                 ...
gi 663856869 595 MLS 597
Cdd:cd05079  205 LLT 207
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
500-603 2.53e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 43.73  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 500 SQIL---RSLVSAVSFMHEEAgVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSPGVPM-----QTPCFtlqYAAP 571
Cdd:cd05080  107 AQLLlfaQQICEGMAYLHSQH-YIHRDLAARNVLLDNDRL---VKIGDFGLAKAVPEGHEYYRvredgDSPVF---WYAP 179
                         90       100       110
                 ....*....|....*....|....*....|..
gi 663856869 572 ELLAQQGYDESCDLWSLGVILYMMLSGQVPFQ 603
Cdd:cd05080  180 ECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
520-604 2.65e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 43.85  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 520 VHRDLKPENILYADDTPgapVKIIDFGFAR-------LRPQSPGvpmQTPcftLQYAAPELLAQQGYDESCDLWSLGVIL 592
Cdd:cd05101  168 IHRDLAARNVLVTENNV---MKIADFGLARdinnidyYKKTTNG---RLP---VKWMAPEALFDRVYTHQSDVWSFGVLM 238
                         90
                 ....*....|...
gi 663856869 593 YMMLS-GQVPFQG 604
Cdd:cd05101  239 WEIFTlGGSPYPG 251
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
504-597 1.19e-03

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 41.59  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 504 RSLVSAVSFMHEEAG--------VVHRDLKPENILYADDTPGApvkIIDFGFA-RLRPQSPGVPM----QTPcfTLQYAA 570
Cdd:cd14055  105 GSLARGLAHLHSDRTpcgrpkipIAHRDLKSSNILVKNDGTCV---LADFGLAlRLDPSLSVDELansgQVG--TARYMA 179
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663856869 571 PELLaqqgydES------------CDLWSLGVILYMMLS 597
Cdd:cd14055  180 PEAL------ESrvnledlesfkqIDVYSMALVLWEMAS 212
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
506-604 1.51e-03

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 41.25  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 506 LVSAVSFMhEEAGVVHRDLKPENILYADDTpgaPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDL 585
Cdd:cd05056  116 LSTALAYL-ESKRFVHRDIAARNVLVSSPD---CVKLGDFGLSRYMEDESYYKASKGKLPIKWMAPESINFRRFTSASDV 191
                         90       100
                 ....*....|....*....|
gi 663856869 586 WSLGVILYMMLS-GQVPFQG 604
Cdd:cd05056  192 WMFGVCMWEILMlGVKPFQG 211
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
505-595 1.76e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 40.92  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 505 SLVSAVSFMHEE-------AGVVHRDLKPENILYADDTPGApvkIIDFGFA-RLRPQSPGV--PMQTPCFTLQYAAPELL 574
Cdd:cd14144  100 SAACGLAHLHTEifgtqgkPAIAHRDIKSKNILVKKNGTCC---IADLGLAvKFISETNEVdlPPNTRVGTKRYMAPEVL 176
                         90       100
                 ....*....|....*....|....*..
gi 663856869 575 AQQGYDES------CDLWSLGVILYMM 595
Cdd:cd14144  177 DESLNRNHfdaykmADMYSFGLVLWEI 203
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
499-656 5.82e-03

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 39.56  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 499 ASQILRSLVSAVSfMHeeagVVHRDLKPENILYADDTPgapVKIIDFGFARLRPQSP-----GVPMqtpcFTLQYAAPEL 573
Cdd:cd05092  128 ASQIASGMVYLAS-LH----FVHRDLATRNCLVGQGLV---VKIGDFGMSRDIYSTDyyrvgGRTM----LPIRWMPPES 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663856869 574 LAQQGYDESCDLWSLGVILYMMLS-GQVPFQgasgQGGQSQAAEimCkIREGRfslDGEAWQGVSEEAKELVRGLLTVDP 652
Cdd:cd05092  196 ILYRKFTTESDIWSFGVVLWEIFTyGKQPWY----QLSNTEAIE--C-ITQGR---ELERPRTCPPEVYAIMQGCWQREP 265

                 ....
gi 663856869 653 AKRL 656
Cdd:cd05092  266 QQRH 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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