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Conserved domains on  [gi|7019333|ref|NP_037524|]
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nuclear receptor-binding protein isoform 1 [Homo sapiens]

Protein Classification

nuclear receptor-binding protein( domain architecture ID 10197139)

nuclear receptor-binding protein is a pseudokinase that functions as an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells, and with the small GTPase Rac3

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
60-334 0e+00

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 579.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   60 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI 139
Cdd:cd14034   3 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNFKLQEEKVKAVFDNLIQLEHLNIVKFHKYWADV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  140 KENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 219
Cdd:cd14034  83 KENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  220 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPL 299
Cdd:cd14034 163 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAINSAIQLLEDPL 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7019333  300 QREFIQKCLQSEPARRPTARELLFHPALFEVPSLK 334
Cdd:cd14034 243 QREFIQKCLEVDPSKRPTARELLFHQALFEVPSLK 277
 
Name Accession Description Interval E-value
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
60-334 0e+00

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 579.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   60 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI 139
Cdd:cd14034   3 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNFKLQEEKVKAVFDNLIQLEHLNIVKFHKYWADV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  140 KENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 219
Cdd:cd14034  83 KENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  220 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPL 299
Cdd:cd14034 163 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAINSAIQLLEDPL 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7019333  300 QREFIQKCLQSEPARRPTARELLFHPALFEVPSLK 334
Cdd:cd14034 243 QREFIQKCLEVDPSKRPTARELLFHQALFEVPSLK 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-325 1.53e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 111.08  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333      83 YLAMDTEEGVEVVWNEVQFSERKNYKlqeEKVRAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFL 162
Cdd:smart00220  16 YLARDKKTGKLVAIKVIKKKKIKKDR---ERILREIKILKKLKHPNIVRLYDVF----EDEDKLYLVMEYCEGGDLFDLL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     163 KKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSvapdtinnhvktCREEQKN 239
Cdd:smart00220  89 KK----RGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLadfGL------------ARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     240 ---------LHFFAPE------YGevtnvtTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAISSAIQLLEDPLQ---- 300
Cdd:smart00220 151 eklttfvgtPEYMAPEvllgkgYG------KAVDIWSLGVILYELLT------GKPPFPGDDQLLELFKKIGKPKPpfpp 218
                          250       260       270
                   ....*....|....*....|....*....|....
gi 7019333     301 ---------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:smart00220 219 pewdispeaKDLIRKLLVKDPEKRLTAEEALQHP 252
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
120-322 2.45e-20

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: 90.63  E-value: 2.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    120 NLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtKKNHKTMNEKAwkRWCTQILSALSYLHSCdpPII 199
Cdd:pfam07714  54 IMKKLDHPNIVKLL----GVCTQGEPLYIVTEYMPGGDLLDFLRK-HKRKLTLKDLL--SMALQIAKGMEYLESK--NFV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    200 HGNLTCDTIFIQHNGLIKIG--SVAPDTINNHVKTCREEQK-NLHFFAPE---YGEvtnVTTAVDIYSFGMCALEMAVLe 273
Cdd:pfam07714 125 HRDLAARNCLVSENLVVKISdfGLSRDIYDDDYYRKRGGGKlPIKWMAPEslkDGK---FTSKSDVWSFGVLLWEIFTL- 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    274 iqgnGESSYVPQEAiSSAIQLLED--PLQR---------EFIQKCLQSEPARRPTARELL 322
Cdd:pfam07714 201 ----GEQPYPGMSN-EEVLEFLEDgyRLPQpencpdelyDLMKQCWAYDPEDRPTFSELV 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
83-446 8.80e-19

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 8.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVV--------WNEVQFSERknykLQEEkVRAvfdnLIQLEHLNIVKFHkywaDIKENKARVIFITEYMS 154
Cdd:COG0515  24 YLARDLRLGRPVAlkvlrpelAADPEARER----FRRE-ARA----LARLNHPNIVRVY----DVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  155 SGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSV-----APDTI 226
Cdd:COG0515  91 GESLADLLRR----RGPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTPDGRVKLidfGIAralggATLTQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  227 NNHVK-TcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAISSAIQLLEDPLQ----- 300
Cdd:COG0515 165 TGTVVgT-------PGYMAPEQARGEPVDPRSDVYSLGVTLYELLT------GRPPFDGDSPAELLRAHLREPPPppsel 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  301 --------REFIQKCLQSEPARRP-TARELLFhpALFEVPSLKLLAAHCIVGHQHMIPENALEEITknmdTSAVLAEIPA 371
Cdd:COG0515 232 rpdlppalDAIVLRALAKDPEERYqSAAELAA--ALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAA----AAAAAAAAAA 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  372 GPGREPVQTLYSQSPALELDKFLEDVRNGIYPLTAFGLPRPQQPQQEEVTSPVVPPSVKTPTPEPAEVETRKVVL 446
Cdd:COG0515 306 AAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAA 380
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
125-325 1.58e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.00  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   125 EHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKqflkktkkNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLT 204
Cdd:PLN00034 130 NHPNVVKCH----DMFDHNGEIQVLLEFMDGGSLE--------GTHIADEQFLADVARQILSGIAYLHR--RHIVHRDIK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   205 CDTIFIQHNGLIKIGSVAPDTI-NNHVKTCREEQKNLHFFAPEygevtNVTT----------AVDIYSFGMCALEMAV-- 271
Cdd:PLN00034 196 PSNLLINSAKNVKIADFGVSRIlAQTMDPCNSSVGTIAYMSPE-----RINTdlnhgaydgyAGDIWSLGVSILEFYLgr 270
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333   272 ----LEIQGNGESSYV------PQEAISSAiqlleDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:PLN00034 271 fpfgVGRQGDWASLMCaicmsqPPEAPATA-----SREFRHFISCCLQREPAKRWSAMQLLQHP 329
 
Name Accession Description Interval E-value
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
60-334 0e+00

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 579.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   60 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI 139
Cdd:cd14034   3 PCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNFKLQEEKVKAVFDNLIQLEHLNIVKFHKYWADV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  140 KENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 219
Cdd:cd14034  83 KENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  220 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPL 299
Cdd:cd14034 163 SVAPDTINNHVKTCREEQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAINSAIQLLEDPL 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7019333  300 QREFIQKCLQSEPARRPTARELLFHPALFEVPSLK 334
Cdd:cd14034 243 QREFIQKCLEVDPSKRPTARELLFHQALFEVPSLK 277
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
73-328 0e+00

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 557.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   73 QRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEY 152
Cdd:cd13984   1 QRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKIFKAQEEKIRAVFDNLIQLDHPNIVKFHRYWTDVQEEKARVIFITEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  153 MSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKT 232
Cdd:cd13984  81 MSSGSLKQFLKKTKKNHKTMNEKSWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDAIHNHVKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  233 CREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPLQREFIQKCLQSEP 312
Cdd:cd13984 161 CREEHRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAALEIQSNGEKVSANEEAIIRAIFSLEDPLQKDFIRKCLSVAP 240
                       250
                ....*....|....*.
gi 7019333  313 ARRPTARELLFHPALF 328
Cdd:cd13984 241 QDRPSARDLLFHPVLF 256
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
73-328 5.75e-148

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 425.11  E-value: 5.75e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   73 QRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEY 152
Cdd:cd14035   1 QGNMPGIESTFLAMDTEEGVEVVWNELFFQDKKAFKAHEDKIKTMFENLTLVDHPNIVKFHKYWLDVKDNHARVVFITEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  153 MSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINN---- 228
Cdd:cd14035  81 VSSGSLKQFLKKTKKNHKTMNARAWKRWCTQILSALSYLHSCEPPIIHGNLTSDTIFIQHNGLIKIGSVWHRLFVNvlpe 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  229 -----HVKTCREEQKNLHFFAPEYGEVTNvTTAVDIYSFGMCALEMAVLEIQGNGESSyVPQEAISSAIQLLEDPLQREF 303
Cdd:cd14035 161 ggvrgPLRQEREELRNLHFFPPEYGSCED-GTAVDIFSFGMCALEMAVLEIQANGDTR-VSEEAIARARHSLEDPNMREF 238
                       250       260
                ....*....|....*....|....*
gi 7019333  304 IQKCLQSEPARRPTARELLFHPALF 328
Cdd:cd14035 239 ILSCLRHNPCKRPTAHDLLFHRVLF 263
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
83-325 1.20e-69

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: 224.03  E-value: 1.20e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFS-----ERKNYKlQEEKVravfdnLIQLEHLNIVKFHKYWADIKENkaRVIFITEYMSSGS 157
Cdd:cd13983  18 YRAFDTEEGIEVAWNEIKLRklpkaERQRFK-QEIEI------LKSLKHPNIIKFYDSWESKSKK--EVIFITELMTSGT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQ-HNGLIKIGSVAPDTINNH--VKTCr 234
Cdd:cd13983  89 LKQYLKR----FKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQsfAKSV- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 eeQKNLHFFAPE-YGEvtNVTTAVDIYSFGMCALEMAV-----LEIQGNGE-----SSYVPQEAISSaiqlLEDPLQREF 303
Cdd:cd13983 164 --IGTPEFMAPEmYEE--HYDEKVDIYAFGMCLLEMATgeypySECTNAAQiykkvTSGIKPESLSK----VKDPELKDF 235
                       250       260
                ....*....|....*....|..
gi 7019333  304 IQKCLQSePARRPTARELLFHP 325
Cdd:cd13983 236 IEKCLKP-PDERPSARELLEHP 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
81-325 3.96e-44

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: 155.51  E-value: 3.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKlqeEKVRAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQ 160
Cdd:cd00180   8 KVYKARDKETGKKVAVKVIPKEKLKKLL---EELLREIEILKKLNHPNIVKLYDVF----ETENFLYLVMEYCEGGSLKD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKtkkNHKTMNEKAWKRWCTQILSALSYLHSCdpPIIHGNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTCREEQ 237
Cdd:cd00180  81 LLKE---NKGPLSEEEALSILRQLLSALEYLHSN--GIIHRDLKPENILLDSDGTVKLadfGLAKDLDSDDSLLKTTGGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLeiqgngessyvpqeaissaiqlledplqREFIQKCLQSEPARRPT 317
Cdd:cd00180 156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYELEEL----------------------------KDLIRRMLQYDPKKRPS 207

                ....*...
gi 7019333  318 ARELLFHP 325
Cdd:cd00180 208 AKELLEHL 215
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
60-329 9.66e-40

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: 145.63  E-value: 9.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   60 PCGRWQKRREEVNQrnvPGIDSAYLAMDTEEGVEVVWNEVQfsERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI 139
Cdd:cd14031   7 PGGRFLKFDIELGR---GAFKTVYKGLDTETWVEVAWCELQ--DRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  140 KENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQH-NGLIKI 218
Cdd:cd14031  82 LKGKKCIVLVTELMTSGTLKTYLKR----FKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGpTGSVKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  219 GSVAPDTInNHVKTCREEQKNLHFFAPEYGEvTNVTTAVDIYSFGMCALEMAVLEIQ----GNGESSY--VPQEAISSAI 292
Cdd:cd14031 158 GDLGLATL-MRTSFAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPysecQNAAQIYrkVTSGIKPASF 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 7019333  293 QLLEDPLQREFIQKCLQSEPARRPTARELLFHPALFE 329
Cdd:cd14031 236 NKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
81-324 1.74e-37

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: 138.98  E-value: 1.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQfsERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQ 160
Cdd:cd14033  16 TVYRGLDTETTVEVAWCELQ--TRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRGHKCIILVTELMTSGTLKT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQH-NGLIKIGSVAPDTINNhVKTCREEQKN 239
Cdd:cd14033  94 YLKRFRE----MKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFITGpTGSVKIGDLGLATLKR-ASFAKSVIGT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  240 LHFFAPEYGEvTNVTTAVDIYSFGMCALEMAVLEIQ----GNGESSY--VPQEAISSAIQLLEDPLQREFIQKCLQSEPA 313
Cdd:cd14033 169 PEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPysecQNAAQIYrkVTSGIKPDSFYKVKVPELKEIIEGCIRTDKD 247
                       250
                ....*....|.
gi 7019333  314 RRPTARELLFH 324
Cdd:cd14033 248 ERFTIQDLLEH 258
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
81-329 4.19e-37

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: 138.29  E-value: 4.19e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQfsERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQ 160
Cdd:cd14032  16 TVYKGLDTETWVEVAWCELQ--DRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGKRCIVLVTELMTSGTLKT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQH-NGLIKIGSVAPDTInNHVKTCREEQKN 239
Cdd:cd14032  94 YLKR----FKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATL-KRASFAKSVIGT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  240 LHFFAPEYGEvTNVTTAVDIYSFGMCALEMAVLEIQ----GNGESSY--VPQEAISSAIQLLEDPLQREFIQKCLQSEPA 313
Cdd:cd14032 169 PEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPysecQNAAQIYrkVTCGIKPASFEKVTDPEIKEIIGECICKNKE 247
                       250
                ....*....|....*.
gi 7019333  314 RRPTARELLFHPALFE 329
Cdd:cd14032 248 ERYEIKDLLSHAFFAE 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
83-325 1.65e-34

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: 130.72  E-value: 1.65e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQ----EEKVravfdnLIQLEHLNIVKFhkYWADIKENKARvIFItEYMSSGSL 158
Cdd:cd06606  17 YLALNLDTGELMAVKEVELSGDSEEELEalerEIRI------LSSLKHPNIVRY--LGTERTENTLN-IFL-EYVPGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  159 KQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---------GSVAPDTINNH 229
Cdd:cd06606  87 ASLLKKFGK----LPEPVVRKYTRQILEGLEYLHSNG--IVHRDIKGANILVDSDGVVKLadfgcakrlAEIATGEGTKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  230 VK-TcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMA---------------VLEIQGNGESSYVPqEAISSAIq 293
Cdd:cd06606 161 LRgT-------PYWMAPEVIRGEGYGRAADIWSLGCTVIEMAtgkppwselgnpvaaLFKIGSSGEPPPIP-EHLSEEA- 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 7019333  294 lledplqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06606 232 -------KDFLRKCLQRDPKKRPTADELLQHP 256
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
60-329 1.22e-32

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: 126.32  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   60 PCGRWQKRREEVNQRNvpgIDSAYLAMDTEEGVEVVWNEVQfsERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI 139
Cdd:cd14030  22 PDGRFLKFDIEIGRGS---FKTVYKGLDTETTVEVAWCELQ--DRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEST 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  140 KENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQH-NGLIKI 218
Cdd:cd14030  97 VKGKKCIVLVTELMTSGTLKTYLKR----FKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGpTGSVKI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  219 GSVAPDTInNHVKTCREEQKNLHFFAPEYGEvTNVTTAVDIYSFGMCALEMAVLEIQ----GNGESSY--VPQEAISSAI 292
Cdd:cd14030 173 GDLGLATL-KRASFAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPysecQNAAQIYrrVTSGVKPASF 250
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 7019333  293 QLLEDPLQREFIQKCLQSEPARRPTARELLFHpALFE 329
Cdd:cd14030 251 DKVAIPEVKEIIEGCIRQNKDERYAIKDLLNH-AFFQ 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
83-325 1.53e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 111.08  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333      83 YLAMDTEEGVEVVWNEVQFSERKNYKlqeEKVRAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFL 162
Cdd:smart00220  16 YLARDKKTGKLVAIKVIKKKKIKKDR---ERILREIKILKKLKHPNIVRLYDVF----EDEDKLYLVMEYCEGGDLFDLL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     163 KKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSvapdtinnhvktCREEQKN 239
Cdd:smart00220  89 KK----RGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLadfGL------------ARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     240 ---------LHFFAPE------YGevtnvtTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAISSAIQLLEDPLQ---- 300
Cdd:smart00220 151 eklttfvgtPEYMAPEvllgkgYG------KAVDIWSLGVILYELLT------GKPPFPGDDQLLELFKKIGKPKPpfpp 218
                          250       260       270
                   ....*....|....*....|....*....|....
gi 7019333     301 ---------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:smart00220 219 pewdispeaKDLIRKLLVKDPEKRLTAEEALQHP 252
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
83-325 5.61e-26

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: 106.52  E-value: 5.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEV---VWNEVQFSERKNYkLQEEKVravfdnLIQLEHLNIVKFHKYWadIKENKarvIFIT-EYMSSGSL 158
Cdd:cd05122  17 YKARHKKTGQIVaikKINLESKEKKESI-LNEIAI------LKKCKHPNIVKYYGSY--LKKDE---LWIVmEFCSGGSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  159 KQFLKKTKKnhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQK 238
Cdd:cd05122  85 KDLLKNTNK---TLTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  239 NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYvPQEAISSAIQL--------LEDPLQ-----REFIQ 305
Cdd:cd05122 160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMA------EGKPPY-SELPPMKALFLiatngppgLRNPKKwskefKDFLK 232
                       250       260
                ....*....|....*....|
gi 7019333  306 KCLQSEPARRPTARELLFHP 325
Cdd:cd05122 233 KCLQKDPEKRPTAEQLLKHP 252
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
81-325 1.07e-23

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: 100.45  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFserknYKLQEEKVRAVFDNLIQLE---HLNIVKFHkywaDIKENKARVIFITEYMSSGS 157
Cdd:cd06626  15 KVYTAVNLDTGELMAMKEIRF-----QDNDPKTIKEIADEMKVLEgldHPNLVRYY----GVEVHREEVYIFMEYCQEGT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LKQFLKKTKknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI--NNHVKTCRE 235
Cdd:cd06626  86 LEELLRHGR----ILDEAVIRVYTLQLLEGLAYLHENG--IVHRDIKPANIFLDSNGLIKLGDFGSAVKlkNNTTTMAPG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  236 EQKNLH----FFAPEYgeVTNVTT-----AVDIYSFGMCALEMAV-------LEIQ-------GNGESSYVPQEaissai 292
Cdd:cd06626 160 EVNSLVgtpaYMAPEV--ITGNKGeghgrAADIWSLGCVVLEMATgkrpwseLDNEwaimyhvGMGHKPPIPDS------ 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 7019333  293 qLLEDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06626 232 -LQLSPEGKDFLSRCLESDPKKRPTASELLDHP 263
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
81-327 8.28e-23

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: 97.92  E-value: 8.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFS-----ERKNYkLQEEKVravfdnLIQLEHLNIVKFHKYWadikENKARVIFITEYMSS 155
Cdd:cd08215  15 SAYLVRRKSDGKLYVLKEIDLSnmsekEREEA-LNEVKL------LSKLKHPNIVKYYESF----EENGKLCIVMEYADG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  156 GSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG--SVApdtinnHVKTC 233
Cdd:cd08215  84 GDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRK--ILHRDLKTQNIFLTKDGVVKLGdfGIS------KVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  234 REEQKN-----LHFFAPE------YGEvtnvttAVDIYSFG-----MCALEMA---------VLEIQgNGESSYVPqEAI 288
Cdd:cd08215 156 TTDLAKtvvgtPYYLSPElcenkpYNY------KSDIWALGcvlyeLCTLKHPfeannlpalVYKIV-KGQYPPIP-SQY 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 7019333  289 SSAIQLLedplqrefIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd08215 228 SSELRDL--------VNSMLQKDPEKRPSANEILSSPFI 258
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
83-325 5.84e-22

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: 95.37  E-value: 5.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQEekVRAVFDNLIQLEHLNIVKFHKYwadiKENKARVIFITEYMSSGSLKQFL 162
Cdd:cd06627  17 YKGLNLNTGEFVAIKQISLEKIPKSDLKS--VMGEIDLLKKLNHPNIVKYIGS----VKTKDSLYIILEYVENGSLASII 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  163 KKtkknHKTMNEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGS--VApdtinnhVKTCREEQKNL 240
Cdd:cd06627  91 KK----FGKFPESLVAVYIYQVLEGLAYLH--EQGVIHRDIKGANILTTKDGLVKLADfgVA-------TKLNEVEKDEN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  241 ------HFFAPEYGEVTNVTTAVDIYSFGMCALEMavLEiqgnGESSYVPQEAISSAIQLLED----------PLQREFI 304
Cdd:cd06627 158 svvgtpYWMAPEVIEMSGVTTASDIWSVGCTVIEL--LT----GNPPYYDLQPMAALFRIVQDdhpplpenisPELRDFL 231
                       250       260
                ....*....|....*....|.
gi 7019333  305 QKCLQSEPARRPTARELLFHP 325
Cdd:cd06627 232 LQCFQKDPTLRPSAKELLKHP 252
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
106-325 1.27e-21

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: 94.35  E-value: 1.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  106 NYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKA--RVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQ 183
Cdd:cd14012  37 NGKKQIQLLEKELESLKKLRHPNLVSYLAFSIERRGRSDgwKVYLLTEYAPGGSLSELLDS----VGSVPLDTARRWTLQ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  184 ILSALSYLHSCDppIIHGNLTCDTIFI---QHNGLIKI----GSVAPDTINNHVKtcREEQKNLHFFAPEYGEVTN-VTT 255
Cdd:cd14012 113 LLEALEYLHRNG--VVHKSLHAGNVLLdrdAGTGIVKLtdysLGKTLLDMCSRGS--LDEFKQTYWLPPELAQGSKsPTR 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  256 AVDIYSFGMCALEMavleIQGN--GESSYVPQEAISSAiqLLEDPLQrEFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14012 189 KTDVWDLGLLFLQM----LFGLdvLEKYTSPNPVLVSL--DLSASLQ-DFLSKCLSLDPKKRPTALELLPHE 253
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
119-329 4.26e-21

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: 93.04  E-value: 4.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  119 DNLIQLEHLNIVKFhkYWADIKEnkARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHScDPPI 198
Cdd:cd06623  51 KTLRSCESPYVVKC--YGAFYKE--GEISIVLEYMDGGSLADLLKKVGK----IPEPVLAYIARQILKGLDYLHT-KRHI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIG-----SVAPDTI---NNHVKTCReeqknlhFFAPE------YGevtnvtTAVDIYSFGM 264
Cdd:cd06623 122 IHRDIKPSNLLINSKGEVKIAdfgisKVLENTLdqcNTFVGTVT-------YMSPEriqgesYS------YAADIWSLGL 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  265 CALEMAVleiqgnGESSYVPQEAIS-----SAIQLLEDPLQ---------REFIQKCLQSEPARRPTARELLFHPALFE 329
Cdd:cd06623 189 TLLECAL------GKFPFLPPGQPSffelmQAICDGPPPSLpaeefspefRDFISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
121-325 5.46e-21

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: 92.47  E-value: 5.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKfhkYWADIKENKARVIFItEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd06632  56 LSKLRHPNIVQ---YYGTEREEDNLYIFL-EYVPGGSIHKLLQR----YGAFEEPVIRLYTRQILSGLAYLHSRN--TVH 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTCReeqKNLHFFAPEY--GEVTNVTTAVDIYSFGMCALEMA----- 270
Cdd:cd06632 126 RDIKGANILVDTNGVVKLadfGMAKHVEAFSFAKSFK---GSPYWMAPEVimQKNSGYGLAVDIWSLGCTVLEMAtgkpp 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  271 ---------VLEIQGNGESSYVPqEAISsaiqlledPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06632 203 wsqyegvaaIFKIGNSGELPPIP-DHLS--------PDAKDFIRLCLQRDPEDRPTASQLLEHP 257
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
102-325 9.48e-21

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: 91.60  E-value: 9.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKnYKLQE----EKVRavfdnliqlEHLNIVKFHKYWadikENKARVIFITEyMSSGSLKQFLKKTkknHKTMNEKAW 177
Cdd:cd14050  42 KDRK-RKLEEverhEKLG---------EHPNCVRFIKAW----EEKGILYIQTE-LCDTSLQQYCEET---HSLPESEVW 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  178 KRWCtQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTnVTTAV 257
Cdd:cd14050 104 NILL-DLLKGLKHLHDHG--LIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEGDPRYMAPELLQGS-FTKAA 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  258 DIYSFGMCALEMAV-LEIQGNGES------SYVPQEAISSaiqlLEDPLqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14050 180 DIFSLGITILELACnLELPSGGDGwhqlrqGYLPEEFTAG----LSPEL-RSIIKLMMDPDPERRPTAEDLLALP 249
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
83-325 2.25e-20

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: 90.73  E-value: 2.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQF-SERKNYKLQEEKVravfdnLIQLEHLNIVKFHKYWADIKEnkarvIFI-TEYMSSGSLKQ 160
Cdd:cd06614  17 YKATDRATGKEVAIKKMRLrKQNKELIINEILI------MKECKHPNIVDYYDSYLVGDE-----LWVvMEYMDGGSLTD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKKnhkTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIG--------SVAPDTINNHVKT 232
Cdd:cd06614  86 IITQNPV---RMNESQIAYVCREVLQGLEYLHS--QNVIHRDIKSDNILLSKDGSVKLAdfgfaaqlTKEKSKRNSVVGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  233 CreeqknlHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYV---PQEAI----SSAIQLLEDP-----LQ 300
Cdd:cd06614 161 P-------YWMAPEVIKRKDYGPKVDIWSLGIMCIEMA------EGEPPYLeepPLRALflitTKGIPPLKNPekwspEF 227
                       250       260
                ....*....|....*....|....*
gi 7019333  301 REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06614 228 KDFLNKCLVKDPEKRPSAEELLQHP 252
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
120-322 2.45e-20

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: 90.63  E-value: 2.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    120 NLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtKKNHKTMNEKAwkRWCTQILSALSYLHSCdpPII 199
Cdd:pfam07714  54 IMKKLDHPNIVKLL----GVCTQGEPLYIVTEYMPGGDLLDFLRK-HKRKLTLKDLL--SMALQIAKGMEYLESK--NFV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    200 HGNLTCDTIFIQHNGLIKIG--SVAPDTINNHVKTCREEQK-NLHFFAPE---YGEvtnVTTAVDIYSFGMCALEMAVLe 273
Cdd:pfam07714 125 HRDLAARNCLVSENLVVKISdfGLSRDIYDDDYYRKRGGGKlPIKWMAPEslkDGK---FTSKSDVWSFGVLLWEIFTL- 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    274 iqgnGESSYVPQEAiSSAIQLLED--PLQR---------EFIQKCLQSEPARRPTARELL 322
Cdd:pfam07714 201 ----GEQPYPGMSN-EEVLEFLEDgyRLPQpencpdelyDLMKQCWAYDPEDRPTFSELV 255
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
121-322 2.69e-20

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: 90.29  E-value: 2.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFhkYWADIKENKaRVIfITEYMSSGSLKQFLKKTKKNhktMNEKAWKRWCTQILSALSYLHScdPPIIH 200
Cdd:cd13999  44 LSKLRHPNIVQF--IGACLSPPP-LCI-VTEYMPGGSLYDLLHKKKIP---LSWSLRLKIALDIARGMNYLHS--PPIIH 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKI---GsvapdtinnhvkTCREEQK----------NLHFFAPEYGEVTNVTTAVDIYSFGMCAL 267
Cdd:cd13999 115 RDLKSLNILLDENFTVKIadfG------------LSRIKNSttekmtgvvgTPRWMAPEVLRGEPYTEKADVYSFGIVLW 182
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  268 EMAVLEIQGNGESSyvPQEAISSAIQLLEDPLQ-------REFIQKCLQSEPARRPTARELL 322
Cdd:cd13999 183 ELLTGEVPFKELSP--IQIAAAVVQKGLRPPIPpdcppelSKLIKRCWNEDPEKRPSFSEIV 242
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
121-322 3.14e-20

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: 90.79  E-value: 3.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYWADIKENkarvIFITEYMSSGSLKQFLKKtkknHKTMNEKAWK---RWCTQILSALSYLH-SCDP 196
Cdd:cd14066  44 LGRLRHPNLVRLLGYCLESDEK----LLVYEYMPNGSLEDRLHC----HKGSPPLPWPqrlKIAKGIARGLEYLHeECPP 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  197 PIIHGNLTCDTIFIQHN--------GLIKIGSVAPDT-INNHVKTcreeqkNLHFFAPEYGEVTNVTTAVDIYSFGMCAL 267
Cdd:cd14066 116 PIIHGDIKSSNILLDEDfepkltdfGLARLIPPSESVsKTSAVKG------TIGYLAPEYIRTGRVSTKSDVYSFGVVLL 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333  268 EM---------AVLEIQGNGESSYVPQEAISSAIQLLEDPLQREFIQK-------------CLQSEPARRPTARELL 322
Cdd:cd14066 190 ELltgkpavdeNRENASRKDLVEWVESKGKEELEDILDKRLVDDDGVEeeeveallrlallCTRSDPSLRPSMKEVV 266
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
83-325 6.87e-20

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: 89.75  E-value: 6.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERK---NYKLQEEKVRAV---FDNLIQLEHLNIVKFHKYwadikENKARVIFI-TEYMSS 155
Cdd:cd06629  18 YLAMNATTGEMLAVKQVELPKTSsdrADSRQKTVVDALkseIDTLKDLDHPNIVQYLGF-----EETEDYFSIfLEYVPG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  156 GSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSV-----APDTINNHV 230
Cdd:cd06629  93 GSIGSCLRK----YGKFEEDLVRFFTRQILDGLAYLHSKG--ILHRDLKADNILVDLEGICKISDFgiskkSDDIYGNNG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  231 KTCReeQKNLHFFAPE----YGEvtNVTTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAI---------SSAIQLLED 297
Cdd:cd06629 167 ATSM--QGSVFWMAPEvihsQGQ--GYSAKVDIWSLGCVVLEMLA------GRRPWSDDEAIaamfklgnkRSAPPVPED 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 7019333  298 ----PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06629 237 vnlsPEALDFLNACFAIDPRDRPTAAELLSHP 268
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
121-322 8.17e-19

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: 86.44  E-value: 8.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFhkYWADIKENKARVIFitEYMSSGSLKQFLKKTKKNHKTMNEKA--WK---RWCTQILSALSYLHSCd 195
Cdd:cd00192  50 MKKLGHPNVVRL--LGVCTEEEPLYLVM--EYMEGGDLLDFLRKSRPVFPSPEPSTlsLKdllSFAIQIAKGMEYLASK- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  196 pPIIHGNLTCDTIFIQHNGLIKIGsvapD-----TINNHVKTCREEQKNLHF--FAPEYGEvTNV-TTAVDIYSFGMCAL 267
Cdd:cd00192 125 -KFVHRDLAARNCLVGEDLVVKIS----DfglsrDIYDDDYYRKKTGGKLPIrwMAPESLK-DGIfTSKSDVWSFGVLLW 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  268 EMAVLeiqgnGESSY--VPQEAISSAIQ---LLEDPLQ-----REFIQKCLQSEPARRPTARELL 322
Cdd:cd00192 199 EIFTL-----GATPYpgLSNEEVLEYLRkgyRLPKPENcpdelYELMLSCWQLDPEDRPTFSELV 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
83-446 8.80e-19

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 8.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVV--------WNEVQFSERknykLQEEkVRAvfdnLIQLEHLNIVKFHkywaDIKENKARVIFITEYMS 154
Cdd:COG0515  24 YLARDLRLGRPVAlkvlrpelAADPEARER----FRRE-ARA----LARLNHPNIVRVY----DVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  155 SGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSV-----APDTI 226
Cdd:COG0515  91 GESLADLLRR----RGPLPPAEALRILAQLAEALAAAHAAG--IVHRDIKPANILLTPDGRVKLidfGIAralggATLTQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  227 NNHVK-TcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAISSAIQLLEDPLQ----- 300
Cdd:COG0515 165 TGTVVgT-------PGYMAPEQARGEPVDPRSDVYSLGVTLYELLT------GRPPFDGDSPAELLRAHLREPPPppsel 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  301 --------REFIQKCLQSEPARRP-TARELLFhpALFEVPSLKLLAAHCIVGHQHMIPENALEEITknmdTSAVLAEIPA 371
Cdd:COG0515 232 rpdlppalDAIVLRALAKDPEERYqSAAELAA--ALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAA----AAAAAAAAAA 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  372 GPGREPVQTLYSQSPALELDKFLEDVRNGIYPLTAFGLPRPQQPQQEEVTSPVVPPSVKTPTPEPAEVETRKVVL 446
Cdd:COG0515 306 AAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAA 380
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
83-325 1.74e-18

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: 84.88  E-value: 1.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVwneVQFSER-KNYKLQEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQF 161
Cdd:cd14003  17 KLARHKLTGEKVA---IKIIDKsKLKEEIEEKIKREIEIMKLLNHPNIIKLY----EVIETENKIYLVMEYASGGELFDY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LkktkKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG----SvapdtinnhvKTCREEQ 237
Cdd:cd14003  90 I----VNNGRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILLDKNGNLKIIdfglS----------NEFRGGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 K------NLHFFAPE-------YGEvtnvttAVDIYSFGMC--AL-----------EMAVLEIQGNGE---SSYVPQEAi 288
Cdd:cd14003 154 LlktfcgTPAYAAPEvllgrkyDGP------KADVWSLGVIlyAMltgylpfdddnDSKLFRKILKGKypiPSHLSPDA- 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 7019333  289 ssaiqlledplqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14003 227 ------------RDLIRRMLVVDPSKRITIEEILNHP 251
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
83-322 3.29e-18

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: 84.56  E-value: 3.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVV--------WNEVQFSERknykLQEEkVRAvfdnLIQLEHLNIVKFHkywaDIKENKARVIFITEYMS 154
Cdd:cd14014  17 YRARDTLLGRPVAikvlrpelAEDEEFRER----FLRE-ARA----LARLSHPNIVRVY----DVGEDDGRPYIVMEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  155 SGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---------GSVAPDT 225
Cdd:cd14014  84 GGSLADLLRE----RGPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANILLTEDGRVKLtdfgiaralGDSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  226 INNHVKTcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSY-----VPQEAISSAIQLLED--- 297
Cdd:cd14014 158 TGSVLGT-------PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAavlakHLQEAPPPPSPLNPDvpp 230
                       250       260
                ....*....|....*....|....*.
gi 7019333  298 PLqREFIQKCLQSEPARRP-TARELL 322
Cdd:cd14014 231 AL-DAIILRALAKDPEERPqSAAELL 255
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
101-325 5.80e-18

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: 83.59  E-value: 5.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  101 FSERKNYkLQEEKVRAVFDnliqlEHLNIVKFHKYWAdikENKarVIFI-TEYMSSGSLKQFLKKTKKNHKTMNEKAWKR 179
Cdd:cd13997  40 PKERARA-LREVEAHAALG-----QHPNIVRYYSSWE---EGG--HLYIqMELCENGSLQDALEELSPISKLSEAEVWDL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  180 WCtQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG--------SVAPDtinnhvktcrEEQKNLHFFAPEY-GEV 250
Cdd:cd13997 109 LL-QVALGLAFIHSKG--IVHLDIKPDNIFISNKGTCKIGdfglatrlETSGD----------VEEGDSRYLAPELlNEN 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  251 TNVTTAVDIYSFGMCALEMAV-LEIQGNGESSYVPQEAIssAIQLLEDPLQREF---IQKCLQSEPARRPTARELLFHP 325
Cdd:cd13997 176 YTHLPKADIFSLGVTVYEAATgEPLPRNGQQWQQLRQGK--LPLPPGLVLSQELtrlLKVMLDPDPTRRPTADQLLAHD 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
83-325 8.31e-18

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: 83.37  E-value: 8.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEV---VWNEVQFSERKNYKLQEEKVRAVFDNLIQ-------LEHLNIVKFHKYWADIKENKarvIF-ITE 151
Cdd:cd14008  10 KLALDTETGQLYaikIFNKSRLRKRREGKNDRGKIKNALDDVRReiaimkkLDHPNIVRLYEVIDDPESDK---LYlVLE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  152 YMSSGSLKQFLKKTKKnhKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG--SVA------P 223
Cdd:cd14008  87 YCEGGPVMELDSGDRV--PPLPEETARKYFRDLVLGLEYLHENG--IVHRDIKPENLLLTADGTVKISdfGVSemfedgN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  224 DTINNHVKTcreeqknLHFFAPE--YGEVTNVTT-AVDIYSFGMCALEMAVLEIQGNGESSYvpqeAISSAIQLLEDPLQ 300
Cdd:cd14008 163 DTLQKTAGT-------PAFLAPElcDGDSKTYSGkAADIWALGVTLYCLVFGRLPFNGDNIL----ELYEAIQNQNDEFP 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 7019333  301 ---------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14008 232 ippelspelKDLLRRMLEKDPEKRITLKEIKEHP 265
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
104-325 2.39e-17

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: 81.75  E-value: 2.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  104 RKNYKLQEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQ 183
Cdd:cd05117  36 KKLKSEDEEMLRREIEILKRLDHPNIVKLY----EVFEDDKNLYLVMELCTGGELFDRIVK----KGSFSEREAAKIMKQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  184 ILSALSYLHSCDppIIH-----GNLTCDTifIQHNGLIKIG----SVAPDTINNHVKTCreeqKNLHFFAPE------YG 248
Cdd:cd05117 108 ILSAVAYLHSQG--IVHrdlkpENILLAS--KDPDSPIKIIdfglAKIFEEGEKLKTVC----GTPYYVAPEvlkgkgYG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  249 EvtnvttAVDIYSFGMCaleMAVLeIQG----NGESSYVPQEAISSAIQLLEDP-------LQREFIQKCLQSEPARRPT 317
Cdd:cd05117 180 K------KCDIWSLGVI---LYIL-LCGyppfYGETEQELFEKILKGKYSFDSPewknvseEAKDLIKRLLVVDPKKRLT 249

                ....*...
gi 7019333  318 ARELLFHP 325
Cdd:cd05117 250 AAEALNHP 257
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
126-325 3.23e-17

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: 82.09  E-value: 3.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKfhkYWADIKENKARVIFIT-EYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLT 204
Cdd:cd06621  58 SPYIVK---YYGAFLDEQDSSIGIAmEYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHS--RKIIHRDIK 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  205 CDTIFIQHNGLIKIGS--VAPDTINNHVKTCREEQknlHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE--IQGNGES 280
Cdd:cd06621 133 PSNILLTRKGQVKLCDfgVSGELVNSLAGTFTGTS---YYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRfpFPPEGEP 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  281 SYVPQEAIS-----SAIQLLEDPLQ--------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06621 210 PLGPIELLSyivnmPNPELKDEPENgikwsesfKDFIEKCLEKDGTRRPGPWQMLAHP 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
123-322 7.19e-17

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: 80.29  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     123 QLEHLNIVKFHkywADIKENKARVIfITEYMSSGSLKQFLKKTKKNHKTMNEKawKRWCTQILSALSYLHSCdpPIIHGN 202
Cdd:smart00221  57 KLDHPNIVKLL---GVCTEEEPLMI-VMEYMPGGDLLDYLRKNRPKELSLSDL--LSFALQIARGMEYLESK--NFIHRD 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     203 LTCDTIFIQHNGLIKIG--SVAPDTINNHVKTCREEQKNLHFFAPE---YGEvtnVTTAVDIYSFGMCALEMAVLeiqgn 277
Cdd:smart00221 129 LAARNCLVGENLVVKISdfGLSRDLYDDDYYKVKGGKLPIRWMAPEslkEGK---FTSKSDVWSFGVLLWEIFTL----- 200
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333     278 GESSYvPQEAISSAIQLLEDPLQRE-----------FIQKCLQSEPARRPTARELL 322
Cdd:smart00221 201 GEEPY-PGMSNAEVLEYLKKGYRLPkppncppelykLMLQCWAEDPEDRPTFSELV 255
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
124-322 9.44e-17

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: 80.41  E-value: 9.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFHKYWadIKENkarVIFI-TEYMSSGSLKQFLKKtKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGN 202
Cdd:cd13996  61 LNHPNIVRYYTAW--VEEP---PLYIqMELCEGGTLRDWIDR-RNSSSKNDRKLALELFKQILKGVSYIHSKG--IVHRD 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHN-GLIKIG--SVAPDTINNHVKTCREEQKN-------------LHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd13996 133 LKPSNIFLDNDdLQVKIGdfGLATSIGNQKRELNNLNNNNngntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIIL 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  267 LEMaVLEIQGNGESSYVPQEA---ISSAIQLLEDPLQREFIQKCLQSEPARRPTARELL 322
Cdd:cd13996 213 FEM-LHPFKTAMERSTILTDLrngILPESFKAKHPKEADLIQSLLSKNPEERPSAEQLL 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
109-325 1.30e-16

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: 79.91  E-value: 1.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVRAVFDNLIQ----LEHLNIVKFHKYWADiKENkarVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQI 184
Cdd:cd14099  39 LTKPKQREKLKSEIKihrsLKHPNIVKFHDCFED-EEN---VYILLELCSNGSLMELLKR----RKALTEPEVRYFMRQI 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  185 LSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHvktcREEQK-------NlhFFAPE--YGEVTNvTT 255
Cdd:cd14099 111 LSGVKYLHSNR--IIHRDLKLGNLFLDENMNVKIGDFGLAARLEY----DGERKktlcgtpN--YIAPEvlEKKKGH-SF 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  256 AVDIYSFGMCALEMAV---------LE-----IQGNgesSY-VPQEAISSaiqlledPLQREFIQKCLQSEPARRPTARE 320
Cdd:cd14099 182 EVDIWSLGVILYTLLVgkppfetsdVKetykrIKKN---EYsFPSHLSIS-------DEAKDLIRSMLQPDPTKRPSLDE 251

                ....*
gi 7019333  321 LLFHP 325
Cdd:cd14099 252 ILSHP 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
128-325 1.34e-16

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: 79.70  E-value: 1.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  128 NIVKFhkYWADIKENkaRVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDT 207
Cdd:cd06605  60 YIVGF--YGAFYSEG--DISICMEYMDGGSLDKILKEVG----RIPERILGKIAVAVVKGLIYLHE-KHKIIHRDVKPSN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  208 IFIQHNGLIKIGS--VAPDTINNHVKT---CReeqknlHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVleiqgnGESSY 282
Cdd:cd06605 131 ILVNSRGQVKLCDfgVSGQLVDSLAKTfvgTR------SYMAPERISGGKYTVKSDIWSLGLSLVELAT------GRFPY 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  283 VP--QEAISSAIQLL-----EDPLQ----------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06605 199 PPpnAKPSMMIFELLsyivdEPPPLlpsgkfspdfQDFVSQCLQKDPTERPSYKELMEHP 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
81-327 1.95e-16

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: 79.50  E-value: 1.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEG-------VEVVWNEVQFSERKNYKLqeEKVRAVFDNLIQLEHLNIVKFhkywADIKENKARVIFITEYM 153
Cdd:cd06628  15 SVYLGMNASSGelmavkqVELPSVSAENKDRKKSML--DALQREIALLRELQHENIVQY----LGSSSDANHLNIFLEYV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  154 SSGSLKQFLKktkkNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG------SVAPDTIN 227
Cdd:cd06628  89 PGGSVATLLN----NYGAFEESLVRNFVRQILKGLNYLHNRG--IIHRDIKGANILVDNKGGIKISdfgiskKLEANSLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 NHVKTCREE-QKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM--------------AVLEIQGNGeSSYVPQEAISSAi 292
Cdd:cd06628 163 TKNNGARPSlQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMltgthpfpdctqmqAIFKIGENA-SPTIPSNISSEA- 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7019333  293 qlledplqREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06628 241 --------RDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
92-325 3.29e-16

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: 78.63  E-value: 3.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   92 VEVVWNEVQFSERKNYKLQEEkvravFDNLIQLEHLNIVKfhkYWADIKENKARVIFItEYMSSGSLKQFLKKtkknHKT 171
Cdd:cd06631  33 VELDTSDKEKAEKEYEKLQEE-----VDLLKTLKHVNIVG---YLGTCLEDNVVSIFM-EFVPGGSIASILAR----FGA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  172 MNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTCREEQKNLH----FFA 244
Cdd:cd06631 100 LEEPVFCRYTKQILEGVAYLHNNN--VIHRDIKGNNIMLMPNGVIKLidfGCAKRLCINLSSGSQSQLLKSMRgtpyWMA 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  245 PEYGEVTNVTTAVDIYSFGMCALEMAVleiqGNGESSYVPQEAISSAI--------QLLED--PLQREFIQKCLQSEPAR 314
Cdd:cd06631 178 PEVINETGHGRKSDIWSIGCTVFEMAT----GKPPWADMNPMAAIFAIgsgrkpvpRLPDKfsPEARDFVHACLTRDQDE 253
                       250
                ....*....|.
gi 7019333  315 RPTARELLFHP 325
Cdd:cd06631 254 RPSAEQLLKHP 264
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
83-325 4.75e-16

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: 78.17  E-value: 4.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFsERKNYKLQEEkVRAvFDNLIQL----EHLNIVKfhkYWADIKENKARVIFItEYMSSGSL 158
Cdd:cd06625  17 YLCYDADTGRELAVKQVEI-DPINTEASKE-VKA-LECEIQLlknlQHERIVQ---YYGCLQDEKSLSIFM-EYMPGGSV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  159 KQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG----SVAPDTINNHvKTCR 234
Cdd:cd06625  90 KDEIKA----YGALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANILRDSNGNVKLGdfgaSKRLQTICSS-TGMK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 EEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM--------------AVLEIQGNGESSYVPQEAissaiqlleDPLQ 300
Cdd:cd06625 163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMlttkppwaefepmaAIFKIATQPTNPQLPPHV---------SEDA 233
                       250       260
                ....*....|....*....|....*
gi 7019333  301 REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06625 234 RDFLSLIFVRNKKQRPSAEELLSHS 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
123-322 5.05e-16

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 77.96  E-value: 5.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     123 QLEHLNIVKFHkywADIKENKARVIfITEYMSSGSLKQFLKKTKKN--HKTMnekawKRWCTQILSALSYLHSCdpPIIH 200
Cdd:smart00219  57 KLDHPNVVKLL---GVCTEEEPLYI-VMEYMEGGDLLSYLRKNRPKlsLSDL-----LSFALQIARGMEYLESK--NFIH 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     201 GNLTCDTIFIQHNGLIKIG------SVAPDTINnhvktcREEQKNL--HFFAPE---YGEvtnVTTAVDIYSFGMCALEM 269
Cdd:smart00219 126 RDLAARNCLVGENLVVKISdfglsrDLYDDDYY------RKRGGKLpiRWMAPEslkEGK---FTSKSDVWSFGVLLWEI 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333     270 AVLeiqgnGESSYvPQEAISSAIQLLED------PLQ-----REFIQKCLQSEPARRPTARELL 322
Cdd:smart00219 197 FTL-----GEQPY-PGMSNEEVLEYLKNgyrlpqPPNcppelYDLMLQCWAEDPEDRPTFSELV 254
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
125-329 1.20e-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: 77.72  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  125 EHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALSYLHScdPPIIHGNLT 204
Cdd:cd06659  76 QHPNVVEMYKSYLVGEE----LWVLMEYLQGGALTDIVSQTR-----LNEEQIATVCEAVLQALAYLHS--QGVIHRDIK 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  205 CDTIFIQHNGLIKI---GSVApdTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESS 281
Cdd:cd06659 145 SDSILLTLDGRVKLsdfGFCA--QISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMV------DGEPP 216
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  282 YVPQEAISsAIQLLED-------------PLQREFIQKCLQSEPARRPTARELLFHPALFE 329
Cdd:cd06659 217 YFSDSPVQ-AMKRLRDspppklknshkasPVLRDFLERMLVRDPQERATAQELLDHPFLLQ 276
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
112-325 1.23e-15

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: 77.01  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  112 EKVRAVFDNLI-------QLEHLNIVKfhkYWADIKENkaRVIFIT-EYMSSGSLKQFLKkTKKNHKTMNEKAWKRWCTQ 183
Cdd:cd06610  37 EKCQTSMDELRkeiqamsQCNHPNVVS---YYTSFVVG--DELWLVmPLLSGGSLLDIMK-SSYPRGGLDEAIIATVLKE 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  184 ILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIG------SVAPDTINNH------VKT-CreeqknlhFFAPE-YGE 249
Cdd:cd06610 111 VLKGLEYLH--SNGQIHRDVKAGNILLGEDGSVKIAdfgvsaSLATGGDRTRkvrktfVGTpC--------WMAPEvMEQ 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  250 VTNVTTAVDIYSFGMCALEMAvleiqgNGE---SSYVPQEAISSAIQllEDPLQ--------------REFIQKCLQSEP 312
Cdd:cd06610 181 VRGYDFKADIWSFGITAIELA------TGAapySKYPPMKVLMLTLQ--NDPPSletgadykkysksfRKMISLCLQKDP 252
                       250
                ....*....|...
gi 7019333  313 ARRPTARELLFHP 325
Cdd:cd06610 253 SKRPTAEELLKHK 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
102-327 1.49e-15

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: 76.66  E-value: 1.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNYKLQEEKVRAVFDN-----------LIQLEHLNIVKFHKYWADIKenkaRVIFITEYMSSGSLKQFLKKTKKNHK 170
Cdd:cd08530  23 SDNQVYALKEVNLGSLSQKeredsvneirlLASVNHPNIIRYKEAFLDGN----RLCIVMEYAPFGDLSKLISKRKKKRR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  171 TMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI--NNHVKTcreEQKNLHFFAPEYG 248
Cdd:cd08530  99 LFPEDDIWRIFIQMLRGLKALHDQK--ILHRDLKSANILLSAGDLVKIGDLGISKVlkKNLAKT---QIGTPLYAAPEVW 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  249 EVTNVTTAVDIYSFGMCALEMAVLEIQGNGES-----------SYVPQEAISSAiqlledPLQrEFIQKCLQSEPARRPT 317
Cdd:cd08530 174 KGRPYDYKSDIWSLGCLLYEMATFRPPFEARTmqelrykvcrgKFPPIPPVYSQ------DLQ-QIIRSLLQVNPKKRPS 246
                       250
                ....*....|
gi 7019333  318 ARELLFHPAL 327
Cdd:cd08530 247 CDKLLQSPAV 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
111-325 1.61e-15

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: 76.15  E-value: 1.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKktkkNHKTMNEKAWKRWCTQILSALSY 190
Cdd:cd14006  33 KEAVLREISILNQLQHPRIIQLH----EAYESPTELVLILELCSGGELLDRLA----ERGSLSEEEVRTYMRQLLEGLQY 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  191 LHSCDppIIHGNLTCDTIFIQHNGLIKIGSVapDTINNHVKTCREEQK----NLHFFAPEYGEVTNVTTAVDIYSFGMca 266
Cdd:cd14006 105 LHNHH--ILHLDLKPENILLADRPSPQIKII--DFGLARKLNPGEELKeifgTPEFVAPEIVNGEPVSLATDMWSIGV-- 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  267 leMAVLEIQG----NGESSYVPQEAISSAIQLLEDP-------LQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14006 179 --LTYVLLSGlspfLGEDDQETLANISACRVDFSEEyfssvsqEAKDFIRKLLVKEPRKRPTAQEALQHP 246
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
81-326 2.93e-15

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: 75.93  E-value: 2.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSeRKNYKLQEEKVRAVFDNLI---QLEHLNIVKFhkyWADIKENKARVIFItEYMSSGS 157
Cdd:cd06630  15 SCYQARDVKTGTLMAVKQVSFC-RNSSSEQEEVVEAIREEIRmmaRLNHPNIVRM---LGATQHKSHFNIFV-EWMAGGS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNG-LIKIGSV-APDTINNHVKTCRE 235
Cdd:cd06630  90 VASLLSK----YGAFSENVIINYTLQILRGLAYLH--DNQIIHRDLKGANLLVDSTGqRLRIADFgAAARLASKGTGAGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  236 EQKNL----HFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGEssyvpqeAISSAIQLLE--------------- 296
Cdd:cd06630 164 FQGQLlgtiAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAE-------KISNHLALIFkiasattpppipehl 236
                       250       260       270
                ....*....|....*....|....*....|
gi 7019333  297 DPLQREFIQKCLQSEPARRPTARELLFHPA 326
Cdd:cd06630 237 SPGLRDVTLRCLELQPEDRPPARELLKHPV 266
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
83-322 1.02e-14

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: 74.23  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKfhkYWADIKENKARVIfITEYMSSGSLKQFL 162
Cdd:cd08224  17 YRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEI-DLLQQLNHPNIIK---YLASFIENNELNI-VLELADAGDLSRLI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  163 KKTKKNHKTMNEKA-WKrWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSV------APDTINNH--VKTC 233
Cdd:cd08224  92 KHFKKQKRLIPERTiWK-YFVQLCSALEHMHSKR--IMHRDIKPANVFITANGVVKLGDLglgrffSSKTTAAHslVGTP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  234 reeqknlHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE--IQGNGESSYVPQEAISSA------IQLLEDPLqREFIQ 305
Cdd:cd08224 169 -------YYMSPERIREQGYDFKSDIWSLGCLLYEMAALQspFYGEKMNLYSLCKKIEKCeypplpADLYSQEL-RDLVA 240
                       250
                ....*....|....*..
gi 7019333  306 KCLQSEPARRPTARELL 322
Cdd:cd08224 241 ACIQPDPEKRPDISYVL 257
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
83-325 1.29e-14

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: 74.11  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQF---SERKNYKLQEEkVRAvfdnLIQLEHLNIVKfhkYWADIKENKARVIFI-TEYMSSGSL 158
Cdd:cd08217  17 RKVRRKSDGKILVWKEIDYgkmSEKEKQQLVSE-VNI----LRELKHPNIVR---YYDRIVDRANTTLYIvMEYCEGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  159 KQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHS---CDPPIIHGNLTCDTIFIQHNGLIKIG--------SVAPDTIN 227
Cdd:cd08217  89 AQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNrsvGGGKILHRDLKPANIFLDSDNNVKLGdfglarvlSHDSSFAK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 NHVKTCreeqknlHFFAPE------YGEVTnvttavDIYSFG-----MCALE-------MAVL--EIQgNGESSYVPQEa 287
Cdd:cd08217 169 TYVGTP-------YYMSPEllneqsYDEKS------DIWSLGcliyeLCALHppfqaanQLELakKIK-EGKFPRIPSR- 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 7019333  288 ISSAIQLLedplqrefIQKCLQSEPARRPTARELLFHP 325
Cdd:cd08217 234 YSSELNEV--------IKSMLNVDPDKRPSVEELLQLP 263
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
149-325 2.83e-14

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: 73.05  E-value: 2.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGS--VAPDTI 226
Cdd:cd06609  77 IMEYCGGGSVLDLLKPGP-----LDETYIAFILREVLLGLEYLHS--EGKIHRDIKAANILLSEEGDVKLADfgVSGQLT 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  227 NNhvktcreeQKNLHFF-------APEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGE---SSYVPQEAIS----SAI 292
Cdd:cd06609 150 ST--------MSKRNTFvgtpfwmAPEVIKQSGYDEKADIWSLGITAIELA------KGEpplSDLHPMRVLFlipkNNP 215
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7019333  293 QLLED----PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06609 216 PSLEGnkfsKPFKDFVELCLNKDPKERPSAKELLKHK 252
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
123-327 4.52e-14

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: 72.48  E-value: 4.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALSYLHScdPPIIHGN 202
Cdd:cd06648  60 DYQHPNIVEMYSSYLVGDE----LWVVMEFLEGGALTDIVTHTR-----MNEEQIATVCRAVLKALSFLHS--QGVIHRD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHNGLIKI------GSVAPDTinnhvktcrEEQKNL----HFFAPE------YGevtnvtTAVDIYSFGMCA 266
Cdd:cd06648 129 IKSDSILLTSDGRVKLsdfgfcAQVSKEV---------PRRKSLvgtpYWMAPEvisrlpYG------TEVDIWSLGIMV 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  267 LEMAvleiqgNGESSYVPQEAIsSAIQLLED-------------PLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06648 194 IEMV------DGEPPYFNEPPL-QAMKRIRDneppklknlhkvsPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
105-324 7.30e-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: 71.75  E-value: 7.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  105 KNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKE-----------NKARVIFI-TEYMSSGSLKQFLKKTK--KNHK 170
Cdd:cd14047  37 KRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFDYdpetsssnssrSKTKCLFIqMEFCEKGTLESWIEKRNgeKLDK 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  171 TMNEKAWKrwctQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTinnHVKTCREEQKN---LHFFAPEY 247
Cdd:cd14047 117 VLALEIFE----QITKGVEYIHSKK--LIHRDLKPSNIFLVDTGKVKIGDFGLVT---SLKNDGKRTKSkgtLSYMSPEQ 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  248 GEVTNVTTAVDIYSFGMCALEMAVLEIQGNgESSYVPQEAISSAIQLLED---PLQREFIQKCLQSEPARRPTARELLFH 324
Cdd:cd14047 188 ISSQDYGKEVDIYALGLILFELLHVCDSAF-EKSKFWTDLRNGILPDIFDkryKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
121-325 7.34e-14

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: 71.69  E-value: 7.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYWADiKENkarVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHscDPPIIH 200
Cdd:cd08222  56 LSKLDHPAIVKFHDSFVE-KES---FCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMH--ERRILH 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQhNGLIKIGSVAPDTInnHVKTCREEQK---NLHFFAPEYGEVTNVTTAVDIYSFG-----MCALE---- 268
Cdd:cd08222 130 RDLKAKNIFLK-NNVIKVGDFGISRI--LMGTSDLATTftgTPYYMSPEVLKHEGYNSKSDIWSLGcilyeMCCLKhafd 206
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  269 ----MAVLEIQGNGESSYVPQEAISSAIQLLEDPLQRefiqkclqsEPARRPTARELLFHP 325
Cdd:cd08222 207 gqnlLSVMYKIVEGETPSLPDKYSKELNAIYSRMLNK---------DPALRPSAAEILKIP 258
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
81-327 6.71e-13

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: 68.80  E-value: 6.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNliqlEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQ 160
Cdd:cd06647  22 TVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMREN----KNPNIVNYLDSYLVGDE----LWVVMEYLAGGSLTD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTCREEQ 237
Cdd:cd06647  94 VVTET-----CMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLtdfGFCAQITPEQSKRSTMVGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KnlHFFAPEYGEVTNVTTAVDIYSFGMCALEM--------------AVLEIQGNGESSYVPQEAISSAIqlledplqREF 303
Cdd:cd06647 167 P--YWMAPEVVTRKAYGPKVDIWSLGIMAIEMvegeppylnenplrALYLIATNGTPELQNPEKLSAIF--------RDF 236
                       250       260
                ....*....|....*....|....
gi 7019333  304 IQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06647 237 LNRCLEMDVEKRGSAKELLQHPFL 260
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
110-321 9.67e-13

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: 68.56  E-value: 9.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQ----LEHLNIVKFhKYWADiKENKARVIFITEYMSSGSLKQFLKKTKKNhktMNEKAWKRWCTQIL 185
Cdd:cd05038  45 GEEQHMSDFKREIEilrtLDHEYIVKY-KGVCE-SPGRRSLRLIMEYLPSGSLRDYLQRHRDQ---IDLKRLLLFASQIC 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  186 SALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIG----SVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYS 261
Cdd:cd05038 120 KGMEYLGS--QRYIHRDLAARNILVESEDLVKISdfglAKVLPEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWS 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  262 FGMCALEMAVLeiqgnGESSYVP-------------QEAISSAIQLLEDP--LQR---------EFIQKCLQSEPARRPT 317
Cdd:cd05038 198 FGVTLYELFTY-----GDPSQSPpalflrmigiaqgQMIVTRLLELLKSGerLPRppscpdevyDLMKECWEYEPQDRPS 272

                ....
gi 7019333  318 AREL 321
Cdd:cd05038 273 FSDL 276
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
104-324 1.03e-12

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: 68.55  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  104 RKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKEnkaRVIFIT-EYMSSGSLKQFLKKtkKNHKTMNEkAWkRWCT 182
Cdd:cd14046  42 RSESKNNSRILREV-MLLSRLNHQHVVRYYQAW--IER---ANLYIQmEYCEKSTLRDLIDS--GLFQDTDR-LW-RLFR 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 QILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG------------SVAPDTINNHVKTCREEQKNL-------HFF 243
Cdd:cd14046 112 QILEGLAYIHSQG--IIHRDLKPVNIFLDSNGNVKIGdfglatsnklnvELATQDINKSTSAALGSSGDLtgnvgtaLYV 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  244 APEygeVTNVTTA-----VDIYSFGMCALEMavleiqgngesSYVPQEA-----ISSAIQLL-----------EDPLQRE 302
Cdd:cd14046 190 APE---VQSGTKStynekVDMYSLGIIFFEM-----------CYPFSTGmervqILTALRSVsiefppdfddnKHSKQAK 255
                       250       260
                ....*....|....*....|..
gi 7019333  303 FIQKCLQSEPARRPTARELLFH 324
Cdd:cd14046 256 LIRWLLNHDPAKRPSAQELLKS 277
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
105-325 1.94e-12

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: 67.63  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  105 KNYKLQEEKVRAVF---DNLIQLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWC 181
Cdd:cd05581  36 KRHIIKEKKVKYVTiekEVLSRLAHPGIVKLYYTFQD----ESKLYFVLEYAPNGDLLEYIRK----YGSLDEKCTRFYT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  182 TQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVA---PDTINNHVKTCREEQKNL------------HFF 243
Cdd:cd05581 108 AEIVLALEYLHSKG--IIHRDLKPENILLDEDMHIKItdfGTAKvlgPDSSPESTKGDADSQIAYnqaraasfvgtaEYV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  244 APEYGEVTNVTTAVDIYSFGmCAL-EMavleIQG----NGESSY-VPQEAISSAIQLLE--DPLQREFIQKCLQSEPARR 315
Cdd:cd05581 186 SPELLNEKPAGKSSDLWALG-CIIyQM----LTGkppfRGSNEYlTFQKIVKLEYEFPEnfPPDAKDLIQKLLVLDPSKR 260
                       250
                ....*....|....*.
gi 7019333  316 PTA------RELLFHP 325
Cdd:cd05581 261 LGVnenggyDELKAHP 276
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
151-325 2.00e-12

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: 67.83  E-value: 2.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  151 EYMSSgSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIG--SVAPDTINN 228
Cdd:cd06617  80 EVMDT-SLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLINRNGQVKLCdfGISGYLVDS 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  229 HVKT----CREeqknlhFFAPEY----GEVTNVTTAVDIYSFGMCALEMAVL----EIQGN----------GESSYVPQE 286
Cdd:cd06617 158 VAKTidagCKP------YMAPERinpeLNQKGYDVKSDVWSLGITMIELATGrfpyDSWKTpfqqlkqvveEPSPQLPAE 231
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7019333  287 AISSAIQlledplqrEFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06617 232 KFSPEFQ--------DFVNKCLKKNYKERPNYPELLQHP 262
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
123-327 2.62e-12

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: 67.05  E-value: 2.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKfhkYWADIKENKARVIFItEYMSSGSLKQFLKkTKKNHKTMNEKAWKRWCTQILSALSYLHscDPPIIHGN 202
Cdd:cd06624  61 RLSHKNIVQ---YLGSVSEDGFFKIFM-EQVPGGSLSALLR-SKWGPLKDNENTIGYYTKQILEGLKYLH--DNKIVHRD 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQ-HNGLIKIGSVAPDTINNHVKTCREEQK-NLHFFAPE--------YGevtnvtTAVDIYSFGMCALEMAV- 271
Cdd:cd06624 134 IKGDNVLVNtYSGVVKISDFGTSKRLAGINPCTETFTgTLQYMAPEvidkgqrgYG------PPADIWSLGCTIIEMATg 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  272 ----LEIqGNGESSY-----------VPQEAISSAiqlledplqREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06624 208 kppfIEL-GEPQAAMfkvgmfkihpeIPESLSEEA---------KSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
83-325 2.76e-12

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: 67.53  E-value: 2.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEV----VWNEvqfserKNYKLQEekvravFDNLIQLEHLNIVKFHKYWADIKENKARVI--FITEYMSSg 156
Cdd:cd14137  21 YQAKLLETGEVVaikkVLQD------KRYKNRE------LQIMRRLKHPNIVKLKYFFYSSGEKKDEVYlnLVMEYMPE- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  157 SLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHG-----NLTCDtifiQHNGLIKI---GSvapdtinn 228
Cdd:cd14137  88 TLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLG--ICHRdikpqNLLVD----PETGVLKLcdfGS-------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  229 hVKTCREEQKNLHFF------APE--YGeVTNVTTAVDIYSFGmCAL-EMAVLEIQGNGESS------------------ 281
Cdd:cd14137 154 -AKRLVPGEPNVSYIcsryyrAPEliFG-ATDYTTAIDIWSAG-CVLaELLLGQPLFPGESSvdqlveiikvlgtptreq 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  282 -------Y-------VPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14137 231 ikamnpnYtefkfpqIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
149-327 3.22e-12

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: 67.36  E-value: 3.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLkktkkNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVA-PDTIN 227
Cdd:cd06657  95 VMEFLEGGALTDIV-----THTRMNEEQIAAVCLAVLKALSVLHA--QGVIHRDIKSDSILLTHDGRVKLSDFGfCAQVS 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 NHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISsAIQLLED---------- 297
Cdd:cd06657 168 KEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMV------DGEPPYFNEPPLK-AMKMIRDnlppklknlh 240
                       170       180       190
                ....*....|....*....|....*....|...
gi 7019333  298 ---PLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06657 241 kvsPSLKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
128-325 3.60e-12

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: 66.52  E-value: 3.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  128 NIVKFhkYWADIKENKarVIFITEYMSSGSLKQFLKKTKKnhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDT 207
Cdd:cd06612  59 YIVKY--YGSYFKNTD--LWIVMEYCGAGSVSDIMKITNK---TLTEEEIAAILYQTLKGLEYLHSNK--KIHRDIKAGN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  208 IFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFF-APEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYV--- 283
Cdd:cd06612 130 ILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTPFWmAPEVIQEIGYNNKADIWSLGITAIEMA------EGKPPYSdih 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019333  284 PQEAISsAI-----QLLEDPLQ-----REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06612 204 PMRAIF-MIpnkppPTLSDPEKwspefNDFVKKCLVKDPEERPSAIQLLQHP 254
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
83-316 4.56e-12

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: 66.59  E-value: 4.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKENKARVIFitEYMSSGSLKQFL 162
Cdd:cd08228  19 YRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEI-DLLKQLNHPNVIKYLDSF--IEDNELNIVL--ELADAGDLSQMI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  163 KKTKKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNL-H 241
Cdd:cd08228  94 KYFKKQKRLIPERTVWKYFVQLCSAVEHMHS--RRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTpY 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  242 FFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEiqgngESSYVPQEAISSAIQLLED----PLQ--------REFIQKCLQ 309
Cdd:cd08228 172 YMSPERIHENGYNFKSDIWSLGCLLYEMAALQ-----SPFYGDKMNLFSLCQKIEQcdypPLPtehyseklRELVSMCIY 246

                ....*..
gi 7019333  310 SEPARRP 316
Cdd:cd08228 247 PDPDQRP 253
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
121-325 5.10e-12

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: 66.35  E-value: 5.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSgSLKQFLKKtkkNHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd07829  52 LKELKHPNIVKLL----DVIHTENKLYLVFEYCDQ-DLKKYLDK---RPGPLPPNLIKSIMYQLLRGLAYCHSHR--ILH 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIG--------SVAPDTINNHVKTcreeqknLHFFAPE--YGEvTNVTTAVDIYSFGMCALEMA 270
Cdd:cd07829 122 RDLKPQNLLINRDGVLKLAdfglarafGIPLRTYTHEVVT-------LWYRAPEilLGS-KHYSTAVDIWSVGCIFAELI 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  271 -----------------VLEIQG--NGES----SYVPQEAIS----SAIQLLE-----DPLQREFIQKCLQSEPARRPTA 318
Cdd:cd07829 194 tgkplfpgdseidqlfkIFQILGtpTEESwpgvTKLPDYKPTfpkwPKNDLEKvlprlDPEGIDLLSKMLQYNPAKRISA 273

                ....*..
gi 7019333  319 RELLFHP 325
Cdd:cd07829 274 KEALKHP 280
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
121-319 5.10e-12

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: 66.00  E-value: 5.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYWADikENKarVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd05123  47 LERVNHPFIVKLHYAFQT--EEK--LYLVLDYVPGGELFSHLSK----EGRFPEERARFYAAEIVLALEYLHSLG--IIY 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKI---GSVAPDtINNHVKT---CREEQknlhFFAPEYGEVTNVTTAVDIYSFGMCALEMA---- 270
Cdd:cd05123 117 RDLKPENILLDSDGHIKLtdfGLAKEL-SSDGDRTytfCGTPE----YLAPEVLLGKGYGKAVDWWSLGVLLYEMLtgkp 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  271 ------VLEIQGNGESS------YVPQEAissaiqlledplqREFIQKCLQSEPARRPTAR 319
Cdd:cd05123 192 pfyaenRKEIYEKILKSplkfpeYVSPEA-------------KSLISGLLQKDPTKRLGSG 239
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
84-322 5.57e-12

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: 66.34  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   84 LAMDTEEG-VEVVWNEVQFserknyklqeekvravfdnLIQLEHL---NIVKFHKYWAdikeNKARVIFITEYMSSGSLK 159
Cdd:cd06917  34 LNLDTDDDdVSDIQKEVAL-------------------LSQLKLGqpkNIIKYYGSYL----KGPSLWIIMDYCEGGSIR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  160 QFLKKTKknhktMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--VAPDTINNHVKtcREEQ 237
Cdd:cd06917  91 TLMRAGP-----IAERYIAVIMREVLVALKFIHKDG--IIHRDIKAANILVTNTGNVKLCDfgVAASLNQNSSK--RSTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KNL-HFFAPEY-GEVTNVTTAVDIYSFGMCALEMAVleiqgnGESSYVPQEAISsAIQL--------LED----PLQREF 303
Cdd:cd06917 162 VGTpYWMAPEViTEGKYYDTKADIWSLGITTYEMAT------GNPPYSDVDALR-AVMLipkskpprLEGngysPLLKEF 234
                       250
                ....*....|....*....
gi 7019333  304 IQKCLQSEPARRPTARELL 322
Cdd:cd06917 235 VAACLDEEPKDRLSADELL 253
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
109-325 6.96e-12

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: 66.13  E-value: 6.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVRAVfDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSAL 188
Cdd:cd14196  51 SREEIEREV-SILRQVLHPNIITLH----DVYENRTDVVLILELVSGGELFDFLAQKE----SLSEEEATSFIKQILDGV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHScdPPIIHGNLTCDTIF-------IQHNGLIKIGsvAPDTINNHVktcreEQKNL----HFFAPEYGEVTNVTTAV 257
Cdd:cd14196 122 NYLHT--KKIAHFDLKPENIMlldknipIPHIKLIDFG--LAHEIEDGV-----EFKNIfgtpEFVAPEIVNYEPLGLEA 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  258 DIYSFGMcalemaVLEIQGNGESSYV---PQEAISSAIQLLED----------PLQREFIQKCLQSEPARRPTARELLFH 324
Cdd:cd14196 193 DMWSIGV------ITYILLSGASPFLgdtKQETLANITAVSYDfdeeffshtsELAKDFIRKLLVKETRKRLTIQEALRH 266

                .
gi 7019333  325 P 325
Cdd:cd14196 267 P 267
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
119-336 1.51e-11

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: 65.15  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  119 DNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKnhkTMNEKAWKRWCTQILSALSYLHScdPPI 198
Cdd:cd06611  54 DILSECKHPNIVGLY----EAYFYENKLWILIEFCDGGALDSIMLELER---GLTEPQIRYVCRQMLEALNFLHS--HKV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVAPDTINNHvktcrEEQKNLHFFAPEY---GEVTNVTT--------AVDIYSFGMCAL 267
Cdd:cd06611 125 IHRDLKAGNILLTLDGDVKLADFGVSAKNKS-----TLQKRDTFIGTPYwmaPEVVACETfkdnpydyKADIWSLGITLI 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  268 EMAVLEIQGNGESSY-VPQEAISSAIQLLEDPLQ-----REFIQKCLQSEPARRPTARELLFHPALFEVPSLKLL 336
Cdd:cd06611 200 ELAQMEPPHHELNPMrVLLKILKSEPPTLDQPSKwsssfNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAI 274
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
125-325 1.58e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.00  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   125 EHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKqflkktkkNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLT 204
Cdd:PLN00034 130 NHPNVVKCH----DMFDHNGEIQVLLEFMDGGSLE--------GTHIADEQFLADVARQILSGIAYLHR--RHIVHRDIK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   205 CDTIFIQHNGLIKIGSVAPDTI-NNHVKTCREEQKNLHFFAPEygevtNVTT----------AVDIYSFGMCALEMAV-- 271
Cdd:PLN00034 196 PSNLLINSAKNVKIADFGVSRIlAQTMDPCNSSVGTIAYMSPE-----RINTdlnhgaydgyAGDIWSLGVSILEFYLgr 270
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333   272 ----LEIQGNGESSYV------PQEAISSAiqlleDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:PLN00034 271 fpfgVGRQGDWASLMCaicmsqPPEAPATA-----SREFRHFISCCLQREPAKRWSAMQLLQHP 329
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
110-322 1.96e-11

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: 64.44  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENkarvIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALS 189
Cdd:cd14664  33 GDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTN----LLVYEYMPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLH-SCDPPIIH-----GNLTCDTIFIQHNGLIKIGSVAPDTiNNHVKTCReeQKNLHFFAPEYGEVTNVTTAVDIYSFG 263
Cdd:cd14664 109 YLHhDCSPLIIHrdvksNNILLDEEFEAHVADFGLAKLMDDK-DSHVMSSV--AGSYGYIAPEYAYTGKVSEKSDVYSYG 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  264 MCALEM--------AVLEIQGNGESSYVP---QEAISSAI---QLLEDPLQREFIQ------KCLQSEPARRPTARELL 322
Cdd:cd14664 186 VVLLELitgkrpfdEAFLDDGVDIVDWVRgllEEKKVEALvdpDLQGVYKLEEVEQvfqvalLCTQSSPMERPTMREVV 264
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
121-219 2.06e-11

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: 64.51  E-value: 2.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd14080  56 LRKLRHPNIIQVY----SIFERGSKVFIFMEYAEHGDLLEYIQK----RGALSESQARIWFRQLALAVQYLHSLD--IAH 125
                        90
                ....*....|....*....
gi 7019333  201 GNLTCDTIFIQHNGLIKIG 219
Cdd:cd14080 126 RDLKCENILLDSNNNVKLS 144
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
81-327 2.30e-11

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: 64.74  E-value: 2.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNliqlEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQ 160
Cdd:cd06656  34 TVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMREN----KNPNIVNYLDSYLVGDE----LWVVMEYLAGGSLTD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI------GSVAPDTINNHVKTcr 234
Cdd:cd06656 106 VVTET-----CMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLtdfgfcAQITPEQSKRSTMV-- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 eeqKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAI-------SSAIQLLEDPLQ-----RE 302
Cdd:cd06656 177 ---GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV------EGEPPYLNENPLralyliaTNGTPELQNPERlsavfRD 247
                       250       260
                ....*....|....*....|....*
gi 7019333  303 FIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06656 248 FLNRCLEMDVDRRGSAKELLQHPFL 272
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
99-325 2.77e-11

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: 63.83  E-value: 2.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   99 VQFSERKNYKlqEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKktkkNHKTMNEKAWK 178
Cdd:cd14115  23 VKFVSKKMKK--KEQAAHEAALLQHLQHPQYITLH----DTYESPTSYILVLELMDDGRLLDYLM----NHDELMEEKVA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  179 RWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHN------GLIKIGSVAPDTINNHVKTCreeQKNLHFFAPEYGEVTN 252
Cdd:cd14115  93 FYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLRipvprvKLIDLEDAVQISGHRHVHHL---LGNPEFAAPEVIQGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  253 VTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLE-------------DPLQREFIQKCLQSEPARRPTAR 319
Cdd:cd14115 168 VSLATDIWSIGVLTYVML------SGVSPFLDESKEETCINVCRvdfsfpdeyfgdvSQAARDFINVILQEDPRRRPTAA 241

                ....*.
gi 7019333  320 ELLFHP 325
Cdd:cd14115 242 TCLQHP 247
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
112-324 3.77e-11

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: 63.28  E-value: 3.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  112 EKVRAVFDNLIQ----LEHLNIVKFHKYWadikeNKARVI-FITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILS 186
Cdd:cd14059  22 KKVRDEKETDIKhlrkLNHPNIIKFKGVC-----TQAPCYcILMEYCPYGQLYEVLRAGRE----ITPSLLVDWSKQIAS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  187 ALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd14059  93 GMNYLHLHK--IIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVL 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  267 LEMAvleiqgNGESSY--VPQEAI-----SSAIQL-LEDPLQREF---IQKCLQSEPARRPTARELLFH 324
Cdd:cd14059 171 WELL------TGEIPYkdVDSSAIiwgvgSNSLQLpVPSTCPDGFkllMKQCWNSKPRNRPSFRQILMH 233
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
152-324 4.33e-11

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: 63.85  E-value: 4.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  152 YMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHS-CDPPIIHGNLTCDTIFIQHNGLIKI---GSVAPDTIn 227
Cdd:cd13986  83 YYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEpELVPYAHRDIKPGNVLLSEDDEPILmdlGSMNPARI- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 nHVKTCREEQK---------NLHFFAPEYGEVTN---VTTAVDIYSFGmCAL----------EMAvlEIQG--------N 277
Cdd:cd13986 162 -EIEGRREALAlqdwaaehcTMPYRAPELFDVKShctIDEKTDIWSLG-CTLyalmygespfERI--FQKGdslalavlS 237
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 7019333  278 GESSYVPQEAISSAIQlledplqrEFIQKCLQSEPARRPTARELLFH 324
Cdd:cd13986 238 GNYSFPDNSRYSEELH--------QLVKSMLVVNPAERPSIDDLLSR 276
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
82-327 4.77e-11

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: 63.44  E-value: 4.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   82 AYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFdnLIQLEHLNIVKFhkyWADIKENkARVIFITEYMSSGSLkqf 161
Cdd:cd08225  16 IYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVIL--LAKMKHPNIVTF---FASFQEN-GRLFIVMEYCDGGDL--- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LKKTKKNHKTM-NEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLI-KIGSVA-PDTINNHVKTCREEQK 238
Cdd:cd08225  87 MKRINRQRGVLfSEDQILSWFVQISLGLKHIH--DRKILHRDIKSQNIFLSKNGMVaKLGDFGiARQLNDSMELAYTCVG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  239 NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSyvpQEAISSAIQLLEDPLQ-------REFIQKCLQSE 311
Cdd:cd08225 165 TPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNL---HQLVLKICQGYFAPISpnfsrdlRSLISQLFKVS 241
                       250
                ....*....|....*.
gi 7019333  312 PARRPTARELLFHPAL 327
Cdd:cd08225 242 PRDRPSITSILKRPFL 257
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
183-325 6.40e-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: 63.11  E-value: 6.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 QILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIG-----SVAPDTINNHVKTCREE-------QKNLHFFAPEYGEV 250
Cdd:cd14011 122 QISEALSFLHN-DVKLVHGNICPESVVINSNGEWKLAgfdfcISSEQATDQFPYFREYDpnlpplaQPNLNYLAPEYILS 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  251 TNVTTAVDIYSFGMCALEM-----AVLEIQGNGESSYV-PQEAISSAIQLLEDPLQ--REFIQKCLQSEPARRPTARELL 322
Cdd:cd14011 201 KTCDPASDMFSLGVLIYAIynkgkPLFDCVNNLLSYKKnSNQLRQLSLSLLEKVPEelRDHVKTLLNVTPEVRPDAEQLS 280

                ...
gi 7019333  323 FHP 325
Cdd:cd14011 281 KIP 283
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
83-326 6.64e-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: 63.12  E-value: 6.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNyklQEEKVRAVFDNLIQL----EHLNIVKFHKYWADiKENKARVIFItEYMSSGSL 158
Cdd:cd06653  19 YLCYDADTGRELAVKQVPFDPDSQ---ETSKEVNALECEIQLlknlRHDRIVQYYGCLRD-PEEKKLSIFV-EYMPGGSV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  159 KQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPD----TINNHVKTCR 234
Cdd:cd06653  94 KDQLKA----YGALTENVTRRYTRQILQGVSYLHS--NMIVHRDIKGANILRDSAGNVKLGDFGASkriqTICMSGTGIK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 EEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLEDPLQ-----------REF 303
Cdd:cd06653 168 SVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEML------TEKPPWAEYEAMAAIFKIATQPTKpqlpdgvsdacRDF 241
                       250       260
                ....*....|....*....|...
gi 7019333  304 IQKCLQSEpARRPTARELLFHPA 326
Cdd:cd06653 242 LRQIFVEE-KRRPTAEFLLRHPF 263
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
83-316 1.06e-10

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: 62.74  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKENKARVIFitEYMSSGSLKQFL 162
Cdd:cd08229  41 YRATCLLDGVPVALKKVQIFDLMDAKARADCIKEI-DLLKQLNHPNVIKYYASF--IEDNELNIVL--ELADAGDLSRMI 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  163 KKTKKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNL-H 241
Cdd:cd08229 116 KHFKKQKRLIPEKTVWKYFVQLCSALEHMHS--RRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTpY 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  242 FFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGES-------------SYVPQEAISSAIQLledplqREFIQKCL 308
Cdd:cd08229 194 YMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlyslckkieqcDYPPLPSDHYSEEL------RQLVNMCI 267

                ....*...
gi 7019333  309 QSEPARRP 316
Cdd:cd08229 268 NPDPEKRP 275
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
149-327 1.36e-10

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: 62.36  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLkktkkNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVA-PDTIN 227
Cdd:cd06658  97 VMEFLEGGALTDIV-----THTRMNEEQIATVCLSVLRALSYLHN--QGVIHRDIKSDSILLTSDGRIKLSDFGfCAQVS 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 NHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISsAIQLLEDPLQ------- 300
Cdd:cd06658 170 KEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMI------DGEPPYFNEPPLQ-AMRRIRDNLPprvkdsh 242
                       170       180       190
                ....*....|....*....|....*....|...
gi 7019333  301 ------REFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06658 243 kvssvlRGFLDLMLVREPSQRATAQELLQHPFL 275
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
110-325 1.42e-10

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: 62.12  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDnLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSALS 189
Cdd:cd14105  52 REDIEREVSI-LRQVLHPNIITLH----DVFENKTDVVLILELVAGGELFDFLAEKE----SLSEEEATEFLKQILDGVN 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHSCDppIIHGNLTCDTIFIQ-------HNGLIKIGSVapdtinnHVKTCREEQKNLH----FFAPEYGEVTNVTTAVD 258
Cdd:cd14105 123 YLHTKN--IAHFDLKPENIMLLdknvpipRIKLIDFGLA-------HKIEDGNEFKNIFgtpeFVAPEIVNYEPLGLEAD 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  259 IYSFGMcalemaVLEIQGNGESSYV---PQEA---ISSAIQLLED-------PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14105 194 MWSIGV------ITYILLSGASPFLgdtKQETlanITAVNYDFDDeyfsntsELAKDFIRQLLVKDPRKRMTIQESLRHP 267
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
147-327 1.46e-10

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: 61.90  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  147 IFITEYMSSGSLKQFLKKTKKNHKTMNEkaWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNG--LIKI---GSV 221
Cdd:cd14133  76 LCIVFELLSQNLYEFLKQNKFQYLSLPR--IRKIAQQILEALVFLHSLG--LIHCDLKPENILLASYSrcQIKIidfGSS 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 A--PDTINNHVKTcreeqknLHFFAPE------YGEvtnvttAVDIYSFGMCALEMAVLEI--QGNGESS---------- 281
Cdd:cd14133 152 CflTQRLYSYIQS-------RYYRAPEvilglpYDE------KIDMWSLGCILAELYTGEPlfPGASEVDqlariigtig 218
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019333  282 YVPQEAISSAIQllEDPLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd14133 219 IPPAHMLDQGKA--DDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
Pkinase pfam00069
Protein kinase domain;
123-325 1.86e-10

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 60.72  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    123 QLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSylhscdppiihgn 202
Cdd:pfam00069  54 KLNHPNIVRLYDAF----EDKDNLYLVLEYVEGGSLFDLLSE----KGAFSEREAKFIMKQILEGLE------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    203 ltcdtifiqhnglikiGSVAPDTInnhVKTcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMA--VLEIQGNGES 280
Cdd:pfam00069 113 ----------------SGSSLTTF---VGT-------PWYMAPEVLGGNPYGPKVDVWSLGCILYELLtgKPPFPGINGN 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 7019333    281 SYVPQE-----AISSAIQLLEDPLqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:pfam00069 167 EIYELIidqpyAFPELPSNLSEEA-KDLLKKLLKKDPSKRLTATQALQHP 215
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
121-325 2.45e-10

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: 61.34  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKktkkNHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd14098  55 LKSLEHPGIVRLI----DWYEDDQHIYLVMEYVEGGDLMDFIM----AWGAIPEQHARELTKQILEAMAYTHSMG--ITH 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNG--LIKIGS------VAPDTI-NNHVKTcreeqknLHFFAPEYGEVTNVT------TAVDIYSFGMC 265
Cdd:cd14098 125 RDLKPENILITQDDpvIVKISDfglakvIHTGTFlVTFCGT-------MAYLAPEILMSKEQNlqggysNLVDMWSVGCL 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  266 ALEMAVLEIQGNGESSYVPQEAISSAiQLLEDPLQ--------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14098 198 VYVMLTGALPFDGSSQLPVEKRIRKG-RYTQPPLVdfniseeaIDFILRLLDVDPEKRMTAAQALDHP 264
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
81-327 3.10e-10

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: 61.28  E-value: 3.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAvfdnLIQLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQ 160
Cdd:cd06655  34 TVFTAIDVATGQEVAIKQINLQKQPKKELIINEILV----MKELKNPNIVNFLDSFLVGDE----LFVVMEYLAGGSLTD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTCREEQ 237
Cdd:cd06655 106 VVTET-----CMDEAQIAAVCRECLQALEFLHANQ--VIHRDIKSDNVLLGMDGSVKLtdfGFCAQITPEQSKRSTMVGT 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KnlHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLED------------PLQREFIQ 305
Cdd:cd06655 179 P--YWMAPEVVTRKAYGPKVDIWSLGIMAIEMV------EGEPPYLNENPLRALYLIATNgtpelqnpeklsPIFRDFLN 250
                       250       260
                ....*....|....*....|..
gi 7019333  306 KCLQSEPARRPTARELLFHPAL 327
Cdd:cd06655 251 RCLEMDVEKRGSAKELLQHPFL 272
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
110-325 3.18e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 62.58  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   110 QEEKVRAV--FDNLIQLEHLNIVKFHKYWA----DIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQ 183
Cdd:PTZ00283  72 EADKNRAQaeVCCLLNCDFFSIVKCHEDFAkkdpRNPENVLMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   184 ILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVA-----PDTINNHV-KT-CREEqknlHFFAPEYGEVTNVTTA 256
Cdd:PTZ00283 152 VLLAVHHVHS--KHMIHRDIKSANILLCSNGLVKLGDFGfskmyAATVSDDVgRTfCGTP----YYVAPEIWRRKPYSKK 225
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333   257 VDIYSFGMCALEMAVLEIQGNGESSyvpQEAISSAIQLLEDPL-------QREFIQKCLQSEPARRPTARELLFHP 325
Cdd:PTZ00283 226 ADMFSLGVLLYELLTLKRPFDGENM---EEVMHKTLAGRYDPLppsispeMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
102-321 3.50e-10

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: 60.53  E-value: 3.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNYklqEEKVRavfdNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwKRWC 181
Cdd:cd14058  28 SEKKAF---EVEVR----QLSRVDHPNIIKLY----GACSNQKPVCLVMEYAEGGSLYNVLHGKEPKPIYTAAHA-MSWA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  182 TQILSALSYLHSCDP-PIIHGNLTCDTIFIQHNG-LIKI---GSVApdTINNHvKTcrEEQKNLHFFAPEYGEVTNVTTA 256
Cdd:cd14058  96 LQCAKGVAYLHSMKPkALIHRDLKPPNLLLTNGGtVLKIcdfGTAC--DISTH-MT--NNKGSAAWMAPEVFEGSKYSEK 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  257 VDIYSFGMCALEMAV--LEIQGNGESSYVPQEAISSA-----IQLLEDPLQrEFIQKCLQSEPARRPTAREL 321
Cdd:cd14058 171 CDVFSWGIILWEVITrrKPFDHIGGPAFRIMWAVHNGerpplIKNCPKPIE-SLMTRCWSKDPEKRPSMKEI 241
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
83-325 4.78e-10

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: 60.48  E-value: 4.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQE-EKVRAVFDNLIQLEHLNIVKFHKYWADIKEnKARVIFItEYMSSGSLKQF 161
Cdd:cd06651  24 YLCYDVDTGRELAAKQVQFDPESPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRAE-KTLTIFM-EYMPGGSVKDQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LKKtkknHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPD----TINNHVKTCREEQ 237
Cdd:cd06651 102 LKA----YGALTESVTRKYTRQILEGMSYLHS--NMIVHRDIKGANILRDSAGNVKLGDFGASkrlqTICMSGTGIRSVT 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLEDPLQ-----------REFIqK 306
Cdd:cd06651 176 GTPYWMSPEVISGEGYGRKADVWSLGCTVVEML------TEKPPWAEYEAMAAIFKIATQPTNpqlpshisehaRDFL-G 248
                       250
                ....*....|....*....
gi 7019333  307 CLQSEPARRPTARELLFHP 325
Cdd:cd06651 249 CIFVEARHRPSAEELLRHP 267
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
126-323 4.79e-10

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: 60.43  E-value: 4.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFHKYWADIKENKARVIFITEYmSSGSLKQFLKKTKKNHKTmnEKAWKRWCTQILSALSYLHSCDPPIIHGNLTC 205
Cdd:cd13985  57 HPNIVQYYDSAILSSEGRKEVLLLMEY-CPGSLVDILEKSPPSPLS--EEEVLRIFYQICQAVGHLHSQSPPIIHRDIKI 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  206 DTIFIQHNGLIKI---GSVapdTINNHVKTCREE--------QKN--LHFFAPEYGEVTN---VTTAVDIYSFG-----M 264
Cdd:cd13985 134 ENILFSNTGRFKLcdfGSA---TTEHYPLERAEEvniieeeiQKNttPMYRAPEMIDLYSkkpIGEKADIWALGcllykL 210
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  265 CALEM-----AVLEIQgNGESSYVPQEAISsaiqlledPLQREFIQKCLQSEPARRPTARELLF 323
Cdd:cd13985 211 CFFKLpfdesSKLAIV-AGKYSIPEQPRYS--------PELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
121-325 5.13e-10

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: 60.63  E-value: 5.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQL-EHLNIVKFHKYwadIKENKaRVIFITEYMSsGSLKQFLKKtkKNHKTMNEKAWKRWCTQILSALSYLHScdppii 199
Cdd:cd07830  51 LRKLnEHPNIVKLKEV---FREND-ELYFVFEYME-GNLYQLMKD--RKGKPFSESVIRSIIYQILQGLAHIHK------ 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  200 HG----NLTCDTIFIQHNGLIKIG---------SVAPDTinNHVKT--CReeqknlhffAPeygEV----TNVTTAVDIY 260
Cdd:cd07830 118 HGffhrDLKPENLLVSGPEVVKIAdfglareirSRPPYT--DYVSTrwYR---------AP---EIllrsTSYSSPVDIW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  261 SFGMCALEMAVL-----------------EIQGNGESSYVPqEAISSAIQL-----------LEDPLQR------EFIQK 306
Cdd:cd07830 184 ALGCIMAELYTLrplfpgsseidqlykicSVLGTPTKQDWP-EGYKLASKLgfrfpqfaptsLHQLIPNaspeaiDLIKD 262
                       250
                ....*....|....*....
gi 7019333  307 CLQSEPARRPTARELLFHP 325
Cdd:cd07830 263 MLRWDPKKRPTASQALQHP 281
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
124-322 5.36e-10

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: 59.97  E-value: 5.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFhkyWADIKENKARVIfITEYMSSGSLKQFLkkTKKNHKTMNEKAWKRWCTQILSALSYLHSCDP-PIIHGN 202
Cdd:cd14060  39 LSHRNIIQF---YGAILEAPNYGI-VTEYASYGSLFDYL--NSNESEEMDMDQIMTWATDIAKGMHYLHMEAPvKVIHRD 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHNGLIKIGSVAPDTINNHVkTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEI-----QG- 276
Cdd:cd14060 113 LKSRNVVIAADGVLKICDFGASRFHSHT-THMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVpfkglEGl 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7019333  277 --------NGESSYVPQEAISSAIQLLedplqrefiQKCLQSEPARRPTARELL 322
Cdd:cd14060 192 qvawlvveKNERPTIPSSCPRSFAELM---------RRCWEADVKERPSFKQII 236
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
81-327 5.66e-10

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: 60.51  E-value: 5.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNliqlEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQ 160
Cdd:cd06654  35 TVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMREN----KNPNIVNYLDSYLVGDE----LWVVMEYLAGGSLTD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI------GSVAPDTINNHVKTcr 234
Cdd:cd06654 107 VVTET-----CMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILLGMDGSVKLtdfgfcAQITPEQSKRSTMV-- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 eeqKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAI-------SSAIQLLEDPLQ-----RE 302
Cdd:cd06654 178 ---GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI------EGEPPYLNENPLralyliaTNGTPELQNPEKlsaifRD 248
                       250       260
                ....*....|....*....|....*
gi 7019333  303 FIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06654 249 FLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
149-325 6.08e-10

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: 60.16  E-value: 6.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKKNHKtmnekaWK---RWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHN--------GLIK 217
Cdd:cd13978  70 VMEYMENGSLKSLLEREIQDVP------WSlrfRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHfhvkisdfGLSK 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  218 IGSVApdTINNHVKTCREEQKNLHFFAPEYGEVTNV--TTAVDIYSFGMC-----------------ALEMAVLeIQGN- 277
Cdd:cd13978 144 LGMKS--ISANRRRGTENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIViwavltrkepfenainpLLIMQIV-SKGDr 220
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019333  278 ----GESSYVPQEAISSAIQLledplqrefIQKCLQSEPARRPTARELLFHP 325
Cdd:cd13978 221 psldDIGRLKQIENVQELISL---------MIRCWDGNPDARPTFLECLDRL 263
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
121-325 1.23e-09

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: 59.26  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd14194  62 LKEIQHPNVITLH----EVYENKTDVILILELVAGGELFDFLAEKE----SLTEEEATEFLKQILNGVYYLHSLQ--IAH 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNL----HFFAPEYGEVTNVTTAVDIYSFGMcalemaVLEIQG 276
Cdd:cd14194 132 FDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIfgtpEFVAPEIVNYEPLGLEADMWSIGV------ITYILL 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  277 NGESSYV---PQEAIS--SAI--QLLED------PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14194 206 SGASPFLgdtKQETLAnvSAVnyEFEDEyfsntsALAKDFIRRLLVKDPKKRMTIQDSLQHP 267
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
83-324 1.38e-09

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: 58.90  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   83 YLAMDTEEGVEVVWNEVQFSERKNYKLQE-EKVRAVFDNLIQLEHLNIVKFHKYWADIKEnKARVIFItEYMSSGSLKQF 161
Cdd:cd06652  19 YLCYDADTGRELAVKQVQFDPESPETSKEvNALECEIQLLKNLLHERIVQYYGCLRDPQE-RTLSIFM-EYMPGGSIKDQ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LKktkkNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPD----TINNHVKTCREEQ 237
Cdd:cd06652  97 LK----SYGALTENVTRKYTRQILEGVHYLHS--NMIVHRDIKGANILRDSVGNVKLGDFGASkrlqTICLSGTGMKSVT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLEDPLQ-----------REFIQK 306
Cdd:cd06652 171 GTPYWMSPEVISGEGYGRKADIWSVGCTVVEML------TEKPPWAEFEAMAAIFKIATQPTNpqlpahvsdhcRDFLKR 244
                       250
                ....*....|....*...
gi 7019333  307 CLqSEPARRPTARELLFH 324
Cdd:cd06652 245 IF-VEAKLRPSADELLRH 261
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
82-327 1.53e-09

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: 58.59  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   82 AYLAMDTEEGVEVVWNEVQFSerknyKLQEEKVRAVF---DNLIQLEHLNIVKFHKYWADikenkARVIFI-TEYMSSGS 157
Cdd:cd08221  16 AVLYRKTEDNSLVVWKEVNLS-----RLSEKERRDALneiDILSLLNHDNIITYYNHFLD-----GESLFIeMEYCNGGN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LkqFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG----SVAPDTINNHVKTC 233
Cdd:cd08221  86 L--HDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAG--ILHRDIKTLNIFLTKADLVKLGdfgiSKVLDSESSMAESI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  234 reeQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE---------------IQGNGEssyVPQEAISSAIQlledp 298
Cdd:cd08221 162 ---VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKrtfdatnplrlavkiVQGEYE---DIDEQYSEEII----- 230
                       250       260
                ....*....|....*....|....*....
gi 7019333  299 lqrEFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd08221 231 ---QLVHDCLHQDPEDRPTAEELLERPLL 256
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
151-325 1.58e-09

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: 59.37  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  151 EYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYL---HScdppIIHGNLTCDTIFIQHNGLIKI------GSV 221
Cdd:cd06615  79 EHMDGGSLDQVLKKAGR----IPENILGKISIAVLRGLTYLrekHK----IMHRDVKPSNILVNSRGEIKLcdfgvsGQL 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 APDTINNHVKTcREeqknlhFFAPEYGEVTNVTTAVDIYSFGMCALEMAV------------LEIQGNGE---------- 279
Cdd:cd06615 151 IDSMANSFVGT-RS------YMSPERLQGTHYTVQSDIWSLGLSLVEMAIgrypipppdakeLEAMFGRPvsegeakesh 223
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  280 ---SSYVPQEAISSAI-QLL----EDPLQR-----------EFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06615 224 rpvSGHPPDSPRPMAIfELLdyivNEPPPKlpsgafsdefqDFVDKCLKKNPKERADLKELTKHP 288
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
126-325 1.97e-09

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: 58.47  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFHKYWadIKENKarvIFIT-EYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLT 204
Cdd:cd06613  56 HPNIVAYFGSY--LRRDK---LWIVmEYCGGGSLQDIYQVTG----PLSELQIAYVCRETLKGLAYLHSTG--KIHRDIK 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  205 CDTIFIQHNGLIKIGS--VAPD---TI---NNHVKTcreeqknLHFFAPEYGEV---TNVTTAVDIYSFGMCALEMAVLE 273
Cdd:cd06613 125 GANILLTEDGDVKLADfgVSAQltaTIakrKSFIGT-------PYWMAPEVAAVerkGGYDGKCDIWALGITAIELAELQ 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  274 -----------IQGNGESSYVPQEaissaiqlLED-----PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06613 198 ppmfdlhpmraLFLIPKSNFDPPK--------LKDkekwsPDFHDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
105-325 3.28e-09

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: 58.10  E-value: 3.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  105 KNYKLQEEKVravfdnLIQLEHLNIVKFhkywADIKENKARVIFITEYMSSgSLKQFLKKTKKNhktMNEKAWKRWCTQI 184
Cdd:cd07833  44 KKTALREVKV------LRQLRHENIVNL----KEAFRRKGRLYLVFEYVER-TLLELLEASPGG---LPPDAVRSYIWQL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  185 LSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI-----------GSVAPDTinNHVKTCREEQKNLHFFAPEYGEvtnv 253
Cdd:cd07833 110 LQAIAYCHSHN--IIHRDIKPENILVSESGVLKLcdfgfaraltaRPASPLT--DYVATRWYRAPELLVGDTNYGK---- 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  254 ttAVDIYSFGMCALEMavleIQGN----GESS----YVPQEA----ISSAIQLLE----------------DPLQR---- 301
Cdd:cd07833 182 --PVDVWAIGCIMAEL----LDGEplfpGDSDidqlYLIQKClgplPPSHQELFSsnprfagvafpepsqpESLERrypg 255
                       250       260       270
                ....*....|....*....|....*....|.
gi 7019333  302 -------EFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd07833 256 kvsspalDFLKACLRMDPKERLTCDELLQHP 286
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
181-336 5.95e-09

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: 57.35  E-value: 5.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  181 CTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINnhVKTCREEQKNL---HFFAPEYGEVTNVTTA- 256
Cdd:cd06644 116 CRQMLEALQYLHS--MKIIHRDLKAGNVLLTLDGDIKLADFGVSAKN--VKTLQRRDSFIgtpYWMAPEVVMCETMKDTp 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  257 ----VDIYSFGMCALEMAVLEiqgngessyVPQEAISSAIQLLE----DPLQ-----------REFIQKCLQSEPARRPT 317
Cdd:cd06644 192 ydykADIWSLGITLIEMAQIE---------PPHHELNPMRVLLKiaksEPPTlsqpskwsmefRDFLKTALDKHPETRPS 262
                       170
                ....*....|....*....
gi 7019333  318 ARELLFHPALFEVPSLKLL 336
Cdd:cd06644 263 AAQLLEHPFVSSVTSNRPL 281
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
121-322 6.01e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 57.11  E-value: 6.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKY-WADikENkarvIFITEYMSSGSLKQFLKKtKKNHKTMnekAWKRWCT-QILSALSYLHscDPPI 198
Cdd:cd05037  56 MSQISHKHLVKLYGVcVAD--EN----IMVQEYVRYGPLDKYLRR-MGNNVPL---SWKLQVAkQLASALHYLE--DKKL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGL------IKIGSVApdtINNHVKTCREEQKNLHFFAPEY--GEVTNVTTAVDIYSFGMcalemA 270
Cdd:cd05037 124 IHGNVRGRNILLAREGLdgyppfIKLSDPG---VPITVLSREERVDRIPWIAPEClrNLQANLTIAADKWSFGT-----T 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  271 VLEIQGNGE---SSYVPQE-----AISSAIQLLEDPLQREFIQKCLQSEPARRPTARELL 322
Cdd:cd05037 196 LWEICSGGEeplSALSSQEklqfyEDQHQLPAPDCAELAELIMQCWTYEPTKRPSFRAIL 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
102-325 9.14e-09

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: 56.49  E-value: 9.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNYKLQEEkvravFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYmSSGSLKQFLKktkkNHKTMNEKAWKRWC 181
Cdd:cd14002  40 SEKELRNLRQE-----IEILRKLNHPNIIEML----DSFETKKEFVVVTEY-AQGELFQILE----DDGTLPEEEVRSIA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  182 TQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKI---GSVAPDTINNHVKTcreEQKNLHFF-APEYGEVTNVTTAV 257
Cdd:cd14002 106 KQLVSALHYLHS--NRIIHRDMKPQNILIGKGGVVKLcdfGFARAMSCNTLVLT---SIKGTPLYmAPELVQEQPYDHTA 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  258 DIYSFGMCALEMAVleiqgnGESSYVpQEAISSAIQL-LEDPLQ---------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14002 181 DLWSLGCILYELFV------GQPPFY-TNSIYQLVQMiVKDPVKwpsnmspefKSFLQGLLNKDPSKRLSWPDLLEHP 251
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
123-322 1.24e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 56.07  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKENkarvIFITEYMSSGSLKQFLKKTKKNHKTmnekAWKRWCT-QILSALSYLHscDPPIIHG 201
Cdd:cd05076  71 QVSHTHLVFVHGVCVRGSEN----IMVEEFVEHGPLDVWLRKEKGHVPM----AWKFVVArQLASALSYLE--NKNLVHG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  202 NLTCDTIFIQHNGLIKIGS----VAPDTINNHVKTCREEQKNLHFFAPE-YGEVTNVTTAVDIYSFGMcalemAVLEIQG 276
Cdd:cd05076 141 NVCAKNILLARLGLEEGTSpfikLSDPGVGLGVLSREERVERIPWIAPEcVPGGNSLSTAADKWGFGA-----TLLEICF 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7019333  277 NGE-----SSYVPQEAISSAIQLLEDPLQRE---FIQKCLQSEPARRPTARELL 322
Cdd:cd05076 216 NGEaplqsRTPSEKERFYQRQHRLPEPSCPElatLISQCLTYEPTQRPSFRTIL 269
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
125-325 1.29e-08

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: 56.13  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  125 EHLNIVKFHkywadIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTM-NEKAWKRWCTQILSALSYLHSCDppIIHGNL 203
Cdd:cd13982  53 EHPNVIRYF-----CTEKDRQFLYIALELCAASLQDLVESPRESKLFLrPGLEPVRLLRQIASGLAHLHSLN--IVHRDL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  204 TcdtifiQHNGLIkigsvAPDTINNHVKT-------CREEQKNLHFF-------------APEY---GEVTNVTTAVDIY 260
Cdd:cd13982 126 K------PQNILI-----STPNAHGNVRAmisdfglCKKLDVGRSSFsrrsgvagtsgwiAPEMlsgSTKRRQTRAVDIF 194
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  261 SFGmC----ALEMAV------LEIQGN---GESSYV-PQEAISsaiqllEDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd13982 195 SLG-CvfyyVLSGGShpfgdkLEREANilkGKYSLDkLLSLGE------HGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
82-273 1.30e-08

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: 55.97  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   82 AYLAMDTEEGVEVVWNEVQFSERKNyKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQF 161
Cdd:cd08218  16 ALLVKSKEDGKQYVIKEINISKMSP-KEREESRKEV-AVLSKMKHPNIVQYQESF----EENGNLYIVMDYCDGGDLYKR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LKKTKKnhKTMNEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQKNL 240
Cdd:cd08218  90 INAQRG--VLFPEDQILDWFVQLCLALKHVH--DRKILHRDIKSQNIFLTKDGIIKLGDFGiARVLNSTVELARTCIGTP 165
                       170       180       190
                ....*....|....*....|....*....|...
gi 7019333  241 HFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE 273
Cdd:cd08218 166 YYLSPEICENKPYNNKSDIWALGCVLYEMCTLK 198
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
101-325 1.34e-08

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: 56.28  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  101 FSERKNYKLQEEKVrAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFLKKTKKnHKTMNEkaWKRW 180
Cdd:cd14052  38 YAGAKDRLRRLEEV-SILRELTLDGHDNIVQLIDSW----EYHGHLYIQTELCENGSLDVFLSELGL-LGRLDE--FRVW 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  181 --CTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG-----SVAPDTINNHVKTCREeqknlhFFAPEYGEVTNV 253
Cdd:cd14052 110 kiLVELSLGLRFIHDHH--FVHLDLKPANVLITFEGTLKIGdfgmaTVWPLIRGIEREGDRE------YIAPEILSEHMY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  254 TTAVDIYSFGMCALEMAV-LEIQGNGES---------------------SYVPQEAISSAIQL----LEDPLQReFIQKC 307
Cdd:cd14052 182 DKPADIFSLGLILLEAAAnVVLPDNGDAwqklrsgdlsdaprlsstdlhSASSPSSNPPPDPPnmpiLSGSLDR-VVRWM 260
                       250
                ....*....|....*...
gi 7019333  308 LQSEPARRPTARELLFHP 325
Cdd:cd14052 261 LSPEPDRRPTADDVLATP 278
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
112-318 1.41e-08

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: 55.86  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  112 EKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtkKNHKtMNEKAWKRWCTQILSALSYL 191
Cdd:cd13992  41 RTILQELNQLKELVHDNLNKFI----GICINPPNIAVVTEYCTRGSLQDVLLN--REIK-MDWMFKSSFIKDIVKGMNYL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  192 HScDPPIIHGNLTCDTIFIQHNGLIKIGSVApdtinnhVKTCREEQKNLHF-----------FAPE----YGEVTNVTTA 256
Cdd:cd13992 114 HS-SSIGYHGRLKSSNCLVDSRWVVKLTDFG-------LRNLLEEQTNHQLdedaqhkkllwTAPEllrgSLLEVRGTQK 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  257 VDIYSFGMCALEM-------------AVLEIQGNGESSYVPQEAISSAIQLLEDPLqrEFIQKCLQSEPARRPTA 318
Cdd:cd13992 186 GDVYSFAIILYEIlfrsdpfalerevAIVEKVISGGNKPFRPELAVLLDEFPPRLV--LLVKQCWAENPEKRPSF 258
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
124-325 1.64e-08

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: 55.79  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVK-FHKYwaDIKENKarviFIT--EYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIH 200
Cdd:cd13990  61 LDHPRIVKlYDVF--EIDTDS----FCTvlEYCDGNDLDFYLKQ----HKSIPEREARSIIMQVVSALKYLNEIKPPIIH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 -----GNL------TCDTIFIQHNGLIKI---GSVAPDTInnhvKTCREEQKNLHFFAPEYGEVTN----VTTAVDIYSF 262
Cdd:cd13990 131 ydlkpGNIllhsgnVSGEIKITDFGLSKImddESYNSDGM----ELTSQGAGTYWYLPPECFVVGKtppkISSKVDVWSV 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  263 GMCALEM--------------AVLE---IQGNGESSYVPQEAISSAIQlledplqrEFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd13990 207 GVIFYQMlygrkpfghnqsqeAILEentILKATEVEFPSKPVVSSEAK--------DFIRRCLTYRKEDRPDVLQLANDP 278
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
103-325 2.11e-08

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: 55.53  E-value: 2.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  103 ERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKEN---KARVIFITEYMSSGSLKQFLKktkkNHKTMNEKAWKR 179
Cdd:cd14077  42 LKKEREKRLEKEISRDIRTIREAALSSLLNHPHICRLRDFlrtPNHYYMLFEYVDGGQLLDYII----SHGKLKEKQARK 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  180 WCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVT-TAVD 258
Cdd:cd14077 118 FARQIASALDYLHRNS--IVHRDLKIENILISKSGNIKIIDFGLSNLYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVD 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  259 IYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIqlLEDP--LQRE---FIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14077 196 VWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGK--VEYPsyLSSEcksLISRMLVVDPKKRATLEQVLNHP 265
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
81-327 2.24e-08

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: 55.63  E-value: 2.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSerknykLQEEKVRAVFDNLIQLEHLN---IVKFhkYWADIKENKarVIFITEYMSSGS 157
Cdd:cd06622  16 SVYKVLHRPTGVTMAMKEIRLE------LDESKFNQIIMELDILHKAVspyIVDF--YGAFFIEGA--VYMCMEYMDAGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LKQfLKKTKKNHKTMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIGS--VAPDTINNHVKT--- 232
Cdd:cd06622  86 LDK-LYAGGVATEGIPEDVLRRITYAVVKGLKFLKE-EHNIIHRDVKPTNVLVNGNGQVKLCDfgVSGNLVASLAKTnig 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  233 CREeqknlhFFAPEY----GEVTNVTTAV--DIYSFGMCALEMAVleiqgnGESSYVPQ--EAISSAIQLLED------- 297
Cdd:cd06622 164 CQS------YMAPERiksgGPNQNPTYTVqsDVWSLGLSILEMAL------GRYPYPPEtyANIFAQLSAIVDgdpptlp 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 7019333  298 ----PLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06622 232 sgysDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
104-316 2.57e-08

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: 55.20  E-value: 2.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  104 RKNYKLQEEKVRAVFD--NLI--QLEHLNIVKFHKYWAdikENKaRVIFITEYMSSGSLKQFLKKTK-KNHKTMNEKAWK 178
Cdd:cd08528  42 GRTEQERDKSVGDIISevNIIkeQLRHPNIVRYYKTFL---END-RLYIVMELIEGAPLGEHFSSLKeKNEHFTEDRIWN 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  179 RWcTQILSALSYLHScDPPIIHGNLTCDTIFIQHN--------GLIKIGSVAPDTINNHVKT----CREEQKNLhffapE 246
Cdd:cd08528 118 IF-VQMVLALRYLHK-EKQIVHRDLKPNNIMLGEDdkvtitdfGLAKQKGPESSKMTSVVGTilysCPEIVQNE-----P 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  247 YGEvtnvttAVDIYSFGMCALEMAVLeiqgngESSYVPQEAISSAIQLLE---DPLQ--------REFIQKCLQSEPARR 315
Cdd:cd08528 191 YGE------KADIWALGCILYQMCTL------QPPFYSTNMLTLATKIVEaeyEPLPegmysddiTFVIRSCLTPDPEAR 258

                .
gi 7019333  316 P 316
Cdd:cd08528 259 P 259
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
126-325 2.73e-08

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: 55.14  E-value: 2.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFhkYWADIKENKaRVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDPpIIHGNLTC 205
Cdd:cd06620  62 SPYIVSF--YGAFLNENN-NIIICMEYMDCGSLDKILKKKGP----FPEEVLGKIAVAVLEGLTYLYNVHR-IIHRDIKP 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  206 DTIFIQHNGLIK----------IGSVApDTInnhVKTCReeqknlhFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQ 275
Cdd:cd06620 134 SNILVNSKGQIKlcdfgvsgelINSIA-DTF---VGTST-------YMSPERIQGGKYSVKSDVWSLGLSIIELALGEFP 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333  276 GNGE----SSYVPQEAISSAIQLL--EDPLQ-----------REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06620 203 FAGSndddDGYNGPMGILDLLQRIvnEPPPRlpkdrifpkdlRDFVDRCLLKDPRERPSPQLLLDHD 269
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
108-321 2.91e-08

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: 55.41  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  108 KLQ---EEKVRAvFDNLIQ----LEHLNIVKFHKYWADIKENKARVIFitEYMSSGSLKQFLKKTKKNhktMNEKAWKRW 180
Cdd:cd14205  40 KLQhstEEHLRD-FEREIEilksLQHDNIVKYKGVCYSAGRRNLRLIM--EYLPYGSLRDYLQKHKER---IDHIKLLQY 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  181 CTQILSALSYLhsCDPPIIHGNLTCDTIFIQHNGLIKIG-----SVAPDtiNNHVKTCREE-QKNLHFFAPEYGEVTNVT 254
Cdd:cd14205 114 TSQICKGMEYL--GTKRYIHRDLATRNILVENENRVKIGdfgltKVLPQ--DKEYYKVKEPgESPIFWYAPESLTESKFS 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  255 TAVDIYSFGMCALEM------------AVLEIQGNGESSyvpQEAISSAIQLLE------------DPLQReFIQKCLQS 310
Cdd:cd14205 190 VASDVWSFGVVLYELftyieksksppaEFMRMIGNDKQG---QMIVFHLIELLKnngrlprpdgcpDEIYM-IMTECWNN 265
                       250
                ....*....|.
gi 7019333  311 EPARRPTAREL 321
Cdd:cd14205 266 NVNQRPSFRDL 276
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
121-269 3.03e-08

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: 55.32  E-value: 3.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYWADIKENKARVIFitEYMSSGSLKQFLKKTkKNHktMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd05079  60 LRNLYHENIVKYKGICTEDGGNGIKLIM--EFLPSGSLKEYLPRN-KNK--INLKQQLKYAVQICKGMDYLGSRQ--YVH 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  201 GNLTCDTIFIQHNGLIKIG------SVAPDTINNHVKTCREEQknLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd05079 133 RDLAARNVLVESEHQVKIGdfgltkAIETDKEYYTVKDDLDSP--VFWYAPECLIQSKFYIASDVWSFGVTLYEL 205
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
121-274 5.93e-08

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: 54.07  E-value: 5.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYWADikeNKARVIFITEYMSSGSLKQFLKKTKKNhktMNEKAWKRWCTQILSALSYLHSCDPPIIH 200
Cdd:cd14064  45 LCRLNHPCVIQFVGACLD---DPSQFAIVTQYVSGGSLFSLLHEQKRV---IDLQSKLIIAVDVAKGMEYLHNLTQPIIH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGlikiGSVAPDTINNHVKTCREEQK------NLHFFAPE-YGEVTNVTTAVDIYSFGMCALEMAVLE 273
Cdd:cd14064 119 RDLNSHNILLYEDG----HAVVADFGESRFLQSLDEDNmtkqpgNLRWMAPEvFTQCTRYSIKADVFSYALCLWELLTGE 194

                .
gi 7019333  274 I 274
Cdd:cd14064 195 I 195
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
105-325 6.66e-08

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: 54.22  E-value: 6.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  105 KNYKL---QEEKVRAVFDNLI---QLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLKKTKKNhkTMNEKAWK 178
Cdd:cd08216  31 KKINLesdSKEDLKFLQQEILtsrQLQHPNILPYVTSFVV----DNDLYVVTPLMAYGSCRDLLKTHFPE--GLPELAIA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  179 RWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG--SVAPDTIN--NHVKTC----REEQKNLHFFAPE---- 246
Cdd:cd08216 105 FILRDVLNALEYIHSKG--YIHRSVKASHILISGDGKVVLSglRYAYSMVKhgKRQRVVhdfpKSSEKNLPWLSPEvlqq 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  247 ----YGEVTnvttavDIYSFGMCALEMA-------------------------------VLEIQGNGESSYVPQEAISSA 291
Cdd:cd08216 183 nllgYNEKS------DIYSVGITACELAngvvpfsdmpatqmllekvrgttpqlldcstYPLEEDSMSQSEDSSTEHPNN 256
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 7019333  292 IQLLEDPLQR-------EFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd08216 257 RDTRDIPYQRtfseafhQFVELCLQRDPELRPSASQLLAHS 297
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
120-322 7.50e-08

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: 53.93  E-value: 7.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  120 NLIQLEHLNIVKFHKYWADIKENKARVIfITEYMSSGSLKQFLKKTKKnhkTMNEKAWKRWCTQILSALSYLHSCDppII 199
Cdd:cd13979  52 NAARLRHENIVRVLAAETGTDFASLGLI-IMEYCGNGTLQQLIYEGSE---PLPLAHRILISLDIARALRFCHSHG--IV 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  200 HGNLTCDTIFIQHNGLIKIG----SV---APDTINNHVK----TCReeqknlhFFAPEYGEVTNVTTAVDIYSFGMCALE 268
Cdd:cd13979 126 HLDVKPANILISEQGVCKLCdfgcSVklgEGNEVGTPRShiggTYT-------YRAPELLKGERVTPKADIYSFGITLWQ 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  269 MAVLEIQGNGESSYVPQEAISSAIQLLEDPLQ--------REFIQKCLQSEPARRPTARELL 322
Cdd:cd13979 199 MLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEdsefgqrlRSLISRCWSAQPAERPNADESL 260
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
106-324 7.78e-08

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: 53.72  E-value: 7.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  106 NYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADI-------KENKARVIFITEYMSSGSLKQFLKKTKknhkTMNEKAW- 177
Cdd:cd14048  43 NNELAREKVLREVRALAKLDHPGIVRYFNAWLERppegwqeKMDEVYLYIQMQLCRKENLKDWMNRRC----TMESRELf 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  178 --KRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTinnHVKTCREEQKNLH-------------- 241
Cdd:cd14048 119 vcLNIFKQIASAVEYLH--SKGLIHRDLKPSNVFFSLDDVVKVGDFGLVT---AMDQGEPEQTVLTpmpayakhtgqvgt 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  242 --FFAPEYGEVTNVTTAVDIYSFGMCALEMaVLEIQGNGESSYVPQEAISSAIQLLED---PLQREFIQKCLQSEPARRP 316
Cdd:cd14048 194 rlYMSPEQIHGNQYSEKVDIFALGLILFEL-IYSFSTQMERIRTLTDVRKLKFPALFTnkyPEERDMVQQMLSPSPSERP 272

                ....*...
gi 7019333  317 TARELLFH 324
Cdd:cd14048 273 EAHEVIEH 280
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
110-322 9.48e-08

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: 53.40  E-value: 9.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALS 189
Cdd:cd14187  50 QKEKMSMEIAIHRSLAHQHVVGFHGFF----EDNDFVYVVLELCRRRSLLELHKR----RKALTEPEARYYLRQIILGCQ 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTinnHVKTCREEQKNL----HFFAPEYGEVTNVTTAVDIYSFGMC 265
Cdd:cd14187 122 YLHR--NRVIHRDLKLGNLFLNDDMEVKIGDFGLAT---KVEYDGERKKTLcgtpNYIAPEVLSKKGHSFEVDIWSIGCI 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  266 ALEMAV----LEIQGNGESsYVPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELL 322
Cdd:cd14187 197 MYTLLVgkppFETSCLKET-YLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 256
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
111-324 1.13e-07

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: 53.54  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQLEHLNIVKFHKYWAD-IKENKARVIFitEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALS 189
Cdd:cd06641  43 EDEIEDIQQEITVLSQCDSPYVTKYYGSyLKDTKLWIIM--EYLGGGSALDLLEPGP-----LDETQIATILREILKGLD 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHScdPPIIHGNLTCDTIFIQHNGLIKIGS--VAPDTINNHVKtcREEQKNLHFF-APEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd06641 116 YLHS--EKKIHRDIKAANVLLSEHGEVKLADfgVAGQLTDTQIK--RN*FVGTPFWmAPEVIKQSAYDSKADIWSLGITA 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333  267 LEMAvleiQGNGESSYVPQEAISSAIQLLEDPLQ--------REFIQKCLQSEPARRPTARELLFH 324
Cdd:cd06641 192 IELA----RGEPPHSELHPMKVLFLIPKNNPPTLegnyskplKEFVEACLNKEPSFRPTAKELLKH 253
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
126-324 1.21e-07

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: 53.06  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFHKYWAD-IKENKARVIFITEYMSSGSLKQFLKkTKKNHKTMNEKAWKRWCtQILSALSYLHSCDPPIIHGNLT 204
Cdd:cd14037  60 HKNIVGYIDSSANrSGNGVYEVLLLMEYCKGGGVIDLMN-QRLQTGLTESEILKIFC-DVCEAVAAMHYLKPPLIHRDLK 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  205 CDTIFIQHNGLIKI---GSVA-PDTINNHVKTCR----EEQKN--LHFFAPE----YGEVTnVTTAVDIYSFGmCAL--- 267
Cdd:cd14037 138 VENVLISDSGNYKLcdfGSATtKILPPQTKQGVTyveeDIKKYttLQYRAPEmidlYRGKP-ITEKSDIWALG-CLLykl 215
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  268 --------EMAVLEIQgNGESSYVPQEAISSAIQLLedplqrefIQKCLQSEPARRPTARELLFH 324
Cdd:cd14037 216 cfyttpfeESGQLAIL-NGNFTFPDNSRYSKRLHKL--------IRYMLEEDPEKRPNIYQVSYE 271
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
124-218 1.27e-07

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: 53.07  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFHKywadIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNL 203
Cdd:cd14162  57 LKHPNLICFYE----AIETTSRVYIIMELAENGDLLDYIRK----NGALPEPQARRWFRQLVAGVEYCHSKG--VVHRDL 126
                        90
                ....*....|....*
gi 7019333  204 TCDTIFIQHNGLIKI 218
Cdd:cd14162 127 KCENLLLDKNNNLKI 141
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
119-326 1.29e-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: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  119 DNLIQLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKKNHKTmnekAWKRWCTQILS---ALSYLHSCD 195
Cdd:cd14159  44 EKLSRFRHPNIVDLAGYSAQQGN----YCLIYVYLPNGSLEDRLHCQVSCPCL----SWSQRLHVLLGtarAIQYLHSDS 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  196 PPIIHGNLTCDTIFIQHNGLIKIG-------SVAPDTINNHVKTCREE--QKNLHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd14159 116 PSLIHGDVKSSNILLDAALNPKLGdfglarfSRRPKQPGMSSTLARTQtvRGTLAYLPEEYVKTGTLSVEIDVYSFGVVL 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  267 LEMAV----LEIQGNGESSYvpqeaissaiqlLEDPLQREfiqKCLQSEPARRPTARELLFHPA 326
Cdd:cd14159 196 LELLTgrraMEVDSCSPTKY------------LKDLVKEE---EEAQHTPTTMTHSAEAQAAQL 244
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
82-324 1.54e-07

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: 52.49  E-value: 1.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   82 AYLAMDTEEG-VEVVWNEVQFSERKNYkLQEEKVravfdnLIQLEHLNIVKFHKYWadIKENKarVIFITEYMSSGSLKQ 160
Cdd:cd14065   9 VYKVTHRETGkVMVMKELKRFDEQRSF-LKEVKL------MRRLSHPNILRFIGVC--VKDNK--LNFITEYVNGGTLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKknhKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTcdtifiQHNGLIKIGS------VA--------PDTI 226
Cdd:cd14065  78 LLKSMD---EQLPWSQRVSLAKDIASGMAYLHSKN--IIHRDLN------SKNCLVREANrgrnavVAdfglaremPDEK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  227 NNhvKTCREEQKNL----HFFAPEY--GEVTNvtTAVDIYSFGmcaleMAVLEIQG--NGESSYVPQEA-----ISSAIQ 293
Cdd:cd14065 147 TK--KPDRKKRLTVvgspYWMAPEMlrGESYD--EKVDVFSFG-----IVLCEIIGrvPADPDYLPRTMdfgldVRAFRT 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 7019333  294 LLEDPLQREFIQ---KCLQSEPARRPTARELLFH 324
Cdd:cd14065 218 LYVPDCPPSFLPlaiRCCQLDPEKRPSFVELEHH 251
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
110-332 1.54e-07

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: 53.18  E-value: 1.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQL-EHLNIVKFhkYWADIKENKA----RVIFITEYMSSGSLKQFLKKTKKNhkTMNEKAWKRWCTQI 184
Cdd:cd06637  45 EEEEIKQEINMLKKYsHHRNIATY--YGAFIKKNPPgmddQLWLVMEFCGAGSVTDLIKNTKGN--TLKEEWIAYICREI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  185 LSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDT-INNHVKTCREEQKNLHFFAPEYGEVTNVTTAV-----D 258
Cdd:cd06637 121 LRGLSHLHQ--HKVIHRDIKGQNVLLTENAEVKLVDFGVSAqLDRTVGRRNTFIGTPYWMAPEVIACDENPDATydfksD 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  259 IYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLEDPLQR-----------EFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd06637 199 LWSLGITAIEMA------EGAPPLCDMHPMRALFLIPRNPAPRlkskkwskkfqSFIESCLVKNHSQRPSTEQLMKHPFI 272

                ....*
gi 7019333  328 FEVPS 332
Cdd:cd06637 273 RDQPN 277
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
124-285 1.61e-07

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: 52.65  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFhkywADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRwctQILSALSYLHSCDppIIHGNL 203
Cdd:cd14221  47 LEHPNVLKF----IGVLYKDKRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFAK---DIASGMAYLHSMN--IIHRDL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  204 TCDTIFIQHNG-----------LIKIGSVAPDTINNHVKTCREEQ----KNLHFFAPEYGEVTNVTTAVDIYSFGmcale 268
Cdd:cd14221 118 NSHNCLVRENKsvvvadfglarLMVDEKTQPEGLRSLKKPDRKKRytvvGNPYWMAPEMINGRSYDEKVDVFSFG----- 192
                       170
                ....*....|....*....
gi 7019333  269 MAVLEIQG--NGESSYVPQ 285
Cdd:cd14221 193 IVLCEIIGrvNADPDYLPR 211
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
99-322 1.75e-07

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: 52.98  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   99 VQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADikENKARVIFITEYMSSGSLKQFLKKTKKNHKTMnekawK 178
Cdd:cd05080  38 VKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSE--QGGKSLQLIMEYVPLGSLRDYLPKHSIGLAQL-----L 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  179 RWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVApdtINNHVKT------CREEQKNLHF-FAPEYGEVT 251
Cdd:cd05080 111 LFAQQICEGMAYLHS--QHYIHRDLAARNVLLDNDRLVKIGDFG---LAKAVPEgheyyrVREDGDSPVFwYAPECLKEY 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  252 NVTTAVDIYSFGMcalemAVLEIQGNGESSYVP----QEAISSA---------IQLLED----------PLQ-REFIQKC 307
Cdd:cd05080 186 KFYYASDVWSFGV-----TLYELLTHCDSSQSPptkfLEMIGIAqgqmtvvrlIELLERgerlpcpdkcPQEvYHLMKNC 260
                       250
                ....*....|....*
gi 7019333  308 LQSEPARRPTARELL 322
Cdd:cd05080 261 WETEASFRPTFENLI 275
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
144-324 1.77e-07

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: 52.75  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  144 ARVIFITEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGS--V 221
Cdd:cd06642  75 TKLWIIMEYLGGGSALDLLKPGP-----LEETYIATILREILKGLDYLHS--ERKIHRDIKAANVLLSEQGDVKLADfgV 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 APDTINNHVKtcREEQKNLHFF-APEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSY-----------VPQEAIS 289
Cdd:cd06642 148 AGQLTDTQIK--RNTFVGTPFWmAPEVIKQSAYDFKADIWSLGITAIELA------KGEPPNsdlhpmrvlflIPKNSPP 219
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7019333  290 SAIQLLEDPLqREFIQKCLQSEPARRPTARELLFH 324
Cdd:cd06642 220 TLEGQHSKPF-KEFVEACLNKDPRFRPTAKELLKH 253
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
109-325 2.15e-07

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: 52.31  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRWCTQILSAL 188
Cdd:cd14195  50 VSREEIEREVNILREIQHPNIITLH----DIFENKTDVVLILELVSGGELFDFLAEKE----SLTEEEATQFLKQILDGV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNL----HFFAPEYGEVTNVTTAVDIYSFGM 264
Cdd:cd14195 122 HYLHS--KRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIfgtpEFVAPEIVNYEPLGLEADMWSIGV 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  265 calemaVLEIQGNGESSYV---PQEAIS--SAIQLLED--------PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14195 200 ------ITYILLSGASPFLgetKQETLTniSAVNYDFDeeyfsntsELAKDFIRRLLVKDPKKRMTIAQSLEHS 267
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
144-324 2.23e-07

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: 52.36  E-value: 2.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  144 ARVIFITEYMSSGSLKQFLKKTKknhktMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGS--V 221
Cdd:cd06640  75 TKLWIIMEYLGGGSALDLLRAGP-----FDEFQIATMLKEILKGLDYLHS--EKKIHRDIKAANVLLSEQGDVKLADfgV 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 APDTINNHVKtcREEQKNLHFF-APEYGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLEDPLQ 300
Cdd:cd06640 148 AGQLTDTQIK--RNTFVGTPFWmAPEVIQQSAYDSKADIWSLGITAIELA------KGEPPNSDMHPMRVLFLIPKNNPP 219
                       170       180       190
                ....*....|....*....|....*....|....
gi 7019333  301 ----------REFIQKCLQSEPARRPTARELLFH 324
Cdd:cd06640 220 tlvgdfskpfKEFIDACLNKDPSFRPTAKELLKH 253
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
121-325 2.25e-07

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: 52.51  E-value: 2.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSgSLKQFLKKTKKNHKTMNEKawKRWCTQILSALSYLHScdPPIIH 200
Cdd:cd07860  53 LKELNHPNIVKLL----DVIHTENKLYLVFEFLHQ-DLKKFMDASALTGIPLPLI--KSYLFQLLQGLAFCHS--HRVLH 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQKNLHFFAPEYGEVTNV-TTAVDIYSFGMCALEMAVLEIQGNG 278
Cdd:cd07860 124 RDLKPQNLLINTEGAIKLADFGlARAFGVPVRTYTHEVVTLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTRRALFPG 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  279 ESSY-----------VPQEAISSAIQLLED------------------PLQ---REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd07860 204 DSEIdqlfrifrtlgTPDEVVWPGVTSMPDykpsfpkwarqdfskvvpPLDedgRDLLSQMLHYDPNKRISAKAALAHP 282
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
102-322 2.74e-07

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: 51.92  E-value: 2.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNYKlqeEKVRAVFDNLIQLEHLNIVKFHKYwadIKENKARVIFITEYMSSGSLKQFLKKTKknHKTMNEKA--WKr 179
Cdd:cd13994  35 SKRKDYV---KRLTSEYIISSKLHHPNIVKVLDL---CQDLHGKWCLVMEYCPGGDLFTLIEKAD--SLSLEEKDcfFK- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  180 wctQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVapdtinNHVKTCREEQKNLH--------FFAPE-Y 247
Cdd:cd13994 106 ---QILRGVAYLHSHG--IAHRDLKPENILLDEDGVLKLtdfGTA------EVFGMPAEKESPMSaglcgsepYMAPEvF 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  248 GEVTNVTTAVDIYSFG--MCAL-------EMAVLEiqgngESSYvpQEAISSAIQLLEDPLQ---------REFIQKCLQ 309
Cdd:cd13994 175 TSGSYDGRAVDVWSCGivLFALftgrfpwRSAKKS-----DSAY--KAYEKSGDFTNGPYEPienllpsecRRLIYRMLH 247
                       250
                ....*....|...
gi 7019333  310 SEPARRPTARELL 322
Cdd:cd13994 248 PDPEKRITIDEAL 260
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
121-325 3.98e-07

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: 51.80  E-value: 3.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFhkYWADIKENkaRVIFITEYMSSGSLKQFlkktkknhKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd06619  53 LYKCDSPYIIGF--YGAFFVEN--RISICTEFMDGGSLDVY--------RKIPEHVLGRIAVAVVKGLTYLWSLK--ILH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIGS--VAPDTINNHVKTCREEQKnlhFFAPEYGEVTNVTTAVDIYSFGMCALEMAV-----LE 273
Cdd:cd06619 119 RDVKPSNMLVNTRGQVKLCDfgVSTQLVNSIAKTYVGTNA---YMAPERISGEQYGIHSDVWSLGISFMELALgrfpyPQ 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  274 IQGNgESSYVPQEAISSAIQllEDPLQR----------EFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06619 196 IQKN-QGSLMPLQLLQCIVD--EDPPVLpvgqfsekfvHFITQCMRKQPKERPAPENLMDHP 254
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
129-327 4.55e-07

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: 51.46  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  129 IVKFHkywaDIKENKARVIFITEYMSSGSLkqFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTI 208
Cdd:cd14198  70 VVNLH----EVYETTSEIILILEYAAGGEI--FNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNN--IVHLDLKPQNI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  209 F---IQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE---IQGNGESSY 282
Cdd:cd14198 142 LlssIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHEspfVGEDNQETF 221
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7019333  283 V---------PQEAISSAIQLLEDplqreFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd14198 222 LnisqvnvdySEETFSSVSQLATD-----FIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
129-327 5.20e-07

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: 51.09  E-value: 5.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  129 IVKFHkywaDIKENKARVIFITEYMSSGSLkqFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTI 208
Cdd:cd14197  71 VINLH----EVYETASEMILVLEYAAGGEI--FNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNN--VVHLDLKPQNI 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  209 FIQHN---GLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM--AVLEIQGNGESSY- 282
Cdd:cd14197 143 LLTSEsplGDIKIVDFGLSRILKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMltGISPFLGDDKQETf 222
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7019333  283 --VPQEAISSAIQLLE--DPLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd14197 223 lnISQMNVSYSEEEFEhlSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
121-325 5.48e-07

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: 50.89  E-value: 5.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKfhkYWADIKENKARVIfITEYMSSGSLKQFLKKtkKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIH 200
Cdd:cd08220  53 LSMLHHPNIIE---YYESFLEDKALMI-VMEYAPGGTLFEYIQQ--RKGSLLSEEEILHFFVQILLALHHVHS--KQILH 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFI-QHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLeiQGNGE 279
Cdd:cd08220 125 RDLKTQNILLnKKRTVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASL--KRAFE 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019333  280 SSYVP------QEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd08220 203 AANLPalvlkiMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQP 254
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
121-321 5.74e-07

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: 51.14  E-value: 5.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFhkyWADIKENKARVIFITEYMSSGSLKQFLKktKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd05082  53 MTQLRHSNLVQL---LGVIVEEKGGLYIVTEYMAKGSLVDYLR--SRGRSVLGGDCLLKFSLDVCEAMEYLEGNN--FVH 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHN--------GLIKIGSVAPDTINNHVKtcreeqknlhFFAPEYGEVTNVTTAVDIYSFGMCalemaVL 272
Cdd:cd05082 126 RDLAARNVLVSEDnvakvsdfGLTKEASSTQDTGKLPVK----------WTAPEALREKKFSTKSDVWSFGIL-----LW 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  273 EIQGNGESSYvPQEAISSAIQLLED-----------PLQREFIQKCLQSEPARRPTAREL 321
Cdd:cd05082 191 EIYSFGRVPY-PRIPLKDVVPRVEKgykmdapdgcpPAVYDVMKNCWHLDAAMRPSFLQL 249
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
103-325 5.79e-07

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: 50.90  E-value: 5.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  103 ERKNYKlQEEKVravfdnLIQLEHLNIVKFHKYWADikeNKARVIFITEYMSSGSLKQFLKKtkKNHKTMNEKAWKRWCT 182
Cdd:cd08223  42 ERKAAE-QEAKL------LSKLKHPNIVSYKESFEG---EDGFLYIVMGFCEGGDLYTRLKE--QKGVLLEERQVVEWFV 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 QILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVApdtinnhVKTCREEQKNL--------HFFAPEYGEVTNVT 254
Cdd:cd08223 110 QIAMALQYMHERN--ILHRDLKTQNIFLTKSNIIKVGDLG-------IARVLESSSDMattligtpYYMSPELFSNKPYN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  255 TAVDIYSFGMCALEMAVLEIQGNGES----SY------VPQEAISSAIQLLedplqrEFIQKCLQSEPARRPTARELLFH 324
Cdd:cd08223 181 HKSDVWALGCCVYEMATLKHAFNAKDmnslVYkilegkLPPMPKQYSPELG------ELIKAMLHQDPEKRPSVKRILRQ 254

                .
gi 7019333  325 P 325
Cdd:cd08223 255 P 255
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
104-327 5.89e-07

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: 51.20  E-value: 5.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  104 RKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKywadIKENKARVIFITEYMSSGSLKQFLKktkkNHKTMNEKAWKRWCTQ 183
Cdd:cd14106  45 RRGQDCRNEILHEIAVLELCKDCPRVVNLHE----VYETRSELILILELAAGGELQTLLD----EEECLTEADVRRLMRQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  184 ILSALSYLHSCDppIIHGNLTCDTIFIQH---NGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIY 260
Cdd:cd14106 117 ILEGVQYLHERN--IVHLDLKPQNILLTSefpLGDIKLCDFGISRVIGEGEEIREILGTPDYVAPEILSYEPISLATDMW 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  261 SFGMCALEMAvleiqgNGESSY-----------VPQEAISSAIQLLED--PLQREFIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd14106 195 SIGVLTYVLL------TGHSPFggddkqetflnISQCNLDFPEELFKDvsPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
111-324 6.59e-07

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: 51.17  E-value: 6.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQL-EHLNIVKFHK-YWADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSAL 188
Cdd:cd06638  58 DEEIEAEYNILKALsDHPNVVKFYGmYYKKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGL 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFF-APEYGEV-----TNVTTAVDIYSF 262
Cdd:cd06638 138 QHLH--VNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWmAPEVIACeqqldSTYDARCDVWSL 215
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  263 GMCALEMavleiqGNGESSYVPQEAISSAIQLLEDP---LQR---------EFIQKCLQSEPARRPTARELLFH 324
Cdd:cd06638 216 GITAIEL------GDGDPPLADLHPMRALFKIPRNPpptLHQpelwsnefnDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
119-325 6.70e-07

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: 51.18  E-value: 6.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  119 DNLIQLEHLNIVKFHKywADIKENKARVIFitEYMSSGSLKQFLKKTKKnhkTMNEKAWKRWCTQILSALSYLHscDPPI 198
Cdd:cd06643  54 DILASCDHPNIVKLLD--AFYYENNLWILI--EFCAGGAVDAVMLELER---PLTEPQIRVVCKQTLEALVYLH--ENKI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVAPDTinnhvKTCREEQKNLHFFAPEY---GEVTNVTTA--------VDIYSFGMCAL 267
Cdd:cd06643 125 IHRDLKAGNILFTLDGDIKLADFGVSA-----KNTRTLQRRDSFIGTPYwmaPEVVMCETSkdrpydykADVWSLGVTLI 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7019333  268 EMAVLEiqgngessyVPQEAISSAIQLLE---------------DPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06643 200 EMAQIE---------PPHHELNPMRVLLKiaksepptlaqpsrwSPEFKDFLRKCLEKNVDARWTTSQLLQHP 263
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
92-269 6.90e-07

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: 50.71  E-value: 6.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   92 VEVVWNEVQFSE--RKNYkLQEEKVravfdnLIQLEHLNIVKFhkywADIKENKARVIFITEYMSSGSLKQFLKktkknh 169
Cdd:cd14222  20 VMVMKELIRCDEetQKTF-LTEVKV------MRSLDHPNVLKF----IGVLYKDKRLNLLTEFIEGGTLKDFLR------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  170 kTMNEKAWK---RWCTQILSALSYLHSCDppIIHGNLTcdtifiQHNGLIKIGSVA-------------------PDTIN 227
Cdd:cd14222  83 -ADDPFPWQqkvSFAKGIASGMAYLHSMS--IIHRDLN------SHNCLIKLDKTVvvadfglsrliveekkkppPDKPT 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 7019333  228 NHVKTCREEQK--------NLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd14222 154 TKKRTLRKNDRkkrytvvgNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEI 203
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
119-263 7.39e-07

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: 50.80  E-value: 7.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  119 DNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLkqFLKKTkkNHKTMNEKAWKRWCTQILSALSYLHSCDppI 198
Cdd:cd14075  53 SSMEKLHHPNIIRLY----EVVETLSKLHLVMEYASGGEL--YTKIS--TEGKLSESEAKPLFAQIVSAVKHMHENN--I 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVAPDTinnhvkTCREEQKnLHFF-------APEYGEVTN-VTTAVDIYSFG 263
Cdd:cd14075 123 IHRDLKAENVFYASNNCVKVGDFGFST------HAKRGET-LNTFcgsppyaAPELFKDEHyIGIYVDIWALG 188
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
122-270 7.79e-07

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong 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 (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, 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 TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 50.90  E-value: 7.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  122 IQLEHLNIVKFhkYWADIKENKA--RVIFITEYMSSGSLKQFLkktkkNHKTMNEKAWKRWCTQILSALSYLH------S 193
Cdd:cd14143  44 VMLRHENILGF--IAADNKDNGTwtQLWLVSDYHEHGSLFDYL-----NRYTVTVEGMIKLALSIASGLAHLHmeivgtQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  194 CDPPIIHGNLTCDTIFIQHNGLIKIGSV--------APDTI----NNHVKTCReeqknlhFFAPEYGEVTNVTTA----- 256
Cdd:cd14143 117 GKPAIAHRDLKSKNILVKKNGTCCIADLglavrhdsATDTIdiapNHRVGTKR-------YMAPEVLDDTINMKHfesfk 189
                       170
                ....*....|....*
gi 7019333  257 -VDIYSFGMCALEMA 270
Cdd:cd14143 190 rADIYALGLVFWEIA 204
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
121-325 1.28e-06

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: 50.26  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFH-----KYWADIKENkarVIFITEYMS---SGSLKQflkktkKNHKtMNEKAWKRWCTQILSALSYLH 192
Cdd:cd07840  52 LQKLDHPNVVRLKeivtsKGSAKYKGS---IYMVFEYMDhdlTGLLDN------PEVK-FTESQIKCYMKQLLEGLQYLH 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  193 SCDppIIHGNLTCDTIFIQHNGLIKIG---------SVAPDTINNHVKTcreeqknLHFFAPE--YGEvTNVTTAVDIYS 261
Cdd:cd07840 122 SNG--ILHRDIKGSNILINNDGVLKLAdfglarpytKENNADYTNRVIT-------LWYRPPEllLGA-TRYGPEVDMWS 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  262 FGMCALEM----AVLeiQGNGESSYV---------PQEAISSAIQLLE-----------------------DPLQREFIQ 305
Cdd:cd07840 192 VGCILAELftgkPIF--QGKTELEQLekifelcgsPTEENWPGVSDLPwfenlkpkkpykrrlrevfknviDPSALDLLD 269
                       250       260
                ....*....|....*....|
gi 7019333  306 KCLQSEPARRPTARELLFHP 325
Cdd:cd07840 270 KLLTLDPKKRISADQALQHE 289
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
126-326 1.29e-06

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 50.09  E-value: 1.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFHKYWAdikENKARVIfITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTC 205
Cdd:cd14051  59 HPHVVRYYSAWA---EDDHMII-QNEYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQN--LVHMDIKP 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  206 DTIFIQHNGLI-KIGSVAPDTINNHVktcREEQKNLHFFAPEYGEVTNVT------------------------TAVDIY 260
Cdd:cd14051 133 GNIFISRTPNPvSSEEEEEDFEGEED---NPESNEVTYKIGDLGHVTSISnpqveegdcrflaneilqenyshlPKADIF 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  261 SFGMCALEMA---VLEIQG-------NGESSYVPQeaissaiqlledpLQREF---IQKCLQSEPARRPTARELLFHPA 326
Cdd:cd14051 210 ALALTVYEAAgggPLPKNGdewheirQGNLPPLPQ-------------CSPEFnelLRSMIHPDPEKRPSAAALLQHPV 275
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
102-218 1.36e-06

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: 49.95  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNyKLQEEK----VRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAW 177
Cdd:cd14161  34 SIRKD-RIKDEQdllhIRREIEIMSSLNHPHIISVY----EVFENSSKIVIVMEYASRGDLYDYISERQR----LSELEA 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7019333  178 KRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI 218
Cdd:cd14161 105 RHFFRQIVSAVHYCHANG--IVHRDLKLENILLDANGNIKI 143
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
181-327 1.40e-06

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: 49.76  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  181 CTQILSALSYLHSCDPpiIHGNLTCDTIFIQHNGLIKIGSVAPDTI----NNHVKTCreeqknlHFFAPEY------GEV 250
Cdd:cd06607 107 CHGALQGLAYLHSHNR--IHRDVKAGNILLTEPGTVKLADFGSASLvcpaNSFVGTP-------YWMAPEVilamdeGQY 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  251 TNvttAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLE-DP--LQ--------REFIQKCLQSEPARRPTAR 319
Cdd:cd06607 178 DG---KVDVWSLGITCIELA------ERKPPLFNMNAMSALYHIAQnDSptLSsgewsddfRNFVDSCLQKIPQDRPSAE 248

                ....*...
gi 7019333  320 ELLFHPAL 327
Cdd:cd06607 249 DLLKHPFV 256
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
123-218 1.43e-06

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: 49.70  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKywadIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGN 202
Cdd:cd14071  55 MLNHPHIIKLYQ----VMETKDMLYLVTEYASNGEIFDYLAQ----HGRMSEKEARKKFWQILSAVEYCHKRH--IVHRD 124
                        90
                ....*....|....*.
gi 7019333  203 LTCDTIFIQHNGLIKI 218
Cdd:cd14071 125 LKAENLLLDANMNIKI 140
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
110-325 2.08e-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: 49.64  E-value: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALS 189
Cdd:cd14138  48 EQNALREVYAHAVLGQHSHVVRYYSAWAE----DDHMLIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLK 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTIN-------------NHVKTCRE---EQKNLHFFAPEY--GEVT 251
Cdd:cd14138 124 YIHSMS--LVHMDIKPSNIFISRTSIPNAASEEGDEDEwasnkvifkigdlGHVTRVSSpqvEEGDSRFLANEVlqENYT 201
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333  252 NVTTAvDIYSFGMCALEMAVLE-IQGNGESSY-VPQEAISSAIQLLEDPLQrEFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14138 202 HLPKA-DIFALALTVVCAAGAEpLPTNGDQWHeIRQGKLPRIPQVLSQEFL-DLLKVMIHPDPERRPSAVALVKHS 275
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
103-325 2.31e-06

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: 49.29  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  103 ERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLkqFLKKTKKNHKTmnEKAWKRWCT 182
Cdd:cd14083  37 DKKALKGKEDSLENEIAVLRKIKHPNIVQLL----DIYESKSHLYLVMELVTGGEL--FDRIVEKGSYT--EKDASHLIR 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 QILSALSYLHSCDppIIHGNLTCDT-----------IFIQHNGLIKI-------------GSVAPDTInnhvktcreEQK 238
Cdd:cd14083 109 QVLEAVDYLHSLG--IVHRDLKPENllyyspdedskIMISDFGLSKMedsgvmstacgtpGYVAPEVL---------AQK 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  239 NlhffapeYGEvtnvttAVDIYSFGMCA-----------------LEMAVLEIQGNGESSYvpQEAIS-SAiqlledplq 300
Cdd:cd14083 178 P-------YGK------AVDCWSIGVISyillcgyppfydendskLFAQILKAEYEFDSPY--WDDISdSA--------- 233
                       250       260
                ....*....|....*....|....*
gi 7019333  301 REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14083 234 KDFIRHLMEKDPNKRYTCEQALEHP 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
113-325 2.32e-06

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: 49.83  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  113 KVRAVFDNLIQ-------------LEHLNIVKFHkywaDIKENKAR-----VIFITEYMSSGslkqfLKKTKKNHKTMNE 174
Cdd:cd07834  32 KISNVFDDLIDakrilreikilrhLKHENIIGLL----DILRPPSPeefndVYIVTELMETD-----LHKVIKSPQPLTD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  175 KAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG------SVAPDtinnhvktcrEEQKNLHFF----- 243
Cdd:cd07834 103 DHIQYFLYQILRGLKYLHSAG--VIHRDLKPSNILVNSNCDLKICdfglarGVDPD----------EDKGFLTEYvvtrw 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  244 --APE-YGEVTNVTTAVDIYSFGmCAL-EMA-----------------VLEIQGNGESSYVPQEAISSAIQLLE------ 296
Cdd:cd07834 171 yrAPElLLSSKKYTKAIDIWSVG-CIFaELLtrkplfpgrdyidqlnlIVEVLGTPSEEDLKFISSEKARNYLKslpkkp 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 7019333  297 -----------DPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd07834 250 kkplsevfpgaSPEAIDLLEKMLVFNPKKRITADEALAHP 289
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
121-325 2.43e-06

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: 49.21  E-value: 2.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSgSLKQFLKKTKknHKTMNEKAWKRWCTQILSALSYLHScdPPIIH 200
Cdd:cd07835  52 LKELNHPNIVRLL----DVVHSENKLYLVFEFLDL-DLKKYMDSSP--LTGLDPPLIKSYLYQLLQGIAFCHS--HRVLH 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIGSVA-------PdtinnhVKTCREEQKNLHFFAPE--YGeVTNVTTAVDIYSFGMCALEMA- 270
Cdd:cd07835 123 RDLKPQNLLIDTEGALKLADFGlarafgvP------VRTYTHEVVTLWYRAPEilLG-SKHYSTPVDIWSVGCIFAEMVt 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  271 -------------------VL----EIQGNGESSYV---------PQEAISSAIQLLeDPLQREFIQKCLQSEPARRPTA 318
Cdd:cd07835 196 rrplfpgdseidqlfrifrTLgtpdEDVWPGVTSLPdykptfpkwARQDLSKVVPSL-DEDGLDLLSQMLVYDPAKRISA 274

                ....*..
gi 7019333  319 RELLFHP 325
Cdd:cd07835 275 KAALQHP 281
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
81-324 2.52e-06

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: 49.65  E-value: 2.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKENKARVIFitEYmSSGSLKQ 160
Cdd:cd06633  36 AVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEV-KFLQQLKHPNTIEYKGCY--LKDHTAWLVM--EY-CLGSASD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKKnhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI----NNHVKTCree 236
Cdd:cd06633 110 LLEVHKK---PLQEVEIAAITHGALQGLAYLHSHN--MIHRDIKAGNILLTEPGQVKLADFGSASIaspaNSFVGTP--- 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  237 qknlHFFAPEY---GEVTNVTTAVDIYSFGMCALEMAVLE---IQGNGESS-YVPQEAISSAIQLLE--DPLqREFIQKC 307
Cdd:cd06633 182 ----YWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKpplFNMNAMSAlYHIAQNDSPTLQSNEwtDSF-RGFVDYC 256
                       250
                ....*....|....*..
gi 7019333  308 LQSEPARRPTARELLFH 324
Cdd:cd06633 257 LQKIPQERPSSAELLRH 273
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
148-318 2.75e-06

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: 49.15  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  148 FITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFI---QHNGLIKIgSVAPD 224
Cdd:cd14000  85 LVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAM--IIYRDLKSHNVLVwtlYPNSAIII-KIADY 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNHvkTCREEQKNLH----FFAPE---YGEVTNvtTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLLE- 296
Cdd:cd14000 162 GISRQ--CCRMGAKGSEgtpgFRAPEiarGNVIYN--EKVDVFSFGMLLYEIL------SGGAPMVGHLKFPNEFDIHGg 231
                       170       180       190
                ....*....|....*....|....*....|....
gi 7019333  297 --DPL-QRE---------FIQKCLQSEPARRPTA 318
Cdd:cd14000 232 lrPPLkQYEcapwpevevLMKKCWKENPQQRPTA 265
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
109-316 2.97e-06

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: 48.59  E-value: 2.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVravfdnLIQLEHLNIVKFhkywADIKENKARVIFITEYMSSGSLKQFLKKTKknhKTMNEKAWKRWCTQILSAL 188
Cdd:cd05041  41 LQEARI------LKQYDHPNIVKL----IGVCVQKQPIMIVMELVPGGSLLTFLRKKG---ARLTVKQLLQMCLDAAAGM 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHS--CdppiIHGNLTCDTIFIQHNGLIKIGSVApdtinnhvkTCREE------------QKNLHFFAPE---YGEvt 251
Cdd:cd05041 108 EYLESknC----IHRDLAARNCLVGENNVLKISDFG---------MSREEedgeytvsdglkQIPIKWTAPEalnYGR-- 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333  252 nVTTAVDIYSFGMCALEMAVLeiqgnGESSYV------PQEAISS-----AIQLLEDPLqREFIQKCLQSEPARRP 316
Cdd:cd05041 173 -YTSESDVWSFGILLWEIFSL-----GATPYPgmsnqqTREQIESgyrmpAPELCPEAV-YRLMLQCWAYDPENRP 241
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
111-325 3.15e-06

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: 48.79  E-value: 3.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQLEHLNIVKFHKYWADikENKARVIFITEYmSSGSLKQFLKKTKKNHKTMnekaWK--RWCTQILSAL 188
Cdd:cd14119  38 EANVKREIQILRRLNHRNVIKLVDVLYN--EEKQKLYMVMEY-CVGGLQEMLDSAPDKRLPI----WQahGYFVQLIDGL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHSCDppIIH-----GNL---TCDTIFIQHNGLIK-IGSVAPDTinnhvkTCREEQKNLHFFAPE--YGEVTNVTTAV 257
Cdd:cd14119 111 EYLHSQG--IIHkdikpGNLlltTDGTLKISDFGVAEaLDLFAEDD------TCTTSQGSPAFQPPEiaNGQDSFSGFKV 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  258 DIYSFGMCALEMAVLEIQGNGESSYVPQEAISS---AIQLLEDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14119 183 DIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKgeyTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
109-322 3.27e-06

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: 49.04  E-value: 3.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVravfdnLIQLEHLNIVKFHKYWAdikENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWK------RWCT 182
Cdd:cd14049  53 LREVKV------LAGLQHPNIVGYHTAWM---EHVQLMLYIQMQLCELSLWDWIVERNKRPCEEEFKSAPytpvdvDVTT 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 ----QILSALSYLHSCDppIIHGNLTCDTIFIQHNGL-IKIGS---VAPDTINNHVKTCREEQKN-LH---------FFA 244
Cdd:cd14049 124 kilqQLLEGVTYIHSMG--IVHRDLKPRNIFLHGSDIhVRIGDfglACPDILQDGNDSTTMSRLNgLThtsgvgtclYAA 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  245 PEYGEVTNVTTAVDIYSFGMCALE--------MAVLEIQGNGESSYVPQEAISSAiqlledPLQREFIQKCLQSEPARRP 316
Cdd:cd14049 202 PEQLEGSHYDFKSDMYSIGVILLElfqpfgteMERAEVLTQLRNGQIPKSLCKRW------PVQAKYIKLLTSTEPSERP 275

                ....*.
gi 7019333  317 TARELL 322
Cdd:cd14049 276 SASQLL 281
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
123-325 3.55e-06

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: 48.63  E-value: 3.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHkywaDIKENKARVIFITEYMSsGSLKQFLKkTKKNHKTMNEKAWKRWCTQILSALSYLHscDPPIIHGN 202
Cdd:cd07836  54 ELKHENIVRLH----DVIHTENKLMLVFEYMD-KDLKKYMD-THGVRGALDPNTVKSFTYQLLKGIAFCH--ENRVLHRD 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHNGLIKIGS--------VAPDTINNHVKTcreeqknLHFFAPE--YGEVTnVTTAVDIYSFGMCALEMA-- 270
Cdd:cd07836 126 LKPQNLLINKRGELKLADfglarafgIPVNTFSNEVVT-------LWYRAPDvlLGSRT-YSTSIDIWSVGCIMAEMItg 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  271 ---------------VLEIQGNGESSYVPQEAIS---------------SAIQLLEDPLQREFIQKCLQSEPARRPTARE 320
Cdd:cd07836 198 rplfpgtnnedqllkIFRIMGTPTESTWPGISQLpeykptfpryppqdlQQLFPHADPLGIDLLHRLLQLNPELRISAHD 277

                ....*
gi 7019333  321 LLFHP 325
Cdd:cd07836 278 ALQHP 282
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
82-322 3.59e-06

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: 48.61  E-value: 3.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   82 AYLAMDTEEGVEVVWNEVQFSERKNYKLQEEkVRAVFDNLIQLEHLNIVKFhkyWADIKENKARVIfITEYMSSGSLKQF 161
Cdd:cd05046  24 AKAKGIEEEGGETLVLVKALQKTKDENLQSE-FRRELDMFRKLSHKNVVRL---LGLCREAEPHYM-ILEYTDLGDLKQF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  162 LKKTKKNHKT-----MNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG--SVAPDTINNHVKTCR 234
Cdd:cd05046  99 LRATKSKDEKlkpppLSTKQKVALCTQIALGMDHLSNAR--FVHRDLAARNCLVSSQREVKVSllSLSKDVYNSEYYKLR 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  235 EEQKNLHFFAPEYGEVTNVTTAVDIYSFGmcaleMAVLEIQGNGESSY--VPQEAISSAIQL--LEDPLQ-------REF 303
Cdd:cd05046 177 NALIPLRWLAPEAVQEDDFSTKSDVWSFG-----VLMWEVFTQGELPFygLSDEEVLNRLQAgkLELPVPegcpsrlYKL 251
                       250
                ....*....|....*....
gi 7019333  304 IQKCLQSEPARRPTARELL 322
Cdd:cd05046 252 MTRCWAVNPKDRPSFSELV 270
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
171-323 3.98e-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: 48.40  E-value: 3.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  171 TMNEKAWKRWctQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAP------------------DTINNHvkT 232
Cdd:cd13980  95 NLIEKKWIAF--QLLHALNQCHKRG--VCHGDIKTENVLVTSWNWVYLTDFASfkptylpednpadfsyffDTSRRR--T 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  233 CR---EE-QKNLHFFAPEYGEVTNVTTAVDIYSFGmCALemAVLEIQGN-------------GESSyvpQEAISSAIqll 295
Cdd:cd13980 169 CYiapERfVDALTLDAESERRDGELTPAMDIFSLG-CVI--AELFTEGRplfdlsqllayrkGEFS---PEQVLEKI--- 239
                       170       180
                ....*....|....*....|....*...
gi 7019333  296 EDPLQREFIQKCLQSEPARRPTARELLF 323
Cdd:cd13980 240 EDPNIRELILHMIQRDPSKRLSAEDYLK 267
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
183-327 4.46e-06

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: 48.28  E-value: 4.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  183 QILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI---GSVAPdtINNHV-KTCREEQKNLHFFAPEY--GEVtnVTTA 256
Cdd:cd14111 107 QILQGLEYLHGRR--VLHLDIKPDNIMVTNLNAIKIvdfGSAQS--FNPLSlRQLGRRTGTLEYMAPEMvkGEP--VGPP 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  257 VDIYSFGMcalemaVLEIQGNGESSYVPQEAISSAIQLLE---DPLQ---------REFIQKCLQSEPARRPTARELLFH 324
Cdd:cd14111 181 ADIWSIGV------LTYIMLSGRSPFEDQDPQETEAKILVakfDAFKlypnvsqsaSLFLKKVLSSYPWSRPTTKDCFAH 254

                ...
gi 7019333  325 PAL 327
Cdd:cd14111 255 AWL 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
121-315 6.50e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 48.28  E-value: 6.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   121 LIQLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLKKTKKnhkTMNEKAwKRWCTQILSALSYLHSCDppIIH 200
Cdd:PTZ00263  72 LMELSHPFIVNMMCSFQD----ENRVYFLLEFVVGGELFTHLRKAGR---FPNDVA-KFYHAELVLAFEYLHSKD--IIY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   201 GNLTCDTIFIQHNGLIKIgsvapdTINNHVKTCREEQKNL----HFFAPEYGEVTNVTTAVDIYSFGMCALEMAVleiqg 276
Cdd:PTZ00263 142 RDLKPENLLLDNKGHVKV------TDFGFAKKVPDRTFTLcgtpEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA----- 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 7019333   277 nGESSYVPQEAISSAIQLLEDPLQ---------REFIQKCLQSEPARR 315
Cdd:PTZ00263 211 -GYPPFFDDTPFRIYEKILAGRLKfpnwfdgraRDLVKGLLQTDHTKR 257
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
123-317 6.77e-06

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 47.93  E-value: 6.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIkenkARVIFITEYMSSGSLKQFLkktkknhktMNEKAWKRW------CTQILSALSYLHscDP 196
Cdd:cd14045  58 ELDHPNLCKFIGGCIEV----PNVAIITEYCPKGSLNDVL---------LNEDIPLNWgfrfsfATDIARGMAYLH--QH 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  197 PIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLH----FFAPEYGEVTN--VTTAVDIYSFGMCALEMA 270
Cdd:cd14045 123 KIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGYQQRlmqvYLPPENHSNTDtePTQATDVYSYAIILLEIA 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333  271 -----VLEIQGNGESSYVP--QEAISS-AIQLLEDPLQR-EFIQKCLQSEPARRPT 317
Cdd:cd14045 203 trndpVPEDDYSLDEAWCPplPELISGkTENSCPCPADYvELIRRCRKNNPAQRPT 258
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
151-324 7.05e-06

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: 48.13  E-value: 7.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  151 EYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKI------GSVAPD 224
Cdd:cd06650  83 EHMDGGSLDQVLKKAGR----IPEQILGKVSIAVIKGLTYLRE-KHKIMHRDVKPSNILVNSRGEIKLcdfgvsGQLIDS 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNHVKTcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAV------------LEI------------------ 274
Cdd:cd06650 158 MANSFVGT-------RSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVgrypipppdakeLELmfgcqvegdaaetpprpr 230
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333  275 -QGNGESSYVPQEAISSAI-QLL-----EDPLQ----------REFIQKCLQSEPARRPTARELLFH 324
Cdd:cd06650 231 tPGRPLSSYGMDSRPPMAIfELLdyivnEPPPKlpsgvfslefQDFVNKCLIKNPAERADLKQLMVH 297
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
101-270 7.85e-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: 47.82  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  101 FSERKNYKLQEEKVRAVFdnliqLEHLNIVKFhkYWADIKENKARV--IFITEYMSSGSLKQFLKKTKKNhktmnekaWK 178
Cdd:cd13998  28 SRDKQSWFREKEIYRTPM-----LKHENILQF--IAADERDTALRTelWLVTAFHPNGSL*DYLSLHTID--------WV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  179 RWCTQILSA---LSYLHS----CD---PPIIHGNLTCDTIFIQHNGLIKIGSVA-----------PDTINNH-VKTCRee 236
Cdd:cd13998  93 SLCRLALSVargLAHLHSeipgCTqgkPAIAHRDLKSKNILVKNDGTCCIADFGlavrlspstgeEDNANNGqVGTKR-- 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7019333  237 qknlhFFAPEYGEVT-NVTTA-----VDIYSFGMCALEMA 270
Cdd:cd13998 171 -----YMAPEVLEGAiNLRDFesfkrVDIYAMGLVLWEMA 205
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
87-322 8.06e-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: 47.72  E-value: 8.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   87 DTEEGVEVVWNEVQFSERKNYkLQEEKVRAVFDNLiqlehlNIVKFhkYWADIKENKARVIFitEYMSSGSLKQFLKKTK 166
Cdd:cd05032  36 ETRVAIKTVNENASMRERIEF-LNEASVMKEFNCH------HVVRL--LGVVSTGQPTLVVM--ELMAKGDLKSYLRSRR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  167 KNHKTMN-------EKAWkRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--VAPDtINNHvKTCREEQ 237
Cdd:cd05032 105 PEAENNPglgpptlQKFI-QMAAEIADGMAYLAAKK--FVHRDLAARNCMVAEDLTVKIGDfgMTRD-IYET-DYYRKGG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  238 KNL---HFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQ-----GNGES-SYVPQEAISSAIQLLEDPLQrEFIQKCL 308
Cdd:cd05032 180 KGLlpvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQpyqglSNEEVlKFVIDGGHLDLPENCPDKLL-ELMRMCW 258
                       250
                ....*....|....
gi 7019333  309 QSEPARRPTARELL 322
Cdd:cd05032 259 QYNPKMRPTFLEIV 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
123-268 8.88e-06

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: 47.65  E-value: 8.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHkywaDIKENKARV------IFITEYMSSGSLKQFLKKTKkNHKTMNEKAWKRWCTQILSALSYLHscDP 196
Cdd:cd14038  48 RLNHPNVVAAR----DVPEGLQKLapndlpLLAMEYCQGGDLRKYLNQFE-NCCGLREGAILTLLSDISSALRYLH--EN 120
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  197 PIIHGNLTCDTIFIQH--NGLI-KIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALE 268
Cdd:cd14038 121 RIIHRDLKPENIVLQQgeQRLIhKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFE 195
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
123-218 9.00e-06

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: 47.74  E-value: 9.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKENKARVIfitEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIH-- 200
Cdd:cd14040  66 ELDHPRIVKLYDYFSLDTDTFCTVL---EYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVNALRYLNEIKPPIIHyd 138
                        90       100
                ....*....|....*....|....*..
gi 7019333  201 ---GNL------TCDTIFIQHNGLIKI 218
Cdd:cd14040 139 lkpGNIllvdgtACGEIKITDFGLSKI 165
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
96-268 9.75e-06

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: 47.44  E-value: 9.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   96 W-NEVQFSERKNYklqEEKVRAVfdnLIQlEHLNIVKFHKYwadikenkarVIFITEYMSSGSLKQFLKKTKkNHKTMNE 174
Cdd:cd13989  40 WcLEVQIMKKLNH---PNVVSAR---DVP-PELEKLSPNDL----------PLLAMEYCSGGDLRKVLNQPE-NCCGLKE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  175 KAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNG------LIKIGsVAPDTINNHVktCREEQKNLHFFAPEYG 248
Cdd:cd13989 102 SEVRTLLSDISSAISYLHENR--IIHRDLKPENIVLQQGGgrviykLIDLG-YAKELDQGSL--CTSFVGTLQYLAPELF 176
                       170       180
                ....*....|....*....|
gi 7019333  249 EVTNVTTAVDIYSFGMCALE 268
Cdd:cd13989 177 ESKKYTCTVDYWSFGTLAFE 196
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
110-301 1.03e-05

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: 47.22  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALS 189
Cdd:cd05572  36 QQEHIFSEKEILEECNSPFIVKLYRTFKD----KKYLYMLMEYCLGGELWTILRD----RGLFDEYTARFYTACVVLAFE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHSCDppIIHGNLTCDTIFIQHNGLIKIGsvapD-----TINNHVKT---CreeqKNLHFFAPEYGEVTNVTTAVDIYS 261
Cdd:cd05572 108 YLHSRG--IIYRDLKPENLLLDSNGYVKLV----DfgfakKLGSGRKTwtfC----GTPEYVAPEIILNKGYDFSVDYWS 177
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019333  262 FGMCALE---------------MAVLEI--QGNGE---SSYVPQEAISSAIQLLED-PLQR 301
Cdd:cd05572 178 LGILLYElltgrppfggddedpMKIYNIilKGIDKiefPKYIDKNAKNLIKQLLRRnPEER 238
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
109-322 1.12e-05

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: 47.06  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVravfdnLIQLEHLNIVKFhkYWADIKEnkaRVIFI-TEYMSSGSLKQFLKKTKKNHKTmnekAW-KRWCTQILS 186
Cdd:cd05059  47 IEEAKV------MMKLSHPKLVQL--YGVCTKQ---RPIFIvTEYMANGCLLNYLRERRGKFQT----EQlLEMCKDVCE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  187 ALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS------VAPDTInnhvkTCREEQK-NLHFFAPEYGEVTNVTTAVDI 259
Cdd:cd05059 112 AMEYLESNG--FIHRDLAARNCLVGEQNVVKVSDfglaryVLDDEY-----TSSVGTKfPVKWSPPEVFMYSKFSSKSDV 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  260 YSFGMCALEMAVL-----EIQGNGESSyvpqEAISSAIQL----LEDPLQREFIQKCLQSEPARRPTARELL 322
Cdd:cd05059 185 WSFGVLMWEVFSEgkmpyERFSNSEVV----EHISQGYRLyrphLAPTEVYTIMYSCWHEKPEERPTFKILL 252
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
124-270 1.12e-05

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: 47.47  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFhkYWADIKENKA--RVIFITEYMSSGSLKQFLKKTkknhkTMNEKAWKRWCTQILSALSYLHS------CD 195
Cdd:cd14144  46 MRHENILGF--IAADIKGTGSwtQLYLITDYHENGSLYDFLRGN-----TLDTQSMLKLAYSAACGLAHLHTeifgtqGK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  196 PPIIHGNLTCDTIFIQHNGLIKIGSVA------PDT------INNHVKTCReeqknlhFFAPE-YGEVTNVTT-----AV 257
Cdd:cd14144 119 PAIAHRDIKSKNILVKKNGTCCIADLGlavkfiSETnevdlpPNTRVGTKR-------YMAPEvLDESLNRNHfdaykMA 191
                       170
                ....*....|...
gi 7019333  258 DIYSFGMCALEMA 270
Cdd:cd14144 192 DMYSFGLVLWEIA 204
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
123-328 1.43e-05

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: 46.98  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKENKARVIfitEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIH-- 200
Cdd:cd14041  66 ELDHPRIVKLYDYFSLDTDSFCTVL---EYCEGNDLDFYLKQ----HKLMSEKEARSIIMQIVNALKYLNEIKPPIIHyd 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 ---GNL------TCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEY----GEVTNVTTAVDIYS------ 261
Cdd:cd14041 139 lkpGNIllvngtACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECfvvgKEPPKISNKVDVWSvgvify 218
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  262 --------FGMCALEMAVLE---IQGNGESSYVPQEAISsaiqlledPLQREFIQKCLQSEPARRPTARELLFHPALF 328
Cdd:cd14041 219 qclygrkpFGHNQSQQDILQentILKATEVQFPPKPVVT--------PEAKAFIRRCLAYRKEDRIDVQQLACDPYLL 288
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
121-327 1.49e-05

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: 47.00  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHscDPPIIH 200
Cdd:cd14084  65 LKKLSHPCIIKIE----DFFDAEDDYYIVLELMEGGELFDRVVSNKR----LKEAICKLYFYQMLLAVKYLH--SNGIIH 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNG---LIKIGSVAPDTINNHVKTCREEQKNLHFFAPE---YGEVTNVTTAVDIYSFGmCAL------- 267
Cdd:cd14084 135 RDLKPENVLLSSQEeecLIKITDFGLSKILGETSLMKTLCGTPTYLAPEvlrSFGTEGYTRAVDCWSLG-VILficlsgy 213
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  268 --------EMAVLEIQGNGESSYVPQE--AISSAIQLLedplqrefIQKCLQSEPARRPTARELLFHPAL 327
Cdd:cd14084 214 ppfseeytQMSLKEQILSGKYTFIPKAwkNVSEEAKDL--------VKKMLVVDPSRRPSIEEALEHPWL 275
PHA02988 PHA02988
hypothetical protein; Provisional
105-328 1.51e-05

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 47.04  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   105 KNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQFLKKTKK-NHKTMNEKAWKrwCTQ 183
Cdd:PHA02988  56 KGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIVDDLPRLSLILEYCTRGYLREVLDKEKDlSFKTKLDMAID--CCK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   184 ILSALsYLHSCDPpiiHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTcreeqKNLHFFA-PEYGEVTNV----TTAVD 258
Cdd:PHA02988 134 GLYNL-YKYTNKP---YKNLTSVSFLVTENYKLKIICHGLEKILSSPPF-----KNVNFMVyFSYKMLNDIfseyTIKDD 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333   259 IYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPLQ-----REFIQKCLQSEPARRPTARELLFHPALF 328
Cdd:PHA02988 205 IYSLGVVLWEIFTGKIPFENLTTKEIYDLIINKNNSLKLPLDcpleiKCIVEACTSHDSIKRPNIKEILYNLSLY 279
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
124-316 1.95e-05

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: 46.35  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKF-HKYWADIKENkarviFITEYMSSGSLKQFLKktkknhkTMNEK-AWK---RWCTQILSALSYLHSCDppI 198
Cdd:cd14154  47 LDHPNVLKFiGVLYKDKKLN-----LITEYIPGGTLKDVLK-------DMARPlPWAqrvRFAKDIASGMAYLHSMN--I 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHN--------GLIKI--------GSVAPDTINNHVKTCREEQK-----NLHFFAPEYGEVTNVTTAV 257
Cdd:cd14154 113 IHRDLNSHNCLVREDktvvvadfGLARLiveerlpsGNMSPSETLRHLKSPDRKKRytvvgNPYWMAPEMLNGRSYDEKV 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  258 DIYSFGMCAlemavLEIQG--NGESSYVPQeaiSSAIQLLEDPLQREFIQKCLQS-----------EPARRP 316
Cdd:cd14154 193 DIFSFGIVL-----CEIIGrvEADPDYLPR---TKDFGLNVDSFREKFCAGCPPPffklaflccdlDPEKRP 256
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
146-322 2.34e-05

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 46.05  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  146 VIFITEYMSSGSLKQFLKKtkKNHKTMNEKAWK-RWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNG------LIKI 218
Cdd:cd14208  76 SIMVQEFVCHGALDLYLKK--QQQKGPVAISWKlQVVKQLAYALNYLE--DKQLVHGNVSAKKVLLSREGdkgsppFIKL 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  219 GS--VAPDTINNHVKTCReeqknLHFFAPE-YGEVTNVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAISSAIQLL 295
Cdd:cd14208 152 SDpgVSIKVLDEELLAER-----IPWVAPEcLSDPQNLALEADKWGFGATLWEIF------SGGHMPLSALDPSKKLQFY 220
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7019333  296 EDPLQ---------REFIQKCLQSEPARRPTARELL 322
Cdd:cd14208 221 NDRKQlpaphwielASLIQQCMSYNPLLRPSFRAII 256
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
124-270 2.36e-05

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: 46.11  E-value: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFhkYWADIKENKA--RVIFITEYMSSGSLKQFLKKTkknhkTMNEKAWKRWCTQILSALSYLHS------CD 195
Cdd:cd14056  46 LRHENILGF--IAADIKSTGSwtQLWLITEYHEHGSLYDYLQRN-----TLDTEEALRLAYSAASGLAHLHTeivgtqGK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  196 PPIIHGNLTCDTIFIQHNGLIKIG------------SVAPDTINNHVKTCReeqknlhFFAPEYGEVT-NVTT-----AV 257
Cdd:cd14056 119 PAIAHRDLKSKNILVKRDGTCCIAdlglavrydsdtNTIDIPPNPRVGTKR-------YMAPEVLDDSiNPKSfesfkMA 191
                       170
                ....*....|...
gi 7019333  258 DIYSFGMCALEMA 270
Cdd:cd14056 192 DIYSFGLVLWEIA 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
120-317 2.62e-05

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: 46.19  E-value: 2.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  120 NLIQ-LEHLNIVKFhkYWADIKENKarVIFITEYMSSGSLKQFLkKTKKNHKTMNEKAWKrWCTQILSALSYLHSCDppI 198
Cdd:cd05072  54 NLMKtLQHDKLVRL--YAVVTKEEP--IYIITEYMAKGSLLDFL-KSDEGGKVLLPKLID-FSAQIAEGMAYIERKN--Y 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVL-EIQ 275
Cdd:cd05072 126 IHRDLRAANVLVSESLMCKIADFGlARVIEDNEYTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYgKIP 205
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7019333  276 GNGESSYVPQEAISSAIQL--LED-PLQ-REFIQKCLQSEPARRPT 317
Cdd:cd05072 206 YPGMSNSDVMSALQRGYRMprMENcPDElYDIMKTCWKEKAEERPT 251
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
180-327 3.19e-05

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: 45.77  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  180 WCTQ-ILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVD 258
Cdd:cd13995 100 WVTKhVLKGLDFLHSKN--IIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYVPKDLRGTEIYMSPEVILCRGHNTKAD 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  259 IYSFGMCALEMAvleiqgNGESSYV---PQEAISSAIQL-------LED------PLQREFIQKCLQSEPARRPTARELL 322
Cdd:cd13995 178 IYSLGATIIHMQ------TGSPPWVrryPRSAYPSYLYIihkqappLEDiaqdcsPAMRELLEAALERNPNHRSSAAELL 251

                ....*
gi 7019333  323 FHPAL 327
Cdd:cd13995 252 KHEAL 256
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
110-324 3.23e-05

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: 45.69  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWADiKENkarvIFI-TEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSAL 188
Cdd:cd14189  44 QREKIVNEIELHRDLHHKHVVKFSHHFED-AEN----IYIfLELCSRKSLAHIWKA----RHTLLEPEVRYYLKQIISGL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSVApdtINNHVKTCREEQKNL----HFFAPEYGEVTNVTTAVDIYSFG- 263
Cdd:cd14189 115 KYLH--LKGILHRDLKLGNFFINENMELKVGDFG---LAARLEPPEQRKKTIcgtpNYLAPEVLLRQGHGPESDVWSLGc 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  264 -----MCA---LEMAVLeiqgngESSYVPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELLFH 324
Cdd:cd14189 190 vmytlLCGnppFETLDL------KETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
181-335 3.34e-05

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 44.70  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     181 CTQILSALSYLHSCDPPiihgnltcDTIFIQHNGLIKI-GSVAPDTINNHvktcREEQknlHFFAPEYGEVTNVTTAVDI 259
Cdd:smart00750  23 CLQCLGALRELHRQAKS--------GNILLTWDGLLKLdGSVAFKTPEQS----RPDP---YFMAPEVIQGQSYTEKADI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333     260 YSFGMCALEMA--------------VLEIQGNG-----ESSYVPQEAISSAIQLledplqREFIQKCLQSEPARRPTARE 320
Cdd:smart00750  88 YSLGITLYEALdyelpyneerelsaILEILLNGmpaddPRDRSNLEGVSAARSF------EDFMRLCASRLPQRREAANH 161
                          170
                   ....*....|....*
gi 7019333     321 LLFHPALFEVPSLKL 335
Cdd:smart00750 162 YLAHCRALFAETLEL 176
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
109-322 3.85e-05

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: 45.26  E-value: 3.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVravfdnLIQLEHLNIVKFHKYWAdikenKARVIFI-TEYMSSGSLKQFLKKTKKnHKTMNEKAwkRWCTQILSA 187
Cdd:cd05113  47 IEEAKV------MMNLSHEKLVQLYGVCT-----KQRPIFIiTEYMANGCLLNYLREMRK-RFQTQQLL--EMCKDVCEA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  188 LSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGS------VAPDTINNHVKTcreeQKNLHFFAPEYGEVTNVTTAVDIYS 261
Cdd:cd05113 113 MEYLES--KQFLHRDLAARNCLVNDQGVVKVSDfglsryVLDDEYTSSVGS----KFPVRWSPPEVLMYSKFSSKSDVWA 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  262 FGMCALEMAVL-----EIQGNGESSyvpqEAISSAIQLLEDPLQREFIQK----CLQSEPARRPTARELL 322
Cdd:cd05113 187 FGVLMWEVYSLgkmpyERFTNSETV----EHVSQGLRLYRPHLASEKVYTimysCWHEKADERPTFKILL 252
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
122-276 4.23e-05

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone 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. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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 BMPR1a, 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 BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 45.42  E-value: 4.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  122 IQLEHLNIVKFhkYWADIKENKA--RVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCtqilsALSYLHS------ 193
Cdd:cd14220  44 VLMRHENILGF--IAADIKGTGSwtQLYLITDYHENGSLYDFLKCTTLDTRALLKLAYSAAC-----GLCHLHTeiygtq 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  194 CDPPIIHGNLTCDTIFIQHNGLIKIGSVA------PDT------INNHVKTCReeqknlhFFAPEYGEVT------NVTT 255
Cdd:cd14220 117 GKPAIAHRDLKSKNILIKKNGTCCIADLGlavkfnSDTnevdvpLNTRVGTKR-------YMAPEVLDESlnknhfQAYI 189
                       170       180
                ....*....|....*....|.
gi 7019333  256 AVDIYSFGMCALEMAVLEIQG 276
Cdd:cd14220 190 MADIYSFGLIIWEMARRCVTG 210
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
145-269 5.54e-05

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: 45.38  E-value: 5.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  145 RVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--VA 222
Cdd:cd05595  69 RLCFVMEYANGGELFFHLSR----ERVFTEDRARFYGAEIVSALEYLHSRD--VVYRDIKLENLMLDKDGHIKITDfgLC 142
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7019333  223 PDTINNHVkTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd05595 143 KEGITDGA-TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 188
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
158-325 5.57e-05

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: 45.23  E-value: 5.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  158 LKQFLKKTkkNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNG-----LIKIGSvapdtinnhvkT 232
Cdd:cd14210 101 LYELLKSN--NFQGLSLSLIRKFAKQILQALQFLHKLN--IIHCDLKPENILLKQPSkssikVIDFGS-----------S 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  233 CREEQKnLH------FF-APE------YGevtnvtTAVDIYSFGmCAL-EMA-----------------VLEIQG----- 276
Cdd:cd14210 166 CFEGEK-VYtyiqsrFYrAPEvilglpYD------TAIDMWSLG-CILaELYtgyplfpgeneeeqlacIMEVLGvppks 237
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  277 ---NG-------ESSYVPQEAISSAIQLL-------------EDPLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14210 238 lidKAsrrkkffDSNGKPRPTTNSKGKKRrpgskslaqvlkcDDPSFLDFLKKCLRWDPSERMTPEEALQHP 309
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
146-317 6.29e-05

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: 45.06  E-value: 6.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  146 VIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwkRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVA-PD 224
Cdd:cd05069  81 IYIVTEFMGKGSLLDFLKEGDGKYLKLPQLV--DMAAQIADGMAYIERMN--YIHRDLRAANILVGDNLVCKIADFGlAR 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMA--------------VLEIQGNGESSYVPQEAIS 289
Cdd:cd05069 157 LIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtkgrvpypgmvnreVLEQVERGYRMPCPQGCPE 236
                       170       180
                ....*....|....*....|....*...
gi 7019333  290 SAiqlledplqREFIQKCLQSEPARRPT 317
Cdd:cd05069 237 SL---------HELMKLCWKKDPDERPT 255
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
105-317 6.79e-05

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: 44.63  E-value: 6.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  105 KNYKLQEEKVRAVFD--NLIQ-LEHLNIVKFHKYwadikENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwkRWC 181
Cdd:cd05073  41 KTMKPGSMSVEAFLAeaNVMKtLQHDKLVKLHAV-----VTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLI--DFS 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  182 TQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDI 259
Cdd:cd05073 114 AQIAEGMAFIEQRN--YIHRDLRAANILVSASLVCKIADFGlARVIEDNEYTAREGAKfPIKWTAPEAINFGSFTIKSDV 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  260 YSFGMCalemaVLEIQGNGESSYvPQEAISSAIQLLED--PLQR---------EFIQKCLQSEPARRPT 317
Cdd:cd05073 192 WSFGIL-----LMEIVTYGRIPY-PGMSNPEVIRALERgyRMPRpencpeelyNIMMRCWKNRPEERPT 254
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
123-322 7.32e-05

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: 44.65  E-value: 7.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFhkywADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKawKRWCTQILSALSYLHScdPPIIHGN 202
Cdd:cd05039  56 TLRHPNLVQL----LGVVLEGNGLYIVTEYMAKGSLVDYLRSRGRAVITRKDQ--LGFALDVCEGMEYLES--KKFVHRD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHNGLIKIGSVApdtinnhvkTCREEQKNLH-------FFAPEYGEVTNVTTAVDIYSFGmcalemaVL--E 273
Cdd:cd05039 128 LAARNVLVSEDNVAKVSDFG---------LAKEASSNQDggklpikWTAPEALREKKFSTKSDVWSFG-------ILlwE 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  274 IQGNGESSY--VPQEAISSAIQL---LEDPLQ-----REFIQKCLQSEPARRPTARELL 322
Cdd:cd05039 192 IYSFGRVPYprIPLKDVVPHVEKgyrMEAPEGcppevYKVMKNCWELDPAKRPTFKQLR 250
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
138-325 8.30e-05

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: 44.50  E-value: 8.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  138 DIKENKARVIFITEYMSSGSL--KQFLKKTkknhktMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGL 215
Cdd:cd14107  65 DQFETRKTLILILELCSSEELldRLFLKGV------VTEAEVKLYIQQVLEGIGYLHGMN--ILHLDIKPDNILMVSPTR 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  216 --IKIGSVApdtINNHVKTCREEQKNL---HFFAPEYGEVTNVTTAVDIYSFGMCAL-------------EMAVLEIQGN 277
Cdd:cd14107 137 edIKICDFG---FAQEITPSEHQFSKYgspEFVAPEIVHQEPVSAATDIWALGVIAYlsltchspfagenDRATLLNVAE 213
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 7019333  278 GESSYVPQEAISsaiqLLEDPlqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14107 214 GVVSWDTPEITH----LSEDA--KDFIKRVLQPDPEKRPSASECLSHE 255
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
120-325 8.52e-05

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: 44.44  E-value: 8.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  120 NLIQL--EHLNIVKFHKYWADIKENKARVIFITEYMSSgSLKQFLKKTKK-NHKTMNEKAWKRWCTQILSALSYLHScdP 196
Cdd:cd07837  52 SLLQMlsQSIYIVRLLDVEHVEENGKPLLYLVFEYLDT-DLKKFIDSYGRgPHNPLPAKTIQSFMYQLCKGVAHCHS--H 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  197 PIIHGNLTCDTIFI-QHNGLIKIGSVA-PDTINNHVKTCREEQKNLHFFAPE--YGEvTNVTTAVDIYSFGMCALEMAVL 272
Cdd:cd07837 129 GVMHRDLKPQNLLVdKQKGLLKIADLGlGRAFTIPIKSYTHEIVTLWYRAPEvlLGS-THYSTPVDMWSVGCIFAEMSRK 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  273 EIQGNGES---------------------------------SYVPQEaISSAIQLLEdPLQREFIQKCLQSEPARRPTAR 319
Cdd:cd07837 208 QPLFPGDSelqqllhifrllgtpneevwpgvsklrdwheypQWKPQD-LSRAVPDLE-PEGVDLLTKMLAYDPAKRISAK 285

                ....*.
gi 7019333  320 ELLFHP 325
Cdd:cd07837 286 AALQHP 291
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
123-322 9.03e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   123 QLEHLNIVKFhkyWADIKENKARVIfITEYMSSGSLKQFLkktkknhktmNEKAWKR---WCTQILSALSYLH-SCDPPI 198
Cdd:PLN00113 739 KLQHPNIVKL---IGLCRSEKGAYL-IHEYIEGKNLSEVL----------RNLSWERrrkIAIGIAKALRFLHcRCSPAV 804
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   199 IHGNLTCDTIFIQHNGLIKIGSVAPDTInnhvktCREEQKNLH--FFAPEYGEVTNVTTAVDIYSFGMCALEM------A 270
Cdd:PLN00113 805 VVGNLSPEKIIIDGKDEPHLRLSLPGLL------CTDTKCFISsaYVAPETRETKDITEKSDIYGFGLILIELltgkspA 878
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333   271 VLEIQGNGE----SSYVPQEA-----ISSAIQLLEDPLQREFIQ------KCLQSEPARRPTARELL 322
Cdd:PLN00113 879 DAEFGVHGSivewARYCYSDChldmwIDPSIRGDVSVNQNEIVEvmnlalHCTATDPTARPCANDVL 945
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
84-303 9.43e-05

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 45.03  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333    84 LAMDTEEGVEV--VWNEVQFSERKNYKLQeekvravfdnliQLEHLNIV--KFHKYWADIKENKARVIF--ITEYMSSgS 157
Cdd:PTZ00036  86 ICIDTSEKVAIkkVLQDPQYKNRELLIMK------------NLNHINIIflKDYYYTECFKKNEKNIFLnvVMEFIPQ-T 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   158 LKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHN----GLIKIGSvapdtinnhVKTC 233
Cdd:PTZ00036 153 VHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHS--KFICHRDLKPQNLLIDPNthtlKLCDFGS---------AKNL 221
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333   234 REEQKNLHFF------APEYG-EVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYvpqEAISSAIQLLEDPLQREF 303
Cdd:PTZ00036 222 LAGQRSVSYIcsrfyrAPELMlGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSV---DQLVRIIQVLGTPTEDQL 295
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
149-317 9.60e-05

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: 44.26  E-value: 9.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKKNHKTMnekAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIG----SVAPD 224
Cdd:cd05040  75 VTELAPLGSLLDRLRKDQGHFLIS---TLCDYAVQIANGMAYLES--KRFIHRDLAARNILLASKDKVKIGdfglMRALP 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNHVKTcrEEQKNLHFF--APEYGEVTNVTTAVDIYSFGMCALEMAVleiqgNGESSYV----PQ--EAISSAIQLLE 296
Cdd:cd05040 150 QNEDHYVM--QEHRKVPFAwcAPESLKTRKFSHASDVWMFGVTLWEMFT-----YGEEPWLglngSQilEKIDKEGERLE 222
                       170       180
                ....*....|....*....|....*.
gi 7019333  297 DP--LQREFIQ---KCLQSEPARRPT 317
Cdd:cd05040 223 RPddCPQDIYNvmlQCWAHKPADRPT 248
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
120-317 1.01e-04

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: 44.11  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  120 NLI-QLEHLNIVKFHKYwadikENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwkRWCTQILSALSYLHSCDppI 198
Cdd:cd05067  54 NLMkQLQHQRLVRLYAV-----VTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLL--DMAAQIAEGMAFIEERN--Y 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCalemaVLEIQG 276
Cdd:cd05067 125 IHRDLRAANILVSDTLSCKIADFGlARLIEDNEYTAREGAKfPIKWTAPEAINYGTFTIKSDVWSFGIL-----LTEIVT 199
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019333  277 NGESSYvPQEAISSAIQLLED----------PLQ-REFIQKCLQSEPARRPT 317
Cdd:cd05067 200 HGRIPY-PGMTNPEVIQNLERgyrmprpdncPEElYQLMRLCWKERPEDRPT 250
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
149-321 1.28e-04

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 43.95  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKKnhKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS------VA 222
Cdd:cd05052  80 ITEFMPYGNLLDYLRECNR--EELNAVVLLYMATQIASAMEYLEKKN--FIHRDLAARNCLVGENHLVKVADfglsrlMT 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  223 PDTINNHVKTcreeQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLeiqgnGESSYvPQEAISSAIQLLED----- 297
Cdd:cd05052 156 GDTYTAHAGA----KFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATY-----GMSPY-PGIDLSQVYELLEKgyrme 225
                       170       180       190
                ....*....|....*....|....*....|
gi 7019333  298 ------PLQREFIQKCLQSEPARRPTAREL 321
Cdd:cd05052 226 rpegcpPKVYELMRACWQWNPSDRPSFAEI 255
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
81-324 1.29e-04

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: 44.24  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKENKARVIFitEYmSSGSLKQ 160
Cdd:cd06634  30 AVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEV-KFLQKLRHPNTIEYRGCY--LREHTAWLVM--EY-CLGSASD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKKNHKTMNEKAWKRWCTQilsALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI----NNHVKTCree 236
Cdd:cd06634 104 LLEVHKKPLQEVEIAAITHGALQ---GLAYLHSHN--MIHRDVKAGNILLTEPGLVKLGDFGSASImapaNSFVGTP--- 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  237 qknlHFFAPEY---GEVTNVTTAVDIYSFGMCALEMA-----VLEIQGNGESSYVPQEAiSSAIQLLE-DPLQREFIQKC 307
Cdd:cd06634 176 ----YWMAPEVilaMDEGQYDGKVDVWSLGITCIELAerkppLFNMNAMSALYHIAQNE-SPALQSGHwSEYFRNFVDSC 250
                       250
                ....*....|....*..
gi 7019333  308 LQSEPARRPTARELLFH 324
Cdd:cd06634 251 LQKIPQDRPTSDVLLKH 267
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
133-269 1.49e-04

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: 43.92  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  133 HKYWADIK---ENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIF 209
Cdd:cd05593  74 HPFLTSLKysfQTKDRLCFVMEYVNGGELFFHLSR----ERVFSEDRTRFYGAEIVSALDYLHS--GKIVYRDLKLENLM 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7019333  210 IQHNGLIKIGS--VAPDTINNhVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd05593 148 LDKDGHIKITDfgLCKEGITD-AATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 208
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
121-331 1.50e-04

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: 43.89  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHKYwadIKENKARVIF-ITEYmssgsLKQFLKKTKKNHKT-MNEKAWKRWCTQILSALSYLHscDPPI 198
Cdd:cd07845  60 LLNLRHPNIVELKEV---VVGKHLDSIFlVMEY-----CEQDLASLLDNMPTpFSESQVKCLMLQLLRGLQYLH--ENFI 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  199 IHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQKNLHFFAPE--YGeVTNVTTAVDIYSFGmCAL-------- 267
Cdd:cd07845 130 IHRDLKVSNLLLTDKGCLKIADFGlARTYGLPAKPMTPKVVTLWYRAPEllLG-CTTYTTAIDMWAVG-CILaellahkp 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  268 ------EMAVLE--IQGNGessyVPQEAI---------SSAIQLLEDP---LQREF----------IQKCLQSEPARRPT 317
Cdd:cd07845 208 llpgksEIEQLDliIQLLG----TPNESIwpgfsdlplVGKFTLPKQPynnLKHKFpwlseaglrlLNFLLMYDPKKRAT 283
                       250
                ....*....|....
gi 7019333  318 ARELLFHPALFEVP 331
Cdd:cd07845 284 AEEALESSYFKEKP 297
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
181-322 1.57e-04

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: 43.54  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  181 CTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQK---NLHFFAPE---YGEVTNVT 254
Cdd:cd14062  95 ARQTAQGMDYLHAKN--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQptgSILWMAPEvirMQDENPYS 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  255 TAVDIYSFGMCALEMAvleiqgngeSSYVPQEAISSAIQLL-----------------EDPLQ-REFIQKCLQSEPARRP 316
Cdd:cd14062 173 FQSDVYAFGIVLYELL---------TGQLPYSHINNRDQILfmvgrgylrpdlskvrsDTPKAlRRLMEDCIKFQRDERP 243

                ....*.
gi 7019333  317 TARELL 322
Cdd:cd14062 244 LFPQIL 249
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
98-321 1.62e-04

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: 43.80  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   98 EVQFSERKNYKLQEEKvravfdnLIQLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAW 177
Cdd:cd05092  45 EATESARQDFQREAEL-------LTVLQHQHIVRFYGVCTEGEP----LIMVFEYMRHGDLNRFLRSHGPDAKILDGGEG 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  178 KRW-----------CTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--VAPDTIN-NHVKTCREEQKNLHFF 243
Cdd:cd05092 114 QAPgqltlgqmlqiASQIASGMVYLASLH--FVHRDLATRNCLVGQGLVVKIGDfgMSRDIYStDYYRVGGRTMLPIRWM 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  244 APEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVpqEAISSAIQ--LLEDPLQ-----REFIQKCLQSEPARRP 316
Cdd:cd05092 192 PPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNT--EAIECITQgrELERPRTcppevYAIMQGCWQREPQQRH 269

                ....*
gi 7019333  317 TAREL 321
Cdd:cd05092 270 SIKDI 274
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
149-320 1.64e-04

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: 43.64  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKKnhkTMNEKAwkRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINN 228
Cdd:cd14027  69 VMEYMEKGNLMHVLKKVSV---PLSVKG--RIILEIIEGMAYLH--GKGVIHKDLKPENILVDNDFHIKIADLGLASFKM 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  229 HVKTCREEQK--------------NLHFFAPEYGEVTNV--TTAVDIYSFGMC---------ALEMAVLE-------IQG 276
Cdd:cd14027 142 WSKLTKEEHNeqrevdgtakknagTLYYMAPEHLNDVNAkpTEKSDVYSFAIVlwaifankePYENAINEdqiimciKSG 221
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 7019333  277 NGES-----SYVPQEAISsaiqlledplqreFIQKCLQSEPARRPTARE 320
Cdd:cd14027 222 NRPDvdditEYCPREIID-------------LMKLCWEANPEARPTFPG 257
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
148-321 1.68e-04

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: 43.73  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  148 FITEYMSSGSLKQFLKKTKK--NHKTMNEKAWkrwctQILSALSYLHS--CdppiIHGNLTCDTIFIQHNGLIKIGSVAP 223
Cdd:cd05081  84 LVMEYLPSGCLRDFLQRHRArlDASRLLLYSS-----QICKGMEYLGSrrC----VHRDLAARNILVESEAHVKIADFGL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  224 DTI---NNHVKTCREE-QKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESS--------YVPQEAISSA 291
Cdd:cd05081 155 AKLlplDKDYYVVREPgQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAeflrmmgcERDVPALCRL 234
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7019333  292 IQLLED----------PLQ-REFIQKCLQSEPARRPTAREL 321
Cdd:cd05081 235 LELLEEgqrlpappacPAEvHELMKLCWAPSPQDRPSFSAL 275
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
146-317 1.87e-04

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: 43.37  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  146 VIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwkRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVA-PD 224
Cdd:cd14203  64 IYIVTEFMSKGSLLDFLKDGEGKYLKLPQLV--DMAAQIASGMAYIERMN--YIHRDLRAANILVGDNLVCKIADFGlAR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMA--------------VLEIQGNGESSYVPQEAIS 289
Cdd:cd14203 140 LIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtkgrvpypgmnnreVLEQVERGYRMPCPPGCPE 219
                       170       180
                ....*....|....*....|....*...
gi 7019333  290 SAIQLLEdplqrefiqKCLQSEPARRPT 317
Cdd:cd14203 220 SLHELMC---------QCWRKDPEERPT 238
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
146-317 1.90e-04

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. 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 Frk-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: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 43.16  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  146 VIFITEYMSSGSLKQFLKKTKKNHK--TMNEKAwkrwcTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--V 221
Cdd:cd05068  78 IYIITELMKHGSLLEYLQGKGRSLQlpQLIDMA-----AQVASGMAYLESQN--YIHRDLAARNVLVGENNICKVADfgL 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 APDTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCalemaVLEIQGNGESSYvPQEAISSAIQLLED--- 297
Cdd:cd05068 151 ARVIKVEDEYEAREGAKfPIKWTAPEAANYNRFSIKSDVWSFGIL-----LTEIVTYGRIPY-PGMTNAEVLQQVERgyr 224
                       170       180
                ....*....|....*....|....*...
gi 7019333  298 -------PLQ-REFIQKCLQSEPARRPT 317
Cdd:cd05068 225 mpcppncPPQlYDIMLECWKADPMERPT 252
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
108-325 2.03e-04

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: 43.31  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  108 KLQEEKVravfDNLIQLEHLNIVkfhkYWADIKENKARVIFITEYMSSGSLKQFLkktkkNHKTMNEKAWKRWCTQIL-S 186
Cdd:cd14097  45 KLLEREV----DILKHVNHAHII----HLEEVFETPKRMYLVMELCEDGELKELL-----LRKGFFSENETRHIIQSLaS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  187 ALSYLHSCDppIIHGNLTCDTIFIQHN---------------GL-IKIGSVAPDTINNHVKTcreeqknLHFFAPEYGEV 250
Cdd:cd14097 112 AVAYLHKND--IVHRDLKLENILVKSSiidnndklnikvtdfGLsVQKYGLGEDMLQETCGT-------PIYMAPEVISA 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  251 TNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSA-IQLLEDPLQR------EFIQKCLQSEPARRPTARELLF 323
Cdd:cd14097 183 HGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGdLTFTQSVWQSvsdaakNVLQQLLKVDPAHRMTASELLD 262

                ..
gi 7019333  324 HP 325
Cdd:cd14097 263 NP 264
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
102-321 2.13e-04

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: 43.07  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  102 SERKNYKLQEEKVravfdnLIQLEHLNIVKFhkywADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTmneKAWKRWC 181
Cdd:cd05085  34 QELKIKFLSEARI------LKQYDHPNIVKL----IGVCTQRQPIYIVMELVPGGDFLSFLRKKKDELKT---KQLVKFS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  182 TQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS--VAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDI 259
Cdd:cd05085 101 LDAAAGMAYLESKN--CIHRDLAARNCLVGENNALKISDfgMSRQEDDGVYSSSGLKQIPIKWTAPEALNYGRYSSESDV 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7019333  260 YSFGMCALEMAVLEI-QGNGESSYVPQEAIS-----SAIQLLEDPLQReFIQKCLQSEPARRPTAREL 321
Cdd:cd05085 179 WSFGILLWETFSLGVcPYPGMTNQQAREQVEkgyrmSAPQRCPEDIYK-IMQRCWDYNPENRPKFSEL 245
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
124-325 2.24e-04

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: 43.05  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDppIIHGNL 203
Cdd:cd14010  51 LKHPNVLKFYEWY----ETSNHLWLVVEYCTGGDLETLLRQDGN----LPESSVRKFGRDLVRGLHYIHSKG--IIYCDL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  204 TCDTIFIQHNGLIK-----------------IGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd14010 121 KPSNILLDGNGTLKlsdfglarregeilkelFGQFSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVL 200
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333  267 LEMAVleiqGNgessyvPQEAISSAIQLLEDPLQREF------------------IQKCLQSEPARRPTARELLFHP 325
Cdd:cd14010 201 YEMFT----GK------PPFVAESFTELVEKILNEDPpppppkvsskpspdfkslLKGLLEKDPAKRLSWDELVKHP 267
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
95-327 2.35e-04

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: 43.09  E-value: 2.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   95 VWnEVQFSER----KNYKLQEEKV----RAVFDNLIqLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQFLKKtk 166
Cdd:cd14053  11 VW-KAQYLNRlvavKIFPLQEKQSwlteREIYSLPG-MKHENILQFIGAEKHGESLEAEYWLITEFHERGSLCDYLKG-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  167 knhktmNEKAWK---RWCTQILSALSYLHS--------CDPPIIH-----------GNLTCdtiFIQHNGLIKIGSVAPD 224
Cdd:cd14053  87 ------NVISWNelcKIAESMARGLAYLHEdipatnggHKPSIAHrdfksknvllkSDLTA---CIADFGLALKFEPGKS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 TINNH--VKTCReeqknlhFFAPEYGE-VTNVTT----AVDIYSFGMCALEMA--VLEIQGNGESSYVPQEAISSAIQLL 295
Cdd:cd14053 158 CGDTHgqVGTRR-------YMAPEVLEgAINFTRdaflRIDMYAMGLVLWELLsrCSVHDGPVDEYQLPFEEEVGQHPTL 230
                       250       260       270
                ....*....|....*....|....*....|...
gi 7019333  296 EDpLQREFIQKCLqseparRPTAREL-LFHPAL 327
Cdd:cd14053 231 ED-MQECVVHKKL------RPQIRDEwRKHPGL 256
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
123-268 2.36e-04

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: 43.37  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFhkywADIKENKARVI-----FITEYMSSGSLKQFLKKtKKNHKTMNEKAWKRWCTQILSALSYLHscDPP 197
Cdd:cd14039  47 KLNHPNVVKA----CDVPEEMNFLVndvplLAMEYCSGGDLRKLLNK-PENCCGLKESQVLSLLSDIGSGIQYLH--ENK 119
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019333  198 IIHGNLTCDTIFIQHNG------LIKIGsVAPDTinNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALE 268
Cdd:cd14039 120 IIHRDLKPENIVLQEINgkivhkIIDLG-YAKDL--DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
109-326 2.75e-04

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: 42.63  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKnhkTMNEKAWKRWCTQILSAL 188
Cdd:cd05112  41 MSEEDFIEEAEVMMKLSHPKLVQLY----GVCLEQAPICLVFEFMEHGCLSDYLRTQRG---LFSAETLLGMCLDVCEGM 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI--NNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd05112 114 AYLEEAS--VIHRDLAARNCLVGENQVVKVSDFGMTRFvlDDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLM 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019333  267 LEM-----AVLEIQGNGESSyvpqEAISSAIQLLEDPLQR----EFIQKCLQSEPARRPTARELLFHPA 326
Cdd:cd05112 192 WEVfsegkIPYENRSNSEVV----EDINAGFRLYKPRLASthvyEIMNHCWKERPEDRPSFSLLLRQLA 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
124-325 2.76e-04

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: 42.63  E-value: 2.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  124 LEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNL 203
Cdd:cd14081  58 IEHPNVLKLY----DVYENKKYLYLVLEYVSGGELFDYLVK----KGRLTEKEARKFFRQIISALDYCHSHS--ICHRDL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  204 TCDTIFIQHNGLIKIG-----SVAPDtiNNHVKT-CreeqKNLHFFAPE--YGEVTNVTTAvDIYSFGMCALEMAV---- 271
Cdd:cd14081 128 KPENLLLDEKNNIKIAdfgmaSLQPE--GSLLETsC----GSPHYACPEviKGEKYDGRKA-DIWSCGVILYALLVgalp 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7019333  272 ---------LEIQGNGEssYVPQEAISSAIQLLedplqrefIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14081 201 fdddnlrqlLEKVKRGV--FHIPHFISPDAQDL--------LRRMLEVNPEKRITIEEIKKHP 253
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
110-315 2.77e-04

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: 42.81  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFhkYWADIKENKARVIFitEYMSSGSLKQFLKKTKKNHKTMNekawKRWCTQILSALS 189
Cdd:cd05612  44 QEQHVHNEKRVLKEVSHPFIIRL--FWTEHDQRFLYMLM--EYVPGGELFSYLRNSGRFSNSTG----LFYASEIVCALE 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHSCDppIIHGNLTCDTIFIQHNGLIKIGSV--APDTINNHVKTCREEQknlhFFAPEYGEVTNVTTAVDIYSFGMCAL 267
Cdd:cd05612 116 YLHSKE--IVYRDLKPENILLDKEGHIKLTDFgfAKKLRDRTWTLCGTPE----YLAPEVIQSKGHNKAVDWWALGILIY 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7019333  268 EMAVLEIQGNGESSY-VPQEAISSAIQLLE--DPLQREFIQKCLQSEPARR 315
Cdd:cd05612 190 EMLVGYPPFFDDNPFgIYEKILAGKLEFPRhlDLYAKDLIKKLLVVDRTRR 240
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
149-324 2.99e-04

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: 42.65  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKTKKNHKTMNEKAwkRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGsvapD---- 224
Cdd:cd05034  68 VTELMSKGSLLDYLRTGEGRALRLPQLI--DMAAQIASGMAYLESRN--YIHRDLAARNILVGENNVCKVA----Dfgla 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 -TINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGmcalemaVL--EIQGNGEssyVPQEAISSA--IQLLE-- 296
Cdd:cd05034 140 rLIEDDEYTAREGAKfPIKWTAPEAALYGRFTIKSDVWSFG-------ILlyEIVTYGR---VPYPGMTNRevLEQVErg 209
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7019333  297 ----------DPLQrEFIQKCLQSEPARRPTArELLFH 324
Cdd:cd05034 210 yrmpkppgcpDELY-DIMLQCWKKEPEERPTF-EYLQS 245
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
123-316 3.06e-04

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 42.60  E-value: 3.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAwkrWCTQILSALSYLhsCDPPIIHGN 202
Cdd:cd05064  62 QFDHSNIVRLE----GVITRGNTMMIVTEYMSNGALDSFLRKHEGQLVAGQLMG---MLPGLASGMKYL--SEMGYVHKG 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHNGLIKIGSVAP---DTINNHVKTCREEQKNLhFFAPEYGEVTNVTTAVDIYSFGmcaleMAVLEIQGNGE 279
Cdd:cd05064 133 LAAHKVLVNSDLVCKISGFRRlqeDKSEAIYTTMSGKSPVL-WAAPEAIQYHHFSSASDVWSFG-----IVMWEVMSYGE 206
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 7019333  280 SSYVPQEAiSSAIQLLED-----------PLQREFIQKCLQSEPARRP 316
Cdd:cd05064 207 RPYWDMSG-QDVIKAVEDgfrlpaprncpNLLHQLMLDCWQKERGERP 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
111-325 3.08e-04

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: 42.64  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSY 190
Cdd:cd14079  46 EEKIRREIQILKLFRHPHIIRLY----EVIETPTDIFMVMEYVSGGELFDYIVQ----KGRLSEDEARRFFQQIISGVEY 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  191 LHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTInnhvktcreeQKNLHFF-----APEYG--EVTN----VTTAVDI 259
Cdd:cd14079 118 CHR--HMVVHRDLKPENLLLDSNMNVKIADFGLSNI----------MRDGEFLktscgSPNYAapEVISgklyAGPEVDV 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7019333  260 YSFG--MCALEMAVLEIqgngESSYVPQ--EAISSAIQLLED---PLQREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14079 186 WSCGviLYALLCGSLPF----DDEHIPNlfKKIKSGIYTIPShlsPGARDLIKRMLVVDPLKRITIPEIRQHP 254
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
120-270 3.25e-04

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, 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 ACVR1 and ALK1, 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 ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 42.81  E-value: 3.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  120 NLIQLEHLNIVKFhkYWADI--KENKARVIFITEYMSSGSLKQFLKKTKKNHKTMnekawKRWCTQILSALSYLHS---- 193
Cdd:cd14142  52 NTVLLRHENILGF--IASDMtsRNSCTQLWLITHYHENGSLYDYLQRTTLDHQEM-----LRLALSAASGLVHLHTeifg 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  194 --CDPPIIHGNLTCDTIFIQHNGLIKIG--------SVAPDTI----NNHVKTCReeqknlhFFAPEYGEVTNVTTA--- 256
Cdd:cd14142 125 tqGKPAIAHRDLKSKNILVKSNGQCCIAdlglavthSQETNQLdvgnNPRVGTKR-------YMAPEVLDETINTDCfes 197
                       170
                ....*....|....*..
gi 7019333  257 ---VDIYSFGMCALEMA 270
Cdd:cd14142 198 ykrVDIYAFGLVLWEVA 214
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
109-317 3.63e-04

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: 42.75  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  109 LQEEKVravfdnLIQLEHLNIVKFhkyWADIKENKarVIFITEYMSSGSLKQFLKktKKNHKTMNEKAWKRWCTQILSAL 188
Cdd:cd05071  52 LQEAQV------MKKLRHEKLVQL---YAVVSEEP--IYIVTEYMSKGSLLDFLK--GEMGKYLRLPQLVDMAAQIASGM 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  189 SYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVA-PDTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCA 266
Cdd:cd05071 119 AYVERMN--YVHRDLRAANILVGENLVCKVADFGlARLIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILL 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  267 LEMA--------------VLEIQGNGESSYVPQEAISSAiqlledplqREFIQKCLQSEPARRPT 317
Cdd:cd05071 197 TELTtkgrvpypgmvnreVLDQVERGYRMPCPPECPESL---------HDLMCQCWRKEPEERPT 252
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
81-324 5.12e-04

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: 42.34  E-value: 5.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333   81 SAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVfDNLIQLEHLNIVKFHKYWadIKENKARVIFitEYmSSGSLKQ 160
Cdd:cd06635  40 AVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEV-KFLQRIKHPNSIEYKGCY--LREHTAWLVM--EY-CLGSASD 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  161 FLKKTKKNHKTMNEKAWKRWCTQilsALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVAPDTI----NNHVKTCree 236
Cdd:cd06635 114 LLEVHKKPLQEIEIAAITHGALQ---GLAYLHSHN--MIHRDIKAGNILLTEPGQVKLADFGSASIaspaNSFVGTP--- 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  237 qknlHFFAPEY---GEVTNVTTAVDIYSFGMCALEMA-----VLEIQGNGESSYVPQEAiSSAIQLLE-DPLQREFIQKC 307
Cdd:cd06635 186 ----YWMAPEVilaMDEGQYDGKVDVWSLGITCIELAerkppLFNMNAMSALYHIAQNE-SPTLQSNEwSDYFRNFVDSC 260
                       250
                ....*....|....*..
gi 7019333  308 LQSEPARRPTARELLFH 324
Cdd:cd06635 261 LQKIPQDRPTSEELLKH 277
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
123-316 5.99e-04

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: 41.88  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCT---QILSALSYLH---SCDP 196
Cdd:cd05063  62 QFSHHNIIRLEGVVTKFKP----AMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAagmKYLSDMNYVHrdlAARN 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  197 PIIHGNLTCDtifIQHNGLIKIGSVAPDTinnhVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGmcaleMAVLEIQG 276
Cdd:cd05063 138 ILVNSNLECK---VSDFGLSRVLEDDPEG----TYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFG-----IVMWEVMS 205
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 7019333  277 NGESSY--VPQEAISSAIQ---LLEDPLQ-----REFIQKCLQSEPARRP 316
Cdd:cd05063 206 FGERPYwdMSNHEVMKAINdgfRLPAPMDcpsavYQLMLQCWQQDRARRP 255
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
123-316 6.09e-04

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: 41.78  E-value: 6.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  123 QLEHLNIVKFHKYWADIKEnkarVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRwctQILSALSYLhsCDPPIIHGN 202
Cdd:cd05066  61 QFDHPNIIHLEGVVTRSKP----VMIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLR---GIASGMKYL--SDMGYVHRD 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  203 LTCDTIFIQHN--------GLIKIGSVAPDTinnhVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGmcaleMAVLEI 274
Cdd:cd05066 132 LAARNILVNSNlvckvsdfGLSRVLEDDPEA----AYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYG-----IVMWEV 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7019333  275 QGNGESSY---VPQEAISSAIQ--LLEDPLQ-----REFIQKCLQSEPARRP 316
Cdd:cd05066 203 MSYGERPYwemSNQDVIKAIEEgyRLPAPMDcpaalHQLMLDCWQKDRNERP 254
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
149-322 6.61e-04

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: 41.83  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKtkknhKTM-NEKAWK---RWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPD 224
Cdd:cd14026  75 VTEYMTNGSLNELLHE-----KDIyPDVAWPlrlRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFHVKIADFGLS 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  225 T------INNHVKTCREEQKNLHFFAPEY---GEVTNVTTAVDIYSFGMCALEMAvleiqgngeSSYVPQEAISSAIQLL 295
Cdd:cd14026 150 KwrqlsiSQSRSSKSAPEGGTIIYMPPEEyepSQKRRASVKHDIYSYAIIMWEVL---------SRKIPFEEVTNPLQIM 220
                       170       180
                ....*....|....*....|....*..
gi 7019333  296 EDPLQREFIQKCLQSEPARRPTaRELL 322
Cdd:cd14026 221 YSVSQGHRPDTGEDSLPVDIPH-RATL 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
125-325 7.39e-04

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: 41.57  E-value: 7.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  125 EHLNIVKFhkYWADIKENKARVIFitEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDPpiIHGNLT 204
Cdd:cd06645  66 KHSNIVAY--FGSYLRRDKLWICM--EFCGGGSLQDIYHVTGP----LSESQIAYVSRETLQGLYYLHSKGK--MHRDIK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  205 CDTIFIQHNGLIKIGSVApdtINNHVKTCREEQKNL----HFFAPEYGEVT---NVTTAVDIYSFGMCALEMAVLE---- 273
Cdd:cd06645 136 GANILLTDNGHVKLADFG---VSAQITATIAKRKSFigtpYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQppmf 212
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  274 -------IQGNGESSYVPQEaissaiqlLEDPLQ-----REFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd06645 213 dlhpmraLFLMTKSNFQPPK--------LKDKMKwsnsfHHFVKMALTKNPKKRPTAEKLLQHP 268
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
115-325 1.18e-03

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: 40.73  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  115 RAVFDNLIQ-LEHLNIVKfHKYWADIKE---NKARVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSY 190
Cdd:cd14121  36 KASTENLLTeIELLKKLK-HPHIVELKDfqwDEEHIYLIMEYCSGGDLSRFIRS----RRTLPESTVRRFLQQLASALQF 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  191 LHSCDppIIHGNLTCDTIFI--QHNGLIKIGSVApdtINNHVKTcREEQKNLH----FFAPEYGEVTNVTTAVDIYSFGM 264
Cdd:cd14121 111 LREHN--ISHMDLKPQNLLLssRYNPVLKLADFG---FAQHLKP-NDEAHSLRgsplYMAPEMILKKKYDARVDLWSVGV 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  265 ----C----------ALEMAVLEIQGNGessyvPQEaISSAIQLLEDPlqREFIQKCLQSEPARRPTARELLFHP 325
Cdd:cd14121 185 ilyeClfgrapfasrSFEELEEKIRSSK-----PIE-IPTRPELSADC--RDLLLRLLQRDPDRRISFEEFFAHP 251
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
122-270 1.44e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone 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. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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 BMPR1b, 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 BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 40.80  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  122 IQLEHLNIVKFhkYWADIKENKA--RVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRwctqiLSALSYLHS------ 193
Cdd:cd14219  54 VLMRHENILGF--IAADIKGTGSwtQLYLITDYHENGSLYDYLKSTTLDTKAMLKLAYSS-----VSGLCHLHTeifstq 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  194 CDPPIIHGNLTCDTIFIQHNGLIKIGSVA------PDT------INNHVKTCReeqknlhFFAPEYGEVT------NVTT 255
Cdd:cd14219 127 GKPAIAHRDLKSKNILVKKNGTCCIADLGlavkfiSDTnevdipPNTRVGTKR-------YMPPEVLDESlnrnhfQSYI 199
                       170
                ....*....|....*
gi 7019333  256 AVDIYSFGMCALEMA 270
Cdd:cd14219 200 MADMYSFGLILWEVA 214
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
128-315 1.45e-03

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: 40.61  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  128 NIVKFHKYWadIKENKarVIFITEYMSSGSLKQFLKK---TKKNHK---------------TMNEKAWKRWCTQILSALS 189
Cdd:cd05576  52 NMVCLRKYI--ISEES--VFLVLQHAEGGKLWSYLSKflnDKEIHQlfadlderlaaasrfYIPEECIQRWAAEMVVALD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  190 YLHscDPPIIHGNLTCDTIFIQHNGLIKI------GSVAPdtinnhvKTCREEQKNLhFFAPEYGEVTNVTTAVDIYSFG 263
Cdd:cd05576 128 ALH--REGIVCRDLNPNNILLNDRGHIQLtyfsrwSEVED-------SCDSDAIENM-YCAPEVGGISEETEACDWWSLG 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7019333  264 MCALE----MAVLEIQGNGESS--------YVPQEAissaiqlledplqREFIQKCLQSEPARR 315
Cdd:cd05576 198 ALLFElltgKALVECHPAGINThttlnipeWVSEEA-------------RSLLQQLLQFNPTER 248
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
111-316 1.76e-03

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 40.25  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  111 EEKVRAVFDNLIQLEHLNIVKFhkyWADIKENKArVIFITEYMSSGSLKQFLKKTKknhkTMNEKAWKRW------CTQI 184
Cdd:cd14044  47 TEKQKIELNKLLQIDYYNLTKF---YGTVKLDTM-IFGVIEYCERGSLRDVLNDKI----SYPDGTFMDWefkisvMYDI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  185 LSALSYLHSCDPPIiHGNLTCDTIFIQHNGLIKIGSVAPDTInnhvktcREEQKNLhFFAPEYGEVTNVTTAVDIYSFGM 264
Cdd:cd14044 119 AKGMSYLHSSKTEV-HGRLKSTNCVVDSRMVVKITDFGCNSI-------LPPSKDL-WTAPEHLRQAGTSQKGDVYSYGI 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7019333  265 CALEM-----------------AVLEIQGN-GESSYVPQEAISSAiqlleDPLQRE---FIQKCLQSEPARRP 316
Cdd:cd14044 190 IAQEIilrketfytaacsdrkeKIYRVQNPkGMKPFRPDLNLESA-----GEREREvygLVKNCWEEDPEKRP 257
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
110-218 1.79e-03

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: 40.57  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLE----HLNIVKFHKYWADIKENK----ARVIFITEyMSSGSLKQFLKKtkknhktmNEKAWKRWC 181
Cdd:cd14036  37 EEEKNKAIIQEINFMKklsgHPNIVQFCSAASIGKEESdqgqAEYLLLTE-LCKGQLVDFVKK--------VEAPGPFSP 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 7019333  182 TQIL-------SALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKI 218
Cdd:cd14036 108 DTVLkifyqtcRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKL 151
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
149-321 1.85e-03

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: 40.17  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKktkkNHKTMNEKAWkRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINN 228
Cdd:cd14025  71 VMEYMETGSLEKLLA----SEPLPWELRF-RIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAKWNG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  229 HVKTCREEQK----NLHFFAPEYGEVTN--VTTAVDIYSFGMCALEMAVLEIQGNGES-----------------SYVPQ 285
Cdd:cd14025 146 LSHSHDLSRDglrgTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAGENnilhimvkvvkghrpslSPIPR 225
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7019333  286 EAISSAIQLLEdplqreFIQKCLQSEPARRPTAREL 321
Cdd:cd14025 226 QRPSECQQMIC------LMKRCWDQDPRKRPTFQDI 255
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
145-321 2.05e-03

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: 40.09  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  145 RVIFITEYMSSGSLKQFLKktkkNHK-TMNEKAWKRWCTQILSALSYLHscDPPIIHGNLTCDTIFIQHNGLIKIGS--V 221
Cdd:cd05057  82 QVQLITQLMPLGCLLDYVR----NHRdNIGSQLLLNWCVQIAKGMSYLE--EKRLVHRDLAARNVLVKTPNHVKITDfgL 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  222 AP--DTINNHVKTcrEEQK-NLHFFAPE---YGEVTNVTtavDIYSFGmcaleMAVLEIQGNGESSY--VPQEAISsaiQ 293
Cdd:cd05057 156 AKllDVDEKEYHA--EGGKvPIKWMALEsiqYRIYTHKS---DVWSYG-----VTVWELMTFGAKPYegIPAVEIP---D 222
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 7019333  294 LLE--DPLQREFI---------QKCLQSEPARRPTAREL 321
Cdd:cd05057 223 LLEkgERLPQPPIctidvymvlVKCWMIDAESRPTFKEL 261
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
121-325 2.13e-03

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: 39.89  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  121 LIQLEHLNIVKFHkywaDIKENKARVIFITEYMSSGSLKQFLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIH 200
Cdd:cd14108  52 LAELDHKSIVRFH----DAFEKRRVVIIVTELCHEELLERITKRP-----TVCESEVRSYMRQLLEGIEYLHQND--VLH 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  201 GNLTCDTIFIQHNGLIKIGSVapDTINNHVKTCREEQKNLH----FFAPEYGEVTNVTTAVDIYSFGMcaleMAVLEIQG 276
Cdd:cd14108 121 LDLKPENLLMADQKTDQVRIC--DFGNAQELTPNEPQYCKYgtpeFVAPEIVNQSPVSKVTDIWPVGV----IAYLCLTG 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  277 ----NGESSYVPQEAISSAIQLLEDP----LQRE---FIQKCLQSEPArRPTARELLFHP 325
Cdd:cd14108 195 ispfVGENDRTTLMNIRNYNVAFEESmfkdLCREakgFIIKVLVSDRL-RPDAEETLEHP 253
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
145-269 2.84e-03

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: 40.01  E-value: 2.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  145 RVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKIGSVApd 224
Cdd:cd05594  99 RLCFVMEYANGGELFFHLSR----ERVFSEDRARFYGAEIVSALDYLHS-EKNVVYRDLKLENLMLDKDGHIKITDFG-- 171
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  225 tinnhvkTCREEQKN----------LHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd05594 172 -------LCKEGIKDgatmktfcgtPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 219
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
148-269 2.92e-03

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 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: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 39.82  E-value: 2.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  148 FITEYMSSGSLKQFLKKTKKNHkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIG-------S 220
Cdd:cd14157  69 LIYPYMPNGSLQDRLQQQGGSH-PLPWEQRLSISLGLLKAVQHLHNFG--ILHGNIKSSNVLLDGNLLPKLGhsglrlcP 145
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 7019333  221 VAPDTINNHVKTcREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd14157 146 VDKKSVYTMMKT-KVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEI 193
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
101-321 3.97e-03

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC 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 TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 39.22  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  101 FSERKNYKLQEEKvravfdnLIQLEHLNIVKFHKYWADikenKARVIFITEYMSSGSLKQFLK------------KTKKN 168
Cdd:cd05094  48 LAARKDFQREAEL-------LTNLQHDHIVKFYGVCGD----GDPLIMVFEYMKHGDLNKFLRahgpdamilvdgQPRQA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  169 HKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGS--VAPDTIN-NHVKTCREEQKNLHFFAP 245
Cdd:cd05094 117 KGELGLSQMLHIATQIASGMVYLAS--QHFVHRDLATRNCLVGANLLVKIGDfgMSRDVYStDYYRVGGHTMLPIRWMPP 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  246 EYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSyvPQEAISSAIQ--LLEDPL-----QREFIQKCLQSEPARRPTA 318
Cdd:cd05094 195 ESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLS--NTEVIECITQgrVLERPRvcpkeVYDIMLGCWQREPQQRLNI 272

                ...
gi 7019333  319 REL 321
Cdd:cd05094 273 KEI 275
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
146-317 3.99e-03

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: 39.28  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  146 VIFITEYMSSGSLKQFLKKTKKnhKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQhNGLI-KIGSVA-P 223
Cdd:cd05070  78 IYIVTEYMSKGSLLDFLKDGEG--RALKLPNLVDMAAQVAAGMAYIERMN--YIHRDLRSANILVG-NGLIcKIADFGlA 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  224 DTINNHVKTCREEQK-NLHFFAPEYGEVTNVTTAVDIYSFGMCALEMA--------------VLEIQGNGESSYVPQEAI 288
Cdd:cd05070 153 RLIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVtkgrvpypgmnnreVLEQVERGYRMPCPQDCP 232
                       170       180
                ....*....|....*....|....*....
gi 7019333  289 SSAiqlledplqREFIQKCLQSEPARRPT 317
Cdd:cd05070 233 ISL---------HELMIHCWKKDPEERPT 252
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
149-321 4.99e-03

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: 38.70  E-value: 4.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  149 ITEYMSSGSLKQFLKKtkKNHKTMNEKAWKRWCTQILSALSYLHScdPPIIHGNLTCDTIFIQHN--------GLIKIGS 220
Cdd:cd05083  76 VMELMSKGNLVNFLRS--RGRALVPVIQLLQFSLDVAEGMEYLES--KKLVHRDLAARNILVSEDgvakisdfGLAKVGS 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  221 VAPDTINNHVK-TCREEQKNLHFfapeygevtnvTTAVDIYSFGMCalemaVLEIQGNGESSYvPQEAISSAIQLLEDPL 299
Cdd:cd05083 152 MGVDNSRLPVKwTAPEALKNKKF-----------SSKSDVWSYGVL-----LWEVFSYGRAPY-PKMSVKEVKEAVEKGY 214
                       170       180       190
                ....*....|....*....|....*....|...
gi 7019333  300 QRE-----------FIQKCLQSEPARRPTAREL 321
Cdd:cd05083 215 RMEppegcppdvysIMTSCWEAEPGKRPSFKKL 247
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
141-316 5.34e-03

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: 38.91  E-value: 5.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  141 ENKARVIFITEYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGS 220
Cdd:cd05592  66 QTESHLFFVMEYLNGGDLMFHIQQSGR----FDEDRARFYGAEIICGLQFLHSRG--IIYRDLKLDNVLLDREGHIKIAD 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  221 --VAPDTINNHVKT---CREEQknlhFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLE--IQGNGESS------------ 281
Cdd:cd05592 140 fgMCKENIYGENKAstfCGTPD----YIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQspFHGEDEDElfwsicndtphy 215
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7019333  282 --YVPQEAISSAIQLLE-DPLQREFIQKCLQSEPARRP 316
Cdd:cd05592 216 prWLTKEAASCLSLLLErNPEKRLGVPECPAGDIRDHP 253
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
126-322 6.06e-03

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: 38.87  E-value: 6.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  126 HLNIVKFHkywaDIKENKARVIFITEYMSSGSLkqFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTC 205
Cdd:cd13993  64 HPNIITLH----DVFETEVAIYIVLEYCPNGDL--FEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLG--IYHRDIKP 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  206 DTIFIQHNGL-IKIGSVAPDTINnhvKTCREEQKNLHFF-APE----YGEVTNV--TTAVDIYSFGMCALEMavleIQGN 277
Cdd:cd13993 136 ENILLSQDEGtVKLCDFGLATTE---KISMDFGVGSEFYmAPEcfdeVGRSLKGypCAAGDIWSLGIILLNL----TFGR 208
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7019333  278 GESSYVPQEAISSAIQLLED--------PLQREF---IQKCLQSEPARRPTARELL 322
Cdd:cd13993 209 NPWKIASESDPIFYDYYLNSpnlfdvilPMSDDFynlLRQIFTVNPNNRILLPELQ 264
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
145-269 7.51e-03

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: 38.49  E-value: 7.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  145 RVIFITEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVApd 224
Cdd:cd05571  69 RLCFVMEYVNGGELFFHLSR----ERVFSEDRTRFYGAEIVLALGYLHSQG--IVYRDLKLENLLLDKDGHIKITDFG-- 140
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7019333  225 tinnhvkTCREEQK----------NLHFFAPEYGEVTNVTTAVDIYSFGMCALEM 269
Cdd:cd05571 141 -------LCKEEISygattktfcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 188
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
151-271 7.91e-03

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: 38.49  E-value: 7.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  151 EYMSSGSLKQFLKKTKKnhktMNEKAWKRWCTQILSALSYLHScDPPIIHGNLTCDTIFIQHNGLIKI------GSVAPD 224
Cdd:cd06649  83 EHMDGGSLDQVLKEAKR----IPEEILGKVSIAVLRGLAYLRE-KHQIMHRDVKPSNILVNSRGEIKLcdfgvsGQLIDS 157
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7019333  225 TINNHVKTcreeqknLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAV 271
Cdd:cd06649 158 MANSFVGT-------RSYMSPERLQGTHYSVQSDIWSMGLSLVELAI 197
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
110-203 9.56e-03

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: 38.16  E-value: 9.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019333  110 QEEKVRAVFDNLIQLEHLNIVKFHKYWadikENKARVIFITEYMSSGSLKQFLKKTKKNhktMNEKAWKRWCTQILSALS 189
Cdd:cd14082  45 QESQLRNEVAILQQLSHPGVVNLECMF----ETPERVFVVMEKLHGDMLEMILSSEKGR---LPERITKFLVTQILVALR 117
                        90
                ....*....|....
gi 7019333  190 YLHSCDppIIHGNL 203
Cdd:cd14082 118 YLHSKN--IVHCDL 129
 
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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