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Conserved domains on  [gi|46577677|sp|O75716|]
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RecName: Full=Serine/threonine-protein kinase 16; AltName: Full=Myristoylated and palmitoylated serine/threonine-protein kinase; Short=MPSK; AltName: Full=Protein kinase PKL12; AltName: Full=TGF-beta-stimulated factor 1; Short=TSF-1; AltName: Full=Tyrosine-protein kinase STK16; AltName: Full=hPSK

Protein Classification

serine/threonine-protein kinase( domain architecture ID 10195650)

serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0005524|GO:0006468|GO:0004674
PubMed:  19614568|17557329
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
19-295 8.92e-174

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: 481.80  E-value: 8.92e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRER-GAKHEAWLL 97
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaGGKKEVYLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHA---KGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd13986  81 LPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQN-QL 253
Cdd:cd13986 161 IEIEGRREALALQDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLALAVLSgNY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQP 295
Cdd:cd13986 241 SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDLIP 282
 
Name Accession Description Interval E-value
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
19-295 8.92e-174

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: 481.80  E-value: 8.92e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRER-GAKHEAWLL 97
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaGGKKEVYLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHA---KGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd13986  81 LPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQN-QL 253
Cdd:cd13986 161 IEIEGRREALALQDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLALAVLSgNY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQP 295
Cdd:cd13986 241 SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDLIP 282
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-281 3.10e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 166.94  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHEAWLLL 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFE----DEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     99 PFFKRGTLWneiERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqaCIHVE 178
Cdd:smart00220  77 EYCEGGDLF---DLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGL----ARQLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    179 GSRQALTLQdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQL----- 253
Cdd:smart00220 149 PGEKLTTFV------GTPEYMAPEVLLGKGY---GKAVDIWSLGVILYELLTGKPPFP-----GDDQLLELFKKIgkpkp 214
                          250       260
                   ....*....|....*....|....*....
gi 46577677    254 -SIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:smart00220 215 pFPPPEWDISPEAKDLIRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-282 6.12e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 169.42  E-value: 6.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYcLRERGakhEAW 95
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrpeLAADPEARERFRREARALARLNHPNIVRVYDV-GEEDG---RPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWneiERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAci 175
Cdd:COG0515  84 LVMEYVEGESLA---DLLRRRGP-LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hvegSRQALTLQDWAAqrCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDmvFQKGDSVALAVQNQLSI 255
Cdd:COG0515 158 ----GGATLTQTGTVV--GTPGYMAPEQARGEP---VDPRSDVYSLGVTLYELLTGRPPFD--GDSPAELLRAHLREPPP 226
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 256 PQS---PRHSSALRQLLNSMMTVDPHQRPH 282
Cdd:COG0515 227 PPSelrPDLPPALDAIVLRALAKDPEERYQ 256
Pkinase pfam00069
Protein kinase domain;
20-296 3.36e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 108.10  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE--AQREADMHRLFNHPNILRLVAYCLRERgakhEAWLL 97
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKD----NLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    98 LPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAihakgyahrdlkptnillgdegqpvlmdLGSMNQACihv 177
Cdd:pfam00069  77 LEYVEGGSLFD---LLSEKGAF-SEREAKFIMKQILEGLES----------------------------GSSLTTFV--- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   178 egsrqaltlqdwaaqrCTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvFQKGDSVALAVQNQLSIPQ 257
Cdd:pfam00069 122 ----------------GTPWYMAPE---VLGGNPYGPKVDVWSLGCILYELLTGKPPFP--GINGNEIYELIIDQPYAFP 180
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 46577677   258 SPRH--SSALRQLLNSMMTVDPHQRPHIPlllsqlEALQPP 296
Cdd:pfam00069 181 ELPSnlSEEAKDLLKKLLKKDPSKRLTAT------QALQHP 215
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
14-282 1.29e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 88.70  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   14 IIDNkRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEA----QREA-DMHRLfNHPNIlrlVA-YCLRE 87
Cdd:NF033483   4 LLGG-RYEIGERIGRGGMAEVYLAKDTRLDRDVAVK-VLRPDLARDPEFvarfRREAqSAASL-SHPNI---VSvYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   88 RGAkheawllLPF----FKRG-TLwNEIerLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:NF033483  78 DGG-------IPYivmeYVDGrTL-KDY--IREHGP-LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  163 VLMDLG---SMNQACI----HVEGsrqaltlqdwaaqrcTISYRAPElfsvQS-HCVIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:NF033483 147 KVTDFGiarALSSTTMtqtnSVLG---------------TVHYLSPE----QArGGTVDARSDIYSLGIVLYEMLTGRPP 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 46577677  235 YDmvfqkGDS-VALAVQNQLSIPQSPRH-SSALRQLLNS----MMTVDPHQRPH 282
Cdd:NF033483 208 FD-----GDSpVSVAYKHVQEDPPPPSElNPGIPQSLDAvvlkATAKDPDDRYQ 256
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
20-281 3.74e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 75.93  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQR--EADMHRLFNHPNILRLVAYCLRErgAKHEAWLL 97
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLviEVNVMRELKHKNIVRYIDRFLNK--ANQKLYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    98 LPFFKRGTLWNEIERLKDKGNFLTEDQILwlllGICRGLeaIHAKGYAH-------------RDLKPTNILLGDEgqpvL 164
Cdd:PTZ00266   93 MEFCDAGDLSRNIQKCYKMFGKIEEHAIV----DITRQL--LHALAYCHnlkdgpngervlhRDLKPQNIFLSTG----I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   165 MDLGSMNQACIHVEGsRQALTLQDWA----------AQRC--TISYRAPELFSVQSHCViDERTDVWSLGCVLYAMMFGE 232
Cdd:PTZ00266  163 RHIGKITAQANNLNG-RPIAKIGDFGlsknigiesmAHSCvgTPYYWSPELLLHETKSY-DDKSDMWALGCIIYELCSGK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 46577677   233 GPydmvFQKGDSVALAVQNQLSIPQSP--RHSSALRQLLNSMMTVDPHQRP 281
Cdd:PTZ00266  241 TP----FHKANNFSQLISELKRGPDLPikGKSKELNILIKNLLNLSAKERP 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
43-297 6.72e-06

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 47.53  E-value: 6.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     43 GHFYALK--RILcHEQQDREEA--QREADMHRLFNHPNILRLVayclrERGaKHEAWLLLPFFKRGTLWNEIERLKDKGN 118
Cdd:TIGR03903    3 GHEVAIKllRTD-APEEEHQRArfRRETALCARLYHPNIVALL-----DSG-EAPPGLLFAVFEYVPGRTLREVLAADGA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    119 FLTEDQILwLLLGICRGLEAIHAKGYAHRDLKPTNILL---GDEGQPVLMDLGsmnqACIHVEGSRQALTLQDWAAQRC- 194
Cdd:TIGR03903   76 LPAGETGR-LMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFG----IGTLLPGVRDADVATLTRTTEVl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    195 -TISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEgpydmVFQKGDSVALAVQNQLS-----IPQSPRhSSALRQL 268
Cdd:TIGR03903  151 gTPTYCAPEQLRGEP---VTPNSDLYAWGLIFLECLTGQ-----RVVQGASVAEILYQQLSpvdvsLPPWIA-GHPLGQV 221
                          250       260       270
                   ....*....|....*....|....*....|
gi 46577677    269 LNSMMTVDPHQRP-HIPLLLSQLEALQPPA 297
Cdd:TIGR03903  222 LRKALNKDPRQRAaSAPALAERFRALELCA 251
 
Name Accession Description Interval E-value
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
19-295 8.92e-174

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: 481.80  E-value: 8.92e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRER-GAKHEAWLL 97
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaGGKKEVYLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHA---KGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd13986  81 LPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGSMNPAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQN-QL 253
Cdd:cd13986 161 IEIEGRREALALQDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLALAVLSgNY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQP 295
Cdd:cd13986 241 SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSRVHDLIP 282
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
19-291 1.58e-51

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: 170.59  E-value: 1.58e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMH-RLFNHPNILRLVAYCLRERGAKHEAWLL 97
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMkRLCGHPNIVQYYDSAILSSEGRKEVLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFkRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKG--YAHRDLKPTNILLGDEGQPVLMDLGSM-NQAC 174
Cdd:cd13985  81 MEYC-PGSLVDILE--KSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSAtTEHY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAaQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkgDSVALAVQN-QL 253
Cdd:cd13985 158 PLERAEEVNIIEEEIQ-KNTTPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPFD------ESSKLAIVAgKY 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd13985 231 SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
26-290 2.01e-51

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: 168.60  E-value: 2.01e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRG 104
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIpKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETEN----FLYLVMEYCEGG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQAL 184
Cdd:cd00180  77 SLKDLLKENKGP---LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 185 TLQDWAaqrctisYRAPELFSVQSHcviDERTDVWSLGCVLYAMmfgegpydmvfqkgdsvalavqnqlsipqsprhsSA 264
Cdd:cd00180 154 GTTPPY-------YAPPELLGGRYY---GPKVDIWSLGVILYEL----------------------------------EE 189
                       250       260
                ....*....|....*....|....*.
gi 46577677 265 LRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd00180 190 LKDLIRRMLQYDPKKRPSAKELLEHL 215
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-281 3.10e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 166.94  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHEAWLLL 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFE----DEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     99 PFFKRGTLWneiERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqaCIHVE 178
Cdd:smart00220  77 EYCEGGDLF---DLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGL----ARQLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    179 GSRQALTLQdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQL----- 253
Cdd:smart00220 149 PGEKLTTFV------GTPEYMAPEVLLGKGY---GKAVDIWSLGVILYELLTGKPPFP-----GDDQLLELFKKIgkpkp 214
                          250       260
                   ....*....|....*....|....*....
gi 46577677    254 -SIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:smart00220 215 pFPPPEWDISPEAKDLIRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-282 6.12e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 169.42  E-value: 6.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYcLRERGakhEAW 95
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrpeLAADPEARERFRREARALARLNHPNIVRVYDV-GEEDG---RPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWneiERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAci 175
Cdd:COG0515  84 LVMEYVEGESLA---DLLRRRGP-LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hvegSRQALTLQDWAAqrCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDmvFQKGDSVALAVQNQLSI 255
Cdd:COG0515 158 ----GGATLTQTGTVV--GTPGYMAPEQARGEP---VDPRSDVYSLGVTLYELLTGRPPFD--GDSPAELLRAHLREPPP 226
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 256 PQS---PRHSSALRQLLNSMMTVDPHQRPH 282
Cdd:COG0515 227 PPSelrPDLPPALDAIVLRALAKDPEERYQ 256
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
19-281 1.05e-48

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: 163.14  E-value: 1.05e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD---REEAQREADMHRLFNHPNILRLVAYcLRERGAkheAW 95
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeefRERFLREARALARLSHPNIVRVYDV-GEDDGR---PY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacI 175
Cdd:cd14014  77 IVMEYVEGGSL---ADLLRERGP-LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG------I 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTLQDwaAQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQNQLSI 255
Cdd:cd14014 147 ARALGDSGLTQTG--SVLGTPAYMAPEQARGGP---VDPRSDIYSLGVVLYELLTGRPP----FDGDSPAAVLAKHLQEA 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 256 PQSPR-----HSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14014 218 PPPPSplnpdVPPALDAIILRALAKDPEERP 248
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
23-283 4.80e-47

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: 159.37  E-value: 4.80e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQK-LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREAD-MHRLFNHPNILRLV-AYCLRERGAKHEAWLLLP 99
Cdd:cd14037   7 IEKyLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEiMKRLSGHKNIVGYIdSSANRSGNGVYEVLLLME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEI-ERLKDKgnfLTEDQILWLLLGICRGLEAIHA--KGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIH 176
Cdd:cd14037  87 YCKGGGVIDLMnQRLQTG---LTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSATTKILP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmvfqkGDSVALAVQN-QLSI 255
Cdd:cd14037 164 PQTKQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPF------EESGQLAILNgNFTF 237
                       250       260
                ....*....|....*....|....*...
gi 46577677 256 PQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14037 238 PDNSRYSKRLHKLIRYMLEEDPEKRPNI 265
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
26-293 1.36e-44

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: 153.05  E-value: 1.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMH-RLFNHPNIlrlVAYCLRERGAKHEA------WLLL 98
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMkKLSGHPNI---VQFCSAASIGKEESdqgqaeYLLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKDKGNFlTEDQILWLLLGICRGLEAIHAKG--YAHRDLKPTNILLGDEGQPVLMDLGSMNQACIH 176
Cdd:cd14036  85 TELCKGQLVDFVKKVEAPGPF-SPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALT---LQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkgDSVALAVQN-Q 252
Cdd:cd14036 164 PDYSWSAQKrslVEDEITRNTTPMYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFE------DGAKLRIINaK 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 253 LSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14036 238 YTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIVEQLQEL 278
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
19-289 4.25e-43

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: 148.38  E-value: 4.25e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHE--QQDREEAQREADMHRLFNHPNIlrlVAYclrergakHEAWL 96
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmsEKEREEALNEVKLLSKLKHPNI---VKY--------YESFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 -------LLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGs 169
Cdd:cd08215  70 engklciVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFG- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 mnqacIhvegSRQaLTLQDWAAQRC--TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSV-A 246
Cdd:cd08215 149 -----I----SKV-LESTTDLAKTVvgTPYYLSPELCENKPY---NYKSDIWALGCVLYELCTLKHPFE-----ANNLpA 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 46577677 247 LAVQ-NQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08215 211 LVYKiVKGQYPPIPSQySSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
19-284 7.59e-41

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: 142.27  E-value: 7.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEA---QREADMHRLFNHPNILRLvaYCLRERGAKHeaW 95
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIK-IIDKSKLKEEIEekiKREIEIMKLLNHPNIIKL--YEVIETENKI--Y 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACI 175
Cdd:cd14003  76 LVMEYASGGEL---FDYIVNNGR-LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG----LSN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTlqdwaaqRC-TISYRAPELFsvQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQLS 254
Cdd:cd14003 148 EFRGGSLLKT-------FCgTPAYAAPEVL--LGRKYDGPKADVWSLGVILYAMLTGYLPFD-----DDNDSKLFRKILK 213
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 255 -IPQSPRH-SSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14003 214 gKYPIPSHlSPDARDLIRRMLVVDPSKRITIE 245
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
19-289 1.52e-39

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: 139.06  E-value: 1.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCH--EQQDREEAQREADMHRLFNHPNILRLvayclrergakHEAWL 96
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGslSQKEREDSVNEIRLLASVNHPNIIRY-----------KEAFL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 L-------LPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLgs 169
Cdd:cd08530  70 DgnrlcivMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 mnqacihveGSRQALTLQDWAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAV 249
Cdd:cd08530 148 ---------GISKVLKKNLAKTQIGTPLYAAPEVWKGRPY---DYKSDIWSLGCLLYEMATFRPP----FEARTMQELRY 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 250 QNQLSI--PQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08530 212 KVCRGKfpPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
20-287 1.30e-37

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 133.87  E-value: 1.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRergaKHEAWLLLP 99
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLK----KDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLwNEIerLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEG 179
Cdd:cd05122  78 FCSGGSL-KDL--LKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFG----LSAQLSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-DMVFQKgdsvAL---AVQNQLSI 255
Cdd:cd05122 151 GKTRNTFVG------TPYWMAPEVIQGKPY---GFKADIWSLGITAIEMAEGKPPYsELPPMK----ALfliATNGPPGL 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 256 PQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd05122 218 RNPKKWSKEFKDFLKKCLQKDPEKRPTAEQLL 249
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-296 3.52e-35

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: 127.59  E-value: 3.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHeQQDREEAQREADMHRLFNHPNILRLVA------------- 82
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkkKLK-SEDEEMLRREIEILKRLDHPNIVKLYEvfeddknlylvme 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  83 YClreRGakheawlllpffkrGTLWneiERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL---GDE 159
Cdd:cd05117  80 LC---TG--------------GELF---DRIVKKGSF-SEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPD 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 160 GQPVLMDLGSmnqACIHVEGSRqaltlqdwAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYD-- 236
Cdd:cd05117 139 SPIKIIDFGL---AKIFEEGEK--------LKTVCgTPYYVAPEVLKGKGY---GKKCDIWSLGVILYILLCGYPPFYge 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 237 ---MVFQKgdsvalAVQNQLSIPQSPRH--SSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd05117 205 teqELFEK------ILKGKYSFDSPEWKnvSEEAKDLIKRLLVVDPKKR------LTAAEALNHP 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
22-281 7.90e-33

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


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 121.43  E-value: 7.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRI-------LCHEQQDReeaqREADMHRLFNHPNILRLVAYClrergakHEA 94
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREKKSGFIVALKVIsksqlqkSGLEHQLR----REIEIQSHLRHPNILRLYGYF-------EDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 ---WLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmn 171
Cdd:cd14007  73 kriYLILEYAPNGELYKELKKQKR----FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGW-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qaCIHVEGSRQaLTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMvfqKGDSVALA-- 248
Cdd:cd14007 147 --SVHAPSNRR-KTF-------CgTLDYLPPEMVEGKEY---DYKVDIWSLGVLCYELLVGKPPFES---KSHQETYKri 210
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 249 VQNQLSIPQSPrhSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14007 211 QNVDIKFPSSV--SPEAKDLISKLLQKDPSKRL 241
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
26-290 8.04e-32

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 118.41  E-value: 8.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSyvDLVEGLHDGHFYALKRILCHEQQDR--EEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKR 103
Cdd:cd13999   1 IGSGSFG--EVYKGKWRGTDVAIKKLKVEDDNDEllKEFRREVSILSKLRHPNIVQFIGACLSPP----PLCIVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNeieRLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRQA 183
Cdd:cd13999  75 GSLYD---LLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGL---SRIKNSTTEKM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTlqdwaaQRCTISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMMFGEGPYDmVFQKGDSVALAVQNQLsIPQSPRH-S 262
Cdd:cd13999 149 TG------VVGTPRWMAPEVL---RGEPYTEKADVYSFGIVLWELLTGEVPFK-ELSPIQIAAAVVQKGL-RPPIPPDcP 217
                       250       260
                ....*....|....*....|....*...
gi 46577677 263 SALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd13999 218 PELSKLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-280 8.59e-30

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: 113.38  E-value: 8.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVaYCLRERGAKHeawLLLPFFK 102
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLrkkEIIKRKEVEHTLNERNILERVNHPFIVKLH-YAFQTEEKLY---LVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQ 182
Cdd:cd05123  77 GGELFS---HLSKEGRF-PEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGL----------AKE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 ALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgdsvalAVQNQLSIP 256
Cdd:cd05123 143 LSSDGDRTYTFCgTPEYLAPEVLLGKGY---GKAVDWWSLGVLLYEMLTGKPPFyaenrKEIYEK------ILKSPLKFP 213
                       250       260
                ....*....|....*....|....
gi 46577677 257 QSPrhSSALRQLLNSMMTVDPHQR 280
Cdd:cd05123 214 EYV--SPEAKSLISGLLQKDPTKR 235
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
18-288 1.09e-29

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: 113.42  E-value: 1.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI----LCHEQQdREEAQREADMHRLFNHPNILRLVAYCLRErgakHE 93
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVpkssLTKPKQ-REKLKSEIKIHRSLKHPNIVKFHDCFEDE----EN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnQA 173
Cdd:cd14099  76 VYILLELCSNGSLMELLKRRKA----LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGL--AA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQaLTLqdwaaqrC-TISYRAPE-LFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVAL---A 248
Cdd:cd14099 150 RLEYDGERK-KTL-------CgTPNYIAPEvLEKKKGH---SFEVDIWSLGVILYTLLVGKPP----FETSDVKETykrI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 249 VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14099 215 KKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILS 254
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
17-290 1.76e-29

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 113.16  E-value: 1.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYL--F--IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRlvaYclrergak 91
Cdd:cd13996   1 NSRYLndFeeIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKvLREVKALAKLNHPNIVR---Y-------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLP-------FFKRGTLWNEIERlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPV 163
Cdd:cd13996  70 YTAWVEEPplyiqmeLCEGGTLRDWIDR-RNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 164 LMDLG---SMNQAciHVEGSRQALTLQDWAAQRC----TISYRAPELFSVQsHCviDERTDVWSLGCVLYAMMFgegPYD 236
Cdd:cd13996 149 IGDFGlatSIGNQ--KRELNNLNNNNNGNTSNNSvgigTPLYASPEQLDGE-NY--NEKADIYSLGIILFEMLH---PFK 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 237 MVFQKgdSVALAVQNQLSIPQS-PRHSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd13996 221 TAMER--STILTDLRNGILPESfKAKHPKEADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
26-287 3.36e-29

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: 112.26  E-value: 3.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI----LCHEQQDREEA----------QRE-ADMHRLfNHPNILRLvayclrerga 90
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFnksrLRKRREGKNDRgkiknalddvRREiAIMKKL-DHPNIVRL---------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kHEA---------WLLLPFFKRGTLwneIERLKDKGNF-LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG 160
Cdd:cd14008  70 -YEViddpesdklYLVLEYCEGGPV---MELDSGDRVPpLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 161 QPVLMDLGS--MnqacihVEGSRQALTlqdwaAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmv 238
Cdd:cd14008 146 TVKISDFGVseM------FEDGNDTLQ-----KTAGTPAFLAPELCDGDSKTYSGKAADIWALGVTLYCLVFGRLPF--- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 46577677 239 fqKGDSV---ALAVQNQ-LSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14008 212 --NGDNIlelYEAIQNQnDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIK 262
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-287 7.87e-29

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: 111.06  E-value: 7.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQ--DREEAQREADMHRLFNHPNIlrlVAY--CLRERGAkheA 94
Cdd:cd08218   1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSpkEREESRKEVAVLSKMKHPNI---VQYqeSFEENGN---L 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd08218  75 YIVMDYCDGGDLYKRIN--AQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTlqdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGdsVALAVQNQLS 254
Cdd:cd08218 153 STVELARTCIG---------TPYYLSPEICENKPY---NNKSDIWALGCVLYEMCTLKHAFEAGNMKN--LVLKIIRGSY 218
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 255 IPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd08218 219 PPVPSRYSYDLRSLVSQLFKRNPRDRPSINSIL 251
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
18-284 9.40e-29

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 110.88  E-value: 9.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI--LCHEQQDREEAQREADMHRLFNHPNILRLvaYCLRERGAKHeaW 95
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmKRAPGDCPENIKKEVCIQKMLSHKNVVRF--YGHRREGEFQ--Y 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIErlKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacI 175
Cdd:cd14069  77 LFLEYASGGELFDKIE--PDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATV--F 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTLqdwaaQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPYD---------MVFQKGDSVA 246
Cdd:cd14069 151 RYKGKERLLNK-----MCGTLPYVAPELLAKKKY--RAEPVDVWSCGIVLFAMLAGELPWDqpsdscqeySDWKENKKTY 223
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 247 LAVQNQLSIPqsprhssALRqLLNSMMTVDPHQRPHIP 284
Cdd:cd14069 224 LTPWKKIDTA-------ALS-LLRKILTENPNKRITIE 253
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
17-296 1.01e-28

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: 111.44  E-value: 1.01e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILcheqQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWL 96
Cdd:cd14137   3 EISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVL----QDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKKDEVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPF-FKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPVLMDLGS----- 169
Cdd:cd14137  79 NLVMeYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFGSakrlv 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNQACIHVEGSRqaltlqdwaaqrctiSYRAPELF--SVQSHCVIdertDVWSLGCVLYAMMFGEgPydmVFQKGDSVAL 247
Cdd:cd14137 159 PGEPNVSYICSR---------------YYRAPELIfgATDYTTAI----DIWSAGCVLAELLLGQ-P---LFPGESSVDQ 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 248 AV--------------------QNQLSIPQSPRH--SSALR--------QLLNSMMTVDPHQRPHIplllsqLEALQPP 296
Cdd:cd14137 216 LVeiikvlgtptreqikamnpnYTEFKFPQIKPHpwEKVFPkrtppdaiDLLSKILVYNPSKRLTA------LEALAHP 288
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-296 2.64e-28

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 109.25  E-value: 2.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQqDREEAQREADMHRLFN----HPNILRLVaYCLRERGAKHeAW 95
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFR-HPKAALREIKLLKHLNdvegHPNIVKLL-DVFEHRGGNH-LC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFkrGTLWNEIerLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPVLMDLGSmnqAC 174
Cdd:cd05118  78 LVFELM--GMNLYEL--IKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLADFGL---AR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IhveGSRQALTlqdwaAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGE----GPYDMvfqkgDSVALAVQ 250
Cdd:cd05118 151 S---FTSPPYT-----PYVATRWYRAPEVLLGAKP--YGSSIDIWSLGCILAELLTGRplfpGDSEV-----DQLAKIVR 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 251 nQLSIPQsprhssaLRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd05118 216 -LLGTPE-------ALDLLSKMLKYDPAKR------ITASQALAHP 247
Pkinase pfam00069
Protein kinase domain;
20-296 3.36e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 108.10  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE--AQREADMHRLFNHPNILRLVAYCLRERgakhEAWLL 97
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKD----NLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    98 LPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAihakgyahrdlkptnillgdegqpvlmdLGSMNQACihv 177
Cdd:pfam00069  77 LEYVEGGSLFD---LLSEKGAF-SEREAKFIMKQILEGLES----------------------------GSSLTTFV--- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   178 egsrqaltlqdwaaqrCTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvFQKGDSVALAVQNQLSIPQ 257
Cdd:pfam00069 122 ----------------GTPWYMAPE---VLGGNPYGPKVDVWSLGCILYELLTGKPPFP--GINGNEIYELIIDQPYAFP 180
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 46577677   258 SPRH--SSALRQLLNSMMTVDPHQRPHIPlllsqlEALQPP 296
Cdd:pfam00069 181 ELPSnlSEEAKDLLKKLLKKDPSKRLTAT------QALQHP 215
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
24-287 1.24e-27

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: 107.61  E-value: 1.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHE--QQDREEAQREADMHRLFNHPNIlrlVAYclreRGAKHEA---WLLL 98
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGdsEEELEALEREIRILSSLKHPNI---VRY----LGTERTEntlNIFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWneiERLKDKGNFlTED-------QILwlllgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmn 171
Cdd:cd06606  79 EYVPGGSLA---SLLKKFGKL-PEPvvrkytrQIL-------EGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFG--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qACIHVEGSRQALTLQdwaAQRCTISYRAPELFSVQSHCvidERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAL--AV 249
Cdd:cd06606 145 -CAKRLAEIATGEGTK---SLRGTPYWMAPEVIRGEGYG---RAADIWSLGCTVIEMATGKPPW---SELGNPVAAlfKI 214
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 250 QNQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06606 215 GSSGEPPPIPEHlSEEAKDFLRKCLQRDPKKRPTADELL 253
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
26-288 9.20e-27

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: 105.47  E-value: 9.20e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVE--GLHDGHFYALK---RILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRErgaKHEAWLLL 98
Cdd:cd13994   1 IGKGATSVVRIVTkkNPRSGVLYAVKeyrRRDDESKRKdyVKRLTSEYIISSKLHHPNIVKVLDLCQDL---HGKWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVE 178
Cdd:cd13994  78 EYCPGGDLFTLIE----KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 gsrqaLTLQDWAAQRCTISYRAPELFSVQSHCviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAV---QNQLSI 255
Cdd:cd13994 154 -----KESPMSAGLCGSEPYMAPEVFTSGSYD--GRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEksgDFTNGP 226
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 256 PQSPRHS--SALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd13994 227 YEPIENLlpSECRRLIYRMLHPDPEKRITIDEALN 261
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
19-287 2.16e-26

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: 104.39  E-value: 2.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIL--CHEQQDREEAQREADMHR-LFNHPNILRLvaYCLRERGAkhEAW 95
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKkpFRGPKERARALREVEAHAaLGQHPNIVRY--YSSWEEGG--HLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqaCI 175
Cdd:cd13997  77 IQMELCENGSLQDALEELSPIS-KLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFG-----LA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRqaltlqdWAAQRCTISYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGegpydMVF-QKGDSVALAVQNQLS 254
Cdd:cd13997 151 TRLETS-------GDVEEGDSRYLAPEL--LNENYTHLPKADIFSLGVTVYEAATG-----EPLpRNGQQWQQLRQGKLP 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 255 IPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd13997 217 LPPGLVLSQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
18-288 3.49e-26

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 104.00  E-value: 3.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQ--QDREEAQREADMHRLFNHPNILRLvaYCLRERGAKheAW 95
Cdd:cd14078   3 KYYELHETIGSGGFAKVKLATHILTGEKVAIK-IMDKKAlgDDLPRVKTEIEALKNLSHQHICRL--YHVIETDNK--IF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERlKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACI 175
Cdd:cd14078  78 MVLEYCPGGELFDYIVA-KDR---LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFG----LCA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRqaltlqDWAAQRCTIS--YRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQL 253
Cdd:cd14078 150 KPKGGM------DHHLETCCGSpaYAAPEL--IQGKPYIGSEADVWSMGVLLYALLCGFLPFD-----DDNVMALYRKIQ 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 254 S----IPQSPRHSSalRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14078 217 SgkyeEPEWLSPSS--KLLLDQMLQVDPKKRITVKELLN 253
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
19-283 4.78e-26

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: 103.50  E-value: 4.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD---REEAQREADMHRLFNHPNILRLVAYCLRErgakHEAW 95
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDakaRQDCLKEIDLLQQLNHPNIIKYLASFIEN----NELN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqaci 175
Cdd:cd08224  77 IVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL------ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hvegSRQaLTLQDWAAQRC--TISYRAPELFSVQSHcviDERTDVWSLGCVLYAM------MFGEGP--YDmVFQKGDSV 245
Cdd:cd08224 151 ----GRF-FSSKTTAAHSLvgTPYYMSPERIREQGY---DFKSDIWSLGCLLYEMaalqspFYGEKMnlYS-LCKKIEKC 221
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 246 ALAvqnqlSIPqSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd08224 222 EYP-----PLP-ADLYSQELRDLVAACIQPDPEKRPDI 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
22-281 5.73e-26

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 103.38  E-value: 5.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     22 FIQKLGEGGFSYV---DLVEGLHDGHF-YALKRIL-CHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWL 96
Cdd:smart00219   3 LGKKLGEGAFGEVykgKLKGKGGKKKVeVAVKTLKeDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEE----EPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     97 LLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMnqacih 176
Cdd:smart00219  79 VMEYMEGGDL---LSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG-L------ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    177 vegSRQALTLQDWAAQRCTISYR--APELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPY-DMvfqKGDSVALAVQNQ 252
Cdd:smart00219 149 ---SRDLYDDDYYRKRGGKLPIRwmAPESL---KEGKFTSKSDVWSFGVLLWEIFtLGEQPYpGM---SNEEVLEYLKNG 219
                          250       260
                   ....*....|....*....|....*....
gi 46577677    253 LSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:smart00219 220 YRLPQPPNCPPELYDLMLQCWAEDPEDRP 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
25-289 6.04e-26

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 103.26  E-value: 6.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLHDGHFYALKRILCH--EQQDREEAQREADMHRLFNHPNILRLVAyCLRERGakhEAWLLLPFFK 102
Cdd:cd08529   7 KLGKGSFGVVYKVVRKVDGRVYALKQIDISrmSRKMREEAIDEARVLSKLNSPYVIKYYD-SFVDKG---KLNIVMEYAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIERlkDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRQ 182
Cdd:cd08529  83 NGDLHSLIKS--QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGV---AKILSDTTNF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 ALTLQDwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkgdsvalaVQNQ----LSI--- 255
Cdd:cd08529 158 AQTIVG------TPYYLSPELCEDKPY---NEKSDVWALGCVLYELCTGKHPFE------------AQNQgaliLKIvrg 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 256 ---PQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08529 217 kypPISASYSQDLSQLIDSCLTKDYRQRPDTTELLRN 253
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
20-281 8.65e-26

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: 103.45  E-value: 8.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQ----READ-MHRLfNHPNILRLvAYCLRERgakHEA 94
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIK-VLDKRHIIKEKKVkyvtIEKEvLSRL-AHPGIVKL-YYTFQDE---SKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd05581  77 YFVLEYAPNGDLLEYIRKYGS----LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ---IHVEGSRQALTLQDWAAQRC-----TISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMMFGEGP-----YDMVFQK 241
Cdd:cd05581 153 pdsSPESTKGDADSQIAYNQARAasfvgTAEYVSPELL---NEKPAGKSSDLWALGCIIYQMLTGKPPfrgsnEYLTFQK 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 242 gdsvalaVQNqLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05581 230 -------IVK-LEYEFPENFPPDAKDLIQKLLVLDPSKRL 261
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-289 1.15e-25

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: 102.73  E-value: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQ--QDREEAQREADMHRLFNHPNILRLVAyCLRERGakhEAWL 96
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMpvKEKEASKKEVILLAKMKHPNIVTFFA-SFQENG---RLFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERlkDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV-LMDLGSmnqaci 175
Cdd:cd08225  77 VMEYCDGGDLMKRINR--QRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGI------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hvegsrqALTLQDWA--AQRC--TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDS---VALA 248
Cdd:cd08225 149 -------ARQLNDSMelAYTCvgTPYYLSPEICQNRPY---NNKTDIWSLGCVLYELCTLKHPFE-----GNNlhqLVLK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 249 VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08225 214 ICQGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILKR 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-287 2.33e-25

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: 101.85  E-value: 2.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIlCHEQQDREEAQ---READMHRLFNHPNIlrlVAYCLRE--RgAKHEA 94
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEI-DYGKMSEKEKQqlvSEVNILRELKHPNI---VRYYDRIvdR-ANTTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYA-----HRDLKPTNILLgDEGQPV-LMDLG 168
Cdd:cd08217  77 YIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSVGggkilHRDLKPANIFL-DSDNNVkLGDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SmnqacihvegSRqALTLQDWAAQRC--TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVA 246
Cdd:cd08217 156 L----------AR-VLSHDSSFAKTYvgTPYYMSPELLNEQSY---DEKSDIWSLGCLIYELCALHPP----FQAANQLE 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 46577677 247 LAV---QNQLS-IPQspRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd08217 218 LAKkikEGKFPrIPS--RYSSELNEVIKSMLNVDPDKRPSVEELL 260
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
22-281 2.63e-25

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: 101.47  E-value: 2.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     22 FIQKLGEGGFSYV---DLVEGLHDGHF-YALKRIL-CHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWL 96
Cdd:smart00221   3 LGKKLGEGAFGEVykgTLKGKGDGKEVeVAVKTLKeDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEE----EPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     97 LLPFFKRGTLwneIERLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMnqaci 175
Cdd:smart00221  79 VMEYMPGGDL---LDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG-L----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    176 hvegSRQALTLQDWAAQRCTISYR--APELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPY-DMvfqKGDSVALAVQN 251
Cdd:smart00221 150 ----SRDLYDDDYYKVKGGKLPIRwmAPESL---KEGKFTSKSDVWSFGVLLWEIFtLGEEPYpGM---SNAEVLEYLKK 219
                          250       260       270
                   ....*....|....*....|....*....|
gi 46577677    252 QLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:smart00221 220 GYRLPKPPNCPPELYKLMLQCWAEDPEDRP 249
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
20-294 4.05e-25

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 101.18  E-value: 4.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRL-VAYCLRErgakhEAW 95
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMnkqKCIEKDSVRNVLNELEILQELEHPFLVNLwYSFQDEE-----DMY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERlkdKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLgsmNQACI 175
Cdd:cd05578  77 MVVDLLLGGDLRYHLQQ---KVKF-SEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF---NIATK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hVEGSRQALTLQDwaaqrcTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSI 255
Cdd:cd05578 150 -LTDGTLATSTSG------TKPYMAPEVFMRAGYSF---AVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASV 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 256 PQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQ 294
Cdd:cd05578 220 LYPAGWSEEAIDLINKLLERDPQKR------LGDLSDLK 252
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-289 4.29e-25

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 100.82  E-value: 4.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNIlrlVAYCLRERGAKHeAWLL 97
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrLPKSSSAVEDSRKEAVLLAKMKHPNI---VAFKESFEADGH-LYIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS-------M 170
Cdd:cd08219  77 MEYCDGGDLMQKIK--LQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSarlltspG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQACIHVEgsrqaltlqdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQ 250
Cdd:cd08219 155 AYACTYVG----------------TPYYVPPEIWENMPY---NNKSDIWSLGCILYELCTLKHP----FQANSWKNLILK 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 251 -NQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08219 212 vCQGSYKPLPSHySYELRSLIKQMFKRNPRSRPSATTILSR 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-296 4.96e-25

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: 100.96  E-value: 4.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGL---HDGHFYALKRILCHEQQDRE--EAQREADMHRLFNHPNILRLvayclrergakHE 93
Cdd:cd08222   1 RYRVVRKLGSGNFGTVYLVSDLkatADEELKVLKEISVGELQPDEtvDANREAKLLSKLDHPAIVKF-----------HD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFF-------KRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEgqpvLMD 166
Cdd:cd08222  70 SFVEKESFcivteycEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN----VIK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 167 LGSMNQACIHVEGSRQALTLQDwaaqrcTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVa 246
Cdd:cd08222 146 VGDFGISRILMGTSDLATTFTG------TPYYMSPE---VLKHEGYNSKSDIWSLGCILYEMCCLKHAFD-----GQNL- 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 247 LAVQNQL---SIPQSPRH-SSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd08222 211 LSVMYKIvegETPSLPDKySKELNAIYSRMLNKDPALRP------SAAEILKIP 258
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
19-281 6.31e-25

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: 100.91  E-value: 6.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYL--F--IQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQRE-ADMHRLfNHPNILRLVAYCLRErgakH 92
Cdd:cd14046   3 RYLtdFeeLQVLGKGAFGQVVKVRNKLDGRYYAIKKIkLRSESKNNSRILREvMLLSRL-NHQHVVRYYQAWIER----A 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLWNEIERlkdkGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd14046  78 NLYIQMEYCEKSTLRDLIDS----GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 ACIHVEGSRQALTLQDWAAQRCTIS---------YRAPELFSvQSHCVIDERTDVWSLGCVLYAMMFgegPYDMVFQKgD 243
Cdd:cd14046 154 NKLNVELATQDINKSTSAALGSSGDltgnvgtalYVAPEVQS-GTKSTYNEKVDMYSLGIIFFEMCY---PFSTGMER-V 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 244 SVALAVQN-QLSIPQSPRHSSALRQ--LLNSMMTVDPHQRP 281
Cdd:cd14046 229 QILTALRSvSIEFPPDFDDNKHSKQakLIRWLLNHDPAKRP 269
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-282 8.36e-25

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: 100.64  E-value: 8.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEqqdrEEAQREADMHRLFNHPNILRLVA------YCLRERGAK----H 92
Cdd:cd14047  11 IELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNN----EKAEREVKALAKLDHPNIVRYNGcwdgfdYDPETSSSNssrsK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLL--LPFFKRGTLWNEIERLKdkGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:cd14047  87 TKCLFiqMEFCEKGTLESWIEKRN--GEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQACIHVEGSRqaltlqdwaaQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFgegPYDMVFQKGDsVALAVQ 250
Cdd:cd14047 165 TSLKNDGKRTK----------SKGTLSYMSPEQISSQDY---GKEVDIYALGLILFELLH---VCDSAFEKSK-FWTDLR 227
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSMMTVDPHQRPH 282
Cdd:cd14047 228 NGILPDIFDKRYKIEKTIIKKMLSKKPEDRPN 259
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
19-296 1.30e-24

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: 99.86  E-value: 1.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHE----QQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEA 94
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvagnDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQ----HI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqPVLMDLGSMNQAC 174
Cdd:cd14098  77 YLVMEYVEGGDL---MDFIMAWGA-IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDD-PVIVKISDFGLAK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSrqalTLQDWAAqrcTISYRAPELF---SVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQ- 250
Cdd:cd14098 152 VIHTGT----FLVTFCG---TMAYLAPEILmskEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFD-----GSSQLPVEKr 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 251 -NQLSIPQSP----RHSSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd14098 220 iRKGRYTQPPlvdfNISEEAIDFILRLLDVDPEKRM------TAAQALDHP 264
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-290 2.08e-24

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: 99.11  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    22 FIQKLGEGGFSYVdlVEG----LHDGHFY--ALKRILC-HEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEA 94
Cdd:pfam07714   3 LGEKLGEGAFGEV--YKGtlkgEGENTKIkvAVKTLKEgADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGE----PL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    95 WLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMnqac 174
Cdd:pfam07714  77 YIVTEYMPGGDL---LDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFG-L---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   175 ihvegSRqalTLQDWAAQRCT------ISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPY-DMvfqKGDSVA 246
Cdd:pfam07714 149 -----SR---DIYDDDYYRKRgggklpIKWMAPESL---KDGKFTSKSDVWSFGVLLWEIFtLGEQPYpGM---SNEEVL 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 46577677   247 LAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:pfam07714 215 EFLEDGYRLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
19-289 2.69e-24

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: 98.66  E-value: 2.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE--AQREADMHRLFNHPNIlrlVAYclRERGAKHEAWL 96
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERkaAEQEAKLLSKLKHPNI---VSY--KESFEGEDGFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 --LLPFFKRGTLWNeieRLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqpvLMDLGSMNQA 173
Cdd:cd08223  76 yiVMGFCEGGDLYT---RLKEqKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSN---IIKVGDLGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQDwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMfgegPYDMVFQKGDSVALaVQNQL 253
Cdd:cd08223 150 RVLESSSDMATTLIG------TPYYMSPELFSNKPY---NHKSDVWALGCCVYEMA----TLKHAFNAKDMNSL-VYKIL 215
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 254 S--IPQSPR-HSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08223 216 EgkLPPMPKqYSPELGELIKAMLHQDPEKRPSVKRILRQ 254
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
19-289 6.04e-24

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: 97.88  E-value: 6.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHE--QQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheawL 96
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQmtKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALM----I 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERLKDKgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVlmDLGSMNQACIH 176
Cdd:cd08220  77 VMEYAPGGTLFEYIQQRKGS--LLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVV--KIGDFGISKIL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRqALTLqdwAAQRCTISyraPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMvfQKGDSVALAVQNQLSIP 256
Cdd:cd08220 153 SSKSK-AYTV---VGTPCYIS---PELCEGKPY---NQKSDIWALGCVLYELASLKRAFEA--ANLPALVLKIMRGTFAP 220
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 257 QSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08220 221 ISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
20-281 6.66e-24

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: 97.67  E-value: 6.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILChEQQDREEAQREADMHRLFNHPNILRLV-AYCLRErgakhEAWLLL 98
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRL-RKQNKELIINEILIMKECKHPNIVDYYdSYLVGD-----ELWVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihve 178
Cdd:cd06614  76 EYMDGGSLTDIITQNPVR---MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQ------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 gsrqaLTLQdwAAQRCTI----SYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVALAVQNQLS 254
Cdd:cd06614 147 -----LTKE--KSKRNSVvgtpYWMAPEVIKRKDY---GPKVDIWSLGIMCIEMAEGEPPY-LEEPPLRALFLITTKGIP 215
                       250       260
                ....*....|....*....|....*...
gi 46577677 255 IPQSPRHSSA-LRQLLNSMMTVDPHQRP 281
Cdd:cd06614 216 PLKNPEKWSPeFKDFLNKCLVKDPEKRP 243
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-289 1.41e-23

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: 97.19  E-value: 1.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDG-HFYALKRILCHEQQDREEAQ-READMHRLFN----------HPNILRLVAYCLRE 87
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINMTNPAFGRTEQeRDKSVGDIISevniikeqlrHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  88 rgakHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIH-AKGYAHRDLKPTNILLGDEGQPVLMD 166
Cdd:cd08528  82 ----DRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 167 LGSMNQAcihvegSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMfgegPYDMVFQKGDSVA 246
Cdd:cd08528 158 FGLAKQK------GPESSKMTSVVG---TILYSCPEIVQNEPY---GEKADIWALGCILYQMC----TLQPPFYSTNMLT 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 247 LA---VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08528 222 LAtkiVEAEYEPLPEGMYSDDITFVIRSCLTPDPEARPDIVEVSSM 267
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
19-284 2.37e-23

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


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 96.32  E-value: 2.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDR----EEAQREADMHRLFNHPNILRLVAYClrerGAKHEA 94
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGESVAIK-IIDKEQVARegmvEQIKREIAIMKLLRHPNIVELHEVM----ATKTKI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqAC 174
Cdd:cd14663  76 FFVMELVTGGELFSKIA----KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFG----LS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQdwaaQRC-TISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQNQL 253
Cdd:cd14663 148 ALSEQFRQDGLLH----TTCgTPNYVAPEVLARRGY--DGAKADIWSCGVILFVLLAGYLP----FDDENLMALYRKIMK 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 254 SIPQSPRHSSA-LRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14663 218 GEFEYPRWFSPgAKSLIKRILDPNPSTRITVE 249
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
19-284 2.64e-23

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 96.21  E-value: 2.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDrEEAQREADMHRLFNHPNILRLVAYCLRergAKHEAwLLL 98
Cdd:cd14665   1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKID-ENVQREIINHRSLRHPNIVRFKEVILT---PTHLA-IVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWneiERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLM--DLGSMNQACIH 176
Cdd:cd14665  76 EYAAGGELF---ERICNAGRF-SEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKicDFGYSKSSVLH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 vegSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDER-TDVWSLGCVLYAMMFGEGPYD-----MVFQKGDSVALAVq 250
Cdd:cd14665 152 ---SQPKSTVG-------TPAYIAPEVLLKKEY---DGKiADVWSCGVTLYVMLVGAYPFEdpeepRNFRKTIQRILSV- 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 46577677 251 nQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14665 218 -QYSIPDYVHISPECRHLISRIFVADPATRITIP 250
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
25-298 2.71e-23

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: 96.98  E-value: 2.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLV-AYCLRErgakhEAWLLLPFFKR 103
Cdd:cd06659  28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYkSYLVGE-----ELWVLMEYLQG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQA 183
Cdd:cd06659 103 GALTDIVSQTR-----LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTLQDWAaqrctisyrAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmvFQkgDSVALAVQNQLSIP-----QS 258
Cdd:cd06659 178 VGTPYWM---------APE---VISRCPYGTEVDIWSLGIMVIEMVDGEPPY---FS--DSPVQAMKRLRDSPppklkNS 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAP 298
Cdd:cd06659 241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLP 280
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
19-284 4.61e-23

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 95.61  E-value: 4.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDrEEAQREADMHRLFNHPNILRLVAYCLRergAKHEAwLLL 98
Cdd:cd14662   1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKID-ENVQREIINHRSLRHPNIIRFKEVVLT---PTHLA-IVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWneiERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLM--DLGSMNQACIH 176
Cdd:cd14662  76 EYAAGGELF---ERICNAGRF-SEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKicDFGYSKSSVLH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 vegSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDER-TDVWSLGCVLYAMMFGEGPYD-----MVFQKGDSVALAVq 250
Cdd:cd14662 152 ---SQPKSTVG-------TPAYIAPEVLSRKEY---DGKvADVWSCGVTLYVMLVGAYPFEdpddpKNFRKTIQRIMSV- 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 46577677 251 nQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14662 218 -QYKIPDYVRVSQDCRHLLSRIFVANPAKRITIP 250
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
20-288 4.62e-23

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: 95.71  E-value: 4.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGH--FYALKRIlcheqqDREEAQ---------READMHRLFNHPNILRLvaYCLRER 88
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGLkeKVACKII------DKKKAPkdflekflpRELEILRKLRHPNIIQV--YSIFER 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 GAKheAWLLLPFFKRGTLwneIERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd14080  74 GSK--VFIFMEYAEHGDL---LEYIQKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SmnqACIHVEGSRQAL--TLqdwaaqrC-TISYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkgDS- 244
Cdd:cd14080 148 F---ARLCPDDDGDVLskTF-------CgSAAYAAPEI--LQGIPYDPKKYDIWSLGVILYIMLCGSMPFD------DSn 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 245 VALAVQNQ----LSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14080 210 IKKMLKDQqnrkVRFPSSVKKlSPECKDLIDQLLEPDPTKRATIEEILN 258
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-283 5.24e-23

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: 95.48  E-value: 5.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD---REEAQREADMHRLFNHPNILRLVAYCLrergAKHEAWL 96
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDakaRQDCVKEIDLLKQLNHPNVIKYLDSFI----EDNELNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG------SM 170
Cdd:cd08228  80 VLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrffsSK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQACIHVEGsrqaltlqdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVALAVQ 250
Cdd:cd08228 160 TTAAHSLVG---------------TPYYMSPERIHENGY---NFKSDIWSLGCLLYEMAALQSPF-----YGDKMNLFSL 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 251 ----NQLSIPQSPR--HSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd08228 217 cqkiEQCDYPPLPTehYSEKLRELVSMCIYPDPDQRPDI 255
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
20-296 5.86e-23

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 95.80  E-value: 5.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHeQQDREEAQREAD---MHRLFNHPNILRLVAyCLRERgakheawl 96
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKH-FKSLEQVNNLREiqaLRRLSPHPNILRLIE-VLFDR-------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 llpffKRGTL--------WNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQpvLMDL 167
Cdd:cd07831  71 -----KTGRLalvfelmdMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIkDDILK--LADF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GSMNQACihvegSRQALTlqDWAAQRCtisYRAPElfsvqshCVI-----DERTDVWSLGCVLYAMM-----F-GEGPYD 236
Cdd:cd07831 144 GSCRGIY-----SKPPYT--EYISTRW---YRAPE-------CLLtdgyyGPKMDIWAVGCVFFEILslfplFpGTNELD 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 237 MVFQKGD---SVALAVQ------NQLSIPQSPRHSSALRQLL-----------NSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07831 207 QIAKIHDvlgTPDAEVLkkfrksRHMNYNFPSKKGTGLRKLLpnasaegldllKKLLAYDPDER------ITAKQALRHP 280
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
18-287 6.13e-23

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 95.08  E-value: 6.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQ----QDREEAQREADMHRLFNHPNILRLVAYClrerGAKHE 93
Cdd:cd14188   1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAK-IIPHSRvskpHQREKIDKEIELHRILHHKHVVQFYHYF----EDKEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqa 173
Cdd:cd14188  76 IYILLEYCSRRSMAHILKARK----VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFG----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 cihvegsrQALTLQDWAAQRCTI----SYRAPELFSVQSH-CvideRTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALA 248
Cdd:cd14188 147 --------LAARLEPLEHRRRTIcgtpNYLSPEVLNKQGHgC----ESDIWALGCVMYTMLLGRPPFETTNLK-ETYRCI 213
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 249 VQNQLSIPQSprHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14188 214 REARYSLPSS--LLAPAKHLIASMLSKNPEDRPSLDEII 250
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
19-280 6.26e-23

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: 95.49  E-value: 6.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIL-------CHEQQDREEAQREADMH-RLFNHPNILRLVayclrERGA 90
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYksgpnskDGNDFQKLPQLREIDLHrRVSRHPNIITLH-----DVFE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 KHEA-WLLLPFFKRGTLWNEIerlKDKGNFLTEDQILW-LLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPVLMDL 167
Cdd:cd13993  76 TEVAiYIVLEYCPNGDLFEAI---TENRIYVGKTELIKnVFLQLIDAVKHCHSLGIYHRDIKPENILLsQDEGTVKLCDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GsmnqacihvegsrqALTLQDWAAQRCTIS--YRAPELFSVqshcVIDERT-------DVWSLGCVLYAMMFGEGPYDMV 238
Cdd:cd13993 153 G--------------LATTEKISMDFGVGSefYMAPECFDE----VGRSLKgypcaagDIWSLGIILLNLTFGRNPWKIA 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 46577677 239 FQKGDSVALAVQNQLSIPQS-PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd13993 215 SESDPIFYDYYLNSPNLFDViLPMSDDFYNLLRQIFTVNPNNR 257
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
19-296 6.48e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 95.80  E-value: 6.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD-------REEAQreadMHRL--FNHPNILRLVAYCLRERG 89
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDglplstvREVAL----LKRLeaFDHPNIVRLMDVCATSRT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHEAWLLLPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS 169
Cdd:cd07863  77 DRETKVTLVFEHVDQDLRTYLDKVPPPG--LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNQACIHVEGSRQALTLqdWaaqrctisYRAPELFsVQShcVIDERTDVWSLGCVlYAMMF-------GEGPYDMVFQKG 242
Cdd:cd07863 155 ARIYSCQMALTPVVVTL--W--------YRAPEVL-LQS--TYATPVDMWSVGCI-FAEMFrrkplfcGNSEADQLGKIF 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 243 DSVALAVQNQLSI----------PQSPRHSSAL--------RQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07863 221 DLIGLPPEDDWPRdvtlprgafsPRGPRPVQSVvpeieesgAQLLLEMLTFNPHKR------ISAFRALQHP 286
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
18-281 7.64e-23

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: 95.12  E-value: 7.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRlvAYClrERGAKHEAWL 96
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIdLEKCQTSMDELRKEIQAMSQCNHPNVVS--YYT--SFVVGDELWL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnQACIH 176
Cdd:cd06610  77 VMPLLSGGSLL-DIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV--SASLA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAAQRCtisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALAVQN---QL 253
Cdd:cd06610 154 TGGDRTRKVRKTFVGTPC---WMAPEV--MEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPM-KVLMLTLQNdppSL 227
                       250       260
                ....*....|....*....|....*....
gi 46577677 254 SIPQSPR-HSSALRQLLNSMMTVDPHQRP 281
Cdd:cd06610 228 ETGADYKkYSKSFRKMISLCLQKDPSKRP 256
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
25-291 8.44e-23

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 94.91  E-value: 8.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGF------SYVDLVEGLHDGhfyALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLL 97
Cdd:cd00192   2 KLGEGAFgevykgKLKGGDGKTVDV---AVKTLkEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEE----EPLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLW-----NEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---S 169
Cdd:cd00192  75 MEYMEGGDLLdflrkSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGlsrD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNQACIHVEGSRQALTLQdWAaqrctisyrAPE-----LFSVQShcvidertDVWSLGCVLY-AMMFGEGPYDMVfqKGD 243
Cdd:cd00192 155 IYDDDYYRKKTGGKLPIR-WM---------APEslkdgIFTSKS--------DVWSFGVLLWeIFTLGATPYPGL--SNE 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 244 SVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd00192 215 EVLEYLRKGYRLPKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
17-288 9.33e-23

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: 95.15  E-value: 9.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCH--------EQQDREEAQREADMHRLFNHPNILRLVAYCLRER 88
Cdd:cd14084   5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRkftigsrrEINKPRNIETEIEILKKLSHPCIIKIEDFFDAED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 gakhEAWLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd14084  85 ----DYYIVLELMEGGELFDRVVSNKR----LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKIT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACIHVEGSrqaltlqdWAAQRC-TISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVAL 247
Cdd:cd14084 157 DFGLSKILGETS--------LMKTLCgTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYPPFS-----EEYTQM 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 248 AVQNQLS------IPQSPRHSSALRQLL-NSMMTVDPHQRPHIPLLLS 288
Cdd:cd14084 224 SLKEQILsgkytfIPKAWKNVSEEAKDLvKKMLVVDPSRRPSIEEALE 271
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
26-283 1.05e-22

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 94.64  E-value: 1.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD---REEAQREADMHRLFNHPNILRLVAYClrergakHEA---WLLLP 99
Cdd:cd14116  13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKagvEHQLRREVEIQSHLRHPNILRLYGYF-------HDAtrvYLILE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLkdkGNFLTEDQILWLLlGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEG 179
Cdd:cd14116  86 YAPLGTVYRELQKL---SKFDEQRTATYIT-ELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG----WSVHAPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQAlTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAvQNQLSIPqs 258
Cdd:cd14116 158 SRRT-TL-------CgTLDYLPPEMIEGRMH---DEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRIS-RVEFTFP-- 223
                       250       260
                ....*....|....*....|....*
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14116 224 DFVTEGARDLISRLLKHNPSQRPML 248
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
19-287 1.76e-22

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: 93.86  E-value: 1.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA--QREADMHRLFNHPNILRLVayclrERGAKHEAWL 96
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRnlRQEIEILRKLNHPNIIEML-----DSFETKKEFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWneiERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---SMnqa 173
Cdd:cd14002  77 VVTEYAQGELF---QILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGfarAM--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 cihvegSRQALTLqdwAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY--DMVFQkgdSVALAVQN 251
Cdd:cd14002 150 ------SCNTLVL---TSIKGTPLYMAPELVQEQPY---DHTADLWSLGCILYELFVGQPPFytNSIYQ---LVQMIVKD 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 252 QLSIPQ--SPRHSSALRQLLNSmmtvDPHQRPHIPLLL 287
Cdd:cd14002 215 PVKWPSnmSPEFKSFLQGLLNK----DPSKRLSWPDLL 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
19-225 2.06e-22

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 94.56  E-value: 2.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDRE----EAQREADMHRLFNHPNILRLV-AYclrerGAKH 92
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIkLGERKEAKDginfTALREIKLLQELKHPNIIGLLdVF-----GHKS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFfkrgtLWNEIERL-KDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmn 171
Cdd:cd07841  76 NINLVFEF-----METDLEKViKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG--- 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 172 QACIHVEGSR----QALTLqdWaaqrctisYRAPELF---SVQSHCVidertDVWSLGCVL 225
Cdd:cd07841 148 LARSFGSPNRkmthQVVTR--W--------YRAPELLfgaRHYGVGV-----DMWSVGCIF 193
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
19-284 2.58e-22

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 94.26  E-value: 2.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDR---------------------------EEAQREADMHRL 71
Cdd:cd14199   3 QYKLKDEIGKGSYGVVKLAYNEDDNTYYAMK-VLSKKKLMRqagfprrppprgaraapegctqprgpiERVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  72 FNHPNILRLVAyCLRERGAKHeAWLLLPFFKRGTLWnEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKP 151
Cdd:cd14199  82 LDHPNVVKLVE-VLDDPSEDH-LYMVFELVKQGPVM-EVPTLKP----LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 152 TNILLGDEGQPVLMDLGSMNQacihVEGSRQALTlqdwaAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFG 231
Cdd:cd14199 155 SNLLVGEDGHIKIADFGVSNE----FEGSDALLT-----NTVGTPAFMAPETLSETRKIFSGKALDVWAMGVTLYCFVFG 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 232 EGPYdmVFQKGDSVALAVQNQ-LSIPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14199 226 QCPF--MDERILSLHSKIKTQpLEFPDQPDISDDLKDLLFRMLDKNPESRISVP 277
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
26-235 2.82e-22

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 94.02  E-value: 2.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADM-HRLFNHPNILRLVAYcLRERgakHEAWLLLPFFKRG 104
Cdd:cd14090  10 LGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETlHQCQGHPNILQLIEY-FEDD---ERFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ--PVLM---DLGSmnqACIHVEG 179
Cdd:cd14090  86 PLLSHIEKRV----HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvsPVKIcdfDLGS---GIKLSST 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 180 SRQALTLQDWAAQRCTISYRAPE---LFSVQSHcVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14090 159 SMTPVTTPELLTPVGSAEYMAPEvvdAFVGEAL-SYDKRCDLWSLGVILYIMLCGYPPF 216
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
26-268 6.12e-22

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 93.62  E-value: 6.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGL--HD-GHFYALK--RILCHEQQDREEAQREADMHRLFNHPNILRLvAYCLRERGakhEAWLLLPF 100
Cdd:cd05582   3 LGQGSFGKVFLVRKItgPDaGTLYAMKvlKKATLKVRDRVRTKMERDILADVNHPFIVKL-HYAFQTEG---KLYLILDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegS 180
Cdd:cd05582  79 LRGGDLFT---RLSKEVMF-TEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGL----------S 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALAVQNQLSIPQ-- 257
Cdd:cd05582 145 KESIDHEKKAYSFCgTVEYMAPEVVNRRGH---TQSADWWSFGVLMFEMLTGSLPFQGKDRK-ETMTMILKAKLGMPQfl 220
                       250
                ....*....|.
gi 46577677 258 SPRHSSALRQL 268
Cdd:cd05582 221 SPEAQSLLRAL 231
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
25-280 6.78e-22

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: 92.51  E-value: 6.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHEAWLLLPFFKRG 104
Cdd:cd06648  14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYL----VGDELWVVMEFLEGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQAL 184
Cdd:cd06648  90 ALTDIVTHTR-----MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 185 TLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVALAVQNQLSIPQSPRH--- 261
Cdd:cd06648 165 GTPYWM---------APEVISRLPY---GTEVDIWSLGIMVIEMVDGEPPY---FNEPPLQAMKRIRDNEPPKLKNLhkv 229
                       250
                ....*....|....*....
gi 46577677 262 SSALRQLLNSMMTVDPHQR 280
Cdd:cd06648 230 SPRLRSFLDRMLVRDPAQR 248
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
26-296 9.84e-22

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 92.79  E-value: 9.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREAD-MHRLFNHPNILRLVAYClrERGAKHeaWLLLPFFKRG 104
Cdd:cd14174  10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVEtLYQCQGNKNILELIEFF--EDDTRF--YLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL--LGDEGQPVLM---DLGS---MNQACIH 176
Cdd:cd14174  86 SILAHIQKRK----HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILceSPDKVSPVKIcdfDLGSgvkLNSACTP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VegSRQALTLQDWAAQrctisYRAPELFSV--QSHCVIDERTDVWSLGCVLYAMMFGEGPY------DMVFQKGDsVALA 248
Cdd:cd14174 162 I--TTPELTTPCGSAE-----YMAPEVVEVftDEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtDCGWDRGE-VCRV 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 249 VQNQL--SIPQSPRH---------SSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14174 234 CQNKLfeSIQEGKYEfpdkdwshiSSEAKDLISKLLVRDAKER------LSAAQVLQHP 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
26-296 1.22e-21

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 92.34  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD-------REEAQreadMHRL--FNHPNILRLVAYCLRERGaKHEAWL 96
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgiplstiREIAL----LKQLesFEHPNVVRLLDVCHGPRT-DRELKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPF-FKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqaCI 175
Cdd:cd07838  82 TLVFeHVDQDLATYLDKCPKPG--LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFG-----LA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTLqdwaaQRCTISYRAPE--LFSVQSHCVidertDVWSLGCVLYAM-----MFgEGPYDM-----VFQ--- 240
Cdd:cd07838 155 RIYSFEMALTS-----VVVTLWYRAPEvlLQSSYATPV-----DMWSVGCIFAELfnrrpLF-RGSSEAdqlgkIFDvig 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 241 ---KGDSVALAVQNQLSIPQSPRHS----------SALrQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd07838 224 lpsEEEWPRNSALPRSSFPSYTPRPfksfvpeideEGL-DLLKKMLTFNPHKRI------SAFEALQHP 285
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
26-280 1.65e-21

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 92.47  E-value: 1.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVE---GLHDGHFYALKRI----LCHEQQDREEAQREADMHRLFNHPNILRLVaYCLRERGakhEAWLLL 98
Cdd:cd05584   4 LGKGGYGKVFQVRkttGSDKGKIFAMKVLkkasIVRNQKDTAHTKAERNILEAVKHPFIVDLH-YAFQTGG---KLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERlkdKGNFLtEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQaciHVE 178
Cdd:cd05584  80 EYLSGGELFMHLER---EGIFM-EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKE---SIH 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALAVQNQLSIPq 257
Cdd:cd05584 153 DGTVTHTF-------CgTIEYMAPEILTRSGH---GKAVDWWSLGALMYDMLTGAPPFTAENRK-KTIDKILKGKLNLP- 220
                       250       260
                ....*....|....*....|...
gi 46577677 258 sPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05584 221 -PYLTNEARDLLKKLLKRNVSSR 242
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
19-287 3.91e-21

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 90.96  E-value: 3.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLH-DGHFYALKRIL-----CHEQQDREEAQ--READMHRLFNHPNILRLVAYclrERGA 90
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVPLRnTGKPVAIKVVRkadlsSDNLKGSSRANilKEVQIMKRLSHPNIVKLLDF---QESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 KHeAWLLLPFFKRGTLWNEIERLkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG------------- 157
Cdd:cd14096  79 EY-YYIVLELADGGEIFHQIVRL----TYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklrk 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 158 --------DEGQPV------------LMDLGsmnqacihvegsrqaLTLQDWAAQR---C-TISYRAPELFSvqshcviD 213
Cdd:cd14096 154 adddetkvDEGEFIpgvggggigivkLADFG---------------LSKQVWDSNTktpCgTVGYTAPEVVK-------D 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 214 ER----TDVWSLGCVLYAMMFGEGP-YD-------MVFQKGDSVALAvqnqlsiPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14096 212 ERyskkVDMWALGCVLYTLLCGFPPfYDesietltEKISRGDYTFLS-------PWWDEISKSAKDLISHLLTVDPAKRY 284

                ....*.
gi 46577677 282 HIPLLL 287
Cdd:cd14096 285 DIDEFL 290
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-289 5.73e-21

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: 89.80  E-value: 5.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE--AQREADMHRLFNHPNILRLVAYCLRERGAKHEawll 97
Cdd:cd08221   2 YIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERrdALNEIDILSLLNHDNIITYYNHFLDGESLFIE---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIerLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqpvLMDLGSMNQACIHV 177
Cdd:cd08221  78 MEYCNGGNLHDKI--AQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKVLD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTLQDwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMfgegPYDMVFQKGDSVALAVQnqlsIPQ 257
Cdd:cd08221 153 SESSMAESIVG------TPYYMSPELVQGVKY---NFKSDIWAVGCVLYELL----TLKRTFDATNPLRLAVK----IVQ 215
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 258 ------SPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd08221 216 geyediDEQYSEEIIQLVHDCLHQDPEDRPTAEELLER 253
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
19-296 1.20e-20

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 90.07  E-value: 1.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRERGAKHEA-- 94
Cdd:cd07866   9 DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfPITALREIKILKKLKHPNVVPLIDMAVERPDKSKRKrg 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 --WLLLPFFKR---GTLWNEieRLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG- 168
Cdd:cd07866  89 svYMVTPYMDHdlsGLLENP--SVK-----LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGl 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 -SMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELfsvqshcVIDER-----TDVWSLGCVLyAMMFGEGPY------- 235
Cdd:cd07866 162 aRPYDGPPPNPKGGGGGGTRKYTNLVVTRWYRPPEL-------LLGERryttaVDIWGIGCVF-AEMFTRRPIlqgksdi 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 236 ---DMVFQK----------GDSVALAVQNQLSIPQSPR--------HSSALRQLLNSMMTVDPHQRphipllLSQLEALQ 294
Cdd:cd07866 234 dqlHLIFKLcgtpteetwpGWRSLPGCEGVHSFTNYPRtleerfgkLGPEGLDLLSKLLSLDPYKR------LTASDALE 307

                ..
gi 46577677 295 PP 296
Cdd:cd07866 308 HP 309
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
24-281 1.91e-20

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 88.51  E-value: 1.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDR--EEAQREADMHRLFNHPNILRLvaYCL---RErgakhEAWLLL 98
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtiKEIADEMKVLEGLDHPNLVRY--YGVevhRE-----EVYIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVE 178
Cdd:cd06626  79 EYCQEGTL----EELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGS---AVKLKN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQA--LTLQDWAAqrcTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGP---YDMVFQKGDSVALavQNQL 253
Cdd:cd06626 152 NTTTMapGEVNSLVG---TPAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMATGKRPwseLDNEWAIMYHVGM--GHKP 226
                       250       260
                ....*....|....*....|....*...
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd06626 227 PIPDSLQLSPEGKDFLSRCLESDPKKRP 254
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
19-284 2.24e-20

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 88.85  E-value: 2.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALK-----RILCHEQQDR------------EEAQREADMHRLF--------- 72
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAYNESDDKYYAMKvlskkKLLKQYGFPRrppprgskaaqgEQAKPLAPLERVYqeiailkkl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  73 NHPNILRLVAycLRERGAKHEAWLLLPFFKRGTLwneIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPT 152
Cdd:cd14200  81 DHVNIVKLIE--VLDDPAEDNLYMVFDLLRKGPV---MEVPSDKP--FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 153 NILLGDEGQPVLMDLGSMNQacihVEGSRQALTlqdwaAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd14200 154 NLLLGDDGHVKIADFGVSNQ----FEGNDALLS-----STAGTPAFMAPETLSDSGQSFSGKALDVWAMGVTLYCFVYGK 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 233 GPYDmvfqkgDSVALAVQNQLS-----IPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14200 225 CPFI------DEFILALHNKIKnkpveFPEEPEISEELKDLILKMLDKNPETRITVP 275
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
20-288 2.43e-20

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: 88.13  E-value: 2.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNIlrlVAYclreRGAkheawlllp 99
Cdd:cd06613   2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNI---VAY----FGS--------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLW--------NEIERLKDKGNFLTEDQILWlllgICR----GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd06613  66 YLRRDKLWivmeycggGSLQDIYQVTGPLSELQIAY----VCRetlkGLAYLHSTGKIHRDIKGANILLTEDGDVKLADF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GSmnqacihvegsrqaltlqdwAAQ-RCTISYR----------APELFSVQSHCVIDERTDVWSLGCVLYAM------MF 230
Cdd:cd06613 142 GV--------------------SAQlTATIAKRksfigtpywmAPEVAAVERKGGYDGKCDIWALGITAIELaelqppMF 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 231 GEGPYDMVFQ--KGDSVALAVQNQlsipqsPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06613 202 DLHPMRALFLipKSNFDPPKLKDK------EKWSPDFHDFIKKCLTKNPKKRPTATKLLQ 255
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
26-236 2.50e-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: 88.48  E-value: 2.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEgLHDGHFYALKRI---LCHEqqDREEAQREADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPFFK 102
Cdd:cd14066   1 IGSGGFGTVYKGV-LENGTVVAVKRLnemNCAA--SKKEFLTELEMLGRLRHPNLVRLLGYCLE----SDEKLLVYEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGY---AHRDLKPTNILLGDEGQPVLMDLGsmnqacIHVEG 179
Cdd:cd14066  74 NGSL-EDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFG------LARLI 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 180 SRQALTLQDWAAQRcTISYRAPELfsVQSHCViDERTDVWSLGCVLYAMMFGEGPYD 236
Cdd:cd14066 147 PPSESVSKTSAVKG-TIGYLAPEY--IRTGRV-STKSDVYSFGVVLLELLTGKPAVD 199
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
20-280 2.84e-20

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: 88.27  E-value: 2.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-------LCHEQQDREEA--------QREADMHRLFNHPNILRLVAYC 84
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnagLKKEREKRLEKeisrdirtIREAALSSLLNHPHICRLRDFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  85 lreRGAKHeAWLLLPFFKRGTLWNEI---ERLKdkgnfltEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ 161
Cdd:cd14077  83 ---RTPNH-YYMLFEYVDGGQLLDYIishGKLK-------EKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 162 PVLMDLGSMNqaciHVEGSRQALTLqdwaaqrC-TISYRAPELFSVQSHCviDERTDVWSLGCVLYAMMFGEGPYDMVfq 240
Cdd:cd14077 152 IKIIDFGLSN----LYDPRRLLRTF-------CgSLYFAAPELLQAQPYT--GPEVDVWSFGVVLYVLVCGKVPFDDE-- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 241 kgDSVALAVQNQLSIPQSPRH-SSALRQLLNSMMTVDPHQR 280
Cdd:cd14077 217 --NMPALHAKIKKGKVEYPSYlSSECKSLISRMLVVDPKKR 255
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
20-284 3.96e-20

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: 87.32  E-value: 3.96e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCH---EQQDREE-AQREADMHRLFNHPNILRLvaYCLRErgAKHEAW 95
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAVK-ILNRqkiKSLDMEEkIRREIQILKLFRHPHIIRL--YEVIE--TPTDIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERlkdKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacI 175
Cdd:cd14079  79 MVMEYVSGGELFDYIVQ---KGR-LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSN---I 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGsrqaltlqDWAAQRC-TISYRAPELFSVQSHCviDERTDVWSLGCVLYAMMFGEGPYD-----MVFQKGDSVALAV 249
Cdd:cd14079 152 MRDG--------EFLKTSCgSPNYAAPEVISGKLYA--GPEVDVWSCGVILYALLCGSLPFDdehipNLFKKIKSGIYTI 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 250 qnqlsipqsPRH-SSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14079 222 ---------PSHlSPGARDLIKRMLVVDPLKRITIP 248
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
24-283 5.71e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 87.78  E-value: 5.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD---REEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLLLPF 100
Cdd:cd08229  30 KKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDakaRADCIKEIDLLKQLNHPNVIKYYASFIED----NELNIVLEL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG------SMNQAC 174
Cdd:cd08229 106 ADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrffsSKTTAA 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGsrqaltlqdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVALAVQ---- 250
Cdd:cd08229 186 HSLVG---------------TPYYMSPERIHENGY---NFKSDIWSLGCLLYEMAALQSPF-----YGDKMNLYSLckki 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 251 NQLSIPQSP--RHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd08229 243 EQCDYPPLPsdHYSEELRQLVNMCINPDPEKRPDI 277
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
46-296 5.93e-20

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 87.78  E-value: 5.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  46 YALKRIlchEQQDREEAQREADMHRLFNHPNILRLVAycLRERGakHEAWLLLPFFKRGTLWNEIERLKdkgnFLTEDQI 125
Cdd:cd14175  29 YAVKVI---DKSKRDPSEEIEILLRYGQHPNIITLKD--VYDDG--KHVYLVTELMRGGELLDKILRQK----FFSEREA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 126 LWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEgqpvlmdlgSMNQACIHVEG---SRQALTLQDWAAQRC-TISYRAP 201
Cdd:cd14175  98 SSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDE---------SGNPESLRICDfgfAKQLRAENGLLMTPCyTANFVAP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 202 ELFSVQSHcviDERTDVWSLGCVLYAMM-----FGEGPYD-----MVFQKGDSVALAVQNQLSIpqsprhSSALRQLLNS 271
Cdd:cd14175 169 EVLKRQGY---DEGCDIWSLGILLYTMLagytpFANGPSDtpeeiLTRIGSGKFTLSGGNWNTV------SDAAKDLVSK 239
                       250       260
                ....*....|....*....|....*
gi 46577677 272 MMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14175 240 MLHVDPHQR------LTAKQVLQHP 258
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
16-297 8.90e-20

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: 87.40  E-value: 8.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYL--FIqKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHE 93
Cdd:cd06658  19 DPREYLdsFI-KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYL----VGDE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQA 173
Cdd:cd06658  94 LWVVMEFLEGGALTDIVTHTR-----MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAL-AVQNQ 252
Cdd:cd06658 169 SKEVPKRKSLVGTPYWM---------APEVISRLPY---GTEVDIWSLGIMVIEMIDGEPPY---FNEPPLQAMrRIRDN 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 253 L--SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ--LEALQPPA 297
Cdd:cd06658 234 LppRVKDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHpfLKLAGPPS 282
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
60-284 1.07e-19

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 86.64  E-value: 1.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  60 EEAQREADMHRLFNHPNILRLVAyCLRErgaKHEAWLLLPFfkrgtlwneieRLKDKG--------NFLTEDQILWLLLG 131
Cdd:cd14118  59 DRVYREIAILKKLDHPNVVKLVE-VLDD---PNEDNLYMVF-----------ELVDKGavmevptdNPLSEETARSYFRD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihVEGSRQALTlqDWAAqrcTISYRAPELFSVQSHCV 211
Cdd:cd14118 124 IVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNE----FEGDDALLS--STAG---TPAFMAPEALSESRKKF 194
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 212 IDERTDVWSLGCVLYAMMFGEGPydmvFQkgDSVALAVQNQLS-----IPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14118 195 SGKALDIWAMGVTLYCFVFGRCP----FE--DDHILGLHEKIKtdpvvFPDDPVVSEQLKDLILRMLDKNPSERITLP 266
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
14-282 1.29e-19

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 88.70  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   14 IIDNkRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEA----QREA-DMHRLfNHPNIlrlVA-YCLRE 87
Cdd:NF033483   4 LLGG-RYEIGERIGRGGMAEVYLAKDTRLDRDVAVK-VLRPDLARDPEFvarfRREAqSAASL-SHPNI---VSvYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   88 RGAkheawllLPF----FKRG-TLwNEIerLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:NF033483  78 DGG-------IPYivmeYVDGrTL-KDY--IREHGP-LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  163 VLMDLG---SMNQACI----HVEGsrqaltlqdwaaqrcTISYRAPElfsvQS-HCVIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:NF033483 147 KVTDFGiarALSSTTMtqtnSVLG---------------TVHYLSPE----QArGGTVDARSDIYSLGIVLYEMLTGRPP 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 46577677  235 YDmvfqkGDS-VALAVQNQLSIPQSPRH-SSALRQLLNS----MMTVDPHQRPH 282
Cdd:NF033483 208 FD-----GDSpVSVAYKHVQEDPPPPSElNPGIPQSLDAvvlkATAKDPDDRYQ 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
19-288 1.30e-19

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 86.12  E-value: 1.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCH--EQQDREEAQREADMHRLFNHPNILRLVAYclreRGAKHEAWL 96
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEkiPKSDLKSVMGEIDLLKKLNHPNIVKYIGS----VKTKDSLYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacih 176
Cdd:cd06627  77 ILEYVENGSLAS---IIKKFGKF-PESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGV------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 veGSRQALTLQDWAAQRCTISYRAPELFSVQSHCvidERTDVWSLGCVLYAMMFGEGPYdmvfqkGDSVALA-----VQN 251
Cdd:cd06627 146 --ATKLNEVEKDENSVVGTPYWMAPEVIEMSGVT---TASDIWSVGCTVIELLTGNPPY------YDLQPMAalfriVQD 214
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 252 QlSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06627 215 D-HPPLPENISPELRDFLLQCFQKDPTLRPSAKELLK 250
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-280 1.61e-19

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 86.59  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheqQDREEAQREADMHRLF-NHPNILRLVAYCLRErgakHEAWLLLPFFKRG 104
Cdd:cd14092  14 LGDGSFSVCRKCVHKKTGQEFAVKIV-----SRRLDTSREVQLLRLCqGHPNIVKLHEVFQDE----LHTYLVMELLRGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLwneIERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV---LMDLGSmnqACIHVEgsR 181
Cdd:cd14092  85 EL---LERIRKKKRF-TESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAeikIVDFGF---ARLKPE--N 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLQdwaaqrC-TISYRAPELFSvQSHCV--IDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVqnqlSIPQS 258
Cdd:cd14092 156 QPLKTP------CfTLPYAAPEVLK-QALSTqgYDESCDLWSLGVILYTMLSGQVP----FQSPSRNESAA----EIMKR 220
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 259 PRH-------------SSALRQLLNSMMTVDPHQR 280
Cdd:cd14092 221 IKSgdfsfdgeewknvSSEAKSLIQGLLTVDPSKR 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
23-281 1.84e-19

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: 85.95  E-value: 1.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLV-AYCLrergaKHEAWLLLPFF 101
Cdd:cd06611  10 IGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYeAYFY-----ENKLWILIEFC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLkDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihveGSR 181
Cdd:cd06611  85 DGGALDSIMLEL-ERG--LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGV---------SAK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLQDWAAQRCTISYRAPEL-----FSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMV--------FQKGDSVALA 248
Cdd:cd06611 153 NKSTLQKRDTFIGTPYWMAPEVvacetFKDNPY---DYKADIWSLGITLIELAQMEPPHHELnpmrvllkILKSEPPTLD 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 249 vqnqlsipQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd06611 230 --------QPSKWSSSFNDFLKSCLVKDPDDRP 254
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
18-280 2.36e-19

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 86.95  E-value: 2.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVaYCLRErgaKHEA 94
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAhvrAERDILADADSPWIVRLH-YAFQD---EDHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS----- 169
Cdd:cd05573  77 YLVMEYMPGGDLMNLLIKYDV----FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLctkmn 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 ------------MNQACIHVEGSRQALTLQDWAAQRCTI---SYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:cd05573 153 ksgdresylndsVNTLFQDNVLARRRPHKQRRVRAYSAVgtpDYIAPEVLRGTG---YGPECDWWSLGVILYEMLYGFPP 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 235 ydmvFQKGDSVA-----LAVQNQLSIPQSPRHSSALRQLLNSMMTvDPHQR 280
Cdd:cd05573 230 ----FYSDSLVEtyskiMNWKESLVFPDDPDVSPEAIDLIRRLLC-DPEDR 275
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
22-291 2.38e-19

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: 85.51  E-value: 2.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVdlVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLF-NHPNILRLVAYCLRERGAKHeAWLLLPF 100
Cdd:cd13979   7 LQEPLGSGGFGSV--YKATYKGETVAVKIVRRRRKNRASRQSFWAELNAARlRHENIVRVLAAETGTDFASL-GLIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS---MNQACIHV 177
Cdd:cd13979  84 CGNGTLQQLIYEGSEP---LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCsvkLGEGNEVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQaltlqdwaaQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDMVFQkgdSVALAVQNQLSIPQ 257
Cdd:cd13979 161 TPRSH---------IGGTYTYRAPELLKGER---VTPKADIYSFGITLWQMLTRELPYAGLRQ---HVLYAVVAKDLRPD 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 258 SPRHSS-----ALRQLLNSMMTVDPHQRPHIPL-LLSQLE 291
Cdd:cd13979 226 LSGLEDsefgqRLRSLISRCWSAQPAERPNADEsLLKSLE 265
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
27-288 2.77e-19

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 85.43  E-value: 2.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  27 GEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLF-NHPNILRLV-AYCLRE-RGAKHEAWLLLPFFKR 103
Cdd:cd06608  15 GEGTYGKVYKARHKKTGQLAAIK-IMDIIEDEEEEIKLEINILRKFsNHPNIATFYgAFIKKDpPGGDDQLWLVMEYCGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQa 183
Cdd:cd06608  94 GSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV----------SAQ- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 ltLQDWAAQRCTI----SYRAPELFSV--QSHCVIDERTDVWSLGCVLYAMMFGEGPY-DM-----VFQkgdsvalavqn 251
Cdd:cd06608 163 --LDSTLGRRNTFigtpYWMAPEVIACdqQPDASYDARCDVWSLGITAIELADGKPPLcDMhpmraLFK----------- 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 46577677 252 qlsIPQSP--------RHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06608 230 ---IPRNPpptlkspeKWSKEFNDFISECLIKNYEQRPFTEELLE 271
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
64-288 2.98e-19

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 85.22  E-value: 2.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRlvAYCLRErGAKHEAWLLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKG 143
Cdd:cd14165  50 RELEILARLNHKSIIK--TYEIFE-TSDGKVYIVMELGVQGDLLEFIK----LRGALPEDVARKMFHQLSSAIKYCHELD 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 144 YAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVEGSRQALTlqdwaAQRC-TISYRAPELfsVQSHCVIDERTDVWSLG 222
Cdd:cd14165 123 IVHRDLKCENLLLDKDFNIKLTDFG-FSKRCLRDENGRIVLS-----KTFCgSAAYAAPEV--LQGIPYDPRIYDIWSLG 194
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 223 CVLYAMMFGEGPYDmvfqkgDS-----VALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14165 195 VILYIMVCGSMPYD------DSnvkkmLKIQKEHRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLS 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
20-296 3.21e-19

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: 85.61  E-value: 3.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREE------AQREADMHRLFNHPNILRLVAYCLRERGAkhe 93
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI----RLDNEEegipstALREISLLKELKHPNIVKLLDVIHTENKL--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 aWLLLPFFKRgTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG----- 168
Cdd:cd07829  74 -YLVFEYCDQ-DLKKYLDKRPGP---LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGlaraf 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACIhvegSRQALTLqdWaaqrctisYRAPELF--------SVqshcvidertDVWSLGCVLYAM-----MF-GEGP 234
Cdd:cd07829 149 GIPLRTY----THEVVTL--W--------YRAPEILlgskhystAV----------DIWSVGCIFAELitgkpLFpGDSE 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 235 YDMVFQ--------KGDS---VALAVQNQLSIPQS---------PRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQ 294
Cdd:cd07829 205 IDQLFKifqilgtpTEESwpgVTKLPDYKPTFPKWpkndlekvlPRLDPEGIDLLSKMLQYNPAKR------ISAKEALK 278

                ..
gi 46577677 295 PP 296
Cdd:cd07829 279 HP 280
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
26-296 3.25e-19

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 85.46  E-value: 3.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADM-HRLFNHPNILRLVAYCLRErgakHEAWLLLPFFKRG 104
Cdd:cd14173  10 LGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMlYQCQGHRNVLELIEFFEEE----DKFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL--GDEGQPVLM---DLGSmnqaCIHVEG 179
Cdd:cd14173  86 SILSHIHRRRH----FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehPNQVSPVKIcdfDLGS----GIKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWAAQRCTISYRAPELFSV--QSHCVIDERTDVWSLGCVLYAMMFGEGPY------DMVFQKGDSVAlAVQN 251
Cdd:cd14173 158 DCSPISTPELLTPCGSAEYMAPEVVEAfnEEASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgsDCGWDRGEACP-ACQN 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 252 QL--SIPQSPRH---------SSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14173 237 MLfeSIQEGKYEfpekdwahiSCAAKDLISKLLVRDAKQR------LSAAQVLQHP 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
26-293 3.54e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 85.09  E-value: 3.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQD----REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd14146   2 IGVGGFGKV--YRATWKGQEVAVKAARQDPDEDikatAESVRQEAKLFSMLRHPNIIKLEGVCLEEP----NLCLVMEFA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDKGNFLTEDQILWLLL-----GICRGLEAIHAKGYA---HRDLKPTNILLGDEGQpvlmdlgsmnqa 173
Cdd:cd14146  76 RGGTLNRALAAANAAPGPRRARRIPPHILvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIE------------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 ciHVEGSRQALTLQDWAAQR-----------CTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVfqKG 242
Cdd:cd14146 144 --HDDICNKTLKITDFGLARewhrttkmsaaGTYAWMAPE---VIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI--DG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 46577677 243 DSVALAVQ-NQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14146 217 LAVAYGVAvNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
24-288 3.85e-19

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: 85.13  E-value: 3.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILC--HEQQDREEAQR--------EADMHRLFNHPNIlrlVAYCLRERGAKHE 93
Cdd:cd06629   7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELpkTSSDRADSRQKtvvdalksEIDTLKDLDHPNI---VQYLGFEETEDYF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AwLLLPFFKRGTLWNEIERLkdkGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQA 173
Cdd:cd06629  84 S-IFLEYVPGGSIGSCLRKY---GKF-EEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CiHVEGSRQALTLQDwaaqrcTISYRAPELFSVQSHCViDERTDVWSLGCVLYAMMFGEGPY--DMVFQkgdsVALAVQN 251
Cdd:cd06629 159 D-DIYGNNGATSMQG------SVFWMAPEVIHSQGQGY-SAKVDIWSLGCVVLEMLAGRRPWsdDEAIA----AMFKLGN 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 252 QLSIPQSPRH---SSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06629 227 KRSAPPVPEDvnlSPEALDFLNACFAIDPRDRPTAAELLS 266
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
19-284 3.87e-19

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 84.75  E-value: 3.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLvaYCLRErgAKHEAW 95
Cdd:cd14073   2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIkkdKIEDEQDMVRIRREIEIMSSLNHPHIIRI--YEVFE--NKDKIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAci 175
Cdd:cd14073  78 IVMEYASGGELYDYISERRR----LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLY-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hvegSRQALtLQDWAAQRCtisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQnQLSI 255
Cdd:cd14073 152 ----SKDKL-LQTFCGSPL---YASPEI--VNGTPYQGPEVDCWSLGVLLYTLVYGTMPFD-----GSDFKRLVK-QISS 215
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 256 PQ--SPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14073 216 GDyrEPTQPSDASGLIRWMLTVNPKRRATIE 246
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
20-296 4.77e-19

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: 84.62  E-value: 4.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVdlVEGLH--DGHFYALKRILCHEqqDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLL 97
Cdd:cd06612   5 FDILEKLGEGSYGSV--YKAIHkeTGQVVAIKVVPVEE--DLQEIIKEISILKQCDSPYIVKYYGSYFKN----TDLWIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLwNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihv 177
Cdd:cd06612  77 MEYCGAGSV-SDIMKITNKT--LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ----- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egsrqaltLQDWAAQRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVALAVQNQ- 252
Cdd:cd06612 149 --------LTDTMAKRNTVIgtpfWMAPEVIQEIGY---NNKADIWSLGITAIEMAEGKPPYSDI--HPMRAIFMIPNKp 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 253 ---LSIPQ--SPRHSSALRQLLnsmmTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd06612 216 pptLSDPEkwSPEFNDFVKKCL----VKDPEERP------SAIQLLQHP 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
44-280 6.57e-19

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: 84.27  E-value: 6.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  44 HFYAlkrILCHEQQDREEAQREADMHRLFNHPNILRLVAYclrergakHEA----WLLLPFFKRGTLWNEIErlKDKGnf 119
Cdd:cd14010  26 EFVA---IKCVDKSKRPEVLNEVRLTHELKHPNVLKFYEW--------YETsnhlWLVVEYCTGGDLETLLR--QDGN-- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqaCIHVEGSRQALTLQDWAAQ------- 192
Cdd:cd14010  91 LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFG-----LARREGEILKELFGQFSDEgnvnkvs 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 193 -----RCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQ------NQLSIPQSPRH 261
Cdd:cd14010 166 kkqakRGTPYYMAPELFQGGVHSF---ASDLWALGCVLYEMFTGKPP----FVAESFTELVEKilnedpPPPPPKVSSKP 238
                       250
                ....*....|....*....
gi 46577677 262 SSALRQLLNSMMTVDPHQR 280
Cdd:cd14010 239 SPDFKSLLKGLLEKDPAKR 257
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
20-284 7.44e-19

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: 83.84  E-value: 7.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLveGLH--DGHFYALKrILCHEQQDREEA----QREADMHRLFNHPNILRLvaYCLRErgAKHE 93
Cdd:cd14081   3 YRLGKTLGKGQTGLVKL--AKHcvTGQKVAIK-IVNKEKLSKESVlmkvEREIAIMKLIEHPNVLKL--YDVYE--NKKY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERlkdKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMnqA 173
Cdd:cd14081  76 LYLVLEYVSGGELFDYLVK---KGR-LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFG-M--A 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSrqaltlqdWAAQRC-TISYRAPELFSVQSHcviDERT-DVWSLGCVLYAMMFGEGPYDmvfqkGDSVA---LA 248
Cdd:cd14081 149 SLQPEGS--------LLETSCgSPHYACPEVIKGEKY---DGRKaDIWSCGVILYALLVGALPFD-----DDNLRqllEK 212
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 249 VQN-QLSIPqsPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14081 213 VKRgVFHIP--HFISPDAQDLLRRMLEVNPEKRITIE 247
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-296 7.60e-19

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 84.78  E-value: 7.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHE--QQDREEAQREADMHRLFNHPNILRLVAyCLRERGAKheaW 95
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKlsARDHQKLEREARICRLLKHPNIVRLHD-SISEEGFH---Y 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG--DEGQPV-LMDLGsmnq 172
Cdd:cd14086  77 LVFDLVTGGELFEDIVARE----FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLAskSKGAAVkLADFG---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 ACIHVEGSRQAltlqdWAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-DMVFQKGDSVALAVQN 251
Cdd:cd14086 149 LAIEVQGDQQA-----WFGFAGTPGYLSPEVLRKDPY---GKPVDIWACGVILYILLVGYPPFwDEDQHRLYAQIKAGAY 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 46577677 252 QLSIPQSPRHSSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd14086 221 DYPSPEWDTVTPEAKDLINQMLTVNPAKRI------TAAEALKHP 259
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
18-288 1.06e-18

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: 83.83  E-value: 1.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALK---RILCHEQQDREEAQREADMHRLFNHPNILRLVAYClrERGakHEA 94
Cdd:cd14187   7 RRYVRGRFLGKGGFAKCYEITDADTKEVFAGKivpKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFF--EDN--DFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQac 174
Cdd:cd14187  83 YVVLELCRRRSLLELHKRRKA----LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATK-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQAlTLqdwaaqrC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAvQNQL 253
Cdd:cd14187 157 VEYDGERKK-TL-------CgTPNYIAPEVLSKKGHSF---EVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIK-KNEY 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 254 SIPQ--SPRHSSALRQLLNSmmtvDPHQRPHIPLLLS 288
Cdd:cd14187 225 SIPKhiNPVAASLIQKMLQT----DPTARPTINELLN 257
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
18-272 1.25e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 83.93  E-value: 1.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYV----DLVEGlhdGHFYALKRIlchEQQDREEAQ-----READMHR---LFNHPNILRLVAYCL 85
Cdd:cd07862   1 QQYECVAEIGEGAYGKVfkarDLKNG---GRFVALKRV---RVQTGEEGMplstiREVAVLRhleTFEHPNVVRLFDVCT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  86 RERGAKHEAWLLLPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLM 165
Cdd:cd07862  75 VSRTDRETKLTLVFEHVDQDLTTYLDKVPEPG--VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 166 DLGSMNQACIHVEGSRQALTLqdWaaqrctisYRAPELFSVQSHCVideRTDVWSLGCVlYAMMF-------GEGPYDMV 238
Cdd:cd07862 153 DFGLARIYSFQMALTSVVVTL--W--------YRAPEVLLQSSYAT---PVDLWSVGCI-FAEMFrrkplfrGSSDVDQL 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 239 FQKGDSVALAVQ----NQLSIPQ---SPRHSSALRQLLNSM 272
Cdd:cd07862 219 GKILDVIGLPGEedwpRDVALPRqafHSKSAQPIEKFVTDI 259
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-280 1.43e-18

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 84.21  E-value: 1.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQR---EADMHRLFNHPNILRLvaYCLRErgAKHEAWLLLP 99
Cdd:cd05574   6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRvltEREILATLDHPFLPTL--YASFQ--TSTHLCFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERlkDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-SMNQACI-HV 177
Cdd:cd05574  82 YCPGGELFRLLQK--QPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDlSKQSSVTpPP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 E----------GSRQALTLQDWAAQRCTIS--------YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY---- 235
Cdd:cd05574 160 VrkslrkgsrrSSVKSIEKETFVAEPSARSnsfvgteeYIAPEVIKGDGH---GSAVDWWTLGILLYEMLYGTTPFkgsn 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 236 -DMVFQKgdsvalAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05574 237 rDETFSN------ILKKELTFPESPPVSSEAKDLIRKLLVKDPSKR 276
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
18-289 1.54e-18

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 83.42  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGlHDGHFYALKRILC--HEQQDREEAQREADM-HRLFNHPNILRLVAYCLRERgaKHEA 94
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLegADEQTLQSYKNEIELlKKLKGSDRIIQLYDYEVTDE--DDYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFfkRGTLWNEIERLKDKGNF-LTEDQILW--LLLGIcrglEAIHAKGYAHRDLKPTNILLGDeGQPVLMDLGSMN 171
Cdd:cd14131  78 YMVMEC--GEIDLATILKKKRPKPIdPNFIRYYWkqMLEAV----HTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 Q-----ACIHVEgsrqaltlqdwaAQRCTISYRAPELFSVQSHCVIDER-------TDVWSLGCVLYAMMFGEGPYDMvF 239
Cdd:cd14131 151 AiqndtTSIVRD------------SQVGTLNYMSPEAIKDTSASGEGKPkskigrpSDVWSLGCILYQMVYGKTPFQH-I 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 240 QKGDSVALAVQNQLSIPQSPRHSS-ALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd14131 218 TNPIAKLQAIIDPNHEIEFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNH 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
26-280 1.57e-18

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 83.04  E-value: 1.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAyCLRErgaKHEAWLLLPFFKR 103
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKklQENLESEIAILKSIKHPNIVRLYD-VQKT---EDFIYLVLEYCAG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPVL--MDLGSmnqacihvegs 180
Cdd:cd14009  77 GDLSQYIRKRGR----LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLsTSGDDPVLkiADFGF----------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 rqALTLQDW--AAQRCTiS--YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALaVQN----- 251
Cdd:cd14009 142 --ARSLQPAsmAETLCG-SplYMAPEILQFQKY---DAKADLWSVGAILFEMLVGKPP----FRGSNHVQL-LRNiersd 210
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 252 -QLSIPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14009 211 aVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
26-235 1.68e-18

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: 83.04  E-value: 1.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCH---EQQDREEAQREADMHRLFNHPNILRLVAYClreRGAKHeAWLLLPFFK 102
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivQTRQQEHIFSEKEILEECNSPFIVKLYRTF---KDKKY-LYMLMEYCL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEierLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihVEGSRQ 182
Cdd:cd05572  77 GGELWTI---LRDRGLF-DEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK----LGSGRK 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 183 ALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05572 149 TWTF-------CgTPEYVAPEIILNKGY---DFSVDYWSLGILLYELLTGRPPF 192
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
20-281 1.93e-18

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 83.45  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEaqrEAD-MHRLFNHPNILRLvaYCLRERGAKheAWLLL 98
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVK-IIDKSKRDPSE---EIEiLLRYGQHPNIITL--RDVYDDGNS--VYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEgqpvlmdlgsmnqacihvE 178
Cdd:cd14091  74 ELLRGGELLDRILRQK----FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADE------------------S 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQD--WAAQ-R---------C-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY--------DM 237
Cdd:cd14091 132 GDPESLRICDfgFAKQlRaengllmtpCyTANFVAPEVLKKQGY---DAACDIWSLGVLLYTMLAGYTPFasgpndtpEV 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 238 VFQK-GDS-VALAVQNQLSIpqsprhSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14091 209 ILARiGSGkIDLSGGNWDHV------SDSAKDLVRKMLHVDPSQRP 248
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
17-296 2.34e-18

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: 82.67  E-value: 2.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLV-AYCLRErgakhEAW 95
Cdd:cd06647   6 KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGD-----ELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacI 175
Cdd:cd06647  81 VVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ--I 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAL---AVQNQ 252
Cdd:cd06647 154 TPEQSKRSTMVG-------TPYWMAPEVVTRKAY---GPKVDIWSLGIMAIEMVEGEPPY---LNENPLRALyliATNGT 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 46577677 253 LSIPQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd06647 221 PELQNPEKLSAIFRDFLNRCLEMDVEKR------GSAKELLQHP 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
19-234 2.66e-18

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: 83.73  E-value: 2.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILcHEQQDREEAQ---READMHRLFNHPNILRLVAyclrergakheaw 95
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIS-NVFDDLIDAKrilREIKILRHLKHENIIGLLD------------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFfkrgtlwnEIERLKD-----------------KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGD 158
Cdd:cd07834  67 ILRPP--------SPEEFNDvyivtelmetdlhkvikSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNS 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 159 EGQPVLMDLGSMNQACIhvEGSRQALTlqDWAAQRCtisYRAPELFSVQSHCviDERTDVWSLGCVLyAMMFGEGP 234
Cdd:cd07834 139 NCDLKICDFGLARGVDP--DEDKGFLT--EYVVTRW---YRAPELLLSSKKY--TKAIDIWSVGCIF-AELLTRKP 204
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
19-231 3.74e-18

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 82.76  E-value: 3.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREAD-MHRLFNHPNILRLVAYCLrergakHEAW 95
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGgiPNQALREIKaLQACQGHPYVVKLRDVFP------HGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPF-FKRGTLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---SMN 171
Cdd:cd07832  75 FVLVFeYMLSSLS---EVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGlarLFS 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 172 QacihvEGSRQaltlqdWAAQRCTISYRAPE-LFSVQSHcviDERTDVWSLGCVLYAMMFG 231
Cdd:cd07832 152 E-----EDPRL------YSHQVATRWYRAPElLYGSRKY---DEGVDLWAVGCIFAELLNG 198
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
24-287 3.81e-18

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 82.07  E-value: 3.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEA----QREADMHRLFNHPNILRLVAyclrerGAKHEA--WL 96
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVsLVDDDKKSRESvkqlEQEIALLSKLRHPNIVQYYG------TEREEDnlYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQaciH 176
Cdd:cd06632  80 FLEYVPGGSIHK---LLQRYGAF-EEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFG-MAK---H 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAaqrctiSYRAPELFsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVALAVQNQLSIP 256
Cdd:cd06632 152 VEAFSFAKSFKGSP------YWMAPEVI-MQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQY--EGVAAIFKIGNSGELP 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 257 QSPRH-SSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06632 223 PIPDHlSPDAKDFIRLCLQRDPEDRPTASQLL 254
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
26-280 4.39e-18

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 82.38  E-value: 4.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMhrLFNHPNIL-----RLVAYCLRERGAKHEAWLLLPF 100
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKL----EKKRIKKRKGEAM--ALNEKQILekvnsRFVVSLAYAYETKDALCLVLTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHV-EG 179
Cdd:cd05630  82 MNGGDLKFHIYHMGQAG--FPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLG----LAVHVpEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 srqaltlQDWAAQRCTISYRAPELfsvqshcVIDER----TDVWSLGCVLYAMMFGEGPYDMVFQK-----GDSVALAVQ 250
Cdd:cd05630 156 -------QTIKGRVGTVGYMAPEV-------VKNERytfsPDWWALGCLLYEMIAGQSPFQQRKKKikreeVERLVKEVP 221
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSmmtvDPHQR 280
Cdd:cd05630 222 EEYSEKFSPQARSLCSMLLCK----DPAER 247
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
19-287 5.35e-18

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 82.09  E-value: 5.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRERgakheAWL 96
Cdd:cd07846   2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKmvKKIAMREIKMLKQLRHENLVNLIEVFRRKK-----RWY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacih 176
Cdd:cd07846  77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQIL---RGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTlqDWAAQRCtisYRAPELFsvqshcVIDER----TDVWSLGCVLYAMMFGE----GPYDM----------- 237
Cdd:cd07846 150 LAAPGEVYT--DYVATRW---YRAPELL------VGDTKygkaVDVWAVGCLVTEMLTGEplfpGDSDIdqlyhiikclg 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 238 --------VFQKGDSVALAVQNQLSIPQS-----PRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd07846 219 nliprhqeLFQKNPLFAGVRLPEVKEVEPlerryPKLSGVVIDLAKKCLHIDPDKRPSCSELL 281
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
24-298 7.65e-18

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 81.59  E-value: 7.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVdlVEGLHDGHFYALK------RILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLR--ERGAKHEAW 95
Cdd:cd05075   6 KTLGEGEFGSV--MEGQLNQDDSVLKvavktmKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQntESEGYPSPV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEI--ERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQA 173
Cdd:cd05075  84 VILPFMKHGDLHSFLlySRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFG-LSKK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQ---DWAAqrctISYRAPELFSVQShcvidertDVWSLGCVLYAMMF-GEGPYDMVFQKGDSVALAV 249
Cdd:cd05075 163 IYNGDYYRQGRISKmpvKWIA----IESLADRVYTTKS--------DVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQ 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 250 QNQLSipQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAP 298
Cdd:cd05075 231 GNRLK--QPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
16-297 1.10e-17

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: 81.22  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYL--FIqKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHE 93
Cdd:cd06657  17 DPRTYLdnFI-KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYL----VGDE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQA 173
Cdd:cd06657  92 LWVVMEFLEGGALTDIVTHTR-----MNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVALA-VQNQ 252
Cdd:cd06657 167 SKEVPRRKSLVGTPYWM---------APELISRLPY---GPEVDIWSLGIMVIEMVDGEPPY---FNEPPLKAMKmIRDN 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 253 L--SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ--LEALQPPA 297
Cdd:cd06657 232 LppKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHpfLAKAGPPS 280
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
20-283 1.27e-17

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 80.63  E-value: 1.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVdlVEGLH--DGHFYALKRIlcHEQQDREEA------QREADMHRLFNHPNILRLVAYCLRErgak 91
Cdd:cd14070   4 YLIGRKLGEGSFAKV--REGLHavTGEKVAIKVI--DKKKAKKDSyvtknlRREGRIQQMIRHPNITQLLDILETE---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN 171
Cdd:cd14070  76 NSYYLVMELCPGGNL---MHRIYDKKR-LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qaCIHVEGSRQALTLQdwaaqrC-TISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMMFGEGPYDM-------VFQKgd 243
Cdd:cd14070 152 --CAGILGYSDPFSTQ------CgSPAYAAPELL---ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVepfslraLHQK-- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 244 svalAVQNQLSiPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14070 219 ----MVDKEMN-PLPTDLSPGAISFLRSLLEPDPLKRPNI 253
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
20-287 1.71e-17

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 80.12  E-value: 1.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALK-----RILCH---EQQDREEAQRE-ADMHRL--FNHPNILRLVAYClrer 88
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDtwvRDRKLGTVPLEiHILDTLnkRSHPNIVKLLDFF---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 GAKHEAWLLLPFFKRGT-LWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd14004  78 EDDEFYYLVMEKHGSGMdLFDFIERKPN----MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GSmnqaCIHVEGSRqaltlqdWAAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPYdmvfqkgDSVAL 247
Cdd:cd14004 154 GS----AAYIKSGP-------FDTFVGTIDYAAPEVLRGNPY--GGKEQDIWALGVLLYTLVFKENPF-------YNIEE 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 248 AVQNQLSIPQSprHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14004 214 ILEADLRIPYA--VSEDLIDLISRMLNRDVGDRPTIEELL 251
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
13-293 2.24e-17

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 80.35  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  13 VIIDNKRYLFIQKLGEGGFSYV-DLVEGLHDGHF--YALK----RILCheQQDREEAQREADMHRLFNHPNILRLVAYCL 85
Cdd:cd05074   4 VLIQEQQFTLGRMLGKGEFGSVrEAQLKSEDGSFqkVAVKmlkaDIFS--SSDIEEFLREAACMKEFDHPNVIKLIGVSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  86 RER--GAKHEAWLLLPFFKRGTL--WNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ 161
Cdd:cd05074  82 RSRakGRLPIPMVILPFMKHGDLhtFLLMSRIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 162 PVLMDLG---SMNQACIHVEGSRQALTLQdWAAqrctISYRAPELFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDM 237
Cdd:cd05074 162 VCVADFGlskKIYSGDYYRQGCASKLPVK-WLA----LESLADNVYTTHS--------DVWAFGVTMWEIMtRGQTPYAG 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 238 VFQKGDSVALAVQNQLSipQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05074 229 VENSEIYNYLIKGNRLK--QPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-280 2.55e-17

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 80.69  E-value: 2.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlchEQQDREEAQREADMHRLF-NHPNILRLvayclrergakHE-------AWLL 97
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKII---SRRMEANTQREVAALRLCqSHPNIVAL-----------HEvlhdqyhTYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLwneIERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHV 177
Cdd:cd14180  80 MELLRGGEL---LDRIKKKARF-SESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARLRP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTlqdwaaqRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmVFQKGDSVALAVQNQLSIP 256
Cdd:cd14180 156 QGSRPLQT-------PCfTLQYAAPELFSNQGY---DESCDLWSLGVILYTMLSGQVPFQ-SKRGKMFHNHAADIMHKIK 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 257 QS---------PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14180 225 EGdfslegeawKGVSEEAKDLVRGLLTVDPAKR 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-280 3.29e-17

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 80.47  E-value: 3.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheqQDREEA--QREADMHRLFN-HPNILRLvayclrergakHE-------AW 95
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIV-----SKRMEAntQREIAALKLCEgHPNIVKL-----------HEvyhdqlhTF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLwneIERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACI 175
Cdd:cd14179  79 LVMELLKGGEL---LERIKKKQHF-SETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTlqdwaaqRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSvALAVQNQLS 254
Cdd:cd14179 155 KPPDNQPLKT-------PCfTLHYAAPELLNYNGY---DESCDLWSLGVILYTMLSGQVP----FQCHDK-SLTCTSAEE 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 255 IPQSPRH-------------SSALRQLLNSMMTVDPHQR 280
Cdd:cd14179 220 IMKKIKQgdfsfegeawknvSQEAKDLIQGLLTVDPNKR 258
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
26-293 3.45e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 79.26  E-value: 3.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQD----REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd14148   2 IGVGGFGKV--YKGLWRGEEVAVKAARQDPDEDiavtAENVRQEARLFWMLQHPNIIALRGVCLNPP----HLCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDKGNFLTEdqilWLLlGICRGLEAIHAKGYA---HRDLKPTNILLGDEGQPvlMDLgsmnqacihve 178
Cdd:cd14148  76 RGGALNRALAGKKVPPHVLVN----WAV-QIARGMNYLHNEAIVpiiHRDLKSSNILILEPIEN--DDL----------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 gSRQALTLQDWAAQR-----------CTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVfqkgDSVAL 247
Cdd:cd14148 138 -SGKTLKITDFGLARewhkttkmsaaGTYAWMAPE---VIRLSLFSKSSDVWSFGVLLWELLTGEVPYREI----DALAV 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 248 A---VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14148 210 AygvAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
46-287 5.21e-17

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 79.67  E-value: 5.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  46 YALKRIlchEQQDREEAQREADMHRLFNHPNILRLVAycLRERGAKheAWLLLPFFKRGTLWNEIERLKdkgnFLTEDQI 125
Cdd:cd14178  31 YAVKII---DKSKRDPSEEIEILLRYGQHPNIITLKD--VYDDGKF--VYLVMELMRGGELLDRILRQK----CFSEREA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 126 LWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQP---VLMDLGSMNQAcihveGSRQALTLQDwaaqrC-TISYRA 200
Cdd:cd14178 100 SAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsGNPesiRICDFGFAKQL-----RAENGLLMTP-----CyTANFVA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 201 PELFSVQSHcviDERTDVWSLGCVLYAMM-----FGEGPYD----MVFQKGD-SVALAVQNQLSIpqsprhSSALRQLLN 270
Cdd:cd14178 170 PEVLKRQGY---DAACDIWSLGILLYTMLagftpFANGPDDtpeeILARIGSgKYALSGGNWDSI------SDAAKDIVS 240
                       250
                ....*....|....*..
gi 46577677 271 SMMTVDPHQRPHIPLLL 287
Cdd:cd14178 241 KMLHVDPHQRLTAPQVL 257
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
26-235 6.03e-17

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 78.42  E-value: 6.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLV-AYclrerGAKHEAWLLLPFFKRG 104
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYdAF-----ETPREMVLVMEYVAGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILlgdegqpvlmdlgsmnqaCIHVEGSRqaL 184
Cdd:cd14103  76 ELF---ERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENIL------------------CVSRTGNQ--I 132
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 185 TLQDWA-AQRC-----------TISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14103 133 KIIDFGlARKYdpdkklkvlfgTPEFVAPEVVNYEP---ISYATDMWSVGVICYVLLSGLSPF 192
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
26-288 6.29e-17

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: 6.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLveGL-HDGHFYALKRILCHE------QQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLLL 98
Cdd:cd06631   9 LGKGAYGTVYC--GLtSTGQLIAVKQVELDTsdkekaEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLED----NVVSIFM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIER---LKDKGNFLTEDQILwlllgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACI 175
Cdd:cd06631  83 EFVPGGSIASILARfgaLEEPVFCRYTKQIL-------EGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTLQdwaAQRCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPY-DM-----VFQKGDSVALav 249
Cdd:cd06631 156 NLSSGSQSQLLK---SMRGTPYWMAPEVINETGHGR---KSDIWSIGCTVFEMATGKPPWaDMnpmaaIFAIGSGRKP-- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 250 qnqlsIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06631 228 -----VPRLPDKfSPEARDFVHACLTRDQDERPSAEQLLK 262
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
26-280 6.47e-17

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 79.63  E-value: 6.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMhrLFNHPNIL-----RLVAYCLRERGAKHEAWLLLPF 100
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRL----EKKRIKKRKGESM--ALNEKQILekvnsQFVVNLAYAYETKDALCLVLTI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacihvegs 180
Cdd:cd05632  84 MNGGDLKFHIYNMGNPG--FEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLG------------ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 rQALTLQDWAAQR---CTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQ--KGDSVALAVQNQLSI 255
Cdd:cd05632 150 -LAVKIPEGESIRgrvGTVGYMAPEVLNNQRYTL---SPDYWGLGCLIYEMIEGQSPFRGRKEkvKREEVDRRVLETEEV 225
                       250       260
                ....*....|....*....|....*
gi 46577677 256 pQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05632 226 -YSAKFSEEAKSICKMLLTKDPKQR 249
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-281 6.87e-17

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 78.55  E-value: 6.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREAD-MHRLfNHPNILRLVAYClrergaKHEAWLLLPFFKRGTLWNEIerLKDKGNFLTEDQILWlLLGI 132
Cdd:cd05060  35 HEKAGKKEFLREASvMAQL-DHPCIVRLIGVC------KGEPLMLVMELAPLGPLLKY--LKKRREIPVSDLKEL-AHQV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 133 CRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVEGSRQALTLQDWAaqrctISYRAPELFsvqSHCVI 212
Cdd:cd05060 105 AMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFG-MSRALGAGSDYYRATTAGRWP-----LKWYAPECI---NYGKF 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 213 DERTDVWSLGCVLYAMM-FGEGPY-DMvfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05060 176 SSKSDVWSYGVTLWEAFsYGAKPYgEM---KGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYRPEDRP 243
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
20-280 7.32e-17

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 79.16  E-value: 7.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCH---EQQDREEAQREADMHRLFNHPNILRLVayclrerGAKHEAW- 95
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAkiiKLKQVEHVLNEKRILSEVRHPFIVNLL-------GSFQDDRn 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 --LLLPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqA 173
Cdd:cd05580  76 lyMVMEYVPGGELFS---LLRRSGRF-PNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFG----F 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGsrQALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YD----MVFQKgdsval 247
Cdd:cd05580 148 AKRVKD--RTYTL-------CgTPEYLAPEIILSKGH---GKAVDWWALGILIYEMLAGYPPfFDenpmKIYEK------ 209
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 248 AVQNQLSIPQSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05580 210 ILEGKIRFPSF--FDPDAKDLIKRLLVVDLTKR 240
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
26-287 7.76e-17

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 78.36  E-value: 7.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYClrerGAKHEAWLLLPFFK 102
Cdd:cd14186   9 LGKGSFACVYRARSLHTGLEVAIKMIdkkAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYF----EDSNYVYLVLEMCH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGtlwnEIER-LKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEgsr 181
Cdd:cd14186  85 NG----EMSRyLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLqdwaaqrC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMvfqkgDSVALAVQN-QLSIPQSP 259
Cdd:cd14186 158 KHFTM-------CgTPNYISPEIATRSAHGL---ESDVWSLGCMFYTLLVGRPPFDT-----DTVKNTLNKvVLADYEMP 222
                       250       260
                ....*....|....*....|....*....
gi 46577677 260 RHSSALRQ-LLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14186 223 AFLSREAQdLIHQLLRKNPADRLSLSSVL 251
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
26-293 7.77e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 78.53  E-value: 7.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQD----REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd14147  11 IGIGGFGKV--YRGSWRGELVAVKAARQDPDEDisvtAESVRQEARLFAMLAHPNIIALKAVCLEEP----NLCLVMEYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDKGNFLTEdqilWLLlGICRGLEAIHAKGYA---HRDLKPTNILLGDEGQPVLMDLGSMNQACIHVE 178
Cdd:cd14147  85 AGGPLSRALAGRRVPPHVLVN----WAV-QIARGMHYLHCEALVpviHRDLKSNNILLLQPIENDDMEHKTLKITDFGLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDWAAqrcTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVALAVQ-NQLSIPQ 257
Cdd:cd14147 160 REWHKTTQMSAAG---TYAWMAPEVIKAST---FSKGSDVWSFGVLLWELLTGEVPYRGI--DCLAVAYGVAvNKLTLPI 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 258 SPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14147 232 PSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
135-281 8.46e-17

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 78.41  E-value: 8.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACI--HVEGSRQALTLQDWAAQR----CTISYRAPELFSVQS 208
Cdd:cd05579 105 ALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVrrQIKLSIQKKSNGAPEKEDrrivGTPDYLAPEILLGQG 184
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 209 HcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgdsvalAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05579 185 H---GKTVDWWSLGVILYEFLVGIPPFhaetpEEIFQN------ILNGKIEWPEDPEVSDEAKDLISKLLTPDPEKRL 253
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
19-280 8.95e-17

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 78.51  E-value: 8.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQK--LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQDREEAQ----READMHRLFNHPNILRLVAYclreRGAKH 92
Cdd:cd14202   1 KFEFSRKdlIGHGAFAVV--FKGRHKEKHDLEVAVKCINKKNLAKSQtllgKEIKILKELKHENIVALYDF----QEIAN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL----GDEGQPvlmdlg 168
Cdd:cd14202  75 SVYLVMEYCNGGDL---ADYLHTMRT-LSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNP------ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 smNQACIHVEGSRQALTLQD--WAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSV 245
Cdd:cd14202 145 --NNIRIKIADFGFARYLQNnmMAATLCgSPMYMAPEVIMSQHY---DAKADLWSIGTIIYQCLTGKAP----FQASSPQ 215
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 246 ALAV---QNQLSIPQSPRHSSA-LRQLLNSMMTVDPHQR 280
Cdd:cd14202 216 DLRLfyeKNKSLSPNIPRETSShLRQLLLGLLQRNQKDR 254
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
26-280 9.26e-17

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 78.72  E-value: 9.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLvAYCLRergAKHEAWLLLPFFK 102
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLdkkRIKKKKGETMALNEKIILEKVSSPFIVSL-AYAFE---TKDKLCLVLTLMN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQ 182
Cdd:cd05577  77 GGDLKYHIYNVGTRG--FSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLG----LAVEFKGGKK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 AltlqdwAAQRCTISYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfQKGDSVALAVQNQLSIPQ----S 258
Cdd:cd05577 151 I------KGRVGTHGYMAPEV--LQKEVAYDFSVDWFALGCMLYEMIAGRSPFR---QRKEKVDKEELKRRTLEMaveyP 219
                       250       260
                ....*....|....*....|..
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05577 220 DSFSPEARSLCEGLLQKDPERR 241
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
54-293 1.05e-16

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 78.37  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLwNEIERLKDkGNFlTEDQILWLLLGIC 133
Cdd:cd05065  44 YTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSR----PVMIITEFMENGAL-DSFLRQND-GQF-TVIQLVGMLRGIA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 134 RGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaciHVEGSRQALTLQDWAAQRCTISYRAPELFSVQShcvID 213
Cdd:cd05065 117 AGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSR----FLEDDTSDPTYTSSLGGKIPIRWTAPEAIAYRK---FT 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 214 ERTDVWSLGCVLYAMM-FGEGPY-DMVFQkgdSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05065 190 SASDVWSYGIVMWEVMsYGERPYwDMSNQ---DVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLD 266

                ..
gi 46577677 292 AL 293
Cdd:cd05065 267 KM 268
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
20-280 1.26e-16

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 78.91  E-value: 1.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIlchEQQDREEAQREADMHRLFNHPNILRLVAycLRERGakHEAWLLLP 99
Cdd:cd14176  21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILLRYGQHPNIITLKD--VYDDG--KYVYVVTE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPV---LMDLGSMNQAci 175
Cdd:cd14176  94 LMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsGNPEsirICDFGFAKQL-- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hveGSRQALTLQDwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMM-----FGEGPYDMvfqKGDSVALAV 249
Cdd:cd14176 168 ---RAENGLLMTP-----CyTANFVAPEVLERQGY---DAACDIWSLGVLLYTMLtgytpFANGPDDT---PEEILARIG 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 250 QNQLSIPQSPRHSSA--LRQLLNSMMTVDPHQR 280
Cdd:cd14176 234 SGKFSLSGGYWNSVSdtAKDLVSKMLHVDPHQR 266
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
18-287 1.50e-16

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: 77.66  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYClrerGAKHEA 94
Cdd:cd14189   1 RSYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIphsRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHF----EDAENI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqac 174
Cdd:cd14189  77 YIFLELCSRKSL----AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGL----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ihveGSRQALTLQDWAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALAVQNQLS 254
Cdd:cd14189 148 ----AARLEPPEQRKKTICGTPNYLAPEVLLRQGH---GPESDVWSLGCVMYTLLCGNPPFETLDLK-ETYRCIKQVKYT 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 255 IPQSprHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14189 220 LPAS--LSLPARHLLAGILKRNPGDRLTLDQIL 250
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
15-290 1.53e-16

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: 77.49  E-value: 1.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLveGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEA 94
Cdd:cd05059   1 IDPSELTFLKELGSGQFGVVHL--GKWRGKIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQR----PI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDKGNfltEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqac 174
Cdd:cd05059  75 FIVTEYMANGCLLNYLRERRGKFQ---TEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGL----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ihvegSRQALTLQDWAAQ--RCTISYRAPELFsvqSHCVIDERTDVWSLGCVLYAmMFGEG--PYDMvfQKGDSVALAVQ 250
Cdd:cd05059 147 -----ARYVLDDEYTSSVgtKFPVKWSPPEVF---MYSKFSSKSDVWSFGVLMWE-VFSEGkmPYER--FSNSEVVEHIS 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd05059 216 QGYRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
22-287 1.83e-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: 77.39  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRILCH-EQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLLLPF 100
Cdd:cd06605   5 YLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQILRELDVLHKCNSPYIVGFYGAFYSE----GDISICMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAK-GYAHRDLKPTNILLGDEGQPVLMDLGsmnqacihVEG 179
Cdd:cd06605  81 MDGGSL----DKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFG--------VSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SrqaltLQDWAAQRC--TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGdsvALAVQNQLSI-- 255
Cdd:cd06605 149 Q-----LVDSLAKTFvgTRSYMAPERISGGKYTV---KSDIWSLGLSLVELATGRFPYPPPNAKP---SMMIFELLSYiv 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 256 ----PQSPRH--SSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06605 218 deppPLLPSGkfSPDFQDFVSQCLQKDPTERPSYKELM 255
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
22-296 2.33e-16

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 77.32  E-value: 2.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQK------LGEGGFSYVDLVEGLHDGHFYALKRI------LCHEQQD--REEAQREAD-MHRLFNHPNILRLV-AYcl 85
Cdd:cd14181   8 FYQKydpkevIGRGVSSVVRRCVHRHTGQEFAVKIIevtaerLSPEQLEevRSSTLKEIHiLRQVSGHPSIITLIdSY-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  86 rergaKHEAWLLLPF--FKRGTLWNEI-ERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:cd14181  86 -----ESSTFIFLVFdlMRRGELFDYLtEKVT-----LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 163 VLMDLGSmnqACiHVEGSRQALTLqdwaaqrC-TISYRAPELFSvqshCVIDE-------RTDVWSLGCVLYAMMFGEGP 234
Cdd:cd14181 156 KLSDFGF---SC-HLEPGEKLREL-------CgTPGYLAPEILK----CSMDEthpgygkEVDLWACGVILFTLLAGSPP 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 235 YdmvFQKGDSVALAV----QNQLSIPQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14181 221 F---WHRRQMLMLRMimegRYQFSSPEWDDRSSTVKDLISRLLVVDPEIR------LTAEQALQHP 277
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
19-232 4.05e-16

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: 76.97  E-value: 4.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWL 96
Cdd:cd07833   2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvKKTALREVKVLRQLRHENIVNLKEAFRRKG----RLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRgTLWNEIERLKdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcih 176
Cdd:cd07833  78 VFEYVER-TLLELLEASP---GGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL--- 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTlqDWAAQRCtisYRAPELFsvqshcVIDER----TDVWSLGCVLYAMMFGE 232
Cdd:cd07833 151 TARPASPLT--DYVATRW---YRAPELL------VGDTNygkpVDVWAIGCIMAELLDGE 199
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
57-293 4.28e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 76.62  E-value: 4.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRLFNHPNILRLVAYCLRERGAkheawLLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGL 136
Cdd:cd14145  47 QTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNL-----CLVMEFARGGPLNRVL----SGKRIPPDILVNWAVQIARGM 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 137 EAIHAKGYA---HRDLKPTNILL------GDEGQPVL--MDLGsmnqacIHVEGSRqalTLQDWAAQrcTISYRAPElfs 205
Cdd:cd14145 118 NYLHCEAIVpviHRDLKSSNILIlekvenGDLSNKILkiTDFG------LAREWHR---TTKMSAAG--TYAWMAPE--- 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 206 VQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVALAV-QNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14145 184 VIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGI--DGLAVAYGVaMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFT 261

                ....*....
gi 46577677 285 LLLSQLEAL 293
Cdd:cd14145 262 NILDQLTAI 270
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
26-280 4.30e-16

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 76.44  E-value: 4.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEgLHDGHFYALKRILCHEQQDRE----EAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd14117  14 LGKGKFGNVYLAR-EKQSKFIVALKVLFKSQIEKEgvehQLRREIEIQSHLRHPNILRLYNYFHDRK----RIYLILEYA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSR 181
Cdd:cd14117  89 PRGELYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG----WSVHAPSLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTlqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVfQKGDSVALAVQNQLSIPqsPR 260
Cdd:cd14117 161 RRTM--------CgTLDYLPPEMIEGRTH---DEKVDLWCIGVLCYELLVGMPPFESA-SHTETYRRIVKVDLKFP--PF 226
                       250       260
                ....*....|....*....|
gi 46577677 261 HSSALRQLLNSMMTVDPHQR 280
Cdd:cd14117 227 LSDGSRDLISKLLRYHPSER 246
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
15-293 4.48e-16

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: 76.24  E-value: 4.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSyvDLVEGLHDGHFYALKRILCHE---QQDREEAqreADMHRLfNHPNILRLVAYCLRERGAk 91
Cdd:cd05039   3 INKKDLKLGELIGKGEFG--DVMLGDYRGQKVAVKCLKDDStaaQAFLAEA---SVMTTL-RHPNLVQLLGVVLEGNGL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 heaWLLLPFFKRGTLwneIERLKDKGN-FLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:cd05039  76 ---YIVTEYMAKGSL---VDYLRSRGRaVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQACIHVEGSrqaltlqdwaaqRCTISYRAPE-----LFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDMVFQKgdS 244
Cdd:cd05039 150 KEASSNQDGG------------KLPIKWTAPEalrekKFSTKS--------DVWSFGILLWEIYsFGRVPYPRIPLK--D 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 46577677 245 VALAVQN--QLSIPQS-PRHssaLRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05039 208 VVPHVEKgyRMEAPEGcPPE---VYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
26-280 5.43e-16

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 76.92  E-value: 5.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKR-----ILCHEQQDREEAQREADMHRLfNHPNILRLvAYCLRergAKHEAWLLLPF 100
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVlqkkvILNRKEQKHIMAERNVLLKNV-KHPFLVGL-HYSFQ---TTDKLYFVLDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACihvegs 180
Cdd:cd05604  79 VNGGELFFHLQRER----SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFG----LC------ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDsVALAVQNQLSIP--Q 257
Cdd:cd05604 145 KEGISNSDTTTTFCgTPEYLAPEVIRKQPY---DNTVDWWCLGSVLYEMLYGLPP----FYCRD-TAEMYENILHKPlvL 216
                       250       260
                ....*....|....*....|...
gi 46577677 258 SPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05604 217 RPGISLTAWSILEELLEKDRQLR 239
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
57-281 5.93e-16

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: 75.94  E-value: 5.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRLFNHPNILRLVAYCLrergaKHEAW-LLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLgiC-R 134
Cdd:cd14058  28 SEKKAFEVEVRQLSRVDHPNIIKLYGACS-----NQKPVcLVMEYAEGGSLYNVLHGKEPKPIYTAAHAMSWALQ--CaK 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHA---KGYAHRDLKPTNILLGDEGQPV-LMDLGSmnqACihvEGSRQALTLQDWAAqrctisYRAPELFsvqSHC 210
Cdd:cd14058 101 GVAYLHSmkpKALIHRDLKPPNLLLTNGGTVLkICDFGT---AC---DISTHMTNNKGSAA------WMAPEVF---EGS 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 211 VIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14058 166 KYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLIKNCPKPIESLMTRCWSKDPEKRP 236
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
18-281 6.27e-16

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: 76.13  E-value: 6.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRerGAKheAWL 96
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLK--GSK--LWI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacih 176
Cdd:cd06609  77 IMEYCGGGSVLDLLKPGP-----LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG-------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSrqaltLQDWAAQRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-DMVFQKgdsvALAVQN 251
Cdd:cd06609 144 VSGQ-----LTSTMSKRNTFVgtpfWMAPEVIKQSGY---DEKADIWSLGITAIELAKGEPPLsDLHPMR----VLFLIP 211
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 252 QLSIPQSPRH--SSALRQLLNSMMTVDPHQRP 281
Cdd:cd06609 212 KNNPPSLEGNkfSKPFKDFVELCLNKDPKERP 243
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
20-284 7.11e-16

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 75.98  E-value: 7.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLveGLH---DGHFY----ALKRILCHEQQDREEA---QREADMHRLFNHPNILRLvaycLRERG 89
Cdd:cd14076   3 YILGRTLGEGEFGKVKL--GWPlpkANHRSgvqvAIKLIRRDTQQENCQTskiMREINILKGLTHPNIVRL----LDVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHEAWLLLPFFKRGTLWNEI---ERLKDKgnfltEDQILWLLLgiCRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD 166
Cdd:cd14076  77 TKKYIGIVLEFVSGGELFDYIlarRRLKDS-----VACRLFAQL--ISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 167 LGSMNQAcihveGSRQALTLQDWAAQRCtisYRAPELFsVQSHCVIDERTDVWSLGCVLYAMMFGEGPY--DMVFQKGDS 244
Cdd:cd14076 150 FGFANTF-----DHFNGDLMSTSCGSPC---YAAPELV-VSDSMYAGRKADIWSCGVILYAMLAGYLPFddDPHNPNGDN 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 245 VALAVQNQLSIP-QSPRHSSAL-RQLLNSMMTVDPHQRPHIP 284
Cdd:cd14076 221 VPRLYRYICNTPlIFPEYVTPKaRDLLRRILVPNPRKRIRLS 262
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
26-281 7.23e-16

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: 75.95  E-value: 7.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKR 103
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIeeRKALLKEAEKMERARHSYVLPLLGVCVERR----SLGLVMEYMEN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKD------KGNFLTEdqilwlllgICRGLEAIH--AKGYAHRDLKPTNILLGDEGQPVLMDLG--SMNQA 173
Cdd:cd13978  77 GSLKSLLEREIQdvpwslRFRIIHE---------IALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGlsKLGMK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQDwaaqrcTISYRAPELFSVQSHcVIDERTDVWSLGCVLYAMMFGEGPYDMVF---------QKGDS 244
Cdd:cd13978 148 SISANRRRGTENLGG------TPIYMAPEAFDDFNK-KPTSKSDVYSFAIVIWAVLTRKEPFENAInpllimqivSKGDR 220
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 245 VALavqNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd13978 221 PSL---DDIGRLKQIENVQELISLMIRCWDGNPDARP 254
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
19-283 7.71e-16

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: 75.82  E-value: 7.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYV----DLVEglhdgHFYALKRIlcHE----------QQDREEAQREADMHRLFNHPNILRLvaYC 84
Cdd:cd13990   1 RYLLLNLLGKGGFSEVykafDLVE-----QRYVACKI--HQlnkdwseekkQNYIKHALREYEIHKSLDHPRIVKL--YD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  85 LRERGAKHEAWLL-------LPFFkrgtlwneierLKDKGNFLTEDQILWlllgICRGLEAI-----HAKGYAHRDLKPT 152
Cdd:cd13990  72 VFEIDTDSFCTVLeycdgndLDFY-----------LKQHKSIPEREARSI----IMQVVSALkylneIKPPIIHYDLKPG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 153 NILLG-----------DEGQPVLMDLGSMNQACIHVEgSRQALTLqdWaaqrctisYRAPELFSV-QSHCVIDERTDVWS 220
Cdd:cd13990 137 NILLHsgnvsgeikitDFGLSKIMDDESYNSDGMELT-SQGAGTY--W--------YLPPECFVVgKTPPKISSKVDVWS 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 221 LGCVLYAMMFGEGPydmvFQKGDSVALAVQNQ-------LSIPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd13990 206 VGVIFYQMLYGRKP----FGHNQSQEAILEENtilkateVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDV 271
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
46-280 7.74e-16

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 76.21  E-value: 7.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  46 YALKRIlchEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLWNEIERLKdkgnFLTEDQI 125
Cdd:cd14177  32 FAVKII---DKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGR----YVYLVTELMKGGELLDRILRQK----FFSEREA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 126 LWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV----LMDLGSMNQacihVEGSRQALTLQDWAAqrctiSYRAP 201
Cdd:cd14177 101 SAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdsirICDFGFAKQ----LRGENGLLLTPCYTA-----NFVAP 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 202 ELFSVQSHcviDERTDVWSLGCVLYAMM-----FGEGPYDmvfqKGDSVALAVQN---QLSIPQSPRHSSALRQLLNSMM 273
Cdd:cd14177 172 EVLMRQGY---DAACDIWSLGVLLYTMLagytpFANGPND----TPEEILLRIGSgkfSLSGGNWDTVSDAAKDLLSHML 244

                ....*..
gi 46577677 274 TVDPHQR 280
Cdd:cd14177 245 HVDPHQR 251
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-281 9.75e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 75.68  E-value: 9.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVayclrergakhEAWLLLPFF 101
Cdd:cd14048  11 IQCLGRGGFGVVFEAKNKVDDCNYAVKRIrLPNNELAREKVLREVRALAKLDHPGIVRYF-----------NAWLERPPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEI-----------ERLKD--KGNFLTEDQ----ILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVL 164
Cdd:cd14048  80 GWQEKMDEVylyiqmqlcrkENLKDwmNRRCTMESRelfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 165 MDLGSMNQAcihVEGSRQALTLQDWAA------QRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDM 237
Cdd:cd14048 160 GDFGLVTAM---DQGEPEQTVLTPMPAyakhtgQVGTRLYMSPEQIHGNQY---SEKVDIFALGLILFELIYSFSTqMER 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 238 V-----FQKGDSVALAVQNqlsIPQSprhssalRQLLNSMMTVDPHQRP 281
Cdd:cd14048 234 IrtltdVRKLKFPALFTNK---YPEE-------RDMVQQMLSPSPSERP 272
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
20-283 1.04e-15

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: 75.07  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLveGLHD--GHFYALKrILCHEQQDrEEAQR----E-ADMHRLfNHPNILRLvaYCLRERGAKh 92
Cdd:cd14075   4 YRIRGELGSGNFSQVKL--GIHQltKEKVAIK-ILDKTKLD-QKTQRllsrEiSSMEKL-HHPNIIRL--YEVVETLSK- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 eAWLLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---- 168
Cdd:cd14075  76 -LHLVMEYASGGELYTKIS----TEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfsth 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 -----SMNQACihveGSRqaltlqdwaaqrctiSYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPYdmvfqKGD 243
Cdd:cd14075 151 akrgeTLNTFC----GSP---------------PYAAPELFKDEHY--IGIYVDIWALGVLLYFMVTGVMPF-----RAE 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 46577677 244 SVA----LAVQNQLSIPqsPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14075 205 TVAklkkCILEGTYTIP--SYVSEPCQELIRGILQPVPSDRYSI 246
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
20-240 1.09e-15

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: 75.68  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILchEQQDREE----AQREADMHRLFNHPNILRLVAYCLRERGAKHEA- 94
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIR--MENEKEGfpitAIREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGs 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 -WLLLPFFKrgtlwNEIERLKDKGNF-LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNq 172
Cdd:cd07840  79 iYMVFEYMD-----HDLTGLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR- 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 173 aCIHVEGSR----QALTLqdWaaqrctisYRAPELF--SVQShcviDERTDVWSLGCVLYAMMFGEgpydMVFQ 240
Cdd:cd07840 153 -PYTKENNAdytnRVITL--W--------YRPPELLlgATRY----GPEVDMWSVGCILAELFTGK----PIFQ 207
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
23-288 1.18e-15

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: 75.32  E-value: 1.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVegLH--DGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLvayclrergakHEAwlllp 99
Cdd:cd06623   6 VKVLGQGSSGVVYKV--RHkpTGKIYALKKIhVDGDEEFRKQLLRELKTLRSCESPYVVKC-----------YGA----- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTL--------WNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGY-AHRDLKPTNILLGDEGQPVLMDLGsm 170
Cdd:cd06623  68 FYKEGEIsivleymdGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRHiIHRDIKPSNLLINSKGEVKIADFG-- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 nqACIHVEGSR-QALTLQDwaaqrcTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQkGDSVAL-- 247
Cdd:cd06623 146 --ISKVLENTLdQCNTFVG------TVTYMSPERIQGESYSY---AADIWSLGLTLLECALGKFPFLPPGQ-PSFFELmq 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 248 AVQNQLSIPQSPRHSSA-LRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06623 214 AICDGPPPSLPAEEFSPeFRDFISACLQKDPKKRPSAAELLQ 255
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-296 1.25e-15

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 76.09  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRiLCHEQQDR---EEAQREADMHRLFNHPNILRLV-----AYCLRERg 89
Cdd:cd07879  15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKK-LSRPFQSEifaKRAYRELTLLKHMQHENVIGLLdvftsAVSGDEF- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 akHEAWLLLPFFKrgtlwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS 169
Cdd:cd07879  93 --QDFYLVMPYMQ-------TDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNqaciHVEGSRQALTLQDWaaqrctisYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEG---------------- 233
Cdd:cd07879 164 AR----HADAEMTGYVVTRW--------YRAPEVILNWMH--YNQTVDIWSVGCIMAEMLTGKTlfkgkdyldqltqilk 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 234 ----PYDMVFQKGDSVAlAVQNQLSIPQSPRH---------SSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07879 230 vtgvPGPEFVQKLEDKA-AKSYIKSLPKYPRKdfstlfpkaSPQAVDLLEKMLELDVDKR------LTATEALEHP 298
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-236 1.50e-15

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: 74.72  E-value: 1.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLvaycLRERGAKHEAWL 96
Cdd:cd14083   3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSlENEIAVLRKIKHPNIVQL----LDIYESKSHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWneiERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTN-----------ILLGDEGQPVLM 165
Cdd:cd14083  79 VMELVTGGELF---DRIVEKGSY-TEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENllyyspdedskIMISDFGLSKME 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 166 DLGSMNQACihvegsrqaltlqdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YD 236
Cdd:cd14083 155 DSGVMSTAC-------------------GTPGYVAPEVLAQKPY---GKAVDCWSIGVISYILLCGYPPfYD 204
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
19-232 1.56e-15

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 75.76  E-value: 1.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRERGAK--HEA 94
Cdd:cd07880  16 RYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSElfAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDrfHDF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFkrGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd07880  96 YLVMPFM--GTDLGKLMKHEK----LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTD 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 175 IHVEGsrqaLTLQDWaaqrctisYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd07880 170 SEMTG----YVVTRW--------YRAPEVILNWMH--YTQTVDIWSVGCIMAEMLTGK 213
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
41-288 1.59e-15

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: 74.70  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  41 HDGHFYALKRILCHEQ-------------------QDREEAQREADMHRLFNHPNILRLVAYCLrERGAKHEAW---LLL 98
Cdd:cd14012   5 PSGTFYLVYEVVLDNSkkpgkfltsqeyfktsngkKQIQLLEKELESLKKLRHPNLVSYLAFSI-ERRGRSDGWkvyLLT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL---GDEGQPVLMDLGSMNQacI 175
Cdd:cd14012  84 EYAPGGSL----SELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKT--L 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQALTlqdwAAQRCTisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGpydmVFQKGDSvALAVQNQLSI 255
Cdd:cd14012 158 LDMCSRGSLD----EFKQTY--WLPPEL--AQGSKSPTRKTDVWDLGLLFLQMLFGLD----VLEKYTS-PNPVLVSLDL 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 256 PQSprhssaLRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14012 225 SAS------LQDFLSKCLSLDPKKRPTALELLP 251
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
26-280 1.68e-15

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 74.60  E-value: 1.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE-AQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRG 104
Cdd:cd14185   8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDmIESEILIIKSLSHPNIVKLFEVYETEK----EIYLILEYVRGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWNEI-ERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG-DEGQPVLMDLGSMNQAcIHVegSRQ 182
Cdd:cd14185  84 DLFDAIiESVK-----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhNPDKSTTLKLADFGLA-KYV--TGP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 ALTLqdwaaqrC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQN---QLSIPQS 258
Cdd:cd14185 156 IFTV-------CgTPTYVAPEILSEKGYGL---EVDMWAAGVILYILLCGFPPFRSPERDQEELFQIIQLghyEFLPPYW 225
                       250       260
                ....*....|....*....|..
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14185 226 DNISEAAKDLISRLLVVDPEKR 247
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
26-280 1.77e-15

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 75.39  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALK-----RILCHEQQDREEAQREADMHRLfNHPNILRLvAYCLRergAKHEAWLLLPF 100
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKvlqkkTILKKKEQNHIMAERNVLLKNL-KHPFLVGL-HYSFQ---TSEKLYFVLDY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIER----LKDKGNFLTEDqilwlllgICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIH 176
Cdd:cd05603  78 VNGGELFFHLQRercfLEPRARFYAAE--------VASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFG------LC 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY--DMVFQKGDSValaVQNQLS 254
Cdd:cd05603 144 KEGMEPEETTSTFCG---TPEYLAPEVLRKEPY---DRTVDWWCLGAVLYEMLYGLPPFysRDVSQMYDNI---LHKPLH 214
                       250       260
                ....*....|....*....|....*.
gi 46577677 255 IPqsPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05603 215 LP--GGKTVAACDLLQGLLHKDQRRR 238
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
20-288 2.18e-15

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 74.27  E-value: 2.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIL--CHEQQDREEAQREADMH-RLFNHPNILRLvayclrergakHEAWL 96
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrFRGEKDRKRKLEEVERHeKLGEHPNCVRF-----------IKAWE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 llpffKRGTLWNEIE-------RLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGs 169
Cdd:cd14050  72 -----EKGILYIQTElcdtslqQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFG- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 mnqacihvegsrqaLTLQDWAAQRCTIS-----YRAPEL----FSVQShcvidertDVWSLGCVLYammfgEGPYDM-VF 239
Cdd:cd14050 146 --------------LVVELDKEDIHDAQegdprYMAPELlqgsFTKAA--------DIFSLGITIL-----ELACNLeLP 198
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 240 QKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14050 199 SGGDGWHQLRQGYLPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLA 247
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
26-293 2.20e-15

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 74.35  E-value: 2.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQD----REEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd14061   2 IGVGGFGKV--YRGIWRGEEVAVKAARQDPDEDisvtLENVRQEARLFWMLRHPNIIALRGVCLQPP----NLCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIerlkdKGNFLTEDQILWLLLGICRGLEAIHAKG---YAHRDLKPTNILLgdegqpvlmdlgsmNQACIHVE 178
Cdd:cd14061  76 RGGALNRVL-----AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILI--------------LEAIENED 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDWAAQR-----------CTISYRAPELFSVQshcVIDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVAL 247
Cdd:cd14061 137 LENKTLKITDFGLARewhkttrmsaaGTYAWMAPEVIKSS---TFSKASDVWSYGVLLWELLTGEVPYKGI--DGLAVAY 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 248 AVQ-NQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14061 212 GVAvNKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
18-280 2.51e-15

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: 74.76  E-value: 2.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILR-LVAYCLRErgakhEAWL 96
Cdd:cd06654  20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGD-----ELWV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEI-ERLKDKGNfltedqilwlLLGICR----GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN 171
Cdd:cd06654  95 VMEYLAGGSLTDVVtETCMDEGQ----------IAAVCReclqALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 QacIHVEGSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVALAVQN 251
Cdd:cd06654 165 Q--ITPEQSKRSTMVG-------TPYWMAPEVVTRKAY---GPKVDIWSLGIMAIEMIEGEPPY-LNENPLRALYLIATN 231
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 252 QLSIPQSPRHSSAL-RQLLNSMMTVDPHQR 280
Cdd:cd06654 232 GTPELQNPEKLSAIfRDFLNRCLEMDVEKR 261
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
18-296 2.89e-15

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: 74.76  E-value: 2.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILR-LVAYCLRErgakhEAWL 96
Cdd:cd06656  19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGD-----ELWV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEI-ERLKDKGNfltedqilwlLLGICR----GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN 171
Cdd:cd06656  94 VMEYLAGGSLTDVVtETCMDEGQ----------IAAVCReclqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 QacIHVEGSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVALAVQN 251
Cdd:cd06656 164 Q--ITPEQSKRSTMVG-------TPYWMAPEVVTRKAY---GPKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATN 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 252 QLSIPQSP-RHSSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd06656 231 GTPELQNPeRLSAVFRDFLNRCLEMDVDRRG------SAKELLQHP 270
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
22-291 3.50e-15

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: 73.86  E-value: 3.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSyvDLVEGLHDGHFYALKRIlcheqQDREEAQR---EADMHRLFNHPNILRLVAYCLRERGAkheAWLLL 98
Cdd:cd05082  10 LLQTIGKGEFG--DVMLGDYRGNKVAVKCI-----KNDATAQAflaEASVMTQLRHSNLVQLLGVIVEEKGG---LYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLwneIERLKDKG-NFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihv 177
Cdd:cd05082  80 EYMAKGSL---VDYLRSRGrSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGL-------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egSRQALTLQDWAaqRCTISYRAPE-----LFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDMVFQKgdSVALAVQN 251
Cdd:cd05082 149 --TKEASSTQDTG--KLPVKWTAPEalrekKFSTKS--------DVWSFGILLWEIYsFGRVPYPRIPLK--DVVPRVEK 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 252 QLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05082 215 GYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
20-281 3.74e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 75.93  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQR--EADMHRLFNHPNILRLVAYCLRErgAKHEAWLL 97
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLviEVNVMRELKHKNIVRYIDRFLNK--ANQKLYIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    98 LPFFKRGTLWNEIERLKDKGNFLTEDQILwlllGICRGLeaIHAKGYAH-------------RDLKPTNILLGDEgqpvL 164
Cdd:PTZ00266   93 MEFCDAGDLSRNIQKCYKMFGKIEEHAIV----DITRQL--LHALAYCHnlkdgpngervlhRDLKPQNIFLSTG----I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   165 MDLGSMNQACIHVEGsRQALTLQDWA----------AQRC--TISYRAPELFSVQSHCViDERTDVWSLGCVLYAMMFGE 232
Cdd:PTZ00266  163 RHIGKITAQANNLNG-RPIAKIGDFGlsknigiesmAHSCvgTPYYWSPELLLHETKSY-DDKSDMWALGCIIYELCSGK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 46577677   233 GPydmvFQKGDSVALAVQNQLSIPQSP--RHSSALRQLLNSMMTVDPHQRP 281
Cdd:PTZ00266  241 TP----FHKANNFSQLISELKRGPDLPikGKSKELNILIKNLLNLSAKERP 287
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
64-284 3.78e-15

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: 73.49  E-value: 3.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRLvaycLRERGAKHEAWLLLPFFKRGTLwneIERLKDKGnFLTEDQILWLLLGICRGLEAIHAKG 143
Cdd:cd14162  49 REIEVIKGLKHPNLICF----YEAIETTSRVYIIMELAENGDL---LDYIRKNG-ALPEPQARRWFRQLVAGVEYCHSKG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 144 YAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDwaaQRCTIS--------YRAPELFSVQSHCviDER 215
Cdd:cd14162 121 VVHRDLKCENLLLDKNNNLKITDFGF----------ARGVMKTKD---GKPKLSetycgsyaYASPEILRGIPYD--PFL 185
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 216 TDVWSLGCVLYAMMFGEGPYDMVFQKgdSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPhQRPHIP 284
Cdd:cd14162 186 SDIWSMGVVLYTMVYGRLPFDDSNLK--VLLKQVQRRVVFPKNPTVSEECKDLILRMLSPVK-KRITIE 251
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
26-280 3.93e-15

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 73.87  E-value: 3.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMhrLFNHPNIL-----RLVAYCLRERGAKHEAWLLLPF 100
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKL----EKKRIKKRKGEAM--ALNEKRILekvnsRFVVSLAYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcihVEGS 180
Cdd:cd05631  82 MNGGDLKFHIYNMGNPG--FDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI---PEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQaltlqdwAAQRCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQ--KGDSVALAVQNQLSiPQS 258
Cdd:cd05631 157 TV-------RGRVGTVGYMAPEVINNEKYTF---SPDWWGLGCLIYEMIQGQSPFRKRKErvKREEVDRRVKEDQE-EYS 225
                       250       260
                ....*....|....*....|..
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05631 226 EKFSEDAKSICRMLLTKNPKER 247
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
48-283 4.53e-15

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: 73.45  E-value: 4.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  48 LKRILCHEQQDREEAQReadMHRLfNHPNILRLVAYCLRERgaKHEAWLLLPFFKrGTLWNEIERLKDKGNFLTEDQILW 127
Cdd:cd14119  31 LRRIPNGEANVKREIQI---LRRL-NHRNVIKLVDVLYNEE--KQKLYMVMEYCV-GGLQEMLDSAPDKRLPIWQAHGYF 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 128 LLLgiCRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSrqaltlqdwaaqRCTISY-----RAPE 202
Cdd:cd14119 104 VQL--IDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEDD------------TCTTSQgspafQPPE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 203 LFSVQS--HCVideRTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQN----QLSIPqsPRHSSALRQLLNSMMTVD 276
Cdd:cd14119 170 IANGQDsfSGF---KVDIWSAGVTLYNMTTGKYPFE-----GDNIYKLFENigkgEYTIP--DDVDPDLQDLLRGMLEKD 239

                ....*..
gi 46577677 277 PHQRPHI 283
Cdd:cd14119 240 PEKRFTI 246
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
19-232 4.75e-15

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 73.95  E-value: 4.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILchEQQD----REEAQREADMHRLFNHPNILRLVAYCLRERGakhea 94
Cdd:cd07847   2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFV--ESEDdpviKKIALREIRMLKQLKHPNLVNLIEVFRRKRK----- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 wLLLPF-FKRGTLWNEIERlKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqA 173
Cdd:cd07847  75 -LHLVFeYCDHTVLNELEK-NPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGF---A 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 174 CIhVEGSRQALTlqDWAAQRCtisYRAPELFsvqshcVIDER----TDVWSLGCVLYAMMFGE 232
Cdd:cd07847 148 RI-LTGPGDDYT--DYVATRW---YRAPELL------VGDTQygppVDVWAIGCVFAELLTGQ 198
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
15-291 5.10e-15

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 73.61  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVdlveglHDGHFYALK--RI--------LCHEQQDREEAQREADMHRLFNHPNILRLVAYC 84
Cdd:cd05056   3 IQREDITLGRCIGEGQFGDV------YQGVYMSPEneKIavavktckNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  85 LRErgakhEAWLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL--------L 156
Cdd:cd05056  77 TEN-----PVWIVMELAPLGELRSYLQVNKYS---LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLvsspdcvkL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 GDEGQPVLMDLGSMNQAcihvegSRQALTLQdWAAQRcTISYRApelFSVQShcvidertDVWSLG-CVLYAMMFGEGPY 235
Cdd:cd05056 149 GDFGLSRYMEDESYYKA------SKGKLPIK-WMAPE-SINFRR---FTSAS--------DVWMFGvCMWEILMLGVKPF 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 236 DMVfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05056 210 QGV--KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
19-280 5.11e-15

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: 73.45  E-value: 5.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGlHDGHFYALKRIL---CHEQQDREEAQREADMHRLFNHPNILRLvaYCLRERGAKheAW 95
Cdd:cd14161   4 RYEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRkdrIKDEQDLLHIRREIEIMSSLNHPHIISV--YEVFENSSK--IV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEI-ERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQac 174
Cdd:cd14161  79 IVMEYASRGDLYDYIsERQR-----LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNL-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ihvegSRQALTLQDWAAQRCtisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqKGDSVALAVQNQLS 254
Cdd:cd14161 152 -----YNQDKFLQTYCGSPL---YASPEI--VNGRPYIGPEVDSWSLGVLLYILVHGTMPFD----GHDYKILVKQISSG 217
                       250       260
                ....*....|....*....|....*.
gi 46577677 255 IPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14161 218 AYREPTKPSDACGLIRWLLMVNPERR 243
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
18-229 5.65e-15

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: 73.42  E-value: 5.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYL-FIQKLGEGGFSYVDLV----EGLHDGHFYALKRIlchEQQDREEA----QREADMHRLFNHPNILRLVAYCLRER 88
Cdd:cd05079   3 KRFLkRIRDLGEGHFGKVELCrydpEGDNTGEQVAVKSL---KPESGGNHiadlKKEIEILRNLYHENIVKYKGICTEDG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 GAKHEawLLLPFFKRGTLWNEIERLKDKGNFlteDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd05079  80 GNGIK--LIMEFLPSGSLKEYLPRNKNKINL---KQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 169 sMNQAcihVEGSRQALTLQD-------WAAQRCTIsyrapelfsvqsHCVIDERTDVWSLGCVLYAMM 229
Cdd:cd05079 155 -LTKA---IETDKEYYTVKDdldspvfWYAPECLI------------QSKFYIASDVWSFGVTLYELL 206
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
42-228 5.86e-15

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: 73.63  E-value: 5.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  42 DGHFYALKrilCHEQQDREEAQREADMHR--LFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIerlkdKGNF 119
Cdd:cd13998  17 KNEPVAVK---IFSSRDKQSWFREKEIYRtpMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL*DYL-----SLHT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAK---------GYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQALTLqDWA 190
Cdd:cd13998  89 IDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFG----LAVRLSPSTGEEDN-ANN 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 46577677 191 AQRCTISYRAPELF--SVQSHCVID-ERTDVWSLGCVLYAM 228
Cdd:cd13998 164 GQVGTKRYMAPEVLegAINLRDFESfKRVDIYAMGLVLWEM 204
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
23-225 6.15e-15

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: 73.61  E-value: 6.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD-REEAQREADMHRLFNHPNILRLVAYCLRErgAKHEAWLLLPFF 101
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDvQKQILRELEINKSCASPYIVKYYGAFLDE--QDSSIGIAMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcihveGSR 181
Cdd:cd06621  84 EGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGEL-----VNS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 46577677 182 QALTLQDwaaqrcTISYRAPELFSVQSHCVideRTDVWSLGCVL 225
Cdd:cd06621 159 LAGTFTG------TSYYMAPERIQGGPYSI---TSDVWSLGLTL 193
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
20-231 6.21e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 73.51  E-value: 6.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGakheawLLL 98
Cdd:cd07871   7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIrLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERC------LTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFfkrGTLWNEIERLKDK-GNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQAcihv 177
Cdd:cd07871  81 VF---EYLDSDLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFG-LARA---- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 178 egsrQALTLQDWAAQRCTISYRAPELF--SVQSHCVIdertDVWSLGCVLYAMMFG 231
Cdd:cd07871 153 ----KSVPTKTYSNEVVTLWYRPPDVLlgSTEYSTPI----DMWGVGCILYEMATG 200
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
25-294 6.22e-15

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 73.15  E-value: 6.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVdlveglHDGHFY---ALKRI-LCHEQQDREEA-QREADMHRLFNHPNILRLVAYCLRergaKHEAWLLLP 99
Cdd:cd14063   7 VIGKGRFGRV------HRGRWHgdvAIKLLnIDYLNEEQLEAfKEEVAAYKNTRHDNLVLFMGACMD----PPHLAIVTS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLKDKGNFlteDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLgDEGQPVLMDLGSMNQACIHVEG 179
Cdd:cd14063  77 LCKGRTLYSLIHERKEKFDF---NKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGLFSLSGLLQPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRqaltLQDWAAQRCTISYRAPELF-------SVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMvfQKGDSVALAV--- 249
Cdd:cd14063 153 RR----EDTLVIPNGWLCYLAPEIIralspdlDFEESLPFTKASDVYAFGTVWYELLAGRWPFKE--QPAESIIWQVgcg 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 250 ----QNQLSIPQSprhssaLRQLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd14063 227 kkqsLSQLDIGRE------VKDILMQCWAYDPEKRPTFSDLLRMLERLP 269
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
26-274 7.09e-15

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 73.88  E-value: 7.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA---QREADMHRLFNHPNILRLvAYCLRErgaKHEAWLLLPFFK 102
Cdd:cd05601   9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsffEEERDIMAKANSPWITKL-QYAFQD---SENLYLVMEYHP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACihvegsrq 182
Cdd:cd05601  85 GGDLLSLLSRYDDI---FEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGS---AA-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 ALTLQDWAAQRC---TISYRAPELFSVQSH---CVIDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVA------LAVQ 250
Cdd:cd05601 151 KLSSDKTVTSKMpvgTPDYIAPEVLTSMNGgskGTYGVECDWWSLGIVAYEMLYGKTPF-----TEDTVIktysniMNFK 225
                       250       260
                ....*....|....*....|....
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSMMT 274
Cdd:cd05601 226 KFLKFPEDPKVSESAVDLIKGLLT 249
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
18-294 7.12e-15

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: 73.13  E-value: 7.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYL-FIQKLGEGGFSYVDLV--EGLHD--GHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRerGAKH 92
Cdd:cd14205   3 ERHLkFLQQLGKGNFGSVEMCryDPLQDntGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYS--AGRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLWNEIERLKDKGNFLtedQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd14205  81 NLRLIMEYLPYGSLRDYLQKHKERIDHI---KLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 acihVEGSRQALTLQDwaAQRCTISYRAPE-----LFSVQShcvidertDVWSLGCVLYAMM-FGEG----PYDMVFQKG 242
Cdd:cd14205 158 ----LPQDKEYYKVKE--PGESPIFWYAPEsltesKFSVAS--------DVWSFGVVLYELFtYIEKskspPAEFMRMIG 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 243 DS---------VALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd14205 224 NDkqgqmivfhLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIR 284
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
18-293 7.58e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 73.18  E-value: 7.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYL-FIQKLGEGGFSYVDLV--EGLHDGHF--YALKRiLCHEQ--QDREEAQREADMHRLFNHPNILRLVAYCLRERGA 90
Cdd:cd05038   3 ERHLkFIKQLGEGHFGSVELCryDPLGDNTGeqVAVKS-LQPSGeeQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 KHEawLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsM 170
Cdd:cd05038  82 SLR--LIMEYLPSGSLRDYLQRHRDQ---IDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFG-L 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQAcihVEGSRQALTLQD-------WAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMM-FGEGPYD------ 236
Cdd:cd05038 156 AKV---LPEDKEYYYVKEpgespifWYAPECLRESR----FSSAS--------DVWSFGVTLYELFtYGDPSQSppalfl 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 237 --MVFQKGDSVALAVQNQL----SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05038 221 rmIGIAQGQMIVTRLLELLksgeRLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
20-296 7.91e-15

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: 72.95  E-value: 7.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRiLCHEQQDREEAQREADMH---RLFNHPNILRLVAyCLRERGAkheawL 96
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKK-MKKKFYSWEECMNLREVKslrKLNEHPNIVKLKE-VFRENDE-----L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPF-FKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaci 175
Cdd:cd07830  74 YFVFeYMEGNLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR---- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEgSRQALTlqDWAAQRCtisYRAPELF---SVQSHCVidertDVWSLGCV---LYAM--MF-GEGPYDMVFQK----G 242
Cdd:cd07830 148 EIR-SRPPYT--DYVSTRW---YRAPEILlrsTSYSSPV-----DIWALGCImaeLYTLrpLFpGSSEIDQLYKIcsvlG 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 243 --------DSVALAVQNQLSIPQS---------PRHSSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd07830 217 tptkqdwpEGYKLASKLGFRFPQFaptslhqliPNASPEAIDLIKDMLRWDPKKRP------TASQALQHP 281
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-280 8.05e-15

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 73.80  E-value: 8.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGL--HD-GHFYALKRI----LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHeawLLL 98
Cdd:cd05614   8 LGTGAYGKVFLVRKVsgHDaNKLYAMKVLrkaaLVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLH---LIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEierLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVE 178
Cdd:cd05614  85 DYVSGGELFTH---LYQRDHF-SEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFG-LSKEFLTEE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRqaltlqdwAAQRC-TISYRAPELFSVQS-HcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQN-QLSI 255
Cdd:cd05614 160 KER--------TYSFCgTIEYMAPEIIRGKSgH---GKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRIlKCDP 228
                       250       260
                ....*....|....*....|....*
gi 46577677 256 PQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05614 229 PFPSFIGPVARDLLQKLLCKDPKKR 253
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
16-294 1.00e-14

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: 73.16  E-value: 1.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYLF--IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRErga 90
Cdd:cd06635  21 EDPEKLFsdLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQdiiKEVKFLQRIKHPNSIEYKGCYLRE--- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kHEAWLLLPFfkrgTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:cd06635  98 -HTAWLVMEY----CLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQAcihvEGSRQALTLQDWAaqrctisyrAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPydmVFQKGDSVAL--A 248
Cdd:cd06635 173 SIA----SPANSFVGTPYWM---------APEVILAMDEGQYDGKVDVWSLGITCIELAERKPP---LFNMNAMSALyhI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 249 VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd06635 237 AQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLR 282
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
23-259 1.10e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 72.72  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHR-LFNHPNILRLVAYCLR-ERGAKHEAWLLLPF 100
Cdd:cd06639  27 IETIGKGTYGKVYKVTNKKDGSLAAVK-ILDPISDVDEEIEAEYNILRsLPNHPNVVKFYGMFYKaDQYVGGQLWLVLEL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGS 180
Cdd:cd06639 106 CNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRR 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTLQDWAaqrctisyrAPELFSV--QSHCVIDERTDVWSLGCVLYAMMFGEGP-YDMvfqkgdsvaLAVQNQLSIPQ 257
Cdd:cd06639 186 NTSVGTPFWM---------APEVIACeqQYDYSYDARCDVWSLGITAIELADGDPPlFDM---------HPVKALFKIPR 247

                ..
gi 46577677 258 SP 259
Cdd:cd06639 248 NP 249
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
64-296 1.19e-14

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 73.17  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILrlvayCLRE--RGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHA 141
Cdd:cd07855  53 RELKILRHFKHDNII-----AIRDilRPKVPYADFKDVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHS 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 142 KGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTlqDWAAqrcTISYRAPEL-FSVQSHcviDERTDVWS 220
Cdd:cd07855 128 ANVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYFMT--EYVA---TRWYRAPELmLSLPEY---TQAIDMWS 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 221 LGCVLYAM---------------------MFGEGPYDMVFQKG-DSVALAVQNQLSIPQSPRHS---SALRQLLN---SM 272
Cdd:cd07855 200 VGCIFAEMlgrrqlfpgknyvhqlqliltVLGTPSQAVINAIGaDRVRRYIQNLPNKQPVPWETlypKADQQALDllsQM 279
                       250       260
                ....*....|....*....|....
gi 46577677 273 MTVDPHQRPHIPlllsqlEALQPP 296
Cdd:cd07855 280 LRFDPSERITVA------EALQHP 297
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
16-289 1.30e-14

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: 72.75  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYLF--IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRErga 90
Cdd:cd06634  11 DDPEKLFsdLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQdiiKEVKFLQKLRHPNTIEYRGCYLRE--- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kHEAWLLLPFfkrgTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSm 170
Cdd:cd06634  88 -HTAWLVMEY----CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGS- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 nqacihvegsrqALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPydmVFQKGDSVAL--A 248
Cdd:cd06634 162 ------------ASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPP---LFNMNAMSALyhI 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 249 VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06634 227 AQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKH 267
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-274 1.62e-14

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 72.79  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLvayclrergakHEA-- 94
Cdd:cd05596  28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAffwEERDIMAHANSEWIVQL-----------HYAfq 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 -----WLLLPFFKRGTLWNEIERL---KDKGNFLTEDQILwlllgicrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD 166
Cdd:cd05596  97 ddkylYMVMDYMPGGDLVNLMSNYdvpEKWARFYTAEVVL--------ALDAIHSMGFVHRDVKPDNMLLDASGHLKLAD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 167 LGSmnqaCIHVEgsRQALTLQDWAAQrcTISYRAPELFSVQS-HCVIDERTDVWSLGCVLYAMMFGEGPY---DMVFQKG 242
Cdd:cd05596 169 FGT----CMKMD--KDGLVRSDTAVG--TPDYISPEVLKSQGgDGVYGRECDWWSVGVFLYEMLVGDTPFyadSLVGTYG 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 243 DsvALAVQNQLSIPQSPRHSSALRQLLNSMMT 274
Cdd:cd05596 241 K--IMNHKNSLQFPDDVEISKDAKSLICAFLT 270
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-296 1.88e-14

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 71.98  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLVAycLRERGAkhEAWLLL 98
Cdd:cd14167   5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSiENEIAVLHKIKHPNIVALDD--IYESGG--HLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWneiERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL---LGDEGQPVLMDLGSMNqaci 175
Cdd:cd14167  81 QLVSGGELF---DRIVEKG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 hVEGSRQALTLQdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMVFQKGDSVALAVQNQL 253
Cdd:cd14167 153 -IEGSGSVMSTA------CgTPGYVAPEVLAQKPY---SKAVDCWSIGVIAYILLCGYPPfYDENDAKLFEQILKAEYEF 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14167 223 DSPYWDDISDSAKDFIQHLMEKDPEKR------FTCEQALQHP 259
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
22-234 1.92e-14

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 71.96  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGgfSYVDLVEGLH--DGHFYALKRILCHEQQDrEEAQREADMHRLFNH-PNILRLVAYCLRERGAKH--EAWL 96
Cdd:cd06636  20 LVEVVGNG--TYGQVYKGRHvkTGQLAAIKVMDVTEDEE-EEIKLEINMLKKYSHhRNIATYYGAFIKKSPPGHddQLWL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIH 176
Cdd:cd06636  97 VMEFCGAGSVTDLVK--NTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VeGSRQALTlqdwaaqrCTISYRAPELFSVQSH--CVIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:cd06636 175 V-GRRNTFI--------GTPYWMAPEVIACDENpdATYDYRSDIWSLGITAIEMAEGAPP 225
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
17-287 1.97e-14

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: 71.99  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWL 96
Cdd:cd06644  11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWD----GKLWI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLwNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacih 176
Cdd:cd06644  87 MIEFCPGGAV-DAIMLELDRG--LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGV------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 veGSRQALTLQDWAAQRCTISYRAPELFSVQS--HCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLS 254
Cdd:cd06644 157 --SAKNVKTLQRRDSFIGTPYWMAPEVVMCETmkDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPT 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 255 IPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06644 235 LSQPSKWSMEFRDFLKTALDKHPETRPSAAQLL 267
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
26-288 2.04e-14

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 71.80  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILC----HEQQDREEA-----QREADMHRLFNHPNIlrlVAYCLRERGAKHeawl 96
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELpsvsAENKDRKKSmldalQREIALLRELQHENI---VQYLGSSSDANH---- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 lLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-----SMN 171
Cdd:cd06628  81 -LNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGiskklEAN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 QACIHVEGSRQALtlqdwaaqRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-DM-----VFQKGDSV 245
Cdd:cd06628 160 SLSTKNNGARPSL--------QGSVFWMAPEVVKQTSY---TRKADIWSLGCLVVEMLTGTHPFpDCtqmqaIFKIGENA 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 46577677 246 AlavqnqlsiPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06628 229 S---------PTIPSNiSSEARDFLEKTFEIDHNKRPTADELLK 263
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
136-280 2.10e-14

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: 71.55  E-value: 2.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAIHAKGYAHRDLKPTNILLGDEGQPVL--MDLGsMNQaciHVEGSRQALTLqdwaaqRCTISYRAPELFSVQSHcviD 213
Cdd:cd14121 108 LQFLREHNISHMDLKPQNLLLSSRYNPVLklADFG-FAQ---HLKPNDEAHSL------RGSPLYMAPEMILKKKY---D 174
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 214 ERTDVWSLGCVLYAMMFGEGPY-DMVFQKgdsVALAVQNQ--LSIPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14121 175 ARVDLWSVGVILYECLFGRAPFaSRSFEE---LEEKIRSSkpIEIPTRPELSADCRDLLLRLLQRDPDRR 241
pknD PRK13184
serine/threonine-protein kinase PknD;
19-280 2.17e-14

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 73.65  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYClrerGAKHEAW 95
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIredLSENPLLKKRFLREAKIAADLIHPGIVPVYSIC----SDGDPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   96 LLLPFFKRGTL-------WNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:PRK13184  79 YTMPYIEGYTLksllksvWQKESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  169 smnqACIHVEGSRQALTLQDWAAQRC-------------TISYRAPE-LFSVQShcviDERTDVWSLGCVLYAMMFGEGP 234
Cdd:PRK13184 159 ----AAIFKKLEEEDLLDIDVDERNIcyssmtipgkivgTPDYMAPErLLGVPA----SESTDIYALGVILYQMLTLSFP 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 46577677  235 YdmvfQKGDSVALAVQNQLSIPQ--SPRHS--SALRQLLNSMMTVDPHQR 280
Cdd:PRK13184 231 Y----RRKKGRKISYRDVILSPIevAPYREipPFLSQIAMKALAVDPAER 276
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
19-235 2.19e-14

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 71.82  E-value: 2.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILChEQQDREEAQREADMHRLFNHPNILRLvayclRERGAKHEAWLLL 98
Cdd:cd14104   1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKV-KGADQVLVKKEISILNIARHRNILRL-----HESFESHEELVMI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGSmnqacih 176
Cdd:cd14104  75 FEFISGV--DIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYikIIEFGQ------- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 177 vegSRQALTLQDWAAQRCTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14104 146 ---SRQLKPGDKFRLQYTSAEFYAPE---VHQHESVSTATDMWSLGCLVYVLLSGINPF 198
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
26-235 2.42e-14

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 71.49  E-value: 2.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLvaYCLRErgAKHEAWLLLPFFKRGT 105
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQL--YEAIE--TPNEIVLFMEYVEGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPV-LMDLGsmnqacihvegsrqa 183
Cdd:cd14190  88 LF---ERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQVkIIDFG--------------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 184 LTLQDWAAQRCTISYRAPELFS--VQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14190 150 LARRYNPREKLKVNFGTPEFLSpeVVNYDQVSFPTDMWSMGVITYMLLSGLSPF 203
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
20-231 2.56e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 71.96  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheawLLL 98
Cdd:cd07873   4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIrLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLT----LVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRgtlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQAcihve 178
Cdd:cd07873  80 EYLDK----DLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG-LARA----- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 46577677 179 gsrQALTLQDWAAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFG 231
Cdd:cd07873 150 ---KSIPTKTYSNEVVTLWYRPPDILLGSTD--YSTQIDMWGVGCIFYEMSTG 197
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
22-280 2.56e-14

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 71.96  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGL--HD-GHFYALKRI----LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHea 94
Cdd:cd05613   4 LLKVLGTGAYGKVFLVRKVsgHDaGKLYAMKVLkkatIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLH-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 wLLLPFFKRGTLWNEI-ERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQA 173
Cdd:cd05613  82 -LILDYINGGELFTHLsQRER-----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHvEGSRqaltlqdwAAQRC-TISYRAPELF--SVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQ 250
Cdd:cd05613 156 LLD-ENER--------AYSFCgTIEYMAPEIVrgGDSGH---DKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRR 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 251 NQLSIPQSPRHSSAL-RQLLNSMMTVDPHQR 280
Cdd:cd05613 224 ILKSEPPYPQEMSALaKDIIQRLLMKDPKKR 254
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
20-290 3.00e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 71.21  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLV-AYCLRERgakheAWLLL 98
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFgSYLSREK-----LWICM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLwNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVE 178
Cdd:cd06646  86 EYCGGGSL-QDIYHVTGP---LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDWAaqrctisyrAPELFSVQSHCVIDERTDVWSLGCV------LYAMMFGEGPYDMVFqkgdsvaLAVQNQ 252
Cdd:cd06646 162 KRKSFIGTPYWM---------APEVAAVEKNGGYNQLCDIWAVGITaielaeLQPPMFDLHPMRALF-------LMSKSN 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46577677 253 LSIPQ---SPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd06646 226 FQPPKlkdKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHL 266
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
17-231 3.01e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 72.76  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILcheqQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWL 96
Cdd:PTZ00036  65 NKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVL----QDPQYKNRELLIMKNLNHINIIFLKDYYYTECFKKNEKNI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   97 LLpffkrGTLWNEIERLKDK--GNFLTEDQILWLLL------GICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV-LMDL 167
Cdd:PTZ00036 141 FL-----NVVMEFIPQTVHKymKHYARNNHALPLFLvklysyQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLkLCDF 215
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677  168 GSmnqacihvegSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIdeRTDVWSLGCVLYAMMFG 231
Cdd:PTZ00036 216 GS----------AKNLLAGQRSVSYICSRFYRAPELMLGATNYTT--HIDLWSLGCIIAEMILG 267
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
12-289 3.02e-14

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 71.58  E-value: 3.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  12 TVIIDN-----KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHR-LFNHPNILRLVA-YC 84
Cdd:cd06638   7 TIIFDSfpdpsDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIHDIDEEIEAEYNILKaLSDHPNVVKFYGmYY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  85 LRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVL 164
Cdd:cd06638  86 KKDVKNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 165 MDLGSMNQACIHVEGSRQALTLQDWAaqrctisyrAPELFSVQSH--CVIDERTDVWSLGcvLYAMMFGEG--------P 234
Cdd:cd06638 166 VDFGVSAQLTSTRLRRNTSVGTPFWM---------APEVIACEQQldSTYDARCDVWSLG--ITAIELGDGdppladlhP 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 235 YDMVFQkgdsvalavqnqlsIPQSPRH--------SSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06638 235 MRALFK--------------IPRNPPPtlhqpelwSNEFNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
56-296 3.79e-14

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 70.85  E-value: 3.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  56 QQDREEAQREADMHRLFN-HPNILRLVAYclrergAKHEAWLLLPF--FKRGTLW---NEIERLKDKGNFLTEDQILwll 129
Cdd:cd14093  49 EELREATRREIEILRQVSgHPNIIELHDV------FESPTFIFLVFelCRKGELFdylTEVVTLSEKKTRRIMRQLF--- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 lgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSrqalTLQDWaaqrC-TISYRAPELFSVQ- 207
Cdd:cd14093 120 ----EAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGF---ATRLDEGE----KLREL----CgTPGYLAPEVLKCSm 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 208 --SHCVIDERTDVWSLGCVLYAMMFGEGPY----DMVF----QKGdsvalavQNQLSIPQSPRHSSALRQLLNSMMTVDP 277
Cdd:cd14093 185 ydNAPGYGKEVDMWACGVIMYTLLAGCPPFwhrkQMVMlrniMEG-------KYEFGSPEWDDISDTAKDLISKLLVVDP 257
                       250
                ....*....|....*....
gi 46577677 278 HQRphipllLSQLEALQPP 296
Cdd:cd14093 258 KKR------LTAEEALEHP 270
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
18-296 4.28e-14

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: 71.29  E-value: 4.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergAKHEAWLL 97
Cdd:cd06655  19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFL----VGDELFVV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacIHV 177
Cdd:cd06655  95 MEYLAGGSLTDVVTE-----TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ--ITP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVALAVQNQLSIPQ 257
Cdd:cd06655 168 EQSKRSTMVG-------TPYWMAPEVVTRKAY---GPKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATNGTPELQ 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 258 SP-RHSSALRQLLNSMMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd06655 237 NPeKLSPIFRDFLNRCLEMDVEKRG------SAKELLQHP 270
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-282 4.30e-14

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: 70.94  E-value: 4.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRilCHEQQDREEAQR-----EADMHRLFNHPNIL--RLVAYCLRERGAKHEAWLLL 98
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKK--CRQELSPSDKNRerwclEVQIMKKLNHPNVVsaRDVPPELEKLSPNDLPLLAM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV---LMDLG-----SM 170
Cdd:cd13989  79 EYCSGGDLRKVLNQPENCCG-LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRViykLIDLGyakelDQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQACIHVEGsrqalTLQdwaaqrctisYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY---------DMVFQK 241
Cdd:cd13989 158 GSLCTSFVG-----TLQ----------YLAPELFESKKY---TCTVDYWSFGTLAFECITGYRPFlpnwqpvqwHGKVKQ 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 242 GDSVALAVQNQLS--------IPqSPRH-SSALRQLLNS----MMTVDPHQRPH 282
Cdd:cd13989 220 KKPEHICAYEDLTgevkfsseLP-SPNHlSSILKEYLESwlqlMLRWDPRQRGG 272
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
26-280 4.75e-14

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 70.85  E-value: 4.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMhrLFNHPNIL-----RLV---AYCLRergAKHEAWLL 97
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMYACKKL----EKKRIKKRKGEAM--ALNEKQILekvnsRFVvslAYAYE---TKDALCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHV 177
Cdd:cd05605  79 LTIMNGGDLKFHIYNMGNPG--FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLG----LAVEI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 -EGsrqaltlqDWAAQRC-TISYRAPElfsvqshcVID-ER----TDVWSLGCVLYAMMFGEGPYDMVFQ--KGDSVALA 248
Cdd:cd05605 153 pEG--------ETIRGRVgTVGYMAPE--------VVKnERytfsPDWWGLGCLIYEMIEGQAPFRARKEkvKREEVDRR 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 249 VQNQlSIPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05605 217 VKED-QEEYSEKFSEEAKSICSQLLQKDPKTR 247
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
57-293 4.80e-14

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 70.48  E-value: 4.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLwNEIERLKDkGNFLTEdQILWLLLGICRGL 136
Cdd:cd05033  47 KQRLDFLTEASIMGQFDHPNVIRLEGVVTKSR----PVMIVTEYMENGSL-DKFLREND-GKFTVT-QLVGMLRGIASGM 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 137 EAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaciHVEGSRQALTLQD------WAAQRcTISYRApelFSVQShc 210
Cdd:cd05033 120 KYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSR----RLEDSEATYTTKGgkipirWTAPE-AIAYRK---FTSAS-- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 211 vidertDVWSLGCVLYAMM-FGEGPY-DMVFQKgdsVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd05033 190 ------DVWSFGIVMWEVMsYGERPYwDMSNQD---VIKAVEDGYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVS 260

                ....*
gi 46577677 289 QLEAL 293
Cdd:cd05033 261 TLDKM 265
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
14-288 5.01e-14

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 70.95  E-value: 5.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  14 IIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILcheqqDREEAQREADMHRLFN-HPNILRLV-AYC-----LR 86
Cdd:cd14171   2 ILEEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILL-----DRPKARTEVRLHMMCSgHPNIVQIYdVYAnsvqfPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  87 ERGAKHEAWLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD 166
Cdd:cd14171  77 ESSPRARLLIVMELMEGGELFDRISQHRH----FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 167 LGSMNQAcihvegsrqALTLQDWAAQRCTISYRAPELFSVQ--------------SHCVIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd14171 153 LCDFGFA---------KVDQGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGY 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 233 GPYdmvFQKGDSVALAVQNQLSI-------PQS--PRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd14171 224 PPF---YSEHPSRTITKDMKRKImtgsyefPEEewSQISEMAKDIVRKLLCVDPEERMTIEEVLH 285
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
20-246 5.13e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 70.99  E-value: 5.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDRE-EAQREADMHRLFNHPNILRLVAYCLRERGAkheawll 97
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrLDNEKEGFPiTAIREIKILRQLNHRSVVNLKEIVTDKQDA------- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 lpffkrgtlwneIERLKDKGNF---------------------LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL 156
Cdd:cd07864  82 ------------LDFKKDKGAFylvfeymdhdlmgllesglvhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 GDEGQPVLMDLGSMNqaCIHVEGSRQaltlqdWAAQRCTISYRAPELFsvqshcVIDER----TDVWSLGCVLyAMMFGE 232
Cdd:cd07864 150 NNKGQIKLADFGLAR--LYNSEESRP------YTNKVITLWYRPPELL------LGEERygpaIDVWSCGCIL-GELFTK 214
                       250
                ....*....|....
gi 46577677 233 GPydmVFQKGDSVA 246
Cdd:cd07864 215 KP---IFQANQELA 225
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
16-281 5.47e-14

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: 71.22  E-value: 5.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYLFI--QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRErga 90
Cdd:cd06633  17 DDPEEIFVdlHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQdiiKEVKFLQQLKHPNTIEYKGCYLKD--- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kHEAWLLLPFfkrgTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:cd06633  94 -HTAWLVMEY----CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQAcihvEGSRQALTLQDWAaqrctisyrAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPydmVFQKGDSVAL--A 248
Cdd:cd06633 169 SIA----SPANSFVGTPYWM---------APEVILAMDEGQYDGKVDIWSLGITCIELAERKPP---LFNMNAMSALyhI 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 249 VQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd06633 233 AQNDSPTLQSNEWTDSFRGFVDYCLQKIPQERP 265
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-235 5.51e-14

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: 70.93  E-value: 5.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHE---QQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLP 99
Cdd:cd05612   6 IKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvirLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQR----FLYMLME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNeieRLKDKGNFLTEDQILWLLLGICrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihveg 179
Cdd:cd05612  82 YVPGGELFS---YLRNSGRFSNSTGLFYASEIVC-ALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF---------- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 180 srqALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05612 148 ---AKKLRDRTWTLCgTPEYLAPEVIQSKGH---NKAVDWWALGILIYEMLVGYPPF 198
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
18-232 5.56e-14

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 71.18  E-value: 5.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDR-EEAQREADMHRLFNHPNILRLVA-YCLRERGAKHEAW 95
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYcLRTLREIKILLRFKHENIIGILDiQRPPTFESFKDVY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKrgtlwNEIERLKdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACI 175
Cdd:cd07849  85 IVQELME-----TDLYKLI-KTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFG---LARI 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 176 HVEGSRQALTLQDWAAQRCtisYRAPE--LFSVQSHCVIdertDVWSLGCVLYAMMFGE 232
Cdd:cd07849 156 ADPEHDHTGFLTEYVATRW---YRAPEimLNSKGYTKAI----DIWSVGCILAEMLSNR 207
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
72-280 5.87e-14

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 70.09  E-value: 5.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  72 FNHPNILRLVAYclreRGAKHEAWLLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKP 151
Cdd:cd14120  49 LSHENVVALLDC----QETSSSVYLVMEYCNGGDL---ADYLQAKGT-LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKP 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 152 TNILLGDEGQPvlmdlgsmnqaciHVEGSRQALTLQDW-----------AAQRC-TISYRAPELFSVQSHcviDERTDVW 219
Cdd:cd14120 121 QNILLSHNSGR-------------KPSPNDIRLKIADFgfarflqdgmmAATLCgSPMYMAPEVIMSLQY---DAKADLW 184
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 220 SLGCVLYAMMFGEGPydmvFQKGDSVALAV---QNQLSIPQSPRH-SSALRQLLNSMMTVDPHQR 280
Cdd:cd14120 185 SIGTIVYQCLTGKAP----FQAQTPQELKAfyeKNANLRPNIPSGtSPALKDLLLGLLKRNPKDR 245
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
54-293 5.88e-14

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: 70.42  E-value: 5.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREA--------------DMHRLFNHPNILRLVAYCLRERGAKHeawlllpFFKRGTLWNEIERLKDKGNf 119
Cdd:cd13995  21 YLAQDTKTKKRMAcklipveqfkpsdvEIQACFRHENIAELYGALLWEETVHL-------FMEAGEGGSVLEKLESCGP- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGdEGQPVLMDLGsmnqacIHVEGSRQALTLQDWaaqRCTISYR 199
Cdd:cd13995  93 MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM-STKAVLVDFG------LSVQMTEDVYVPKDL---RGTEIYM 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKG--DSVALAVQNQL----SIPQSPrhSSALRQLLNSMM 273
Cdd:cd13995 163 SPEVILCRGH---NTKADIYSLGATIIHMQTGSPPWVRRYPRSayPSYLYIIHKQAppleDIAQDC--SPAMRELLEAAL 237
                       250       260
                ....*....|....*....|
gi 46577677 274 TVDPHQRPHIPLLLSQlEAL 293
Cdd:cd13995 238 ERNPNHRSSAAELLKH-EAL 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
25-281 6.09e-14

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 70.38  E-value: 6.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVdlveglHDGHFYALK-------RILCHEQQD---REEAQREADMHRLFNHPNILRLVAYClrergaKHEA 94
Cdd:cd05116   2 ELGSGNFGTV------KKGYYQMKKvvktvavKILKNEANDpalKDELLREANVMQQLDNPYIVRMIGIC------EAES 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLL-LPFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQA 173
Cdd:cd05116  70 WMLvMEMAELGPL----NKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFG-LSKA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQDWAaqrctISYRAPELFSVQShcvIDERTDVWSLGCVLY-AMMFGEGPYDMVfqKGDSVALAVQNQ 252
Cdd:cd05116 145 LRADENYYKAQTHGKWP-----VKWYAPECMNYYK---FSSKSDVWSFGVLMWeAFSYGQKPYKGM--KGNEVTQMIEKG 214
                       250       260
                ....*....|....*....|....*....
gi 46577677 253 LSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05116 215 ERMECPAGCPPEMYDLMKLCWTYDVDERP 243
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
22-287 6.59e-14

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 70.53  E-value: 6.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRIlcheqqdreEAQRE-ADMHRLFNHPNILRLVAYC---LRERGAkheawll 97
Cdd:cd06617   5 VIEELGRGAYGVVDKMRHVPTGTIMAVKRI---------RATVNsQEQKRLLMDLDISMRSVDCpytVTFYGA------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 lpFFKRGTLWNEIE-----------RLKDKGNFLTEDQILWLLLGICRGLEAIHAK-GYAHRDLKPTNILLGDEGQPVLM 165
Cdd:cd06617  69 --LFREGDVWICMEvmdtsldkfykKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLC 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 166 DLGSMNQACIHVegsrqALTLQDWAAQrctisYRAPELFSVQ-SHCVIDERTDVWSLGCVLYAMMFGEGPYD---MVFQK 241
Cdd:cd06617 147 DFGISGYLVDSV-----AKTIDAGCKP-----YMAPERINPElNQKGYDVKSDVWSLGITMIELATGRFPYDswkTPFQQ 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 242 GDSValaVQNqlSIPQSP--RHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06617 217 LKQV---VEE--PSPQLPaeKFSPEFQDFVNKCLKKNYKERPNYPELL 259
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
20-296 6.81e-14

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 69.94  E-value: 6.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHD-------GHFYALKRILCHEQQDREEAQREAdMHRLFNHPNILRLVaYCLRErgaKH 92
Cdd:cd14019   3 YRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSRILNELEC-LERLGGSNNVSGLI-TAFRN---ED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFkrgtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPVLMDLGsmn 171
Cdd:cd14019  78 QVVAVLPYI-------EHDDFRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFG--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qacihvegsrqaltLQDWAAQR--------CTISYRAPE-LFSVQSH-CVIdertDVWSLGCVLYAMMFGEGPydMVFQK 241
Cdd:cd14019 148 --------------LAQREEDRpeqrapraGTRGFRAPEvLFKCPHQtTAI----DIWSAGVILLSILSGRFP--FFFSS 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 242 GDSVALAvqnQL-SIpqspRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14019 208 DDIDALA---EIaTI----FGSDEAYDLLDKLLELDPSKR------ITAEEALKHP 250
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
22-289 6.86e-14

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: 70.46  E-value: 6.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPFF 101
Cdd:cd06645  15 LIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLR----RDKLWICMEFC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSR 181
Cdd:cd06645  91 GGGSL----QDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLQDWAaqrctisyrAPELFSVQSHCVIDERTDVWSLGCV------LYAMMFGEGPYDMVFqkgdsvaLAVQNQLSI 255
Cdd:cd06645 167 SFIGTPYWM---------APEVAAVERKGGYNQLCDIWAVGITaielaeLQPPMFDLHPMRALF-------LMTKSNFQP 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 256 PQ---SPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06645 231 PKlkdKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQH 267
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
26-293 7.84e-14

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 70.26  E-value: 7.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEG---LHDGHF--YALK--RILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLR--ERGAKHEAWL 96
Cdd:cd05035   7 LGEGEFGSV--MEAqlkQDDGSQlkVAVKtmKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTasDLNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEI--ERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQAC 174
Cdd:cd05035  85 ILPFMKHGDLHSYLlySRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFG-LSRKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQ---DWAAqrctISYRAPELFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAVQ 250
Cdd:cd05035 164 YSGDYYRQGRISKmpvKWIA----LESLADNVYTSKS--------DVWSFGVTMWEIAtRGQTPYPGV--ENHEIYDYLR 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05035 230 NGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
43-305 9.11e-14

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 70.45  E-value: 9.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  43 GHFYALKRIlcheqQDREEAQREADMH-RLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNeieRLKDKGN-FL 120
Cdd:cd14170  27 QEKFALKML-----QDCPKARREVELHwRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGGELFS---RIQDRGDqAF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 121 TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacihveGSRQALTLQDWAAQRC-TISYR 199
Cdd:cd14170  99 TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDF--------GFAKETTSHNSLTTPCyTPYYV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmVFQKGDSVALAVQNQLSI-------PQSPRHSSALRQLLNSM 272
Cdd:cd14170 171 APEVLGPEKY---DKSCDMWSLGVIMYILLCGYPPF--YSNHGLAISPGMKTRIRMgqyefpnPEWSEVSEEVKMLIRNL 245
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 273 MTVDPHQRPHIPLLLSQ---LEALQPPAPGQHTTQI 305
Cdd:cd14170 246 LKTEPTQRMTITEFMNHpwiMQSTKVPQTPLHTSRV 281
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
13-298 1.00e-13

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 69.96  E-value: 1.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  13 VIIDNKRYLFIQKLGEGGFSYVdlVEG---LHDG--HFYALK--RILCHEQQDREEAQREADMHRLFNHPNILRLVAYCL 85
Cdd:cd14204   2 VMIDRNLLSLGKVLGEGEFGSV--MEGelqQPDGtnHKVAVKtmKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  86 rERGAKH--EAWLLLPFFKRGTLWNEI--ERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ 161
Cdd:cd14204  80 -EVGSQRipKPMVILPFMKYGDLHSFLlrSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 162 PVLMDLGsMNQACIHVEGSRQALTLQ---DWAAqrctISYRAPELFSVQShcvidertDVWSLGCVLYAMMF-GEGPYDM 237
Cdd:cd14204 159 VCVADFG-LSKKIYSGDYYRQGRIAKmpvKWIA----VESLADRVYTVKS--------DVWAFGVTMWEIATrGMTPYPG 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 238 VFQKGDSVALAVQNQLSIPqsPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAP 298
Cdd:cd14204 226 VQNHEIYDYLLHGHRLKQP--EDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
38-288 1.40e-13

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: 69.22  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  38 EGLHDGHFYALKRIL--CHEQQDRE-EAQREADmhrlfNHPNILRLvaYCLRE-RGAKHEAWLLLPffkrGTLWNEIERL 113
Cdd:cd13982  20 RGTFDGRPVAVKRLLpeFFDFADREvQLLRESD-----EHPNVIRY--FCTEKdRQFLYIALELCA----ASLQDLVESP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 114 KDKGNFLTED-QILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-----GDEGQPVLMDLGsmnqACIHVEGSRQALTLQ 187
Cdd:cd13982  89 RESKLFLRPGlEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFG----LCKKLDVGRSSFSRR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 188 DWAAQrcTISYRAPELFSVQSHCVIDERTDVWSLGCVL-YAMMFGEGPYDMVFQKgDSVALAVQNQLSIPQSPRHSSAL- 265
Cdd:cd13982 165 SGVAG--TSGWIAPEMLSGSTKRRQTRAVDIFSLGCVFyYVLSGGSHPFGDKLER-EANILKGKYSLDKLLSLGEHGPEa 241
                       250       260
                ....*....|....*....|...
gi 46577677 266 RQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd13982 242 QDLIERMIDFDPEKRPSAEEVLN 264
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
26-235 1.53e-13

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: 68.83  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGT 105
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAK-FIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPT----ELVLILELCSGGE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGS---MNQACIHVEgs 180
Cdd:cd14006  76 L---LDRLAERGS-LSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQikIIDFGLarkLNPGEELKE-- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 181 rqaltlqdwaaQRCTISYRAPELfsVQSHcVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14006 150 -----------IFGTPEFVAPEI--VNGE-PVSLATDMWSIGVLTYVLLSGLSPF 190
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
47-293 1.58e-13

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 69.04  E-value: 1.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  47 ALKRIlcHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHeawLLLPFFKRGTLWNEIerlKDKGNFLTEDQIL 126
Cdd:cd05058  30 SLNRI--TDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPL---VVLPYMKHGDLRNFI---RSETHNPTVKDLI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 127 WLLLGICRGLEAIHAKGYAHRDLKPTNILLgDEGQPV-LMDLGSMNQACihvegSRQALTLQDWAAQRCTISYRAPElfS 205
Cdd:cd05058 102 GFGLQVAKGMEYLASKKFVHRDLAARNCML-DESFTVkVADFGLARDIY-----DKEYYSVHNHTGAKLPVKWMALE--S 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 206 VQSHcVIDERTDVWSLGCVLYAMMF-GEGPYDMVFQKGDSVALAVQNQLSIPQ-SPrhsSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd05058 174 LQTQ-KFTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLQGRRLLQPEyCP---DPLYEVMLSCWHPKPEMRPTF 249
                       250
                ....*....|
gi 46577677 284 PLLLSQLEAL 293
Cdd:cd05058 250 SELVSRISQI 259
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
24-235 1.62e-13

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: 69.26  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALK----RILCHEQQ--DREEAQREADMHRLFNHPNILRLvaYCLRERgaKHEAWLL 97
Cdd:cd14195  11 EELGSGQFAIVRKCREKGTGKEYAAKfikkRRLSSSRRgvSREEIEREVNILREIQHPNIITL--HDIFEN--KTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP----VLMDLGSMNQa 173
Cdd:cd14195  87 LELVSGGELFDFLAEKES----LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPnpriKLIDFGIAHK- 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 174 cihVEGSRQALTLQDwaaqrcTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14195 162 ---IEAGNEFKNIFG------TPEFVAPEIVNYEP---LGLEADMWSIGVITYILLSGASPF 211
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
18-281 1.80e-13

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: 69.02  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRErgakHEA 94
Cdd:cd06607   1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQdiiKEVKFLRQLRHPNTIEYKGCYLRE----HTA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFkRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd06607  77 WLVMEYC-LGSASDIVEVHKKP---LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ihvegsrqaltlqdwAAQRC--TISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAL--AVQ 250
Cdd:cd06607 153 ---------------PANSFvgTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPL---FNMNAMSALyhIAQ 214
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 251 NQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd06607 215 NDSPTLSSGEWSDDFRNFVDSCLQKIPQDRP 245
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
56-296 1.81e-13

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 69.17  E-value: 1.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  56 QQDREEAQREAD-MHRLFNHPNILRLvayclrERGAKHEAWLLLPF--FKRGTLWNEI-ERLKdkgnfLTEDQILWLLLG 131
Cdd:cd14182  50 QELREATLKEIDiLRKVSGHPNIIQL------KDTYETNTFFFLVFdlMKKGELFDYLtEKVT-----LSEKETRKIMRA 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRqaltlqdwAAQRC-TISYRAPELFsvqsHC 210
Cdd:cd14182 119 LLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGF---SCQLDPGEK--------LREVCgTPGYLAPEII----EC 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 211 VIDER-------TDVWSLGCVLYAMMFGEGPY----DMVFQKgdsVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQ 279
Cdd:cd14182 184 SMDDNhpgygkeVDMWSTGVIMYTLLAGSPPFwhrkQMLMLR---MIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQK 260
                       250
                ....*....|....*..
gi 46577677 280 RphipllLSQLEALQPP 296
Cdd:cd14182 261 R------YTAEEALAHP 271
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
24-235 1.94e-13

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


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 68.88  E-value: 1.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYV-DLVEGlHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRlvayCLRERGAKHEAWLLLPFFK 102
Cdd:cd14191   8 ERLGSGKFGQVfRLVEK-KTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQ----CVDAFEEKANIVMVLEMVS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL-LGDEGQPV-LMDLGSMNQacIHVEGS 180
Cdd:cd14191  83 GGELF---ERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTKIkLIDFGLARR--LENAGS 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 181 RQALTlqdwaaqrCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14191 158 LKVLF--------GTPEFVAPEVINYEP---IGYATDMWSIGVICYILVSGLSPF 201
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
132-296 2.55e-13

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: 68.45  E-value: 2.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGSMNQACIHVEGSRQALtlqdwaaqrctiSYRAPElfsvqsh 209
Cdd:cd14133 111 ILEALVFLHSLGLIHCDLKPENILLASYSRCQikIIDFGSSCFLTQRLYSYIQSR------------YYRAPE------- 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 210 cVI-----DERTDVWSLGCVLYAMMFGEgpydMVFQkGDSvalaVQNQLS-------------IPQSPRHSSALRQLLNS 271
Cdd:cd14133 172 -VIlglpyDEKIDMWSLGCILAELYTGE----PLFP-GAS----EVDQLAriigtigippahmLDQGKADDELFVDFLKK 241
                       170       180
                ....*....|....*....|....*
gi 46577677 272 MMTVDPHQRPhiplllSQLEALQPP 296
Cdd:cd14133 242 LLEIDPKERP------TASQALSHP 260
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
26-280 2.84e-13

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 68.75  E-value: 2.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFN--HPNILRLVAYCLRergAKHEAWLLLPFFKR 103
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAkvHSRFIVSLAYAFQ---TKTDLCLVMTIMNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIHVEGSRQA 183
Cdd:cd05608  86 GDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLG------LAVELKDGQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALA--VQNQlSIPQSPRH 261
Cdd:cd05608 160 TKTKGYAG---TPGFMAPELLLGEEY---DYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKqrILND-SVTYSEKF 232
                       250
                ....*....|....*....
gi 46577677 262 SSALRQLLNSMMTVDPHQR 280
Cdd:cd05608 233 SPASKSICEALLAKDPEKR 251
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
20-283 3.06e-13

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 68.21  E-value: 3.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ--READMHRLFNHPNILRLvaYCLRERGAKheAWLL 97
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHlfQEVRCMKLVQHPNVVRL--YEVIDTQTK--LYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQPVLMDLGSMNQ---- 172
Cdd:cd14074  81 LELGDGGDMYDYIMK---HENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKfqpg 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 -----ACIHVEGSRQALTLQDwaaqrctiSYRAPELfsvqshcvidertDVWSLGCVLYAMMFGEGPydmvFQK-GDSVA 246
Cdd:cd14074 158 ekletSCGSLAYSAPEILLGD--------EYDAPAV-------------DIWSLGVILYMLVCGQPP----FQEaNDSET 212
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 247 LA--VQNQLSIPqsPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14074 213 LTmiMDCKYTVP--AHVSPECKDLIRRMLIRDPKKRASL 249
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
22-280 3.14e-13

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 69.28  E-value: 3.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALK-----RILCHEQQDREEAQREADMHRLfNHPNILRLvAYCLRergAKHEAWL 96
Cdd:cd05602  11 FLKVIGKGSFGKVLLARHKSDEKFYAVKvlqkkAILKKKEEKHIMSERNVLLKNV-KHPFLVGL-HFSFQ---TTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIER----LKDKGNFLTEDqilwlllgICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd05602  86 VLDYINGGELFYHLQRercfLEPRARFYAAE--------IASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 aciHVEGSRQALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVALAVQN 251
Cdd:cd05602 158 ---NIEPNGTTSTF-------CgTPEYLAPEVLHKQPY---DRTVDWWCLGAVLYEMLYGLPPF-----YSRNTAEMYDN 219
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 252 QLSIPQS--PRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05602 220 ILNKPLQlkPNITNSARHLLEGLLQKDRTKR 250
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
15-290 3.25e-13

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: 68.05  E-value: 3.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFyALKRI---LCHEQQDREEAQReadMHRLfNHPNILRLVAYCLRergaK 91
Cdd:cd05112   1 IDPSELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIregAMSEEDFIEEAEV---MMKL-SHPKLVQLYGVCLE----Q 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmn 171
Cdd:cd05112  72 APICLVFEFMEHGCL---SDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGM-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qacihvegSRQALTLQDWAAQ--RCTISYRAPELFSVQSHcviDERTDVWSLGcVLYAMMFGEG--PYDmvfQKGDSVAL 247
Cdd:cd05112 147 --------TRFVLDDQYTSSTgtKFPVKWSSPEVFSFSRY---SSKSDVWSFG-VLMWEVFSEGkiPYE---NRSNSEVV 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 46577677 248 AVQNQLSIPQSPR-HSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd05112 212 EDINAGFRLYKPRlASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
54-293 3.73e-13

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: 68.08  E-value: 3.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGIC 133
Cdd:cd05063  45 YTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFK----PAMIITEYMENGAL---DKYLRDHDGEFSSYQLVGMLRGIA 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 134 RGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQAltlqdwAAQRCTISYRAPELFSVQShcvID 213
Cdd:cd05063 118 AGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTT------SGGKIPIRWTAPEAIAYRK---FT 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 214 ERTDVWSLGCVLYAMM-FGEGPY-DMVFQKgdsVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05063 189 SASDVWSFGIVMWEVMsFGERPYwDMSNHE---VMKAINDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLD 265

                ..
gi 46577677 292 AL 293
Cdd:cd05063 266 KL 267
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
23-235 3.78e-13

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 69.27  E-value: 3.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ--RE-------------ADMHRLFNHPNILrlvayclre 87
Cdd:cd05624  77 IKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETAcfREernvlvngdcqwiTTLHYAFQDENYL--------- 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  88 rgakheaWLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd05624 148 -------YLVMDYYVGGDLLTLLSKFEDK---LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADF 217
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 168 GS---MNQacihvEGSRQAltlqdwAAQRCTISYRAPELFSVQSHCV--IDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05624 218 GSclkMND-----DGTVQS------SVAVGTPDYISPEILQAMEDGMgkYGPECDWWSLGVCMYEMLYGETPF 279
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
59-291 3.82e-13

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: 67.52  E-value: 3.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  59 REEAQREADMHRLFNHPNILRLVAYCLrergakhEA---WLLLPFFKRGTLWNEIERlkdkGNFLTEDQILWLLLGICRG 135
Cdd:cd14059  25 RDEKETDIKHLRKLNHPNIIKFKGVCT-------QApcyCILMEYCPYGQLYEVLRA----GREITPSLLVDWSKQIASG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcihvegsRQALTLQDWAAqrcTISYRAPELFSVQShcvIDER 215
Cdd:cd14059  94 MNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-------SEKSTKMSFAG---TVAWMAPEVIRNEP---CSEK 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 216 TDVWSLGCVLYAMMFGEGPYDMVfqkgDSVAL---AVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd14059 161 VDIWSFGVVLWELLTGEIPYKDV----DSSAIiwgVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMHLD 235
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
26-235 4.18e-13

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 68.53  E-value: 4.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA---QREAD------------MHRLFNHPNILRLVayclrerga 90
Cdd:cd05597   9 IGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETacfREERDvlvngdrrwitkLHYAFQDENYLYLV--------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kheawllLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSm 170
Cdd:cd05597  80 -------MDYYCGGDLLTLLSKFEDR---LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGS- 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 171 nqaCIHVEGSRqalTLQDWAAQRcTISYRAPELFSV--QSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05597 149 ---CLKLREDG---TVQSSVAVG-TPDYISPEILQAmeDGKGRYGPECDWWSLGVCMYEMLYGETPF 208
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
20-235 4.48e-13

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: 67.90  E-value: 4.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQ------DREEAQREADMHRLFNHPNILRLvaYCLRErgAKHE 93
Cdd:cd14105   7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgvSREDIEREVSILRQVLHPNIITL--HDVFE--NKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV----LMDLGS 169
Cdd:cd14105  83 VVLILELVAGGELFDFLAEKES----LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIprikLIDFGL 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 170 MNQacihVEGSrqaltlQDWAAQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14105 159 AHK----IEDG------NEFKNIFGTPEFVAPEIVNYEP---LGLEADMWSIGVITYILLSGASPF 211
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
19-235 4.50e-13

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 67.61  E-value: 4.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLvayclrergakHEAW--- 95
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINL-----------HDAFedd 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 ----LLLPFFKRGTLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE--GQPVLMDLGS 169
Cdd:cd14114  72 nemvLILEFLSGGELF---ERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 170 MNQAcihveGSRQALTLQDWAAQrctisYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14114 149 ATHL-----DPKESVKVTTGTAE-----FAAPEIVEREP---VGFYTDMWAVGVLSYVLLSGLSPF 201
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
46-283 4.72e-13

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 67.70  E-value: 4.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  46 YALKrILcheqQDREEAQREADMH-RLFNHPNILRLV-AYCLRERGAKheaWLLL--PFFKRGTLWNEIERLKDkGNFlT 121
Cdd:cd14089  29 FALK-VL----RDNPKARREVELHwRASGCPHIVRIIdVYENTYQGRK---CLLVvmECMEGGELFSRIQERAD-SAF-T 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 122 EDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIhvegSRQALTLQdwaAQRCTISYRAP 201
Cdd:cd14089  99 EREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKE----TTTKKSLQ---TPCYTPYYVAP 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 202 ELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMvfqKGDSVALAVQNQLSI-------PQSPRHSSALRQLLNSMM 273
Cdd:cd14089 172 EVLGPEKY---DKSCDMWSLGVIMYILLCGYPPfYSN---HGLAISPGMKKRIRNgqyefpnPEWSNVSEEAKDLIRGLL 245
                       250
                ....*....|
gi 46577677 274 TVDPHQRPHI 283
Cdd:cd14089 246 KTDPSERLTI 255
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
22-280 4.73e-13

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 68.89  E-value: 4.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRergAKHEAWLLL 98
Cdd:cd05617  19 LIRVIGRGSYAKVLLVRLKKNDQIYAMKVVkkeLVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQ---TTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacihvE 178
Cdd:cd05617  96 EYVNGGDLMFHMQRQRK----LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK------E 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDWAAqrcTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGDS------VALAVQNQ 252
Cdd:cd05617 166 GLGPGDTTSTFCG---TPNYIAPEILRGEEYGF---SVDWWALGVLMFEMMAGRSPFDIITDNPDMntedylFQVILEKP 239
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 253 LSIPQ--SPRHSSALRQLLNSmmtvDPHQR 280
Cdd:cd05617 240 IRIPRflSVKASHVLKGFLNK----DPKER 265
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
24-282 4.92e-13

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: 67.47  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSyvDLVEGLHDGHFYALKRILCHE---QQDREEAQREADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPF 100
Cdd:cd05041   1 EKIGRGNFG--DVYRGVLKPDNTEVAVKTCREtlpPDLKRKFLQEARILKQYDHPNIVKLIGVCVQ----KQPIMIVMEL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNeieRLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQacihvEGS 180
Cdd:cd05041  75 VPGGSLLT---FLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFG-MSR-----EEE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTLQDWAAQrCTISYRAPELFSV---QSHCvidertDVWSLGCVLYAMM-FGEGPY-DMVFQKGDSValaVQNQLSI 255
Cdd:cd05041 146 DGEYTVSDGLKQ-IPIKWTAPEALNYgryTSES------DVWSFGILLWEIFsLGATPYpGMSNQQTREQ---IESGYRM 215
                       250       260
                ....*....|....*....|....*...
gi 46577677 256 PqSPRHS-SALRQLLNSMMTVDPHQRPH 282
Cdd:cd05041 216 P-APELCpEAVYRLMLQCWAYDPENRPS 242
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
20-289 5.88e-13

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: 67.82  E-value: 5.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLFNH-PNILRLVAYCLRER--GAKHEAWL 96
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTGDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKNppGMDDQLWL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIH 176
Cdd:cd06637  87 VMEFCGAGSVTDLIK--NTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VeGSRQALTlqdwaaqrCTISYRAPELFSVQSH--CVIDERTDVWSLGCVLYAMMFGEGPY-DMvfQKGDSVALAVQNQL 253
Cdd:cd06637 165 V-GRRNTFI--------GTPYWMAPEVIACDENpdATYDFKSDLWSLGITAIEMAEGAPPLcDM--HPMRALFLIPRNPA 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06637 234 PRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKH 269
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
120-232 6.11e-13

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 68.15  E-value: 6.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGsrqaltlqdWAAQRCtisYR 199
Cdd:cd07878 115 LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTG---------YVATRW---YR 182
                        90       100       110
                ....*....|....*....|....*....|...
gi 46577677 200 APELFSVQSHcvIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd07878 183 APEIMLNWMH--YNQTVDIWSVGCIMAELLKGK 213
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
59-229 6.97e-13

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: 67.68  E-value: 6.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  59 REEA--QREADMH--RLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICR 134
Cdd:cd14056  29 RDEDswFRETEIYqtVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSLYDYLQR-----NTLDTEEALRLAYSAAS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAK--GY------AHRDLKPTNILLGDEGQPVLMDLGsmnqacIHVEGSRQALTLQDWAAQRC-TISYRAPElfs 205
Cdd:cd14056 104 GLAHLHTEivGTqgkpaiAHRDLKSKNILVKRDGTCCIADLG------LAVRYDSDTNTIDIPPNPRVgTKRYMAPE--- 174
                       170       180       190
                ....*....|....*....|....*....|....*
gi 46577677 206 vqshcVIDE-----------RTDVWSLGCVLYAMM 229
Cdd:cd14056 175 -----VLDDsinpksfesfkMADIYSFGLVLWEIA 204
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
20-231 7.04e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 67.71  E-value: 7.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheawLLL 98
Cdd:cd07872   8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIrLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLT----LVF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRgtlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQAcihve 178
Cdd:cd07872  84 EYLDK----DLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG-LARA----- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 46577677 179 gsrQALTLQDWAAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFG 231
Cdd:cd07872 154 ---KSVPTKTYSNEVVTLWYRPPDVLLGSSE--YSTQIDMWGVGCIFFEMASG 201
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
19-236 7.24e-13

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 67.16  E-value: 7.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRERgakhEAW 95
Cdd:cd14072   1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIK-IIDKTQLNPSSLQklfREVRIMKILNHPNIVKLFEVIETEK----TLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEI---ERLKDKGNFLTEDQILwlllgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd14072  76 LVMEYASGGEVFDYLvahGRMKEKEARAKFRQIV-------SAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 173 acihvegsrqaLTLQDWAAQRC-TISYRAPELFsvQSHCVIDERTDVWSLGCVLYAMMFGEGPYD 236
Cdd:cd14072 149 -----------FTPGNKLDTFCgSPPYAAPELF--QGKKYDGPEVDVWSLGVILYTLVSGSLPFD 200
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
17-296 7.27e-13

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 67.33  E-value: 7.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLVayclRERGAKHEAW 95
Cdd:cd14183   5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMiQNEVSILRRVKHPNIVLLI----EEMDMPTELY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL------------LGDEGQPV 163
Cdd:cd14183  81 LVMELVKGGDLFDAIT----STNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLvyehqdgskslkLGDFGLAT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 164 LMDlGSMNQACihvegsrqaltlqdwaaqrCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPY-------D 236
Cdd:cd14183 157 VVD-GPLYTVC-------------------GTPTYVAPEIIAETGYGL---KVDIWAAGVITYILLCGFPPFrgsgddqE 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 237 MVFqkgDSVALAvQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14183 214 VLF---DQILMG-QVDFPSPYWDNVSDSAKELITMMLQVDVDQR------YSALQVLEHP 263
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
23-280 7.43e-13

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 67.12  E-value: 7.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRI-----LCHEQQDREEAQReADMHRLFNHPNILRLVAyclrERGAKHEAWLL 97
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLkksdmIAKNQVTNVKAER-AIMMIQGESPYVAKLYY----SFQSKDYLYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihv 177
Cdd:cd05611  76 MEYLNGGDCASLIKTL----GGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL-------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egSRQALTLQDWAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgdsvalAVQNQ 252
Cdd:cd05611 144 --SRNGLEKRHNKKFVGTPDYLAPETILGVGD---DKMSDWWSLGCVIFEFLFGYPPFhaetpDAVFDN------ILSRR 212
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 253 LSIPQSPRH--SSALRQLLNSMMTVDPHQR 280
Cdd:cd05611 213 INWPEEVKEfcSPEAVDLINRLLCMDPAKR 242
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
26-280 8.34e-13

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 67.66  E-value: 8.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRL-FNHPNILRLvaYCLRErgAKHEAWLLLPFF 101
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAvkaLKKDVVLIDDDVECTMVEKRVLALaWENPFLTHL--YCTFQ--TKEHLFFVMEFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIErlkDKGNFLTEDQILWLLLGICrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQaciHVEGSR 181
Cdd:cd05620  79 NGGDLMFHIQ---DKGRFDLYRATFYAAEIVC-GLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKE---NVFGDN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLqdwaaqrC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQNQLSIPQSPR 260
Cdd:cd05620 152 RASTF-------CgTPDYIAPEILQGLKYTF---SVDWWSFGVLLYEMLIGQSP----FHGDDEDELFESIRVDTPHYPR 217
                       250       260
                ....*....|....*....|.
gi 46577677 261 H-SSALRQLLNSMMTVDPHQR 280
Cdd:cd05620 218 WiTKESKDILEKLFERDPTRR 238
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-231 8.85e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 67.86  E-value: 8.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   18 KRYLFIQK-LGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQ-------------READMHRLFNHPNILRLVA 82
Cdd:PTZ00024   8 ERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVkIIEISNDVTKDRqlvgmcgihfttlRELKIMNEIKHENIMGLVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   83 -YClrergaKHEAWLLLPFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ 161
Cdd:PTZ00024  88 vYV------EGDFINLVMDIMASDL----KKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677  162 PVLMDLGsMNQACIHVEGSRQALTLQDWAAQR------CTISYRAPELF--SVQSHCVIdertDVWSLGCVLYAMMFG 231
Cdd:PTZ00024 158 CKIADFG-LARRYGYPPYSDTLSKDETMQRREemtskvVTLWYRAPELLmgAEKYHFAV----DMWSVGCIFAELLTG 230
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-280 9.17e-13

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 67.03  E-value: 9.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVE---GLHDGHFYALK-----------RILCHEQQDRE--EAQREAdmhrlfnhPNILRLvAYCLRERG 89
Cdd:cd05583   2 LGTGAYGKVFLVRkvgGHDAGKLYAMKvlkkativqkaKTAEHTMTERQvlEAVRQS--------PFLVTL-HYAFQTDA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHeawLLLPFFKRGTLWNEierLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGs 169
Cdd:cd05583  73 KLH---LILDYVNGGELFTH---LYQREHF-TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFG- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNQACIHVEGSRqaltlqdwAAQRC-TISYRAPELF--SVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVA 246
Cdd:cd05583 145 LSKEFLPGENDR--------AYSFCgTIEYMAPEVVrgGSDGH---DKAVDWWSLGVLTYELLTGASPFTVDGERNSQSE 213
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 247 LAVQNQLSIPQSPRH-SSALRQLLNSMMTVDPHQR 280
Cdd:cd05583 214 ISKRILKSHPPIPKTfSAEAKDFILKLLEKDPKKR 248
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
26-288 1.00e-12

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: 67.07  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI----LCHEQQDR--EEAQREADMHRLFNHPNILRLVayclrerGAKHEAWLLLP 99
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVsfcrNSSSEQEEvvEAIREEIRMMARLNHPNIVRML-------GATQHKSHFNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKrgtlW---NEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV-LMDLGSMNQ--A 173
Cdd:cd06630  81 FVE----WmagGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLrIADFGAAARlaS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSRQALTLQdwaaqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDmvfqkgdsvALAVQNQL 253
Cdd:cd06630 157 KGTGAGEFQGQLLG-------TIAFMAPEVLRGEQY---GRSCDVWSVGCVIIEMATAKPPWN---------AEKISNHL 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 254 SI----------PQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06630 218 ALifkiasattpPPIPEHlSPGLRDVTLRCLELQPEDRPPARELLK 263
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
15-291 1.01e-12

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: 66.83  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDL--VEGLHDGHFYALKRILCHEQQDREEAQREADMHrlfnHPNILRLVAYCLRERgakh 92
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYgkWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLS----HEKLVQLYGVCTKQR---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLWNeieRLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnq 172
Cdd:cd05113  73 PIFIITEYMANGCLLN---YLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 acihvegSRQALTLQ--DWAAQRCTISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAV 249
Cdd:cd05113 147 -------SRYVLDDEytSSVGSKFPVRWSPPEVL---MYSKFSSKSDVWAFGVLMWEVYsLGKMPYERF--TNSETVEHV 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 250 QNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05113 215 SQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNIL 256
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
64-280 1.25e-12

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 66.57  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRLvaYCLRErgAKHEAWLLLPFFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKG 143
Cdd:cd14201  54 KEIKILKELQHENIVAL--YDVQE--MPNSVFLVMEYCNGGDL---ADYLQAKGT-LSEDTIRVFLQQIAAAMRILHSKG 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 144 YAHRDLKPTNILLGDEGQPvlmdlgSMNQACIHVE----GSRQALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDV 218
Cdd:cd14201 126 IIHRDLKPQNILLSYASRK------KSSVSGIRIKiadfGFARYLQSNMMAATLCgSPMYMAPEVIMSQHY---DAKADL 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 219 WSLGCVLYAMMFGEGPydmvFQKGDSVALAV---QNQLSIPQSPRHSSA-LRQLLNSMMTVDPHQR 280
Cdd:cd14201 197 WSIGTVIYQCLVGKPP----FQANSPQDLRMfyeKNKNLQPSIPRETSPyLADLLLGLLQRNQKDR 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
141-280 1.29e-12

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 66.96  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 141 AKGYAH------RDLKPTNILLGDEGQPVLMDLGsmnqACihvegsRQALTLQDWAAQRC-TISYRAPELFSVQSHcviD 213
Cdd:cd05575 108 ALGYLHslniiyRDLKPENILLDSQGHVVLTDFG----LC------KEGIEPSDTTSTFCgTPEYLAPEVLRKQPY---D 174
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 214 ERTDVWSLGCVLYAMMFGEGP---------YDMVFQKgdsvalavqnQLSIPqsPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05575 175 RTVDWWCLGAVLYEMLYGLPPfysrdtaemYDNILHK----------PLRLR--TNVSPSARDLLEGLLQKDRTKR 238
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
17-235 1.31e-12

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 66.40  E-value: 1.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSY-VDLVEGLHDGHFYALKRILcHEQQDREEAQREADMHRLFNHPNILRLVAyclrergakheAW 95
Cdd:cd14112   2 TGRFSFGSEIFRGRFSViVKAVDSTTETDAHCAVKIF-EVSDEASEAVREFESLRTLQHENVQRLIA-----------AF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPF--FKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGSMN 171
Cdd:cd14112  70 KPSNFayLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQvkLVDFGRAQ 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 172 QacIHVEGSRQALTLQDWAaqrctisyrAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14112 150 K--VSKLGKVPVDGDTDWA---------SPEF--HNPETPITVQSDIWGLGVLTFCLLSGFHPF 200
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
19-296 1.34e-12

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 66.19  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE-AQREADMHRLFNHPNILRLVayclRERGAKHEAWLL 97
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHmIENEVAILRRVKHPNIVQLI----EEYDTDTELYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqpvlmdLGSMNqacihv 177
Cdd:cd14095  77 MELVKGGDLFDAIT----SSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHE------DGSKS------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egsrqaLTLQDWA-AQRC---------TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYdmVFQKGDSVAL 247
Cdd:cd14095 141 ------LKLADFGlATEVkeplftvcgTPTYVAPEILAETGYGL---KVDIWAAGVITYILLCGFPPF--RSPDRDQEEL 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 248 ---AVQNQLSIPqSPRH---SSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14095 210 fdlILAGEFEFL-SPYWdniSDSAKDLISRMLVVDPEKR------YSAGQVLDHP 257
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
26-239 1.34e-12

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: 66.36  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEG-LHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLVAYCLrergAKHEAWLLLPFFKR 103
Cdd:cd14664   1 IGRGGAGTV--YKGvMPNGTLVAVKRLKGEGTQGGDHGfQAEIQTLGMIRHRNIVRLRGYCS----NPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIH---AKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGS 180
Cdd:cd14664  75 GSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFG---LAKLMDDKD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 181 RQALTlqdwaAQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDMVF 239
Cdd:cd14664 152 SHVMS-----SVAGSYGYIAPEYAYTGK---VSEKSDVYSYGVVLLELITGKRPFDEAF 202
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
18-283 1.34e-12

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: 66.38  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLFNHPNILRLvayclrergakHEAWLL 97
Cdd:cd14111   3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAK-IVPYQAEEKQGVLQEYEILKSLHHERIMAL-----------HEAYIT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFF--------KRGTLWNEIERLKdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS 169
Cdd:cd14111  71 PRYLvliaefcsGKELLHSLIDRFR-----YSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 170 MNqacihvegSRQALTLQDWAAQRCTISYRAPELFSVQshcVIDERTDVWSLGCVLYAMMFGEGP-YDMVFQKGDSVALA 248
Cdd:cd14111 146 AQ--------SFNPLSLRQLGRRTGTLEYMAPEMVKGE---PVGPPADIWSIGVLTYIMLSGRSPfEDQDPQETEAKILV 214
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 249 VQNQlSIPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14111 215 AKFD-AFKLYPNVSQSASLFLKKVLSSYPWSRPTT 248
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
26-235 1.42e-12

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 66.85  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADMHRLFNHPNILRLvAYCLRergAKHEAWLLLPFFK 102
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLdkkRLKKKSGEKMALLEKEILEKVNSPFIVSL-AYAFE---TKTHLCLVMSLMN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQ 182
Cdd:cd05607  86 GGDLKYHIYNVGERG--IEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLG----LAVEVKEGKP 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 183 altlqdwAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05607 160 -------ITQRAgTNGYMAPEILKEESY---SYPVDWFAMGCSIYEMVAGRTPF 203
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
23-289 1.53e-12

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: 66.63  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDR-EEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd06641   9 LEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLKDT----KLWIIMEYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERlkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihvegsr 181
Cdd:cd06641  85 GGGSALDLLEP-----GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 qaltLQDWAAQR----CTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVfQKGDSVALAVQNQLSIPQ 257
Cdd:cd06641 151 ----LTDTQIKRn*fvGTPFWMAPEVIKQSAY---DSKADIWSLGITAIELARGEPPHSEL-HPMKVLFLIPKNNPPTLE 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 258 SpRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06641 223 G-NYSKPLKEFVEACLNKEPSFRPTAKELLKH 253
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
120-231 1.56e-12

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 66.99  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaciHVEGSRQALTLQDWaaqrctisYR 199
Cdd:cd07877 117 LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR----HTDDEMTGYVATRW--------YR 184
                        90       100       110
                ....*....|....*....|....*....|..
gi 46577677 200 APELFSVQSHcvIDERTDVWSLGCVLYAMMFG 231
Cdd:cd07877 185 APEIMLNWMH--YNQTVDIWSVGCIMAELLTG 214
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
26-235 1.59e-12

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 66.14  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLvaYCLRErgAKHEAWLLLPFFKRGT 105
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQL--YDAFE--SKTNLTLIMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE--GQPVLMDLGsmnqacihvegsrqa 183
Cdd:cd14192  88 LF---DRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFG--------------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 184 LTLQDWAAQRCTISYRAPELFS--VQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14192 150 LARRYKPREKLKVNFGTPEFLApeVVNYDFVSFPTDMWSVGVITYMLLSGLSPF 203
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
18-296 1.61e-12

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 66.93  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRiLCHEQQDREEAQ---READMHRLFNHPNILRLV-AYCLRERGAK-H 92
Cdd:cd07851  15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKK-LSRPFQSAIHAKrtyRELRLLKHMKHENVIGLLdVFTPASSLEDfQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFkrGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnq 172
Cdd:cd07851  94 DVYLVTHLM--GADLNNIVKCQK----LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL--- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 acihvegSRQALT-LQDWAAQRCtisYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGE------------------- 232
Cdd:cd07851 165 -------ARHTDDeMTGYVATRW---YRAPEIMLNWMH--YNQTVDIWSVGCIMAELLTGKtlfpgsdhidqlkrimnlv 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 233 -GPYDMVFQKGDSValAVQNQL-SIPQSPR---------HSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07851 233 gTPDEELLKKISSE--SARNYIqSLPQMPKkdfkevfsgANPLAIDLLEKMLVLDPDKR------ITAAEALAHP 299
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-280 1.73e-12

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: 66.48  E-value: 1.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKriLCHEQ---QDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFK 102
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIK--SCRLElsvKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVNDVPLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGtlwNEIERLKDKGNF---LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV---LMDLG---SMNQA 173
Cdd:cd14039  79 SG---GDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIvhkIIDLGyakDLDQG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 --CIHVEGsrqaltlqdwaaqrcTISYRAPELFSVQSHCVIderTDVWSLGCVLYAMMFGEGPY----------DMVFQK 241
Cdd:cd14039 156 slCTSFVG---------------TLQYLAPELFENKSYTVT---VDYWSFGTMVFECIAGFRPFlhnlqpftwhEKIKKK 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 46577677 242 GDSVALAVQN-------QLSIPQSPRHSS----ALRQLLNSMMTVDPHQR 280
Cdd:cd14039 218 DPKHIFAVEEmngevrfSTHLPQPNNLCSlivePMEGWLQLMLNWDPVQR 267
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
64-228 1.89e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 67.18  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   64 READMHRLFNHPNILRLV-AY------CLRERGAKHEawlllpffkrgtLWNEIERLKDkgnfLTEDQILWLLLGICRGL 136
Cdd:PHA03207 135 REIDILKTISHRAIINLIhAYrwkstvCMVMPKYKCD------------LFTYVDRSGP----LPLEQAITIQRRLLEAL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  137 EAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEgsrqalTLQD--WAAqrcTISYRAPELFSVQSHCVide 214
Cdd:PHA03207 199 AYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPD------TPQCygWSG---TLETNSPELLALDPYCA--- 266
                        170
                 ....*....|....
gi 46577677  215 RTDVWSLGCVLYAM 228
Cdd:PHA03207 267 KTDIWSAGLVLFEM 280
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
59-226 1.94e-12

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: 66.31  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  59 REEAQ--READMHR--LFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICR 134
Cdd:cd14142  39 RDEKSwfRETEIYNtvLLRHENILGFIASDMTSRNSCTQLWLITHYHENGSLYDYLQR-----TTLDHQEMLRLALSAAS 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAKGY--------AHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGSRQAltlqDWAAQR--CTISYRAPELF 204
Cdd:cd14142 114 GLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADLG---LAVTHSQETNQL----DVGNNPrvGTKRYMAPEVL 186
                       170       180
                ....*....|....*....|....*
gi 46577677 205 --SVQSHCVID-ERTDVWSLGCVLY 226
Cdd:cd14142 187 deTINTDCFESyKRVDIYAFGLVLW 211
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
57-241 2.12e-12

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: 66.20  E-value: 2.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRL--FNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICR 134
Cdd:cd14053  29 QEKQSWLTEREIYSLpgMKHENILQFIGAEKHGESLEAEYWLITEFHERGSLCDYL-----KGNVISWNELCKIAESMAR 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIH------AKGY----AHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRQALTLqdwaAQRCTISYRAPEL- 203
Cdd:cd14053 104 GLAYLHedipatNGGHkpsiAHRDFKSKNVLLKSDLTACIADFGL---ALKFEPGKSCGDTH----GQVGTRRYMAPEVl 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 46577677 204 -----FSVQSHCvideRTDVWSLGCVLYAMM----FGEGP---YDMVFQK 241
Cdd:cd14053 177 egainFTRDAFL----RIDMYAMGLVLWELLsrcsVHDGPvdeYQLPFEE 222
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
19-283 2.14e-12

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: 65.91  E-value: 2.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHD-GHFYALKRILCH--EQQDREEAQREADMHR---LFNHPNILRLVayclrergakh 92
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVSERVPtGKVYAVKKLKPNyaGAKDRLRRLEEVSILReltLDGHDNIVQLI----------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAW-------LLLPFFKRGTLWNEIERLKDKGNFltEDQILW-LLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVL 164
Cdd:cd14052  70 DSWeyhghlyIQTELCENGSLDVFLSELGLLGRL--DEFRVWkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 165 MDLGsMNQAC-----IHVEGSRQaltlqdwaaqrctisYRAPElfsVQSHCVIDERTDVWSLGCVLYammfgEGPYDMV- 238
Cdd:cd14052 148 GDFG-MATVWplirgIEREGDRE---------------YIAPE---ILSEHMYDKPADIFSLGLILL-----EAAANVVl 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 239 ------FQKGDSVALAVQNQLSI-----------------PQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14052 204 pdngdaWQKLRSGDLSDAPRLSStdlhsasspssnpppdpPNMPILSGSLDRVVRWMLSPEPDRRPTA 271
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
20-231 2.45e-12

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: 65.96  E-value: 2.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRL--VAYClrergakhEAWL 96
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhLDAEEGTPSTAIREISLMKELKHENIVRLhdVIHT--------ENKL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPF-FKRGTLWNEIERLKDKG--NFLTEDQILWLLLgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQA 173
Cdd:cd07836  74 MLVFeYMDKDLKKYMDTHGVRGalDPNTVKSFTYQLL---KGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 174 CIHVEG-SRQALTLqdWaaqrctisYRAPELfsvqshcVIDERT-----DVWSLGCVLYAMMFG 231
Cdd:cd07836 151 GIPVNTfSNEVVTL--W--------YRAPDV-------LLGSRTystsiDIWSVGCIMAEMITG 197
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
24-291 2.48e-12

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: 65.66  E-value: 2.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSyvDLVEGLHDGHFYALKRILCH--EQQDREEAQREADMHrlfnHPNILRLVAYCLrergaKHEAWLLLPFF 101
Cdd:cd05083  12 EIIGEGEFG--AVLQGEYMGQKVAVKNIKCDvtAQAFLEETAVMTKLQ----HKNLVRLLGVIL-----HNGLYIVMELM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNeieRLKDKGNFLTED-QILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIHVEGS 180
Cdd:cd05083  81 SKGNLVN---FLRSRGRALVPViQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG------LAKVGS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTlqdwaaQRCTISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPYDMVFQKGDSVALAVQNQLSIPQS- 258
Cdd:cd05083 152 MGVDN------SRLPVKWTAPEAL---KNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVKEVKEAVEKGYRMEPPEGc 222
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 259 --PRHSsalrqLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05083 223 ppDVYS-----IMTSCWEAEPGKRPSFKKLREKLE 252
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
23-244 2.50e-12

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: 65.77  E-value: 2.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILChEQQDR---EEAQREADMHRLFNHPNILRL--VAYClrergakhEAWLL 97
Cdd:cd07835   4 LEKIGEGTYGVVYKARDKLTGEIVALKKIRL-ETEDEgvpSTAIREISLLKELNHPNIVRLldVVHS--------ENKLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPF-FKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIH 176
Cdd:cd07835  75 LVFeFLDLDLKKYMDSSPLTG--LDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVP 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 177 VEG-SRQALTLqdWaaqrctisYRAPE--LFSVQ-SHCVidertDVWSLGCVlyammFGEgpydMVFQK----GDS 244
Cdd:cd07835 153 VRTyTHEVVTL--W--------YRAPEilLGSKHySTPV-----DIWSVGCI-----FAE----MVTRRplfpGDS 204
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
23-294 2.81e-12

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 65.42  E-value: 2.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVdlVEGLHDGHFyALKrILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRergakheawlllP 99
Cdd:cd14150   5 LKRIGTGSFGTV--FRGKWHGDV-AVK-ILKVTEPTPEQLQafkNEMQVLRKTRHVNILLFMGFMTR------------P 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICR----GLEAIHAKGYAHRDLKPTNILLgDEGQPVlmDLGSMNQACI 175
Cdd:cd14150  69 NFAIITQWCEGSSLYRHLHVTETRFDTMQLIDVARqtaqGMDYLHAKNIIHRDLKSNNIFL-HEGLTV--KIGDFGLATV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 176 HVEGSRQaltlQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSI 255
Cdd:cd14150 146 KTRWSGS----QQVEQPSGSILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSP 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 256 PQSPRHSS---ALRQLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd14150 222 DLSKLSSNcpkAMKRLLIDCLKFKREERPLFPQILVSIELLQ 263
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-280 2.87e-12

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 65.84  E-value: 2.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLVAYclreRGAKHEAWL 96
Cdd:cd14168  10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSiENEIAVLRKIKHENIVALEDI----YESPNHLYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWneiERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL---GDEGQPVLMDLGSMNqa 173
Cdd:cd14168  86 VMQLVSGGELF---DRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 cihVEGSrqaltlQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMVFQKGDSVALAVQN 251
Cdd:cd14168 160 ---MEGK------GDVMSTACgTPGYVAPEVLAQKPY---SKAVDCWSIGVIAYILLCGYPPfYDENDSKLFEQILKADY 227
                       250       260
                ....*....|....*....|....*....
gi 46577677 252 QLSIPQSPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14168 228 EFDSPYWDDISDSAKDFIRNLMEKDPNKR 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
26-296 2.92e-12

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 65.25  E-value: 2.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILcHEQQDREEAQREADMHRLFNHPNILRLV-AYCLRERgakheAWLLLPFFKRG 104
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIE-TKCRGREVCESELNVLRRVRHTNIIQLIeVFETKER-----VYMVMELATGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWneiERLKDKGNFLTED--QILWLLLgicRGLEAIHAKGYAHRDLKPTNILL---GDEGQPVLMDLGSmnqacihveG 179
Cdd:cd14087  83 ELF---DRIIAKGSFTERDatRVLQMVL---DGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGL---------A 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWAAQRC-TISYRAPELFSVQSHCvidERTDVWSLGCVLYAMMFGEGPYD-----MVFQKgdsvALAVQNQL 253
Cdd:cd14087 148 STRKKGPNCLMKTTCgTPEYIAPEILLRKPYT---QSVDMWAVGVIAYILLSGTMPFDddnrtRLYRQ----ILRAKYSY 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 46577677 254 SIPQSPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14087 221 SGEPWPSVSNLAKDFIDRLLTVNPGER------LSATQALKHP 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
26-280 3.01e-12

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: 66.18  E-value: 3.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKrILCHE---QQDrEEAQREADMHRLFN--HPNILRL-VAYCLRERgakheAWLLLP 99
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMK-ILRKEviiAKD-EVAHTVTESRVLQNtrHPFLTALkYAFQTHDR-----LCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIHVEG 179
Cdd:cd05595  76 YANGGELFFHLSRER----VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG------LCKEG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQkgdsvaLAVQNQLS 254
Cdd:cd05595 146 ITDGATMKTFCG---TPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFynqdhERLFE------LILMEEIR 213
                       250       260
                ....*....|....*....|....*.
gi 46577677 255 IPQSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05595 214 FPRT--LSPEAKSLLAGLLKKDPKQR 237
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
24-280 3.10e-12

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 66.08  E-value: 3.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRL-FNHPNILRLVaYCLRergAKHEAWLLLP 99
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAvkvLKKDVILQDDDVECTMTEKRILSLaRNHPFLTQLY-CCFQ---TPDRLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacihvEG 179
Cdd:cd05590  77 FVNGGDLMFHIQ----KSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK------EG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWAAqrcTISYRAPELFSVQSHCVIderTDVWSLGCVLYAMMFGEGPYDMvfQKGDSVALAVQNQLSIPQSP 259
Cdd:cd05590 147 IFNGKTTSTFCG---TPDYIAPEILQEMLYGPS---VDWWAMGVLLYEMLCGHAPFEA--ENEDDLFEAILNDEVVYPTW 218
                       250       260
                ....*....|....*....|.
gi 46577677 260 RHSSALrQLLNSMMTVDPHQR 280
Cdd:cd05590 219 LSQDAV-DILKAFMTKNPTMR 238
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
23-280 3.12e-12

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: 65.60  E-value: 3.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREE------AQREADMHRLFNHPNILRLVAYCLRERgakhEAWL 96
Cdd:cd07860   5 VEKIGEGTYGVVYKARNKLTGEVVALKKI----RLDTETegvpstAIREISLLKELNHPNIVKLLDVIHTEN----KLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFfkrgtLWNEIERLKD--KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQAC 174
Cdd:cd07860  77 VFEF-----LHQDLKKFMDasALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFG-LARAF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 ihvegsrqALTLQDWAAQRCTISYRAPELF---SVQSHCVidertDVWSLGCVLYAMMF------GEGPYDMVFQ----- 240
Cdd:cd07860 151 --------GVPVRTYTHEVVTLWYRAPEILlgcKYYSTAV-----DIWSLGCIFAEMVTrralfpGDSEIDQLFRifrtl 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 241 -KGDSVALAVQNQL-----SIPQSPRH---------SSALRQLLNSMMTVDPHQR 280
Cdd:cd07860 218 gTPDEVVWPGVTSMpdykpSFPKWARQdfskvvpplDEDGRDLLSQMLHYDPNKR 272
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
22-280 3.14e-12

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 66.18  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRergAKHEAWLLL 98
Cdd:cd05616   4 FLMVLGKGSFGKVMLAERKGTDELYAvkiLKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQ---TMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLkdkGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacihvE 178
Cdd:cd05616  81 EYVNGGDLMYHIQQV---GRF-KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK------E 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgdsvalAVQNQL 253
Cdd:cd05616 151 NIWDGVTTKTFCG---TPDYIAPEIIAYQPY---GKSVDWWAFGVLLYEMLAGQAPFegedeDELFQS------IMEHNV 218
                       250       260
                ....*....|....*....|....*..
gi 46577677 254 SIPQSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05616 219 AYPKS--MSKEAVAICKGLMTKHPGKR 243
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
23-289 3.38e-12

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: 65.46  E-value: 3.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSyvDLVEGL--HDGHFYALKRILCHEQQDR-EEAQREADMHRLFNHPNILRLVAYCLRerGAKheAWLLLP 99
Cdd:cd06642   9 LERIGKGSFG--EVYKGIdnRTKEVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYITRYYGSYLK--GTK--LWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihveg 179
Cdd:cd06642  83 YLGGGSALDLL-----KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQ------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 srqaltLQDWAAQRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqkgdSVALAVQNQLSI 255
Cdd:cd06642 151 ------LTDTQIKRNTFVgtpfWMAPEVIKQSAY---DFKADIWSLGITAIELAKGEPPN--------SDLHPMRVLFLI 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 256 PQ-SP-----RHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06642 214 PKnSPptlegQHSKPFKEFVEACLNKDPRFRPTAKELLKH 253
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
63-237 3.50e-12

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 65.73  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  63 QREADMHRLFNHPNILRLVAYCLrergAKHEAWLLLPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAK 142
Cdd:cd08227  47 QGELHVSKLFNHPNIVPYRATFI----ADNELWVVTSFMAYGSAKDLICTHFMDG--MSELAIAYILQGVLKALDYIHHM 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 143 GYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQrcTISYRAPELFSvQSHCVIDERTDVWSLG 222
Cdd:cd08227 121 GYVHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLRVVHDFPKYSVK--VLPWLSPEVLQ-QNLQGYDAKSDIYSVG 197
                       170
                ....*....|....*.
gi 46577677 223 CVLYAMMFGEGPY-DM 237
Cdd:cd08227 198 ITACELANGHVPFkDM 213
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
18-235 3.58e-12

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 65.40  E-value: 3.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYclreRGAKHEAWLL 97
Cdd:cd14166   3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDI----YESTTHYYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWneiERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTN-----------ILLGDEGQPVLMD 166
Cdd:cd14166  79 MQLVSGGELF---DRILERGVY-TEKDASRVINQVLSAVKYLHENGIVHRDLKPENllyltpdenskIMITDFGLSKMEQ 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 167 LGSMNQACihvegsrqaltlqdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14166 155 NGIMSTAC-------------------GTPGYVAPEVLAQKPY---SKAVDCWSIGVITYILLCGYPPF 201
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
22-280 3.62e-12

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 66.21  E-value: 3.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADM-HRLFNHPNILRLVAyCLRergAKHEAWLL 97
Cdd:cd05618  24 LLRVIGRGSYAKVLLVRLKKTERIYAMKVVkkeLVNDDEDIDWVQTEKHVfEQASNHPFLVGLHS-CFQ---TESRLFFV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihv 177
Cdd:cd05618 100 IEYVNGGDLMFHMQRQRK----LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGM-------- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egSRQALTLQDWAAQRC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPYDMVFQKGDS--------VALA 248
Cdd:cd05618 168 --CKEGLRPGDTTSTFCgTPNYIAPEILRGEDYGF---SVDWWALGVLMFEMMAGRSPFDIVGSSDNPdqntedylFQVI 242
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 249 VQNQLSIPQSPRHSSAlrQLLNSMMTVDPHQR 280
Cdd:cd05618 243 LEKQIRIPRSLSVKAA--SVLKSFLNKDPKER 272
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
54-293 3.82e-12

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: 65.27  E-value: 3.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLWNEIErlKDKGNFlTEDQILWLLLGIC 133
Cdd:cd05066  44 YTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSK----PVMIVTEYMENGSLDAFLR--KHDGQF-TVIQLVGMLRGIA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 134 RGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN------QACIHVEGSRQALTlqdWAAQRcTISYRApelFSVQ 207
Cdd:cd05066 117 SGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvleddpEAAYTTRGGKIPIR---WTAPE-AIAYRK---FTSA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 208 ShcvidertDVWSLGCVLYAMM-FGEGPY-DMVFQkgdSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPL 285
Cdd:cd05066 190 S--------DVWSYGIVMWEVMsYGERPYwEMSNQ---DVIKAIEEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQ 258

                ....*...
gi 46577677 286 LLSQLEAL 293
Cdd:cd05066 259 IVSILDKL 266
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-274 4.14e-12

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 66.18  E-value: 4.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVaYCLRErgaKHEAWL 96
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQLF-YAFQD---DRYLYM 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIER--LKDK-GNFLTEDQILwlllgicrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqa 173
Cdd:cd05622 151 VMEYMPGGDLVNLMSNydVPEKwARFYTAEVVL--------ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT---- 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVegSRQALTLQDWAAQrcTISYRAPELFSVQ-SHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGD-SVALAVQN 251
Cdd:cd05622 219 CMKM--NKEGMVRCDTAVG--TPDYISPEVLKSQgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTySKIMNHKN 294
                       250       260
                ....*....|....*....|...
gi 46577677 252 QLSIPQSPRHSSALRQLLNSMMT 274
Cdd:cd05622 295 SLTFPDDNDISKEAKNLICAFLT 317
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
11-289 4.39e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 65.47  E-value: 4.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  11 GTVIIDNKRYL-------FIQKLGEGGFSYVDLVEGLHDGHFYALKRIlcHEQQDREEAQR---EAD-MHRLFNHPNILR 79
Cdd:cd06618   1 GYLTIDGKKYKadlndleNLGEIGSGTCGQVYKMRHKKTGHVMAVKQM--RRSGNKEENKRilmDLDvVLKSHDCPYIVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  80 LVAYCLRErgakHEAWLLLPffKRGTLwneIERLKDK-GNFLTEDQILWLLLGICRGLEAIHAK-GYAHRDLKPTNILLG 157
Cdd:cd06618  79 CYGYFITD----SDVFICME--LMSTC---LDKLLKRiQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 158 DEGQPVLMDLGSMNQACIHVEGSRQAltlqdwaaqRCTiSYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDM 237
Cdd:cd06618 150 ESGNVKLCDFGISGRLVDSKAKTRSA---------GCA-AYMAPERIDPPDNPKYDIRADVWSLGISLVELATGQFPYRN 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 238 VfqKGDSVALAVQNQLSIPQSPRH---SSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06618 220 C--KTEFEVLTKILNEEPPSLPPNegfSPDFCSFVDLCLTKDHRYRPKYRELLQH 272
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
15-287 4.45e-12

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: 65.15  E-value: 4.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD-REEAQREAD-MHRLfNHPNILRLVAYCLRERGakh 92
Cdd:cd06620   2 LKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSvRKQILRELQiLHEC-HSPYIVSFYGAFLNENN--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGY-AHRDLKPTNILLGDEGQPVLMDLGsmn 171
Cdd:cd06620  78 NIIICMEYMDCGSL----DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVHRiIHRDIKPSNILVNSKGQIKLCDFG--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qacihVEGSrqaltLQDWAAQRC--TISYRAPElfSVQSHcVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVA--- 246
Cdd:cd06620 151 -----VSGE-----LINSIADTFvgTSTYMSPE--RIQGG-KYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNgpm 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 247 --LAVQNQL------SIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06620 218 giLDLLQRIvnepppRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
20-232 5.34e-12

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 64.98  E-value: 5.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGgfSYVDLVEGLH--DGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLvayclrergakHEAwl 96
Cdd:cd07870   2 YLNLEKLGEG--SYATVYKGISriNGQLVALKVIsMKTEEGVPFTAIREASLLKGLKHANIVLL-----------HDI-- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 llpFFKRGTLWNEIERLK-DKGNFLTED-------QILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd07870  67 ---IHTKETLTFVFEYMHtDLAQYMIQHpgglhpyNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFG 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 169 SmnqacihveGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDerTDVWSLGCVLYAMMFGE 232
Cdd:cd07870 144 L---------ARAKSIPSQTYSSEVVTLWYRPPDVLLGATDYSSA--LDIWGAGCIFIEMLQGQ 196
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
63-298 5.89e-12

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 65.05  E-value: 5.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  63 QREADMHRLFNHPNILRLVAYCLRERGAKHEAWLllpffKRGTLWNEIERLKDKGNFLtedQILWLLLGICRGLEAIHAK 142
Cdd:cd14149  56 RNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWC-----EGSSLYKHLHVQETKFQMF---QLIDIARQTAQGMDYLHAK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 143 GYAHRDLKPTNILLgDEGQPVlmDLGSMNQACIHVE--GSRQALTLQDwaaqrcTISYRAPELFSVQSHCVIDERTDVWS 220
Cdd:cd14149 128 NIIHRDMKSNNIFL-HEGLTV--KIGDFGLATVKSRwsGSQQVEQPTG------SILWMAPEVIRMQDNNPFSFQSDVYS 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 221 LGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSS---ALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPA 297
Cdd:cd14149 199 YGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNcpkAMKRLVADCIKKVKEERPLFPQILSSIELLQHSL 278

                .
gi 46577677 298 P 298
Cdd:cd14149 279 P 279
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
15-291 6.45e-12

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: 64.35  E-value: 6.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSyvDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEA 94
Cdd:cd05068   5 IDRKSLKLLRKLGSGQFG--EVWEGLWNNTTPVAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLE----EPI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaC 174
Cdd:cd05068  79 YIITELMKHGSL---LEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLAR--V 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTlqdwaAQRCTISYRAPEL-----FSVQShcvidertDVWSLGCVLYAMM-FGEGPY-DMVfqkGDSVAL 247
Cdd:cd05068 154 IKVEDEYEARE-----GAKFPIKWTAPEAanynrFSIKS--------DVWSFGILLTEIVtYGRIPYpGMT---NAEVLQ 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 46577677 248 AVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05068 218 QVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLE 261
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
19-281 6.51e-12

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: 64.84  E-value: 6.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYL--F--IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDRE--EAQREADMHRLFNHPNIlrlVAYclrergakH 92
Cdd:cd14049   3 RYLneFeeIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDcmKVLREVKVLAGLQHPNI---VGY--------H 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWL----LLPFFK----RGTLWNEIERLKDKGNFLTE----------DQILWLLLGICRGLEAIHAKGYAHRDLKPTNI 154
Cdd:cd14049  72 TAWMehvqLMLYIQmqlcELSLWDWIVERNKRPCEEEFksapytpvdvDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 155 LLgdEGQPVLMDLGSMNQACihvegSRQALTLQDWAAQRC-----------TISYRAPELFSvQSHCviDERTDVWSLGC 223
Cdd:cd14049 152 FL--HGSDIHVRIGDFGLAC-----PDILQDGNDSTTMSRlnglthtsgvgTCLYAAPEQLE-GSHY--DFKSDMYSIGV 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 224 VLYAMMFgegPYDMVFQKGDsVALAVQNQlSIPQS-PRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14049 222 ILLELFQ---PFGTEMERAE-VLTQLRNG-QIPKSlCKRWPVQAKYIKLLTSTEPSERP 275
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
23-235 6.81e-12

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: 64.66  E-value: 6.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLLLPFFK 102
Cdd:cd06643  10 VGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYE----NNLWILIEFCA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTL---WNEIERLkdkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihveG 179
Cdd:cd06643  86 GGAVdavMLELERP------LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGV---------S 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 180 SRQALTLQDWAAQRCTISYRAPELFSVQSHC--VIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd06643 151 AKNTRTLQRRDSFIGTPYWMAPEVVMCETSKdrPYDYKADVWSLGVTLIEMAQIEPPH 208
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
47-245 7.44e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 64.71  E-value: 7.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  47 ALKRILCHEQQDREEAQREADMHRLfNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLwneierlKD--KGNFLTEDQ 124
Cdd:cd14055  28 AVKIFPYEEYASWKNEKDIFTDASL-KHENILQFLTAEERGVGLDRQYWLITAYHENGSL-------QDylTRHILSWED 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 125 ILWLLLGICRGLEAIHAKGY---------AHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSrqaLTLQDWA--AQR 193
Cdd:cd14055 100 LCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDGTCVLADFG----LALRLDPS---LSVDELAnsGQV 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 194 CTISYRAPELFSVQSHCVIDE---RTDVWSLGCVLYAMM-----FGE-GPYDMVFqkGDSV 245
Cdd:cd14055 173 GTARYMAPEALESRVNLEDLEsfkQIDVYSMALVLWEMAsrceaSGEvKPYELPF--GSKV 231
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
24-235 7.54e-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: 64.21  E-value: 7.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQ------DREEAQREADMHRLFNHPNILRLvaYCLRERgaKHEAWLL 97
Cdd:cd14196  11 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRasrrgvSREEIEREVSILRQVLHPNIITL--HDVYEN--RTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV----LMDLGSMNQA 173
Cdd:cd14196  87 LELVSGGELFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphikLIDFGLAHEI 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 174 CIHVEgsrqaltlqdWAAQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14196 163 EDGVE----------FKNIFGTPEFVAPEIVNYEP---LGLEADMWSIGVITYILLSGASPF 211
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
20-284 7.80e-12

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: 63.95  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDR---EEAQREADMHRLFNHPNILRLvaYCLRErgAKHEAWL 96
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIK-IIDKSQLDEenlKKIYREVQIMKMLNHPHIIKL--YQVME--TKDMLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacIH 176
Cdd:cd14071  77 VTEYASNG----EIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSN---FF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSrqalTLQDWAAqrcTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQLS-- 254
Cdd:cd14071 150 KPGE----LLKTWCG---SPPYAAPEVFEGKEY--EGPQLDIWSLGVVLYVLVCGALPFD-----GSTLQTLRDRVLSgr 215
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 255 --IPQSprHSSALRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14071 216 frIPFF--MSTDCEHLIRRMLVLDPSKRLTIE 245
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
18-280 8.48e-12

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: 64.11  E-value: 8.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVdlVEGLH--DGHFYALKRIlcheqqDREEA--------QREADMHRLFNHPNILRLV-AYCLR 86
Cdd:cd14097   1 KIYTFGRKLGQGSFGVV--IEATHkeTQTKWAIKKI------NREKAgssavkllEREVDILKHVNHAHIIHLEeVFETP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  87 ERgakheAWLLLPFFKRGtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG----DEGQP 162
Cdd:cd14097  73 KR-----MYLVMELCEDG----ELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssiiDNNDK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 163 VLMDLGSMNQACIHVEGSRQALTlqdwaaQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP------- 234
Cdd:cd14097 144 LNIKVTDFGLSVQKYGLGEDMLQ------ETCgTPIYMAPEVISAHGY---SQQCDIWSIGVIMYMLLCGEPPfvaksee 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 235 --YDMVFQKGDSVALAVQNQLsipqsprhSSALRQLLNSMMTVDPHQR 280
Cdd:cd14097 215 klFEEIRKGDLTFTQSVWQSV--------SDAAKNVLQQLLKVDPAHR 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
24-296 8.90e-12

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: 64.27  E-value: 8.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD------REEAQREADMHRLFNHPNILRLvaYCLRERgaKHEAWLL 97
Cdd:cd14194  11 EELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITL--HEVYEN--KTDVILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWneiERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP----VLMDLGSMNQA 173
Cdd:cd14194  87 LELVAGGELF---DFLAEKES-LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPkpriKIIDFGLAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHvegsrqaltlQDWAAQRCTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVA--LAVQN 251
Cdd:cd14194 163 DFG----------NEFKNIFGTPEFVAPEIVNYEP---LGLEADMWSIGVITYILLSGASPF-LGDTKQETLAnvSAVNY 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 252 QLSiPQSPRHSSAL-RQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14194 229 EFE-DEYFSNTSALaKDFIRRLLVKDPKKR------MTIQDSLQHP 267
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
16-228 1.07e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 64.31  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCheQQDRE----EAQREADMHRLFNHPNILRLVAYC----LRE 87
Cdd:cd07865  10 EVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLM--ENEKEgfpiTALREIKILQLLKHENVVNLIEICrtkaTPY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  88 RGAKHEAWLLLPFFKR---GTLWNEIERLkdkgnflTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVL 164
Cdd:cd07865  88 NRYKGSIYLVFEFCEHdlaGLLSNKNVKF-------TLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 165 MDLGSMNQACIHVEGSRQALTlqdwaAQRCTISYRAPELfsvqshcVIDER-----TDVWSLGCVLYAM 228
Cdd:cd07865 161 ADFGLARAFSLAKNSQPNRYT-----NRVVTLWYRPPEL-------LLGERdygppIDMWGAGCIMAEM 217
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
23-235 1.08e-11

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 64.69  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA---QREADMHRLFNHPNILRLVaYCLRErgaKHEAWLLLP 99
Cdd:cd05627   7 LKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVahiRAERDILVEADGAWVVKMF-YSFQD---KRNLYLIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG----------- 168
Cdd:cd05627  83 FLPGG----DMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGlctglkkahrt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACIH----------VEGSRQALTlqdWAAQRCTISYR--------APELFSVQSHcviDERTDVWSLGCVLYAMMF 230
Cdd:cd05627 159 EFYRNLTHnppsdfsfqnMNSKRKAET---WKKNRRQLAYStvgtpdyiAPEVFMQTGY---NKLCDWWSLGVIMYEMLI 232

                ....*
gi 46577677 231 GEGPY 235
Cdd:cd05627 233 GYPPF 237
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
15-280 1.18e-11

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 64.63  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKR---YLFIQKLGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRer 88
Cdd:cd05615   4 LDRVRltdFNFLMVLGKGSFGKVMLAERKGSDELYAikiLKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQ-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 gAKHEAWLLLPFFKRGTLWNEIERLkdkGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd05615  82 -TVDRLYFVMEYVNGGDLMYHIQQV---GKF-KEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACIhvegsrQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgd 243
Cdd:cd05615 157 MCKEHMV------EGVTTRTFCG---TPDYIAPEIIAYQPY---GRSVDWWAYGVLLYEMLAGQPPFdgedeDELFQS-- 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 244 svalAVQNQLSIPQSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05615 223 ----IMEHNVSYPKS--LSKEAVSICKGLMTKHPAKR 253
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
24-293 1.22e-11

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 63.93  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVdlveglHDGHFYA-----LKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLll 98
Cdd:cd14151  14 QRIGSGSFGTV------YKGKWHGdvavkMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWC-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 pffKRGTLWNEIERLKDKGNFLtedQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVE 178
Cdd:cd14151  86 ---EGSSLYHHLHIIETKFEMI---KLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFG-LATVKSRWS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQALTLQDwaaqrcTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQS 258
Cdd:cd14151 159 GSHQFEQLSG------SILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLS 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 46577677 259 PRHSS---ALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14151 233 KVRSNcpkAMKRLMAECLKKKRDERPLFPQILASIELL 270
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
55-291 1.29e-11

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: 63.64  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  55 EQQDREEAQREADMHRLFNHPNILRLVAYClRErgaKHEAWLLLPFFKRGTL--WNEIERLKDKGNF---LTEDQILWLL 129
Cdd:cd05046  48 DENLQSEFRRELDMFRKLSHKNVVRLLGLC-RE---AEPHYMILEYTDLGDLkqFLRATKSKDEKLKpppLSTKQKVALC 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 LGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQALTLQDWAAQRctisYRAPElfsvqsh 209
Cdd:cd05046 124 TQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLS----LSKDVYNSEYYKLRNALIPLR----WLAPE------- 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 210 CVID----ERTDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAVQN-QLSIPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd05046 189 AVQEddfsTKSDVWSFGVLMWEVFtQGELPFYGL--SDEEVLNRLQAgKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSF 266

                ....*...
gi 46577677 284 PLLLSQLE 291
Cdd:cd05046 267 SELVSALG 274
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
26-280 1.37e-11

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 64.16  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALK-----RILchEQQDREEAQREADMHRLFN-HPNILRLVAyCLRergAKHEAWLLLP 99
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKvlkkeVII--EDDDVECTMTEKRVLALANrHPFLTGLHA-CFQ---TEDRLYFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERlkdKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMnqacihveg 179
Cdd:cd05570  77 YVNGGDLMFHIQR---ARRF-TEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFG-M--------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY-----DMVFQkgdsvalAVQNQL 253
Cdd:cd05570 143 CKEGIWGGNTTSTFCgTPDYIAPEILREQDY---GFSVDWWALGVLLYEMLAGQSPFegddeDELFE-------AILNDE 212
                       250       260
                ....*....|....*....|....*...
gi 46577677 254 siPQSPRH-SSALRQLLNSMMTVDPHQR 280
Cdd:cd05570 213 --VLYPRWlSREAVSILKGLLTKDPARR 238
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
26-235 1.37e-11

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 63.39  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLvaYCLRErgAKHEAWLLLPFFKRGT 105
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQL--YDAFE--SRNDIVLVMEYVDGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL--GDEGQPVLMDLGSmnqacihvegSRQA 183
Cdd:cd14193  88 LF---DRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGL----------ARRY 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 46577677 184 LTLQDWAAQRCTISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14193 155 KPREKLRVNFGTPEFLAPE---VVNYEFVSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
23-235 1.38e-11

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 64.49  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE---AQREADMHRLFNHPNILRLVaYCLRErgaKHEAWLLLP 99
Cdd:cd05629   6 VKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQlahVKAERDVLAESDSPWVVSLY-YSFQD---AQYLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-SMNQACIHVE 178
Cdd:cd05629  82 FLPGGDLMTMLIKY----DTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGlSTGFHKQHDS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQAL-----------------------------TLQDWAAQR--------CTISYRAPELFSVQSHcviDERTDVWSL 221
Cdd:cd05629 158 AYYQKLlqgksnknridnrnsvavdsinltmsskdQIATWKKNRrlmaystvGTPDYIAPEIFLQQGY---GQECDWWSL 234
                       250
                ....*....|....
gi 46577677 222 GCVLYAMMFGEGPY 235
Cdd:cd05629 235 GAIMFECLIGWPPF 248
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
120-292 1.44e-11

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 63.58  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVlmdlgSMNQACI--HVEGSRQALTlqdwaAQRCTIS 197
Cdd:cd13974 129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKI-----TITNFCLgkHLVSEDDLLK-----DQRGSPA 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 198 YRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGP-YDMV----FQKgdsvalAVQNQLSIPQSPRHSSALRQLLNSM 272
Cdd:cd13974 199 YISPDVLSGKPY--LGKPSDMWALGVVLFTMLYGQFPfYDSIpqelFRK------IKAAEYTIPEDGRVSENTVCLIRKL 270
                       170       180
                ....*....|....*....|
gi 46577677 273 MTVDPHQRPHIPLLLSQLEA 292
Cdd:cd13974 271 LVLNPQKRLTASEVLDSLES 290
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
23-235 1.47e-11

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 64.29  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVA--YCLRErgaKHEAWLLLPF 100
Cdd:cd05628   6 LKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKmfYSFQD---KLNLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG------------ 168
Cdd:cd05628  83 LPGG----DMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGlctglkkahrte 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 ---SMNQAC------IHVEGSRQALTlqdWAAQR--------CTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFG 231
Cdd:cd05628 159 fyrNLNHSLpsdftfQNMNSKRKAET---WKRNRrqlafstvGTPDYIAPEVFMQTGY---NKLCDWWSLGVIMYEMLIG 232

                ....
gi 46577677 232 EGPY 235
Cdd:cd05628 233 YPPF 236
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
22-280 1.48e-11

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: 64.33  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHE----QQDREEAQREADMHRLFNHPnILRLVAYCLRergAKHEAWLL 97
Cdd:cd05593  19 YLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEviiaKDEVAHTLTESRVLKNTRHP-FLTSLKYSFQ---TKDRLCFV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIHV 177
Cdd:cd05593  94 MEYVNGGELFFHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG------LCK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMVFQKgdSVALAVQNQLSIP 256
Cdd:cd05593 164 EGITDAATMKTFCG---TPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPfYNQDHEK--LFELILMEDIKFP 235
                       250       260
                ....*....|....*....|....
gi 46577677 257 QSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05593 236 RT--LSADAKSLLSGLLIKDPNKR 257
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
96-287 1.60e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 64.65  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   96 LLLPFFKRGTLWNEI-ERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:PTZ00267 142 LIMEYGSGGDLNKQIkQRLKEHLPF-QEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  175 IHVEgsrqaltlQDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVALAVQNQL 253
Cdd:PTZ00267 221 DSVS--------LDVASSFCgTPYYLAPELWERKRY---SKKADMWSLGVILYELLTLHRPF-----KGPSQREIMQQVL 284
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 46577677  254 SIPQSPRH---SSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:PTZ00267 285 YGKYDPFPcpvSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
58-283 1.73e-11

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 63.47  E-value: 1.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  58 DREEAQREADMH-RLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGL 136
Cdd:cd14172  39 DSPKARREVEHHwRASGGPHIVHILDVYENMHHGKRCLLIIMECMEGGELFSRIQERGDQA--FTEREASEIMRDIGTAI 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 137 EAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacihveGSRQALTLQDWAAQRC-TISYRAPELFSVQSHcviDER 215
Cdd:cd14172 117 QYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDF--------GFAKETTVQNALQTPCyTPYYVAPEVLGPEKY---DKS 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 216 TDVWSLGCVLYAMMFGEGPYdmVFQKGDSVALAVQNQLSI-------PQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14172 186 CDMWSLGVIMYILLCGFPPF--YSNTGQAISPGMKRRIRMgqygfpnPEWAEVSEEAKQLIRHLLKTDPTERMTI 258
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
18-231 1.78e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 63.73  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYV---------DLVeglhdghfyALKRILcHEQQDREEAQReadMHR-------LFNHPNILRLV 81
Cdd:cd07852   7 RRYEILKKLGKGAYGIVwkaidkktgEVV---------ALKKIF-DAFRNATDAQR---TFReimflqeLNDHPNIIKLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  82 AyCLRergAKHEAWLLLPF-FKRGTLWNEIerlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG 160
Cdd:cd07852  74 N-VIR---AENDKDIYLVFeYMETDLHAVI-----RANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDC 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 161 QPVLMDLG---SMNQacIHVEGSRQALTlqDWAAQRCtisYRAPELFsVQSHCViDERTDVWSLGCVLYAMMFG 231
Cdd:cd07852 145 RVKLADFGlarSLSQ--LEEDDENPVLT--DYVATRW---YRAPEIL-LGSTRY-TKGVDMWSVGCILGEMLLG 209
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
19-232 1.80e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 64.03  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI--LCHEQQDREEAQREADMHRLFNHPNILRLvayclrergaKHeawL 96
Cdd:cd07859   1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIndVFEHVSDATRILREIKLLRLLRHPDIVEI----------KH---I 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKR------------GTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVL 164
Cdd:cd07859  68 MLPPSRRefkdiyvvfelmESDLHQVIKANDD---LTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKI 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 165 MDLGsmnQACIHVEGSRQALTLQDWAAQRCtisYRAPEL----FSVQSHCVidertDVWSLGCVLYAMMFGE 232
Cdd:cd07859 145 CDFG---LARVAFNDTPTAIFWTDYVATRW---YRAPELcgsfFSKYTPAI-----DIWSIGCIFAEVLTGK 205
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
55-281 1.82e-11

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 63.43  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  55 EQQDREEAQREAD-MHRLFNhPNILRLVAYClrergaKHEAWLLLPFFKRGTLWNEIerLKDKGNFLTEDQILWLLLGIC 133
Cdd:cd05115  44 EKAVRDEMMREAQiMHQLDN-PYIVRMIGVC------EAEALMLVMEMASGGPLNKF--LSGKKDEITVSNVVELMHQVS 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 134 RGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVEGSRQALTLQDWAaqrctISYRAPELFSVQShcvID 213
Cdd:cd05115 115 MGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFG-LSKALGADDSYYKARSAGKWP-----LKWYAPECINFRK---FS 185
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 214 ERTDVWSLGCVLY-AMMFGEGPYDMVfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05115 186 SRSDVWSYGVTMWeAFSYGQKPYKKM--KGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWEDRP 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
19-296 2.01e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 63.58  E-value: 2.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVE--GLHDGHFYALKR--------ILCheqqdrEEAQREADMHRLF-NHPNILRLVAYCLRE 87
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARnaETSEEETVAIKKitnvfskkILA------KRALRELKLLRHFrGHKNITCLYDMDIVF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  88 RGAKHEAWLLLPFFKRGTlwNEIERlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd07857  75 PGNFNELYLYEELMEADL--HQIIR---SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GsmnQAC-IHVEGSRQALTLQDWAAqrcTISYRAPE-LFSVQSHcviDERTDVWSLGCVLyAMMFGEGPydmVFQKGDSV 245
Cdd:cd07857 150 G---LARgFSENPGENAGFMTEYVA---TRWYRAPEiMLSFQSY---TKAIDVWSVGCIL-AELLGRKP---VFKGKDYV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 246 ALAVQ--NQLSIPQ--------SPRHSSALRQ----------------------LLNSMMTVDPHQRPHIPlllsqlEAL 293
Cdd:cd07857 217 DQLNQilQVLGTPDeetlsrigSPKAQNYIRSlpnipkkpfesifpnanplaldLLEKLLAFDPTKRISVE------EAL 290

                ...
gi 46577677 294 QPP 296
Cdd:cd07857 291 EHP 293
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
26-280 2.05e-11

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: 63.26  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLH--DGHFYALKRI-LCHEQQDREEAQREADMH---RLFNHPNILRLVAYCLRERgakhEAWLLLP 99
Cdd:cd06917   9 VGRGSYGAV--YRGYHvkTGRVVALKVLnLDTDDDDVSDIQKEVALLsqlKLGQPKNIIKYYGSYLKGP----SLWIIMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLwneieRLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEG 179
Cdd:cd06917  83 YCEGGSI-----RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGV---AASLNQN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDwaaqrcTISYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDSVALAVQnqlSIPQS- 258
Cdd:cd06917 155 SSKRSTFVG------TPYWMAPEV--ITEGKYYDTKADIWSLGITTYEMATGNPPY-----SDVDALRAVM---LIPKSk 218
                       250       260
                ....*....|....*....|....*...
gi 46577677 259 -PR-----HSSALRQLLNSMMTVDPHQR 280
Cdd:cd06917 219 pPRlegngYSPLLKEFVAACLDEEPKDR 246
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
22-301 2.14e-11

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 63.14  E-value: 2.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLveGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd05072  11 LVKKLGAGQFGEVWM--GYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEE----PIYIITEYM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacihvegsr 181
Cdd:cd05072  85 AKGSLLDFLK--SDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFG------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLQD--WAAQ---RCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAVQNQLSI 255
Cdd:cd05072 150 LARVIEDneYTARegaKFPIKWTAPEAINFGSFTI---KSDVWSFGILLYEIVtYGKIPYPGM--SNSDVMSALQRGYRM 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 256 PQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQH 301
Cdd:cd05072 225 PRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQY 270
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-274 2.26e-11

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 63.87  E-value: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLvayCLRERGAKHeAWL 96
Cdd:cd05621  54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAffwEERDIMAFANSPWVVQL---FCAFQDDKY-LYM 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIER--LKDK-GNFLTEDQILwlllgicrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqa 173
Cdd:cd05621 130 VMEYMPGGDLVNLMSNydVPEKwAKFYTAEVVL--------ALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGT---- 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 174 CIHVEGSrqALTLQDWAAQrcTISYRAPELFSVQ-SHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGD-SVALAVQN 251
Cdd:cd05621 198 CMKMDET--GMVHCDTAVG--TPDYISPEVLKSQgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTySKIMDHKN 273
                       250       260
                ....*....|....*....|...
gi 46577677 252 QLSIPQSPRHSSALRQLLNSMMT 274
Cdd:cd05621 274 SLNFPDDVEISKHAKNLICAFLT 296
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
23-235 2.67e-11

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 63.40  E-value: 2.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE-----AQR----EADmhrlfnHPNILRLvaYC-------Lr 86
Cdd:cd05599   6 LKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQvahvrAERdilaEAD------NPWVVKL--YYsfqdeenL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  87 ergakheaWLLLPFFKRGTLWNEIERlKDkgnFLTEDQ----ILWLLLGIcrglEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:cd05599  77 --------YLIMEFLPGGDMMTLLMK-KD---TLTEEEtrfyIAETVLAI----ESIHKLGYIHRDIKPDNLLLDARGHI 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 163 VLMDLGsmnqACIHVEGSRQALTLQDwaaqrcTISYRAPELFS---VQSHCvidertDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05599 141 KLSDFG----LCTGLKKSHLAYSTVG------TPDYIAPEVFLqkgYGKEC------DWWSLGVIMYEMLIGYPPF 200
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
63-268 2.86e-11

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 63.15  E-value: 2.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  63 QREADMHRLF--NHPNILRLVAYCLRERGAKHEAWLL-LPFFKRGTLWNeierlkdkgnFLTEDQILW-----LLLGICR 134
Cdd:cd14054  35 QNEKDIYELPlmEHSNILRFIGADERPTADGRMEYLLvLEYAPKGSLCS----------YLRENTLDWmsscrMALSLTR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAK---------GYAHRDLKPTNILLGDEGQPVLMDLG-SMNqacihVEGSRQALTLQDWA-----AQRCTISYR 199
Cdd:cd14054 105 GLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGlAMV-----LRGSSLVRGRPGAAenasiSEVGTLRYM 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELF--SV---QSHCVIdERTDVWSLGCVLY--AM----MF-GE--GPYDMVFQK--GDSV------ALAVQNQL--SI 255
Cdd:cd14054 180 APEVLegAVnlrDCESAL-KQVDVYALGLVLWeiAMrcsdLYpGEsvPPYQMPYEAelGNHPtfedmqLLVSREKArpKF 258
                       250
                ....*....|....
gi 46577677 256 PQS-PRHSSALRQL 268
Cdd:cd14054 259 PDAwKENSLAVRSL 272
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
20-231 3.28e-11

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 62.79  E-value: 3.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDRE-EAQREADMHRLFNHPNILrlvayCLRERGAKHEAWLLL 98
Cdd:cd07869   7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPfTAIREASLLKGLKHANIV-----LLHDIIHTKETLTLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIErlKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihve 178
Cdd:cd07869  82 FEYVHTDLCQYMD--KHPGG-LHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGL--------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 179 GSRQALTLQDWAAQRCTISYRAPELF---SVQSHCVidertDVWSLGCVLYAMMFG 231
Cdd:cd07869 150 ARAKSVPSHTYSNEVVTLWYRPPDVLlgsTEYSTCL-----DMWGVGCIFVEMIQG 200
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
26-235 3.52e-11

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 62.89  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHD--GHFYALKRILCHEQQDREEAQ-READMHRLFNHPNILRLVAyCLRERGAKHEAwLLLPFFK 102
Cdd:cd13988   1 LGQGATANV--FRGRHKktGDLYAVKVFNNLSFMRPLDVQmREFEVLKKLNHKNIVKLFA-IEEELTTRHKV-LVMELCP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIErlkDKGNF--LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL--LGDEGQPV--LMDLGsmnqACIH 176
Cdd:cd13988  77 CGSLYTVLE---EPSNAygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFG----AARE 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 177 VEGSRQALTLQDwaaqrcTISYRAPELFsvqSHCVIDERT--------DVWSLGCVLYAMMFGEGPY 235
Cdd:cd13988 150 LEDDEQFVSLYG------TEEYLHPDMY---ERAVLRKDHqkkygatvDLWSIGVTFYHAATGSLPF 207
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
26-235 3.61e-11

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 62.34  E-value: 3.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheqqdREEAQREADMHRLFN-------HPNILRLVAYCLRERGAKHEAWLLL 98
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFV-------PKPSTKLKDFLREYNislelsvHPHIIKTYDVAFETEDYYVFAQEYA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PffkRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGD-EGQPV-LMDLGsMNQacih 176
Cdd:cd13987  74 P---YGDLFSIIP----PQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDkDCRRVkLCDFG-LTR---- 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 177 vegsRQALTLQdwaAQRCTISYRAPEL--FSVQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd13987 142 ----RVGSTVK---RVSGTIPYTAPEVceAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPW 195
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
23-289 3.66e-11

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: 62.38  E-value: 3.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSyvDLVEGLHD--GHFYALKRILCHEQQDR-EEAQREADMHRLFNHPNILRLVAYCLRerGAKheAWLLLP 99
Cdd:cd06640   9 LERIGKGSFG--EVFKGIDNrtQQVVAIKIIDLEEAEDEiEDIQQEITVLSQCDSPYVTKYYGSYLK--GTK--LWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNeierLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihveg 179
Cdd:cd06640  83 YLGGGSALD----LLRAGPF-DEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQ------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 srqaltLQDWAAQRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvfqkgDSVALAVQNQLSI 255
Cdd:cd06640 151 ------LTDTQIKRNTFVgtpfWMAPEVIQQSAY---DSKADIWSLGITAIELAKGEPP--------NSDMHPMRVLFLI 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 46577677 256 PQSP------RHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06640 214 PKNNpptlvgDFSKPFKEFIDACLNKDPSFRPTAKELLKH 253
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
20-244 3.72e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 62.44  E-value: 3.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLL 97
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQE----NRLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFfkrgtLWNEIERLKD---KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAC 174
Cdd:cd07861  78 FEF-----LSMDLKKYLDslpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 175 IHVEG-SRQALTLqdWaaqrctisYRAPE--LFSVQSHCVIdertDVWSLGCVlYAMMFGEGPydmVFQkGDS 244
Cdd:cd07861 153 IPVRVyTHEVVTL--W--------YRAPEvlLGSPRYSTPV----DIWSIGTI-FAEMATKKP---LFH-GDS 206
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
63-272 3.78e-11

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 62.96  E-value: 3.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  63 QREADMHRLFNHPNILrlVAYCLRERGAkhEAWLLLPFFKRGTLWNEIERLKDKGnfLTEDQILWLLLGICRGLEAIHAK 142
Cdd:cd08226  47 QNEVVLSHFFRHPNIM--THWTVFTEGS--WLWVISPFMAYGSARGLLKTYFPEG--MNEALIGNILYGAIKALNYLHQN 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 143 GYAHRDLKPTNILLGDEGqpvLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTI-SYRAPELFSVQSHCViDERTDVWSL 221
Cdd:cd08226 121 GCIHRSVKASHILISGDG---LVSLSGLSHLYSMVTNGQRSKVVYDFPQFSTSVlPWLSPELLRQDLHGY-NVKSDIYSV 196
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 222 GCVLYAMMFGEGPydmvFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSM 272
Cdd:cd08226 197 GITACELARGQVP----FQDMRRTQMLLQKLKGPPYSPLDIFPFPELESRM 243
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
23-291 3.87e-11

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 62.21  E-value: 3.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYVDLveGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFK 102
Cdd:cd05067  12 VERLGAGQFGEVWM--GYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQE-----PIYIITEYME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLwneIERLK-DKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihVEGSR 181
Cdd:cd05067  85 NGSL---VDFLKtPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARL----IEDNE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 qaLTLQDWAaqRCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMM-FGEGPYdmvfqKGDSVALAVQNQLSIPQSPR 260
Cdd:cd05067 158 --YTAREGA--KFPIKWTAPEAINYGTFTI---KSDVWSFGILLTEIVtHGRIPY-----PGMTNPEVIQNLERGYRMPR 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 46577677 261 HSSALRQLLNSMMTV---DPHQRPHIPLLLSQLE 291
Cdd:cd05067 226 PDNCPEELYQLMRLCwkeRPEDRPTFEYLRSVLE 259
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
19-168 6.04e-11

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 61.70  E-value: 6.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALK---RILCHEQqdreeAQREAD-MHRLFNHPNILRLVAYclrergAKHEA 94
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKiekKDSKHPQ-----LEYEAKvYKLLQGGPGIPRLYWF------GQEGD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 W------LLLPffkrgTLWNEIERLKDKGNFLTEdqilwLLLG---ICRgLEAIHAKGYAHRDLKPTNILLG---DEGQP 162
Cdd:cd14016  70 YnvmvmdLLGP-----SLEDLFNKCGRKFSLKTV-----LMLAdqmISR-LEYLHSKGYIHRDIKPENFLMGlgkNSNKV 138

                ....*.
gi 46577677 163 VLMDLG 168
Cdd:cd14016 139 YLIDFG 144
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
18-296 6.32e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 62.35  E-value: 6.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYV----DLVEGLHdghfYALKRiLCHEQQDREEAQR---EADMHRLFNHPNILRLVAYCLRERGA 90
Cdd:cd07876  21 KRYQQLKPIGSGAQGIVcaafDTVLGIN----VAVKK-LSRPFQNQTHAKRayrELVLLKCVNHKNIISLLNVFTPQKSL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 K--HEAWLLLPFFKrGTLWNEIERLKDkgnfltEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd07876  96 EefQDVYLVMELMD-ANLCQVIHMELD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACIHvegsrqaLTLQDWAAQRctiSYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEgpydMVFQKGDSV--- 245
Cdd:cd07876 169 LARTACTN-------FMMTPYVVTR---YYRAPEVILGMGY---KENVDIWSVGCIMGELVKGS----VIFQGTDHIdqw 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 246 ----------ALAVQNQL--------------------------SIPQSPRH----SSALRQLLNSMMTVDPHQR----- 280
Cdd:cd07876 232 nkvieqlgtpSAEFMNRLqptvrnyvenrpqypgisfeelfpdwIFPSESERdklkTSQARDLLSKMLVIDPDKRisvde 311
                       330       340
                ....*....|....*....|
gi 46577677 281 ----PHIPLLLSQLEALQPP 296
Cdd:cd07876 312 alrhPYITVWYDPAEAEAPP 331
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
56-281 6.43e-11

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: 61.60  E-value: 6.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  56 QQDREEAQREADMHRL-FNHPNILRLvaYCLRErgAKHEAWLLLPFFKRGtlwnEIERLKDKGNFLTEDQILWLLLGICR 134
Cdd:cd14106  48 QDCRNEILHEIAVLELcKDCPRVVNL--HEVYE--TRSELILILELAAGG----ELQTLLDEEECLTEADVRRLMRQILE 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAKGYAHRDLKPTNILLGDE---GQPVLMDLGsMNQACIHVEGSRQALTlqdwaaqrcTISYRAPELFSVQShcv 211
Cdd:cd14106 120 GVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFG-ISRVIGEGEEIREILG---------TPDYVAPEILSYEP--- 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 212 IDERTDVWSLGCVLYAMMFGEGPYdmvfqKGDS---VALAV-QNQLSIPQSPRH--SSALRQLLNSMMTVDPHQRP 281
Cdd:cd14106 187 ISLATDMWSIGVLTYVLLTGHSPF-----GGDDkqeTFLNIsQCNLDFPEELFKdvSPLAIDFIKRLLVKDPEKRL 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
26-235 7.07e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 62.14  E-value: 7.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   26 LGEGGFSYVDLVEGLHDGHFYALK-----RILCHEQQDREEAQREADMHrlFNHPNILRLvaycLRERGAKHEAWLLLPF 100
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKclkkrEILKMKQVQHVAQEKSILME--LSHPFIVNM----MCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  101 FKRGTLWNEIERL----KDKGNFLTEDQILwlllgicrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcih 176
Cdd:PTZ00263 100 VVGGELFTHLRKAgrfpNDVAKFYHAELVL--------AFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV--- 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  177 vegSRQALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:PTZ00263 169 ---PDRTFTL-------CgTPEYLAPEVIQSKGH---GKAVDWWTMGVLLYEFIAGYPPF 215
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
25-235 7.42e-11

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: 61.52  E-value: 7.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLHDGHFYALKRilCHEQ---QDREEAQREADMHRLFNHPNIL--RLVAYCLRERGAKHEAWLLLP 99
Cdd:cd14038   1 RLGTGGFGNVLRWINQETGEQVAIKQ--CRQElspKNRERWCLEIQIMKRLNHPNVVaaRDVPEGLQKLAPNDLPLLAME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV---LMDLG---SMNQA 173
Cdd:cd14038  79 YCQGGDLRKYLNQFENCCG-LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLihkIIDLGyakELDQG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 174 --CIHVEGsrqaltlqdwaaqrcTISYRAPELFSVQSHCVIderTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14038 158 slCTSFVG---------------TLQYLAPELLEQQKYTVT---VDYWSFGTLAFECITGFRPF 203
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
120-296 7.58e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 62.00  E-value: 7.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQR-CTISY 198
Cdd:cd07858 105 LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL----------ARTTSEKGDFMTEYvVTRWY 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 199 RAPELFsvqSHCviDERT---DVWSLGCVLYAMMfGEGPydmVFQKGDSValavqNQL---------------------- 253
Cdd:cd07858 175 RAPELL---LNC--SEYTtaiDVWSVGCIFAELL-GRKP---LFPGKDYV-----HQLklitellgspseedlgfirnek 240
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 254 ------SIPQSPRHSSALR---------QLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07858 241 arryirSLPYTPRQSFARLfphanplaiDLLEKMLVFDPSKR------ITVEEALAHP 292
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
23-300 7.95e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.15  E-value: 7.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   23 IQKLGEGGFSYVDLVEGLHDGHFYALKRILC-HEQQDREEAQREADMHRLFNHPNILRlvAYCLRERGAkhEAWLLLPFF 101
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKVIYGnHEDTVRRQICREIEILRDVNHPNVVK--CHDMFDHNG--EIQVLLEFM 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  102 KRGTLwnEIERLKDKGnFLTE--DQILwlllgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihveG 179
Cdd:PLN00034 155 DGGSL--EGTHIADEQ-FLADvaRQIL-------SGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGV---------S 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  180 SRQALTLQDWAAQRCTISYRAPELFSVQ-SHCVIDERT-DVWSLGCVLYAMMFGEGPYDmVFQKGDSVALAVQNQLS-IP 256
Cdd:PLN00034 216 RILAQTMDPCNSSVGTIAYMSPERINTDlNHGAYDGYAgDIWSLGVSILEFYLGRFPFG-VGRQGDWASLMCAICMSqPP 294
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 46577677  257 QSPRHSSA-LRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQ 300
Cdd:PLN00034 295 EAPATASReFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQG 339
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
26-289 8.58e-11

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 61.25  E-value: 8.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMHRLFNHPNIL------RLVAY--CLRERGAKHEAwLL 97
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQV----QFDPESPETSKEVSALECEIQLLknlqheRIVQYygCLRDRAEKTLT-IF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEierLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS---MNQAC 174
Cdd:cd06651  90 MEYMPGGSVKDQ---LKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAskrLQTIC 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmVFQKGDSVALAVQNQLS 254
Cdd:cd06651 166 MSGTGIRSVTGTPYWM---------SPEVISGEGY---GRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAIFKIATQPT 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 255 IPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd06651 232 NPQLPSHISEHARDFLGCIFVEARHRPSAEELLRH 266
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
17-229 9.14e-11

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: 61.45  E-value: 9.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYL-FIQKLGEGGFSYVDLV--EGLHD--GHFYALKRILCH-EQQDREEAQREADMHRLFNHPNILRLVAYClrERGA 90
Cdd:cd05080   2 HKRYLkKIRDLGEGHFGKVSLYcyDPTNDgtGEMVAVKALKADcGPQHRSGWKQEIDILKTLYHENIVKYKGCC--SEQG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 KHEAWLLLPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqpvLMDLGSM 170
Cdd:cd05080  80 GKSLQLIMEYVPLGSLRDYLPK-----HSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDR---LVKIGDF 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 171 NQACIHVEGSRQALTLQD------WAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMM 229
Cdd:cd05080 152 GLAKAVPEGHEYYRVREDgdspvfWYAPECLKEYK----FYYAS--------DVWSFGVTLYELL 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
25-280 1.12e-10

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: 61.23  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREE------AQREADMHRLFNHPNILRLvaycLRERGAKHEAWLLL 98
Cdd:cd07845  14 RIGEGTYGIVYRARDTTSGEIVALKKV----RMDNERdgipisSLREITLLLNLRHPNIVEL----KEVVVGKHLDSIFL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFfkrGTLWNEIERLKDK-GNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihv 177
Cdd:cd07845  86 VM---EYCEQDLASLLDNmPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGL-------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 eGSRQALTLQDWAAQRCTISYRAPE-LFSVQSHcviDERTDVWSLGCVLyAMMFGEGPY----------DMVFQ----KG 242
Cdd:cd07845 155 -ARTYGLPAKPMTPKVVTLWYRAPElLLGCTTY---TTAIDMWAVGCIL-AELLAHKPLlpgkseieqlDLIIQllgtPN 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 46577677 243 DSV-----ALAVQNQLSIPQSP----RH-----SSALRQLLNSMMTVDPHQR 280
Cdd:cd07845 230 ESIwpgfsDLPLVGKFTLPKQPynnlKHkfpwlSEAGLRLLNFLLMYDPKKR 281
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
19-228 1.15e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 60.91  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIlchEQQDREE-----AQREADMHRLFNHPNILRLVAYCLRErgakHE 93
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRV---RLDDDDEgvpssALREICLLKELKHKNIVRLYDVLHSD----KK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPFFKRgtlwnEIERLKDKGNFLTEDQILW-LLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd07839  74 LTLVFEYCDQ-----DLKKYFDSCNGDIDPEIVKsFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 173 ACIHVegsrqaltlQDWAAQRCTISYRAPE-LFSVQSHcviDERTDVWSLGCVLYAM 228
Cdd:cd07839 149 FGIPV---------RCYSAEVVTLWYRPPDvLFGAKLY---STSIDMWSAGCIFAEL 193
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
27-293 1.16e-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: 60.74  E-value: 1.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  27 GEGGFSYVDLVEGLHDGHFYALKRILcheqqdreEAQREADMHRLFNHPNILRLVAYCLRergAKHEAwLLLPFFKRGTL 106
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLL--------KIEKEAEILSVLSHRNIIQFYGAILE---APNYG-IVTEYASYGSL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 107 WNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKG---YAHRDLKPTNILLGDEGQPVLMDLGSMNqacIHVEGSRQA 183
Cdd:cd14060  70 FDYLN--SNESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASR---FHSHTTHMS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTlqdwaaqrCTISYRAPELfsVQSHCViDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVA-LAVQN--QLSIPQS-- 258
Cdd:cd14060 145 LV--------GTFPWMAPEV--IQSLPV-SETCDTYSYGVVLWEMLTREVPFKGL--EGLQVAwLVVEKneRPTIPSScp 211
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 259 PRHSSALRQLLNSmmtvDPHQRPHIPLLLSQLEAL 293
Cdd:cd14060 212 RSFAELMRRCWEA----DVKERPSFKQIIGILESM 242
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
15-241 1.20e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 60.65  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLveGLHDGHF-YALKRIlcheqqdREEAQREAD-------MHRLfNHPNILRLVAYCLR 86
Cdd:cd05114   1 INPSELTFMKELGSGLFGVVRL--GKWRAQYkVAIKAI-------REGAMSEEDfieeakvMMKL-THPKLVQLYGVCTQ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  87 ERgakhEAWLLLPFFKRGTLWNeieRLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD 166
Cdd:cd05114  71 QK----PIYIVTEFMENGCLLN---YLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSD 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 167 LGsMNQACIHVEGSRQaltlqdwAAQRCTISYRAPELFSVQSHcviDERTDVWSLGcVLYAMMFGEGpyDMVFQK 241
Cdd:cd05114 144 FG-MTRYVLDDQYTSS-------SGAKFPVKWSPPEVFNYSKF---SSKSDVWSFG-VLMWEVFTEG--KMPFES 204
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
26-288 1.26e-10

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: 60.83  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQD-REEA---QREADMHRLFNHPnilRLVAY--CLRERGAkheAWLLL 98
Cdd:cd06625   8 LGQGAFGQVYLCYDADTGRELAVKQVeIDPINTEaSKEVkalECEIQLLKNLQHE---RIVQYygCLQDEKS---LSIFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIerlKDKGNfLTED-------QILwlllgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN 171
Cdd:cd06625  82 EYMPGGSVKDEI---KAYGA-LTENvtrkytrQIL-------EGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 Q-ACIHVEGSRQALTlqdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdmvfqkGDSVALA-- 248
Cdd:cd06625 151 RlQTICSSTGMKSVT--------GTPYWMSPEVINGEGY---GRKADIWSVGCTVVEMLTTKPPW------AEFEPMAai 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 46577677 249 --VQNQLSIPQSPRHSS-ALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06625 214 fkIATQPTNPQLPPHVSeDARDFLSLIFVRNKKQRPSAEELLS 256
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
15-289 1.26e-10

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: 60.71  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFI---QKLGEGGFSYVDLVEGLHDGHFYALKRIlchEQQDREEAQREADMHRLF------NHPNILRLVAYcl 85
Cdd:cd14198   2 MDNFNNFYIltsKELGRGKFAVVRQCISKSTGQEYAAKFL---KKRRRGQDCRAEILHEIAvlelakSNPRVVNLHEV-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  86 reRGAKHEAWLLLPFFKRGTLWNEIerLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGD---EGQP 162
Cdd:cd14198  77 --YETTSEIILILEYAAGGEIFNLC--VPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 163 VLMDLGsMNQACIHVEGSRQALTlqdwaaqrcTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYdmVFQKG 242
Cdd:cd14198 153 KIVDFG-MSRKIGHACELREIMG---------TPEYLAPEILNYDP---ITTATDMWNIGVIAYMLLTHESPF--VGEDN 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 243 DSVALAVqNQLSIPQSPRHSSALRQL----LNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd14198 218 QETFLNI-SQVNVDYSEETFSSVSQLatdfIQKLLVKNPEKRPTAEICLSH 267
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
26-234 1.38e-10

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: 60.99  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQD----REEAQREADMHRLFNHPNILRLVAYCLrERGAKHEAWLLLPff 101
Cdd:cd14159   1 IGEGGFGCV--YQAVMRNTEYAVKRLKEDSELDwsvvKNSFLTEVEKLSRFRHPNIVDLAGYSA-QQGNYCLIYVYLP-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 kRGTLWneiERLKDKGNF--LTEDQILWLLLGICRGLEAIHAKGYA--HRDLKPTNILLGDEGQPVLMDLGsMNQACIHV 177
Cdd:cd14159  76 -NGSLE---DRLHCQVSCpcLSWSQRLHVLLGTARAIQYLHSDSPSliHGDVKSSNILLDAALNPKLGDFG-LARFSRRP 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 178 EGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGP 234
Cdd:cd14159 151 KQPGMSSTLARTQTVRGTLAYLPEEYVKTGTLSV---EIDVYSFGVVLLELLTGRRA 204
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
26-280 1.92e-10

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 60.71  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRL-FNHPNILRLvaYCLRErgAKHEAWLLLPFF 101
Cdd:cd05619  13 LGKGSFGKVFLAELKGTNQFFAikaLKKDVVLMDDDVECTMVEKRVLSLaWEHPFLTHL--FCTFQ--TKENLFFVMEYL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKD----KGNFLTEDQILwlllgicrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIhv 177
Cdd:cd05619  89 NGGDLMFHIQSCHKfdlpRATFYAAEIIC--------GLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENML-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 eGSRQALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAVQNQLSIP 256
Cdd:cd05619 159 -GDAKTSTF-------CgTPDYIAPEILLGQKY---NTSVDWWSFGVLLYEMLIGQSP----FHGQDEEELFQSIRMDNP 223
                       250       260
                ....*....|....*....|....*
gi 46577677 257 QSPRH-SSALRQLLNSMMTVDPHQR 280
Cdd:cd05619 224 FYPRWlEKEAKDILVKLFVREPERR 248
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
136-280 2.06e-10

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 60.79  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIhveGSRQALTLQDWAAQRC--TISYRAPELFSVQSH---C 210
Cdd:cd05598 114 IESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG----LCT---GFRWTHDSKYYLAHSLvgTPNYIAPEVLLRTGYtqlC 186
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 211 vidertDVWSLGCVLYAMMFGEGPYdmVFQKGDSVALAV---QNQLSIPQSPRHSSALRQLLNSMMTvDPHQR 280
Cdd:cd05598 187 ------DWWSVGVILYEMLVGQPPF--LAQTPAETQLKVinwRTTLKIPHEANLSPEAKDLILRLCC-DAEDR 250
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
57-236 2.11e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 60.43  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRL--FNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICR 134
Cdd:cd14140  29 QDKQSWQSEREIFSTpgMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSLTDYL-----KGNIVSWNELCHIAETMAR 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIH-----AKG------YAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQAltlQDWAAQRCTISYRAPEL 203
Cdd:cd14140 104 GLSYLHedvprCKGeghkpaIAHRDFKSKNVLLKNDLTAVLADFG----LAVRFEPGKPP---GDTHGQVGTRRYMAPEV 176
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 46577677 204 FSVQSHCVIDE--RTDVWSLGCVLYAMM----FGEGPYD 236
Cdd:cd14140 177 LEGAINFQRDSflRIDMYAMGLVLWELVsrckAADGPVD 215
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-231 2.40e-10

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 60.09  E-value: 2.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRI-LCHEQQDREEAQREADMHRLFNHPNILRLvayclrergakH-----E 93
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIrLEHEEGAPFTAIREASLLKDLKHANIVTL-----------HdiihtK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWLLLPF-FKRGTLWNEIErlkDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd07844  71 KTLTLVFeYLDTDLKQYMD---DCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 173 ACIHVEG-SRQALTLqdWaaqrctisYRAPEL------FSVQshcviderTDVWSLGCVLYAMMFG 231
Cdd:cd07844 148 KSVPSKTySNEVVTL--W--------YRPPDVllgsteYSTS--------LDMWGVGCIFYEMATG 195
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
18-287 2.44e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 61.04  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFN--HPNILRlvayCLRERGAKHEA- 94
Cdd:PTZ00283  32 KKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNcdFFSIVK----CHEDFAKKDPRn 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   95 -------WLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:PTZ00283 108 penvlmiALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  168 GSMNQACIHVEGsrqaltlqDWAAQRC-TISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVA 246
Cdd:PTZ00283 188 GFSKMYAATVSD--------DVGRTFCgTPYYVAPEIW---RRKPYSKKADMFSLGVLLYELLTLKRPFD-----GENME 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 46577677  247 LAVQNQLS---IPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:PTZ00283 252 EVMHKTLAgryDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
24-292 2.73e-10

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 59.76  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSyvDLVEGLHDGHF-YALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFK 102
Cdd:cd05148  12 RKLGSGYFG--EVWEGLWKNRVrVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGE----PVYIITELME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLwneIERLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacihvegsr 181
Cdd:cd05148  86 KGSL---LAFLRSpEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFG------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QALTLQD--WAAQRCTISYR--APElfsVQSHCVIDERTDVWSLGCVLYAMM-FGEGPYDMVFQKgdSVALAVQNQLSIP 256
Cdd:cd05148 150 LARLIKEdvYLSSDKKIPYKwtAPE---AASHGTFSTKSDVWSFGILLYEMFtYGQVPYPGMNNH--EVYDQITAGYRMP 224
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 257 QSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEA 292
Cdd:cd05148 225 CPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDN 260
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
17-290 2.76e-10

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: 60.07  E-value: 2.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALK-RILCHEQQDREE------AQREADMHRLFNHPNILRLVAYClrerG 89
Cdd:cd14040   5 NERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKiHQLNKSWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYF----S 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHEAWLLLPFFKRGtlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIH--AKGYAHRDLKPTNILLGDE---GQPVL 164
Cdd:cd14040  81 LDTDTFCTVLEYCEG---NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 165 MDLG---SMNQACIHVEGsrqaltlQDWAAQRC-TISYRAPELFSV-QSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVF 239
Cdd:cd14040 158 TDFGlskIMDDDSYGVDG-------MDLTSQGAgTYWYLPPECFVVgKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQ 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 240 QKGDSV---ALAVQNQLSIPQSPRHSSALRQLLNSMMT------VDPHQRPHIPLLLSQL 290
Cdd:cd14040 231 SQQDILqenTILKATEVQFPVKPVVSNEAKAFIRRCLAyrkedrFDVHQLASDPYLLPHM 290
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
122-232 2.88e-10

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 60.28  E-value: 2.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 122 EDQ-ILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGsrqaltlqdWAAQRctiSYRA 200
Cdd:cd07856 106 EKQfIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMTG---------YVSTR---YYRA 173
                        90       100       110
                ....*....|....*....|....*....|...
gi 46577677 201 PE-LFSVQSHcviDERTDVWSLGCVLYAMMFGE 232
Cdd:cd07856 174 PEiMLTWQKY---DVEVDIWSAGCIFAEMLEGK 203
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
20-280 3.01e-10

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 59.72  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILcheqqDREEAQREADMHRLFNHPNILR-----LVAYCLRERGAKHEA 94
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMK-IL-----DKQKVVKLKQVEHTLNEKRILQainfpFLVKLEYSFKDNSNL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqAC 174
Cdd:cd14209  77 YMVMEYVPGGEMFS---HLRRIGRF-SEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFG----FA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALtlqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYD-----MVFQKgdsvalA 248
Cdd:cd14209 149 KRVKGRTWTL---------CgTPEYLAPEIILSKGY---NKAVDWWALGVLIYEMAAGYPPFFadqpiQIYEK------I 210
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 249 VQNQLSIPQspRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd14209 211 VSGKVRFPS--HFSSDLKDLLRNLLQVDLTKR 240
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
26-225 3.22e-10

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 59.41  E-value: 3.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKriLCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErGAKHEawlLLPFFKRGT 105
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALK--MNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQ-GQLHA---LTEYINGGN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LwneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEGQ--PVLMDLGSMNQACIHVEGSRQ 182
Cdd:cd14155  75 L----EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkRDENGytAVVGDFGLAEKIPDYSDGKEK 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 46577677 183 ALTLQD--WAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVL 225
Cdd:cd14155 151 LAVVGSpyWM---------APEVLRGEPY---NEKADVFSYGIIL 183
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
19-235 3.32e-10

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: 59.55  E-value: 3.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYL-FIQKLGEGGFSYV----DLVEG-------LHDGHFyalkrilchEQQDREEAQREADMHRLFNHPNILRLVAYClr 86
Cdd:cd13983   1 RYLkFNEVLGRGSFKTVyrafDTEEGievawneIKLRKL---------PKAERQRFKQEIEILKSLKHPNIIKFYDSW-- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  87 ERGAKHEAWLLLPFFKRGTLWNEIERLKDkgnfLTED-------QILwlllgicRGLEAIHAKGY--AHRDLKPTNILL- 156
Cdd:cd13983  70 ESKSKKEVIFITELMTSGTLKQYLKRFKR----LKLKvikswcrQIL-------EGLNYLHTRDPpiIHRDLKCDNIFIn 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 GDEGQPVLMDLGSmnqacihvegsrqALTLQDWAAQRC--TISYRAPELFSVQshcvIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:cd13983 139 GNTGEVKIGDLGL-------------ATLLRQSFAKSVigTPEFMAPEMYEEH----YDEKVDIYAFGMCLLEMATGEYP 201

                .
gi 46577677 235 Y 235
Cdd:cd13983 202 Y 202
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
121-280 4.14e-10

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


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 59.37  E-value: 4.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 121 TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACihvEGSRQALTlqdwaAQRCTISYRA 200
Cdd:cd05606  96 SEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLG---LAC---DFSKKKPH-----ASVGTHGYMA 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 201 PELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKG----DSVALAVqnQLSIPQSprHSSALRQLLNSMMTVD 276
Cdd:cd05606 165 PEV--LQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDkheiDRMTLTM--NVELPDS--FSPELKSLLEGLLQRD 238

                ....
gi 46577677 277 PHQR 280
Cdd:cd05606 239 VSKR 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
95-235 4.21e-10

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 60.03  E-value: 4.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqaC 174
Cdd:cd05623 148 YLVMDYYVGGDLLTLLSKFEDR---LPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGS----C 220
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 175 IHV--EGSRQAltlqdwAAQRCTISYRAPELFSVQS--HCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05623 221 LKLmeDGTVQS------SVAVGTPDYISPEILQAMEdgKGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
22-280 4.23e-10

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: 60.04  E-value: 4.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFN---HPnILRLVAYCLRergAKHEAWLLL 98
Cdd:cd05594  29 YLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQnsrHP-FLTALKYSFQ---THDRLCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  99 PFFKRGTLWNEIERLKdkgnFLTEDQILWLLLGICRGLEAIHA-KGYAHRDLKPTNILLGDEGQPVLMDLGsmnqacIHV 177
Cdd:cd05594 105 EYANGGELFFHLSRER----VFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG------LCK 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMVFQKgdSVALAVQNQLSIP 256
Cdd:cd05594 175 EGIKDGATMKTFCG---TPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPfYNQDHEK--LFELILMEEIRFP 246
                       250       260
                ....*....|....*....|....
gi 46577677 257 QSprHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05594 247 RT--LSPEAKSLLSGLLKKDPKQR 268
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
20-228 5.25e-10

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: 59.08  E-value: 5.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALK--RILCHEQQDREEAQREADMHRLFNH-PNILRLVAYCLRERGAKHEAWL 96
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKktRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHVEENGKPLLYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRgTLWNEIERL-KDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPVLMDLGSmnqac 174
Cdd:cd07837  83 VFEYLDT-DLKKFIDSYgRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGL----- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 175 ihveGSRQALTLQDWAAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAM 228
Cdd:cd07837 157 ----GRAFTIPIKSYTHEIVTLWYRAPEVLLGSTH--YSTPVDMWSVGCIFAEM 204
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
129-291 5.31e-10

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: 58.94  E-value: 5.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 129 LLGICR----GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGSrqalTLQDWAAQRCTISYRAPELF 204
Cdd:cd14062  91 LIDIARqtaqGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFG---LATVKTRWS----GSQQFEQPTGSILWMAPEVI 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 205 SVQSHCVIDERTDVWSLGCVLYAMMFGEGPY------DMV-FQKGDSVALAVQNQLSiPQSPRhssALRQLLNSMMTVDP 277
Cdd:cd14062 164 RMQDENPYSFQSDVYAFGIVLYELLTGQLPYshinnrDQIlFMVGRGYLRPDLSKVR-SDTPK---ALRRLMEDCIKFQR 239
                       170
                ....*....|....
gi 46577677 278 HQRPHIPLLLSQLE 291
Cdd:cd14062 240 DERPLFPQILASLE 253
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
26-280 6.46e-10

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 58.97  E-value: 6.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRI---LCHEQQDREEAQREADM-HRLFNHPNILRLVAyCLRergAKHEAWLLLPFF 101
Cdd:cd05588   3 IGRGSYAKVLMVELKKTKRIYAMKVIkkeLVNDDEDIDWVQTEKHVfETASNHPFLVGLHS-CFQ---TESRLFFVIEFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacihvEGSR 181
Cdd:cd05588  79 NGGDLMFHMQRQRR----LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCK------EGLR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 QAltlqDWAAQRC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMV--------------FQkgdsva 246
Cdd:cd05588 149 PG----DTTSTFCgTPNYIAPEILRGEDY---GFSVDWWALGVLMFEMLAGRSPFDIVgssdnpdqntedylFQ------ 215
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 247 LAVQNQLSIPQ--SPRHSSALRQLLNSmmtvDPHQR 280
Cdd:cd05588 216 VILEKPIRIPRslSVKAASVLKGFLNK----NPAER 247
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-235 6.91e-10

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 58.75  E-value: 6.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA-QREADMHRLFNHPNILRLvayclrerGAKHEA- 94
Cdd:cd14169   2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMvENEIAVLRRINHENIVSL--------EDIYESp 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 ---WLLLPFFKRGTLWNeieRLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTN-----------ILLGDEG 160
Cdd:cd14169  74 thlYLAMELVTGGELFD---RIIERGSY-TEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENllyatpfedskIMISDFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 161 QPVLMDLGSMNQACihvegsrqaltlqdwaaqrCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14169 150 LSKIEAQGMLSTAC-------------------GTPGYVAPELLEQKPY---GKAVDVWAIGVISYILLCGYPPF 202
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
43-232 8.12e-10

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 58.77  E-value: 8.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  43 GHFYALKRILCHEQqdRE----EAQREADMHRLFNHPNILRLvayclRE--RGAKHEA-WLLLPFFkrgtlwnEIErLKD 115
Cdd:cd07843  30 GEIVALKKLKMEKE--KEgfpiTSLREINILLKLQHPNIVTV-----KEvvVGSNLDKiYMVMEYV-------EHD-LKS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 116 -----KGNFLTEdQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihVEGSRQALTLqdwa 190
Cdd:cd07843  95 lmetmKQPFLQS-EVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE----YGSPLKPYTQ---- 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 46577677 191 aQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVlyammFGE 232
Cdd:cd07843 166 -LVVTLWYRAPELLLGAKE--YSTAIDMWSVGCI-----FAE 199
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
22-281 8.18e-10

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: 58.58  E-value: 8.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVdlveglHDGHFYALKRILCHE-----------QQDREEAQREADMHRLFNHPNILRLVAYCLRERGA 90
Cdd:cd05057  11 KGKVLGSGAFGTV------YKGVWIPEGEKVKIPvaikvlreetgPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  91 kheawLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-- 168
Cdd:cd05057  85 -----LITQLMPLGCL---LDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGla 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 ---SMNQACIHVEGSRQALTlqdWAAQRCtISYRapeLFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDMVfqKGDS 244
Cdd:cd05057 157 kllDVDEKEYHAEGGKVPIK---WMALES-IQYR---IYTHKS--------DVWSYGVTVWELMtFGAKPYEGI--PAVE 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 245 VALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05057 220 IPDLLEKGERLPQPPICTIDVYMVLVKCWMIDAESRP 256
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
65-288 9.74e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 58.73  E-value: 9.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   65 EADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPFFKRGT---LWNEIERLKDKGNFLTEDQILwlllgicRGLEAIHA 141
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVS----GAITCMVLPHYSSDLytyLTKRSRPLPIDQALIIEKQIL-------EGLRYLHA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  142 KGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQRCTISYRAPELFSVQSHcviDERTDVWSL 221
Cdd:PHA03209 176 QRIIHRDVKTENIFINDVDQVCIGDLGA----------AQFPVVAPAFLGLAGTVETNAPEVLARDKY---NSKADIWSA 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  222 GCVLYAMM-FGEGPYDMVFQKGDSVALAVQNQL------------SIPQSP---------RHSSALRQ------------ 267
Cdd:PHA03209 243 GIVLFEMLaYPSTIFEDPPSTPEEYVKSCHSHLlkiistlkvhpeEFPRDPgsrlvrgfiEYASLERQpytrypcfqrvn 322
                        250       260
                 ....*....|....*....|....*...
gi 46577677  268 -------LLNSMMTVDPHQRPHIPLLLS 288
Cdd:PHA03209 323 lpidgefLVHKMLTFDAAMRPSAEEILN 350
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
64-283 1.16e-09

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 57.69  E-value: 1.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRLvaYCLRErGAKHEAWLLLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKG 143
Cdd:cd14163  49 RELQIVERLDHKNIIHV--YEMLE-SADGKIYLVMELAEDGDVFDCVL----HGGPLPEHRAKALFRQLVEAIRYCHGCG 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 144 YAHRDLKPTNILLgdEGQPV-LMDLGSMNQacihVEGSRQALTlQDWAAqrcTISYRAPELFSVQSHcviDERT-DVWSL 221
Cdd:cd14163 122 VAHRDLKCENALL--QGFTLkLTDFGFAKQ----LPKGGRELS-QTFCG---STAYAAPEVLQGVPH---DSRKgDIWSM 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 222 GCVLYAMMFGEGPYD------MVFQKgdsvalavQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14163 189 GVVLYVMLCAQLPFDdtdipkMLCQQ--------QKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSI 248
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
26-235 1.17e-09

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: 58.17  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYA---LKRILCHEQQDREEAQREADMHRL-FNHPNILRLvaYCLRErgAKHEAWLLLPFF 101
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAikaLKKDVVLEDDDVECTMIERRVLALaSQHPFLTHL--FCTFQ--TESHLFFVMEYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIErlkDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQaciHVEGSR 181
Cdd:cd05592  79 NGGDLMFHIQ---QSGRF-DEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKE---NIYGEN 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 182 QALTLqdwaaqrC-TISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05592 152 KASTF-------CgTPDYIAPEILKGQKY---NQSVDWWSFGVLLYEMLIGQSPF 196
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
26-225 1.21e-09

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: 57.90  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEqqdrEEAQR----EADMHRLFNHPNILRLVAYCLRERGAKheawLLLPFF 101
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFD----EEAQRnflkEVKVMRSLDHPNVLKFIGVLYKDKKLN----LITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGSR 181
Cdd:cd14154  73 PGGTLK---DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFG---LARLIVEERL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 182 QALTLQDWAAQRCTIS--------------YRAPELFSVQSHcviDERTDVWSLGCVL 225
Cdd:cd14154 147 PSGNMSPSETLRHLKSpdrkkrytvvgnpyWMAPEMLNGRSY---DEKVDIFSFGIVL 201
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
52-292 1.23e-09

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 58.01  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  52 LCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrergakHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLG 131
Cdd:cd14000  47 ATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGI------HPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQ 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLM-----DLGSMNQACihVEGsrqALTLQDwaaqrcTISYRAPELfsV 206
Cdd:cd14000 121 VADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAIiikiaDYGISRQCC--RMG---AKGSEG------TPGFRAPEI--A 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 207 QSHCVIDERTDVWSLGCVLYAMMFGEGPydMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTV---DPHQRPHI 283
Cdd:cd14000 188 RGNVIYNEKVDVFSFGMLLYEILSGGAP--MVGHLKFPNEFDIHGGLRPPLKQYECAPWPEVEVLMKKCwkeNPQQRPTA 265

                ....*....
gi 46577677 284 PLLLSQLEA 292
Cdd:cd14000 266 VTVVSILNS 274
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
17-283 1.38e-09

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: 58.15  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALK--RILCHEQQDREE-----AQREADMHRLFNHPNILRLVAYClrerG 89
Cdd:cd14041   5 NDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihQLNKNWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYF----S 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHEAWLLLPFFKRGtlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHA--KGYAHRDLKPTNILLGDE---GQPVL 164
Cdd:cd14041  81 LDTDSFCTVLEYCEG---NDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGtacGEIKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 165 MDLGSMNQACIHVEGSRQALTLQDWAAQrcTISYRAPELFSV-QSHCVIDERTDVWSLGCVLYAMMFGEGPY-------D 236
Cdd:cd14041 158 TDFGLSKIMDDDSYNSVDGMELTSQGAG--TYWYLPPECFVVgKEPPKISNKVDVWSVGVIFYQCLYGRKPFghnqsqqD 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 237 MVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLN---------SMMTVDPHQRPHI 283
Cdd:cd14041 236 ILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAyrkedridvQQLACDPYLLPHI 291
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
33-222 1.70e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 57.69  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  33 YVDLVEGLHDGHFYALKRILChEQQDREEA---QREADMHRLFNHPNILRLVAYCLrergAKHEAWLLLPFFKRGTLWNE 109
Cdd:cd08216  15 VVHLAKHKPTNTLVAVKKINL-ESDSKEDLkflQQEILTSRQLQHPNILPYVTSFV----VDNDLYVVTPLMAYGSCRDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 110 IERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM--------NQACIHvEGSR 181
Cdd:cd08216  90 LKTHFPEG--LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAysmvkhgkRQRVVH-DFPK 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 46577677 182 QALTLQDWAaqrctisyrAPELFSvQSHCVIDERTDVWSLG 222
Cdd:cd08216 167 SSEKNLPWL---------SPEVLQ-QNLLGYNEKSDIYSVG 197
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
43-232 2.08e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 57.76  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  43 GHFYALKRILCHEQQDREEAQ-----------READMHRLFNHPNILRLVAYCLRErgAKHEAWLLLPFFKRgTLWNEIE 111
Cdd:cd07868  31 GHVYKAKRKDGKDDKDYALKQiegtgismsacREIALLRELKHPNVISLQKVFLSH--ADRKVWLLFDYAEH-DLWHIIK 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 112 -----RLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG-QPVLMDLGSMNQACIHvegSRQALT 185
Cdd:cd07868 108 fhrasKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLF---NSPLKP 184
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 186 LQDWAAQRCTISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd07868 185 LADLDPVVVTFWYRAPELLLGARH--YTKAIDIWAIGCIFAELLTSE 229
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
26-292 2.19e-09

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: 56.94  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSyvDLVEG-LHDGHFYALKRilCHEQQDREEAQR---EADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPFF 101
Cdd:cd05085   4 LGKGNFG--EVYKGtLKDKTPVAVKT--CKEDLPQELKIKflsEARILKQYDHPNIVKLIGVCTQ----RQPIYIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSR 181
Cdd:cd05085  76 PGGDFLSFLRKKKDE---LKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 182 qaltlqdwAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLY-AMMFGEGPYDMVFQKGDSVALAVQNQLSIPQspR 260
Cdd:cd05085 153 --------GLKQIPIKWTAPEALNYGRY---SSESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKGYRMSAPQ--R 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 46577677 261 HSSALRQLLNSMMTVDPHQRPHIPLLLSQLEA 292
Cdd:cd05085 220 CPEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
26-284 2.25e-09

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: 57.12  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFyALKRILC-HEQQDREEAQ-READMHRLFNHPNILRLVAYCLRERGAKheawLLLPFFKR 103
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGLV-VLKTVYTgPNCIEHNEALlEEGKMMNRLRHSRVVKLLGVILEEGKYS----LVMEYMEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWNEIER----LKDKGNFLTEdqilwlllgICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---SMNQACIH 176
Cdd:cd14027  76 GNLMHVLKKvsvpLSVKGRIILE---------IIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasFKMWSKLT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAAQRC-TISYRAPE-LFSVQSHCVidERTDVWSLGCVLYAMMFGEGPYDMVFQKgDSVALAVQN--- 251
Cdd:cd14027 147 KEEHNEQREVDGTAKKNAgTLYYMAPEhLNDVNAKPT--EKSDVYSFAIVLWAIFANKEPYENAINE-DQIIMCIKSgnr 223
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46577677 252 ---QLSIPQSPRHssaLRQLLNSMMTVDPHQRPHIP 284
Cdd:cd14027 224 pdvDDITEYCPRE---IIDLMKLCWEANPEARPTFP 256
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
62-296 2.75e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 57.42  E-value: 2.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  62 AQREADMHRLFNHPNILRLVAYCLRERGAK--HEAWLLLPFFKrGTLWNEIERLKDkgnfltEDQILWLLLGICRGLEAI 139
Cdd:cd07850  46 AYRELVLMKLVNHKNIIGLLNVFTPQKSLEefQDVYLVMELMD-ANLCQVIQMDLD------HERMSYLLYQMLCGIKHL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 140 HAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcihvegsRQALTLQDWAAQRctiSYRAPElfsvqshcVI-----DE 214
Cdd:cd07850 119 HSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-------GTSFMMTPYVVTR---YYRAPE--------VIlgmgyKE 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 215 RTDVWSLGCVLYAM-----MF----------------GEGPYDMVFQKGDSVALAVQNQ---------------LSIPQS 258
Cdd:cd07850 181 NVDIWSVGCIMGEMirgtvLFpgtdhidqwnkiieqlGTPSDEFMSRLQPTVRNYVENRpkyagysfeelfpdvLFPPDS 260
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 46577677 259 PRHS----SALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07850 261 EEHNklkaSQARDLLSKMLVIDPEKR------ISVDDALQHP 296
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
25-236 2.88e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 57.12  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVdlVEGLHDGHFYALKRIL----CHEQQDREEAQREADMHRLFNHPNILRLVAYclRERGAKHeaWLLLPF 100
Cdd:cd14158  22 KLGEGGFGVV--FKGYINDKNVAVKKLAamvdISTEDLTKQFEQEIQVMAKCQHENLVELLGY--SCDGPQL--CLVYTY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLwneIERL--KDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQAcihve 178
Cdd:cd14158  96 MPNGSL---LDRLacLNDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARAS----- 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 gSRQALTLQdwaAQRC--TISYRAPELFSVQshcvIDERTDVWSLGCVLYAMMFGEGPYD 236
Cdd:cd14158 168 -EKFSQTIM---TERIvgTTAYMAPEALRGE----ITPKSDIFSFGVVLLEIITGLPPVD 219
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
65-281 3.00e-09

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 56.48  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  65 EADMHRLFNHPNILRLVAYCLRergaKHEAWLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGY 144
Cdd:cd05084  44 EARILKQYSHPNIVRLIGVCTQ----KQPIYIVMELVQGGDF---LTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHC 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 145 AHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALtlqdwaaQRCTISYRAPELFSVQSHcviDERTDVWSLGCV 224
Cdd:cd05084 117 IHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATGGM-------KQIPVKWTAPEALNYGRY---SSESDVWSFGIL 186
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 225 LY-AMMFGEGPYDMVFQKGDSVALAVQNQLSIP-QSPrhsSALRQLLNSMMTVDPHQRP 281
Cdd:cd05084 187 LWeTFSLGAVPYANLSNQQTREAVEQGVRLPCPeNCP---DEVYRLMEQCWEYDPRKRP 242
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
120-269 3.11e-09

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 57.38  E-value: 3.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACihvegsrqALTLQDWAAQRCTISYR 199
Cdd:cd05633 105 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLG---LAC--------DFSKKKPHASVGTHGYM 173
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 200 APELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKG----DSVALAVQNQLSIPQSPRHSSALRQLL 269
Cdd:cd05633 174 APEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheiDRMTLTVNVELPDSFSPELKSLLEGLL 245
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
18-235 3.14e-09

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 56.58  E-value: 3.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREE-AQREADMHRLFNHPNILRLVayclRERGAKHEAWL 96
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHlIENEVSILRRVKHPNIIMLI----EEMDTPAELYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIErlkdKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGD--EGQPVLmDLGSMNQAC 174
Cdd:cd14184  77 VMELVKGGDLFDAIT----SSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypDGTKSL-KLGDFGLAT 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 175 IhVEGSRQALtlqdwaaqrC-TISYRAPELFSVQSHCVideRTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14184 152 V-VEGPLYTV---------CgTPTYVAPEIIAETGYGL---KVDIWAAGVITYILLCGFPPF 200
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
146-288 3.24e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 56.60  E-value: 3.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 146 HRDLKPTNILLGDEGQPVLMDLGSMNQacihvegsrqaltLQDWAAQR----CTiSYRAPE-LFSVQSHCVIDERTDVWS 220
Cdd:cd06616 133 HRDVKPSNILLDRNGNIKLCDFGISGQ-------------LVDSIAKTrdagCR-PYMAPErIDPSASRDGYDVRSDVWS 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 221 LGCVLYAMMFGEGPY---DMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd06616 199 LGITLYEVATGKFPYpkwNSVFDQLTQVVKGDPPILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLK 269
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
26-293 3.51e-09

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: 56.38  E-value: 3.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKRILCHEQQDREEAQ---READMHRLFNHPNILRLVAYCLRErgAKHEAwLLLPFFK 102
Cdd:cd14064   1 IGSGSFGKV--YKGRCRNKIVAIKRYRANTYCSKSDVDmfcREVSILCRLNHPCVIQFVGACLDD--PSQFA-IVTQYVS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLW---NEIERLKDKGNFLTedqilwLLLGICRGLEAIH--AKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihv 177
Cdd:cd14064  76 GGSLFsllHEQKRVIDLQSKLI------IAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGE-------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 egSR--QALTLQDWAAQRCTISYRAPELFSVQSHCVIdeRTDVWSLGCVLYAMMFGEGPY----------DMVFQKGdsv 245
Cdd:cd14064 142 --SRflQSLDEDNMTKQPGNLRWMAPEVFTQCTRYSI--KADVFSYALCLWELLTGEIPFahlkpaaaaaDMAYHHI--- 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 246 alavqnQLSIPQS-PRHSSAlrqLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14064 215 ------RPPIGYSiPKPISS---LLMRGWNAEPESRPSFVEIVALLEPC 254
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
46-232 3.77e-09

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 57.00  E-value: 3.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  46 YALKRIlcHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheAWLLLPFFKRgTLWNEIE-----RLKDKGNFL 120
Cdd:cd07867  32 YALKQI--EGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRK--VWLLFDYAEH-DLWHIIKfhrasKANKKPMQL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 121 TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG-QPVLMDLGSMNQACIHvegSRQALTLQDWAAQRCTISYR 199
Cdd:cd07867 107 PRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLF---NSPLKPLADLDPVVVTFWYR 183
                       170       180       190
                ....*....|....*....|....*....|...
gi 46577677 200 APELFSVQSHcvIDERTDVWSLGCVLYAMMFGE 232
Cdd:cd07867 184 APELLLGARH--YTKAIDIWAIGCIFAELLTSE 214
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
26-281 3.84e-09

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: 56.19  E-value: 3.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCH---EQQDREEAQREADMHRLFNHPNIlRLVAY--CLRERGAKHEAwLLLPF 100
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGRELAVKQVPFDpdsQETSKEVNALECEIQLLKNLRHD-RIVQYygCLRDPEEKKLS-IFVEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 FKRGTLWNEierLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS---MNQACIHV 177
Cdd:cd06653  88 MPGGSVKDQ---LKAYGA-LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAskrIQTICMSG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 178 EGSRQALTLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYDMVfqKGDSVALAVQNQLSIPQ 257
Cdd:cd06653 164 TGIKSVTGTPYWM---------SPEVISGEGY---GRKADVWSVACTVVEMLTEKPPWAEY--EAMAAIFKIATQPTKPQ 229
                       250       260
                ....*....|....*....|....*
gi 46577677 258 SPRH-SSALRQLLNSMMtVDPHQRP 281
Cdd:cd06653 230 LPDGvSDACRDFLRQIF-VEEKRRP 253
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
18-294 4.25e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 56.44  E-value: 4.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYL-FIQKLGEGGFSYVDLVE----GLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLrERGaKH 92
Cdd:cd05081   3 ERHLkYISQLGKGNFGSVELCRydplGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSY-GPG-RR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd05081  81 SLRLVMEYLPSGCLR---DFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 acihVEGSRQALTLQDwaAQRCTISYRAPELFsvqSHCVIDERTDVWSLGCVLYA-----------------MMFGEGPY 235
Cdd:cd05081 158 ----LPLDKDYYVVRE--PGQSPIFWYAPESL---SDNIFSRQSDVWSFGVVLYElftycdkscspsaeflrMMGCERDV 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 236 DMVFqkgdSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd05081 229 PALC----RLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLW 283
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
120-235 4.52e-09

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 56.96  E-value: 4.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsMNQACI---HVEGSRQALT-LQDWAAQRCT 195
Cdd:cd05600 108 LSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFG-LASGTLspkKIESMKIRLEeVKNTAFLELT 186
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 196 ISYR-------------------------APELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05600 187 AKERrniyramrkedqnyansvvgspdymAPEVLRGEGY---DLTVDYWSLGCILFECLVGFPPF 248
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
25-291 4.60e-09

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 55.75  E-value: 4.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVdlVEGLHDGHFYALKRILCHEQQDREEAQREAD-MHRLfNHPNILRLVAYCLRERgakheawlllPFF-- 101
Cdd:cd05034   2 KLGAGQFGEV--WMGVWNGTTKVAVKTLKPGTMSPEAFLQEAQiMKKL-RHDKLVQLYAVCSDEE----------PIYiv 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 ----KRGTLwneIERLK-DKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDegqpvlmdlgsmNQACiH 176
Cdd:cd05034  69 telmSKGSL---LDYLRtGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGE------------NNVC-K 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQD--WAAQRCT---ISYRAPEL-----FSVQShcvidertDVWSLGCVLYAMM-FGEGPYD-MVfqkGDS 244
Cdd:cd05034 133 VADFGLARLIEDdeYTAREGAkfpIKWTAPEAalygrFTIKS--------DVWSFGILLYEIVtYGRVPYPgMT---NRE 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 245 VALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05034 202 VLEQVERGYRMPKPPGCPDELYDIMLQCWKKEPEERPTFEYLQSFLE 248
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
19-168 5.39e-09

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 55.73  E-value: 5.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrilcheqqdreeaqreadMHRLFNHPNILRLVAYCLRE-RGAKHEAWLL 97
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMK------------------VESKSQPKQVLKMEVAVLKKlQGKPHFCRLI 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LpfFKRGTLWN---------EIERLKDKGN--FLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG----DEGQP 162
Cdd:cd14017  63 G--CGRTERYNyivmtllgpNLAELRRSQPrgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGrgpsDERTV 140

                ....*.
gi 46577677 163 VLMDLG 168
Cdd:cd14017 141 YILDFG 146
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
26-239 5.72e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 56.16  E-value: 5.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQD--REEAQREADMHRLFNHPNILRLvAYCLRERGakhEAWLLLPFFKR 103
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEevKETTLRELKMLRTLKQENIVEL-KEAFRRRG---KLYLVFEYVEK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 gtlwNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACihvEGSRQA 183
Cdd:cd07848  85 ----NMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLS---EGSNAN 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 184 LTlqDWAAQRCtisYRAPELFSVQSHcviDERTDVWSLGCVLYAM-----MF-GEGPYDMVF 239
Cdd:cd07848 158 YT--EYVATRW---YRSPELLLGAPY---GKAVDMWSVGCILGELsdgqpLFpGESEIDQLF 211
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
20-283 5.77e-09

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 55.64  E-value: 5.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIlcheqqDREEAQ---------READMHRLFNHPNILRLVA-------- 82
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIV------DRRRASpdfvqkflpRELSILRRVNHPNIVQMFEcievangr 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  83 -YCLRERGAKHeawlllpffkrgtLWNEIERLKDKGNFLTEDqilwLLLGICRGLEAIHAKGYAHRDLKPTNILL-GDEG 160
Cdd:cd14164  76 lYIVMEAAATD-------------LLQKIQEVHHIPKDLARD----MFAQMVGAVNYLHDMNIVHRDLKCENILLsADDR 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 161 QPVLMDLGSmnqacihvegSRQALTLQDWAAQRC-TISYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGEGPYDmvf 239
Cdd:cd14164 139 KIKIADFGF----------ARFVEDYPELSTTFCgSRAYTPPEVILGTPY--DPKKYDVWSLGVVLYVMVTGTMPFD--- 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 240 qkGDSVALAVQNQ--LSIPQSPRHSSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd14164 204 --ETNVRRLRLQQrgVLYPSGVALEEPCRALIRTLLQFNPSTRPSI 247
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
132-280 6.35e-09

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 56.21  E-value: 6.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACihvegsrqALTLQDWAAQRCTISYRAPELfsVQSHCV 211
Cdd:cd14223 112 IILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLG---LAC--------DFSKKKPHASVGTHGYMAPEV--LQKGVA 178
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 212 IDERTDVWSLGCVLYAMMFGEGPYDMVFQKG----DSVALAVQNQLSIPQSPRhssaLRQLLNSMMTVDPHQR 280
Cdd:cd14223 179 YDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheiDRMTLTMAVELPDSFSPE----LRSLLEGLLQRDVNRR 247
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
26-287 6.45e-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: 55.82  E-value: 6.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRIlcheQQDREEAQREADMHRLFNHPNIL------RLVAY--CLRERGAKHEAwLL 97
Cdd:cd06652  10 LGQGAFGRVYLCYDADTGRELAVKQV----QFDPESPETSKEVNALECEIQLLknllheRIVQYygCLRDPQERTLS-IF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEierLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGS---MNQAC 174
Cdd:cd06652  85 MEYMPGGSIKDQ---LKSYGA-LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGAskrLQTIC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 175 IHVEGSRQALTLQDWAaqrctisyrAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVaLAVQNQLS 254
Cdd:cd06652 161 LSGTGMKSVTGTPYWM---------SPEVISGEGY---GRKADIWSVGCTVVEMLTEKPPW-AEFEAMAAI-FKIATQPT 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 46577677 255 IPQSPRH-SSALRQLLNSMMtVDPHQRPHIPLLL 287
Cdd:cd06652 227 NPQLPAHvSDHCRDFLKRIF-VEAKLRPSADELL 259
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
60-296 6.74e-09

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 56.01  E-value: 6.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  60 EEAQREADMHRLFNHPNILRLvaycLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAI 139
Cdd:cd14094  50 EDLKREASICHMLKHPHIVEL----LETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYC 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 140 HAKGYAHRDLKPTNILLGDEGqpvlmdlgsmNQACIHVEGSRQALTLQDWAAQRC----TISYRAPElfsvqshcVIDER 215
Cdd:cd14094 126 HDNNIIHRDVKPHCVLLASKE----------NSAPVKLGGFGVAIQLGESGLVAGgrvgTPHFMAPE--------VVKRE 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 216 -----TDVWSLGCVLYAMMFGEGPYdmVFQKGDSVALAVQNQLSI--PQSPRHSSALRQLLNSMMTVDPHQRphipllLS 288
Cdd:cd14094 188 pygkpVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGKYKMnpRQWSHISESAKDLVRRMLMLDPAER------IT 259

                ....*...
gi 46577677 289 QLEALQPP 296
Cdd:cd14094 260 VYEALNHP 267
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
60-281 9.02e-09

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 55.80  E-value: 9.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  60 EEAQREADMHRLFNHPNILRLVAYCLRErgAKHEAWLLLPFfkrGTLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAI 139
Cdd:cd05108  54 KEILDEAYVMASVDNPHVCRLLGICLTS--TVQLITQLMPF---GCLLDYVREHKDN---IGSQYLLNWCVQIAKGMNYL 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 140 HAKGYAHRDLKPTNILLGDEGQPVLMDLG-----SMNQACIHVEGSRQALTlqdWAAQRCTIsyrapelfsvqsHCVIDE 214
Cdd:cd05108 126 EDRRLVHRDLAARNVLVKTPQHVKITDFGlakllGAEEKEYHAEGGKVPIK---WMALESIL------------HRIYTH 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 215 RTDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05108 191 QSDVWSYGVTVWELMtFGSKPYDGI--PASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRP 256
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
54-293 9.24e-09

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 55.36  E-value: 9.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREADMHRLFNHPNILRLVAYCLRergAKHEAwLLLPFFKRGTLWNEIerlKDKGNFLTEDQILWLLLGIC 133
Cdd:cd14152  35 NNQDHLKLFKKEVMNYRQTRHENVVLFMGACMH---PPHLA-IITSFCKGRTLYSFV---RDPKTSLDINKTRQIAQEII 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 134 RGLEAIHAKGYAHRDLKPTNILLgDEGQPVLMDLGSMNQACIHVEGSRQ-ALTL-QDWaaqrctISYRAPELF-----SV 206
Cdd:cd14152 108 KGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLFGISGVVQEGRREnELKLpHDW------LCYLAPEIVremtpGK 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 207 QSHCV-IDERTDVWSLGCVLYAMMFGEGPYD------MVFQKGDSVALAvqnqlSIPQSPRHSSALRQLLNSMMTVDPHQ 279
Cdd:cd14152 181 DEDCLpFSKAADVYAFGTIWYELQARDWPLKnqpaeaLIWQIGSGEGMK-----QVLTTISLGKEVTEILSACWAFDLEE 255
                       250
                ....*....|....
gi 46577677 280 RPHIPLLLSQLEAL 293
Cdd:cd14152 256 RPSFTLLMDMLEKL 269
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
26-280 9.43e-09

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 55.65  E-value: 9.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQR---EADMHRLFNHPNILRLvAYCLRergAKHEAWLLLPFFK 102
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHtlaERTVLAQVDCPFIVPL-KFSFQ---SPEKLYLVLAFIN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RGTLWNEIERlkdKGNFLTEDQILWLLLGICrGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACihvegsRQ 182
Cdd:cd05585  78 GGELFHHLQR---EGRFDLSRARFYTAELLC-ALECLHKFNVIYRDLKPENILLDYTGHIALCDFG----LC------KL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 ALTLQDWAAQRC-TISYRAPELFSVQSHCvidERTDVWSLGCVLYAMMFGEGPY-----DMVFQKgdsvalAVQNQLSIP 256
Cdd:cd05585 144 NMKDDDKTNTFCgTPEYLAPELLLGHGYT---KAVDWWTLGVLLYEMLTGLPPFydentNEMYRK------ILQEPLRFP 214
                       250       260
                ....*....|....*....|....
gi 46577677 257 QSPRHSSalRQLLNSMMTVDPHQR 280
Cdd:cd05585 215 DGFDRDA--KDLLIGLLNRDPTKR 236
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
59-226 1.42e-08

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: 54.76  E-value: 1.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  59 REEAQ--READMHR--LFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICR 134
Cdd:cd14143  29 REERSwfREAEIYQtvMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNR-----YTVTVEGMIKLALSIAS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAK--------GYAHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGSRqalTLQDWAAQRC-TISYRAPELF- 204
Cdd:cd14143 104 GLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLG---LAVRHDSATD---TIDIAPNHRVgTKRYMAPEVLd 177
                       170       180
                ....*....|....*....|....*
gi 46577677 205 ---SVQSHCVIdERTDVWSLGCVLY 226
Cdd:cd14143 178 dtiNMKHFESF-KRADIYALGLVFW 201
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-294 1.46e-08

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 54.66  E-value: 1.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFY--ALKRI--LCHEQQDREEAQREADMHRLFNHPNILRLVAYClRERGAKHEAWLLLPF- 100
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMdaAIKRMkeYASKDDHRDFAGELEVLCKLGHHPNIINLLGAC-EHRGYLYLAIEYAPHg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 101 ----FKRGTLWNEIERLKDKGN----FLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd05047  82 nlldFLRKSRVLETDPAFAIANstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 ACIHVEGSRQALTLQdWAAqrctisyrapelFSVQSHCVIDERTDVWSLGCVLYAMM-FGEGPYdmvfqKGDSVALAVQN 251
Cdd:cd05047 162 QEVYVKKTMGRLPVR-WMA------------IESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPY-----CGMTCAELYEK 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 252 qlsIPQSPRHSSALR------QLLNSMMTVDPHQRPHIPLLLSQLEALQ 294
Cdd:cd05047 224 ---LPQGYRLEKPLNcddevyDLMRQCWREKPYERPSFAQILVSLNRML 269
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
19-296 1.50e-08

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 55.17  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGG----FSYVDLVEGLHdghfYALKRILCHEQQDREEAQREADMHRLFNHPNILRlVAYCLRERGAKHEA 94
Cdd:cd07854   6 RYMDLRPLGCGSnglvFSAVDSDCDKR----VAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVK-VYEVLGPSGSDLTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGT------LWNEIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEgqPVLMDLG 168
Cdd:cd07854  81 DVGSLTELNSVyivqeyMETDLANVLEQGP-LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTE--DLVLKIG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQACI------HVEGSRQALTLQdWaaqrctisYRAPELFSVQSHcvIDERTDVWSLGCVLYAMMFGE----GPYDM- 237
Cdd:cd07854 158 DFGLARIvdphysHKGYLSEGLVTK-W--------YRSPRLLLSPNN--YTKAIDMWAAGCIFAEMLTGKplfaGAHELe 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 238 ----------VFQKGD------SVALAVQNQLSIPQSPrhssaLRQL-----------LNSMMTVDPHQRphipllLSQL 290
Cdd:cd07854 227 qmqlilesvpVVREEDrnellnVIPSFVRNDGGEPRRP-----LRDLlpgvnpealdfLEQILTFNPMDR------LTAE 295

                ....*.
gi 46577677 291 EALQPP 296
Cdd:cd07854 296 EALMHP 301
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
21-283 1.56e-08

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) 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 to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 54.78  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  21 LFIQKLGEGGFSYVDLVEGLH-----DGHFYALKRILCHEQQD-REEAQREADMHRLFNHPNILRLVAYClrergAKHEA 94
Cdd:cd05049   8 VLKRELGEGAFGKVFLGECYNlepeqDKMLVAVKTLKDASSPDaRKDFEREAELLTNLQHENIVKFYGVC-----TEGDP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLL-PFFKRGTLwNEIERLKD-----------KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:cd05049  83 LLMVfEYMEHGDL-NKFLRSHGpdaaflasedsAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 163 VLMDLGsMNQAC-----IHVEGSRQaLTLQdWAAQRcTISYRApelFSVQShcvidertDVWSLGCVLYAMM-FGEGPYd 236
Cdd:cd05049 162 KIGDFG-MSRDIystdyYRVGGHTM-LPIR-WMPPE-SILYRK---FTTES--------DVWSFGVVLWEIFtYGKQPW- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 237 mvFQKGDSVALAVQNQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHI 283
Cdd:cd05049 226 --FQLSNTEVIECITQGRLLQRPRTcPSEVYAVMLGCWKREPQQRLNI 271
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
24-291 1.80e-08

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: 54.15  E-value: 1.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLveGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFKR 103
Cdd:cd14203   1 VKLGQGCFGEVWM--GTWNGTTKVAIKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEE-----PIYIVTEFMSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLwneIERLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQ 182
Cdd:cd14203  74 GSL---LDFLKDgEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 183 altlqdwaAQRCTISYRAPEL-----FSVQShcvidertDVWSLGCVLYAMMF-GEGPYDMVFQKgdSVALAVQNQLSIP 256
Cdd:cd14203 151 --------GAKFPIKWTAPEAalygrFTIKS--------DVWSFGILLTELVTkGRVPYPGMNNR--EVLEQVERGYRMP 212
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 257 QSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd14203 213 CPPGCPESLHELMCQCWRKDPEERPTFEYLQSFLE 247
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
135-240 1.97e-08

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 54.33  E-value: 1.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD-----LGSMNQACIHVEGSRQALTLQDWAAQRC-TISYRAPELFSVQS 208
Cdd:cd05609 112 ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDfglskIGLMSLTTNLYEGHIEKDTREFLDKQVCgTPEYIAPEVILRQG 191
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 46577677 209 HcviDERTDVWSLGCVLYAMM------FGEGPYDMVFQ 240
Cdd:cd05609 192 Y---GKPVDWWAMGIILYEFLvgcvpfFGDTPEELFGQ 226
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-296 2.06e-08

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 54.45  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRIlcHEQQDREEAQREADMHRLFNHPNILRLVAycLRERGAkhEAWLLLPFFKR 103
Cdd:cd14085   9 SELGRGATSVVYRCRQKGTQKPYAVKKL--KKTVDKKIVRTEIGVLLRLSHPNIIKLKE--IFETPT--EISLVLELVTG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLWneiERLKDKGnFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacihveGSRQA 183
Cdd:cd14085  83 GELF---DRIVEKG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADF--------GLSKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTLQDWAAQRC-TISYRAPElfsVQSHCVIDERTDVWSLGCVLYAMMFGEGP-YDmvfQKGDSVA----LAVQNQLSIPQ 257
Cdd:cd14085 151 VDQQVTMKTVCgTPGYCAPE---ILRGCAYGPEVDMWSVGVITYILLCGFEPfYD---ERGDQYMfkriLNCDYDFVSPW 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 46577677 258 SPRHSSALRQLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd14085 225 WDDVSLNAKDLVKKLIVLDPKKR------LTTQQALQHP 257
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
23-235 2.34e-08

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: 54.27  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFS--YVDLVEGLHDGHFY---ALKRIL-CHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWL 96
Cdd:cd05032  11 IRELGQGSFGmvYEGLAKGVVKGEPEtrvAIKTVNeNASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQ----PTLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEI------ERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-- 168
Cdd:cd05032  87 VMELMAKGDLKSYLrsrrpeAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGmt 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 169 -SMNQACIHVEGSRQALtlqdwaaqrcTISYRAPElfSVQSHcVIDERTDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05032 167 rDIYETDYYRKGGKGLL----------PVRWMAPE--SLKDG-VFTTKSDVWSFGVVLWEMAtLAEQPY 222
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
50-290 2.61e-08

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: 53.77  E-value: 2.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  50 RILCHEQQDREEAQREADMHRlFNHPNILRLVAYCLRergaKHEAWLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLL 129
Cdd:cd05064  42 RAGCSDKQRRGFLAEALTLGQ-FDHSNIVRLEGVITR----GNTMMIVTEYMSNGALDSFLRKHEGQ---LVAGQLMGML 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 LGICRGLEAIHAKGYAHRDLKPTNILLgdegqpvlmdlgSMNQACiHVEGSRQaLTLQDWAAQRCTISYRAPELFS---- 205
Cdd:cd05064 114 PGLASGMKYLSEMGYVHKGLAAHKVLV------------NSDLVC-KISGFRR-LQEDKSEAIYTTMSGKSPVLWAapea 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 206 VQSHcVIDERTDVWSLGCVLYAMM-FGEGPY-DMvfqKGDSVALAVQNQLSIPqSPRH-SSALRQLLNSMMTVDPHQRP- 281
Cdd:cd05064 180 IQYH-HFSSASDVWSFGIVMWEVMsYGERPYwDM---SGQDVIKAVEDGFRLP-APRNcPNLLHQLMLDCWQKERGERPr 254
                       250
                ....*....|.
gi 46577677 282 --HIPLLLSQL 290
Cdd:cd05064 255 fsQIHSILSKM 265
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
65-291 2.89e-08

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 53.88  E-value: 2.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  65 EADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFKRGTLWNEIErlKDKGNFLTEDQILWLLLGICRGLEAIHAKGY 144
Cdd:cd05073  56 EANVMKTLQHDKLVKLHAVVTKE-----PIYIITEFMAKGSLLDFLK--SDEGSKQPLPKLIDFSAQIAEGMAFIEQRNY 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 145 AHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQaltlqdwaAQRCTISYRAPELFSVQSHCVideRTDVWSLGCV 224
Cdd:cd05073 129 IHRDLRAANILVSASLVCKIADFGLARVIEDNEYTARE--------GAKFPIKWTAPEAINFGSFTI---KSDVWSFGIL 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 225 LYAMM-FGEGPYdmvfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMM---TVDPHQRPHIPLLLSQLE 291
Cdd:cd05073 198 LMEIVtYGRIPY-----PGMSNPEVIRALERGYRMPRPENCPEELYNIMMrcwKNRPEERPTFEYIQSVLD 263
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
53-241 2.89e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 54.23  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   53 CHEQQDREE-----AQR-----EADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRGTLWneieRLKDKGNFLTE 122
Cdd:PHA03212 111 CIDNKTCEHvvikaGQRggtatEAHILRAINHPSIIQLKGTFTYNK----FTCLILPRYKTDLYC----YLAAKRNIAIC 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  123 DqILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRQalTLQDWAAqrcTISYRAPE 202
Cdd:PHA03212 183 D-ILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGA---ACFPVDINAN--KYYGWAG---TIATNAPE 253
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 46577677  203 LFSVQSHcviDERTDVWSLGCVLYAMMFGEgpyDMVFQK 241
Cdd:PHA03212 254 LLARDPY---GPAVDIWSAGIVLFEMATCH---DSLFEK 286
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
125-229 3.29e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 54.31  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  125 ILWLLLGICRGL----EAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacIHVEGSRQALTLqDWAAqrcTISYRA 200
Cdd:PHA03210 265 LLKQTRAIMKQLlcavEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTA----MPFEKEREAFDY-GWVG---TVATNS 336
                         90       100
                 ....*....|....*....|....*....
gi 46577677  201 PELFSVQSHCVIderTDVWSLGCVLYAMM 229
Cdd:PHA03210 337 PEILAGDGYCEI---TDIWSCGLILLDML 362
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
25-292 3.46e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 53.82  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGLH-----DGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLP 99
Cdd:cd05092  12 ELGEGAFGKVFLAECHNllpeqDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGE----PLIMVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLwNEIER-------LKDKGNF-----LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd05092  88 YMRHGDL-NRFLRshgpdakILDGGEGqapgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GsMNQACIHVE----GSRQALTLQdWAAQRcTISYRApelFSVQShcvidertDVWSLGCVLYAMM-FGEGPYdmvFQKG 242
Cdd:cd05092 167 G-MSRDIYSTDyyrvGGRTMLPIR-WMPPE-SILYRK---FTTES--------DIWSFGVVLWEIFtYGKQPW---YQLS 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 243 DSVALAVQNQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLSQLEA 292
Cdd:cd05092 230 NTEAIECITQGRELERPRTcPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
23-162 4.62e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 53.10  E-value: 4.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFSYV-DLVEGLhDGHFYALKRIL--CHEQQDREEAQREADMHR-LFNHPNILRLvayclrergakHEAW--- 95
Cdd:cd14138  10 LEKIGSGEFGSVfKCVKRL-DGCIYAIKRSKkpLAGSVDEQNALREVYAHAvLGQHSHVVRY-----------YSAWaed 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677  96 --LLL--PFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQP 162
Cdd:cd14138  78 dhMLIqnEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSIP 148
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
93-235 4.71e-08

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: 53.02  E-value: 4.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRGTLWNEIerLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE---GQPVLMDLGs 169
Cdd:cd14197  83 EMILVLEYAAGGEIFNQC--VADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFG- 159
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 170 MNQACIHVEGSRQALTlqdwaaqrcTISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14197 160 LSRILKNSEELREIMG---------TPEYVAPEILSYEP---ISTATDMWSIGVLAYVMLTGISPF 213
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
57-236 5.25e-08

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 53.12  E-value: 5.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQREADMHRL--FNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICR 134
Cdd:cd14141  29 QDKLSWQNEYEIYSLpgMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSLTDYL-----KANVVSWNELCHIAQTMAR 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 135 GLEAIHAK----------GYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHVEGSRQAltlQDWAAQRCTISYRAPELF 204
Cdd:cd14141 104 GLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFG----LALKFEAGKSA---GDTHGQVGTRRYMAPEVL 176
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 46577677 205 SVQSHCVIDE--RTDVWSLGCVLYAM----MFGEGPYD 236
Cdd:cd14141 177 EGAINFQRDAflRIDMYAMGLVLWELasrcTASDGPVD 214
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
26-225 6.53e-08

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: 6.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKR-ILCHEQQDreeAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFFKRG 104
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKElKRFDEQRS---FLKEVKLMRRLSHPNILRFIGVCVKDN----KLNFITEYVNGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLWneiERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ---PVLMDLGSMNQACIH--VEG 179
Cdd:cd14065  74 TLE---ELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRgrnAVVADFGLAREMPDEktKKP 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 180 SRQ-ALTLQDWAaqrctiSYRAPELFSVQSHcviDERTDVWSLGCVL 225
Cdd:cd14065 151 DRKkRLTVVGSP------YWMAPEMLRGESY---DEKVDVFSFGIVL 188
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
16-238 7.42e-08

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 52.93  E-value: 7.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  16 DNKRYLFIQKLGEGGFSYVdlVEGLHDGHFY--ALKrILCHEQQDReeAQREAD-MHRLFNHPNILRLVAyCLRERGAKH 92
Cdd:cd14132  16 SQDDYEIIRKIGRGKYSEV--FEGINIGNNEkvVIK-VLKPVKKKK--IKREIKiLQNLRGGPNIVKLLD-VVKDPQSKT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAwLLLPFFkrgtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV-LMDLG--- 168
Cdd:cd14132  90 PS-LIFEYV-------NNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLrLIDWGlae 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 --SMNQA-CIHVeGSRQaltlqdwaaqrctisYRAPE-LFSVQSHcviDERTDVWSLGCVLYAMMF-------GEGPYDM 237
Cdd:cd14132 162 fyHPGQEyNVRV-ASRY---------------YKGPElLVDYQYY---DYSLDMWSLGCMLASMIFrkepffhGHDNYDQ 222

                .
gi 46577677 238 V 238
Cdd:cd14132 223 L 223
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
20-235 7.93e-08

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 53.09  E-value: 7.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEA---QREADMHRLFNHPNILRLVaYCLRErgaKHEAWL 96
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVahvKAERDILAEADNEWVVKLY-YSFQD---KDNLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGIcrglEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-------- 168
Cdd:cd05626  79 VMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAI----ESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGlctgfrwt 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 ---SMNQACIHVE------------------GSRqALTLQDWAA---QRC-------TISYRAPELFSVQSHCvidERTD 217
Cdd:cd05626 155 hnsKYYQKGSHIRqdsmepsdlwddvsncrcGDR-LKTLEQRATkqhQRClahslvgTPNYIAPEVLLRKGYT---QLCD 230
                       250
                ....*....|....*...
gi 46577677 218 VWSLGCVLYAMMFGEGPY 235
Cdd:cd05626 231 WWSVGVILFEMLVGQPPF 248
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
120-296 8.87e-08

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 52.82  E-value: 8.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqaCIHVEGSRQALTLqdwAAQRCTISYR 199
Cdd:cd07853 100 LSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFG-----LARVEEPDESKHM---TQEVVTQYYR 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELFSVQSHcvIDERTDVWSLGCVlYAMMFG-------EGP---YDMVF---------QKGDSVALAVQNQLSIPQSPR 260
Cdd:cd07853 172 APEILMGSRH--YTSAVDIWSVGCI-FAELLGrrilfqaQSPiqqLDLITdllgtpsleAMRSACEGARAHILRGPHKPP 248
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 261 HSSALR-----------QLLNSMMTVDPHQRphipllLSQLEALQPP 296
Cdd:cd07853 249 SLPVLYtlssqatheavHLLCRMLVFDPDKR------ISAADALAHP 289
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
19-281 9.29e-08

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 52.56  E-value: 9.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQRE----ADMHRlfNHPNILRLvAYCLRERGAKheA 94
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREfwalSSIQR--QHPNVIQL-EECVLQRDGL--A 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLKDKGNFLTEDQ---ILWLLLGICRG---------------------------LEAIHAKGY 144
Cdd:cd13977  76 QRMSHGSSKSDLYLLLVETSLKGERCFDPRsacYLWFVMEFCDGgdmneyllsrrpdrqtntsfmlqlssaLAFLHRNQI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 145 AHRDLKPTNILLGD-EGQPVL--MDLGsMNQAC--IHVEGSRQALTLQDWAAQRC-TISYRAPELFsvQSHcvIDERTDV 218
Cdd:cd13977 156 VHRDLKPDNILISHkRGEPILkvADFG-LSKVCsgSGLNPEEPANVNKHFLSSACgSDFYMAPEVW--EGH--YTAKADI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 219 WSLGCVLYAMM----FGE--------GPYdmVFQKGDSVALA---VQN---QLSIPQSPRHS--SALRQLLNSMMTVDPH 278
Cdd:cd13977 231 FALGIIIWAMVeritFRDgetkkellGTY--IQQGKEIVPLGealLENpklELQIPLKKKKSmnDDMKQLLRDMLAANPQ 308

                ...
gi 46577677 279 QRP 281
Cdd:cd13977 309 ERP 311
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
54-229 1.01e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 52.78  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  54 HEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAK--HEAWLLLPFFKrGTLWNEIERLKDkgnfltEDQILWLLLG 131
Cdd:cd07874  55 QNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEefQDVYLVMELMD-ANLCQVIQMELD------HERMSYLLYQ 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQRCTISYRAPELFSVQSHcv 211
Cdd:cd07874 128 MLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL----------ARTAGTSFMMTPYVVTRYYRAPEVILGMGY-- 195
                       170
                ....*....|....*...
gi 46577677 212 iDERTDVWSLGCVLYAMM 229
Cdd:cd07874 196 -KENVDIWSVGCIMGEMV 212
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
126-280 1.24e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 51.86  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 126 LWLLLGICRG-LEAI---HAKGYAHRDLKPTNILLGDEGQPV-LMDLGSMNQacihvEGSRQALTLQdwaaqrcTISYRA 200
Cdd:cd14020 109 MWMIQHCARDvLEALaflHHEGYVHADLKPRNILWSAEDECFkLIDFGLSFK-----EGNQDVKYIQ-------TDGYRA 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 201 PEL--------FSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ---KGDSVALA----VQNQLSIPQSPRHSsaL 265
Cdd:cd14020 177 PEAelqnclaqAGLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSqewKDNSSAIIdhifASNAVVNPAIPAYH--L 254
                       170
                ....*....|....*
gi 46577677 266 RQLLNSMMTVDPHQR 280
Cdd:cd14020 255 RDLIKSMLHNDPGKR 269
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
24-235 1.29e-07

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: 51.83  E-value: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQdREEAQREADMHRLFNHPNILRLvayclrergakHEAwlllpFFKR 103
Cdd:cd14108   8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKK-KTSARRELALLAELDHKSIVRF-----------HDA-----FEKR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 104 GTLW--------NEIERLKDKGNFLtEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG--QPVLMDLGSmnqa 173
Cdd:cd14108  71 RVVIivtelcheELLERITKRPTVC-ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGN---- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 174 cihvegsrqALTLQDWAAQRC---TISYRAPELFSvQSHcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14108 146 ---------AQELTPNEPQYCkygTPEFVAPEIVN-QSP--VSKVTDIWPVGVIAYLCLTGISPF 198
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
19-234 1.40e-07

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 51.74  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   19 RYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILChEQQDR---EEAQREADMHRLFNHPNILRL--VAYClrergakhE 93
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRL-EQEDEgvpSTAIREISLLKEMQHGNIVRLqdVVHS--------E 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   94 AWLLLPFfkrGTLWNEIERLKDKGNFLTEDQ--ILWLLLGICRGLEAIHAKGYAHRDLKPTNILlgdegqpvlmdlgsmn 171
Cdd:PLN00009  74 KRLYLVF---EYLDLDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLL---------------- 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677  172 qacihVEGSRQALTLQDWAAQRC-------------TISYRAPELFSVQSHcvIDERTDVWSLGCVlYAMMFGEGP 234
Cdd:PLN00009 135 -----IDRRTNALKLADFGLARAfgipvrtfthevvTLWYRAPEILLGSRH--YSTPVDIWSVGCI-FAEMVNQKP 202
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
146-287 1.43e-07

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 51.77  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 146 HRDLKPTNILLGDEGQPVLMDLGsmnqacihVEGSRQA-LTLQDWAAQrctiSYRAPE-----------LFSVQShcvid 213
Cdd:cd06622 126 HRDVKPTNVLVNGNGQVKLCDFG--------VSGNLVAsLAKTNIGCQ----SYMAPEriksggpnqnpTYTVQS----- 188
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 214 ertDVWSLGCVLYAMMFGEGPY-----DMVFQKGDsvALAVQNQLSIPqsPRHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06622 189 ---DVWSLGLSILEMALGRYPYppetyANIFAQLS--AIVDGDPPTLP--SGYSDDAQDFVAKCLNKIPNRRPTYAQLL 260
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
120-239 1.49e-07

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 51.74  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ-PVLMDLGsmNQACIHVEGSRQALTLQDWAAQrcTISY 198
Cdd:cd13991  95 LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFG--HAECLDPDGLGKSLFTGDYIPG--TETH 170
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46577677 199 RAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPYDMVF 239
Cdd:cd13991 171 MAPEVVLGKP---CDAKVDVWSSCCMMLHMLNGCHPWTQYY 208
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
22-292 1.94e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 51.55  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVD----LVEGLHDGHFYALKRIL-CHEQQDREEAQREADMHRLFNHPNILRLVAYCLRER-------- 88
Cdd:cd05090   9 FMEELGECAFGKIYkghlYLPGMDHAQLVAIKTLKdYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQpvcmlfef 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  89 ---GAKHEAWLLL-PFFKRGTLWNEIERLK---DKGNFLTedqilwLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQ 161
Cdd:cd05090  89 mnqGDLHEFLIMRsPHSDVGCSSDEDGTVKsslDHGDFLH------IAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 162 PVLMDLGSmnqacihvegSRQALTLQDWAAQRCT---ISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPYdM 237
Cdd:cd05090 163 VKISDLGL----------SREIYSSDYYRVQNKSllpIRWMPPEAI---MYGKFSSDSDIWSFGVVLWEIFsFGLQPY-Y 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 238 VFQKGDSVALAVQNQLsIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEA 292
Cdd:cd05090 229 GFSNQEVIEMVRKRQL-LPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLRS 282
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
22-281 2.38e-07

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: 51.25  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQ--KLGEGGFSYV-DLVEGLhDGHFYALKRIL--CHEQQDREEAQREADMHR-LFNHPNILRlvaYclrergakHEAW 95
Cdd:cd14051   2 FHEveKIGSGEFGSVyKCINRL-DGCVYAIKKSKkpVAGSVDEQNALNEVYAHAvLGKHPHVVR---Y--------YSAW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 -----LLL--PFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVlmdlg 168
Cdd:cd14051  70 aeddhMIIqnEYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPV----- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 smnQACIHVEGSRQAltlQDWAAQRCTIsYRAPELFSVQS---------HC------VIDE------RTDVWSLGCVLYA 227
Cdd:cd14051 145 ---SSEEEEEDFEGE---EDNPESNEVT-YKIGDLGHVTSisnpqveegDCrflaneILQEnyshlpKADIFALALTVYE 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 228 MMFGE-----GPYDMVFQKGDsvalavqnqlsIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14051 218 AAGGGplpknGDEWHEIRQGN-----------LPPLPQCSPEFNELLRSMIHPDPEKRP 265
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
120-231 2.44e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 51.58  E-value: 2.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQRCTISYR 199
Cdd:cd07875 123 LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL----------ARTAGTSFMMTPYVVTRYYR 192
                        90       100       110
                ....*....|....*....|....*....|..
gi 46577677 200 APELFSVQSHcviDERTDVWSLGCVLYAMMFG 231
Cdd:cd07875 193 APEVILGMGY---KENVDIWSVGCIMGEMIKG 221
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
20-281 2.58e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 51.08  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRIL--CHEQQDREEAQREADMHR-LFNHPNILRLvayclrergakHEAW- 95
Cdd:cd14139   2 FLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMrpFAGSSNEQLALHEVYAHAvLGHHPHVVRY-----------YSAWa 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 ------LLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL------------- 156
Cdd:cd14139  71 eddhmiIQNEYCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvgee 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 ----GDEGQPVLM-----DLG---SMNQACIHvEGSRQALTLQDWAAQRCTISyrapelfsvqshcvideRTDVWSLGCV 224
Cdd:cd14139 151 vsneEDEFLSANVvykigDLGhvtSINKPQVE-EGDSRFLANEILQEDYRHLP-----------------KADIFALGLT 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 225 LyAMMFGEGPYDmvfQKGDSVALAVQNQL-SIPQSPRHSsaLRQLLNSMMTVDPHQRP 281
Cdd:cd14139 213 V-ALAAGAEPLP---TNGAAWHHIRKGNFpDVPQELPES--FSSLLKNMIQPDPEQRP 264
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
68-291 3.04e-07

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 50.95  E-value: 3.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  68 MHRLFNHPNILRLVAYClrergAKHEAWLLLPFFKR-GTLWNEIERLKDKgnFLTEDQILWLLLGICRGLEAIHAKGYAH 146
Cdd:cd05055  92 MSHLGNHENIVNLLGAC-----TIGGPILVITEYCCyGDLLNFLRRKRES--FLTLEDLLSFSYQVAKGMAFLASKNCIH 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 147 RDLKPTNILLgDEGQPV-LMDLG----SMNQACIHVEGSrqaltlqdwaaQRCTISYRAPE-LFsvqsHCVIDERTDVWS 220
Cdd:cd05055 165 RDLAARNVLL-THGKIVkICDFGlardIMNDSNYVVKGN-----------ARLPVKWMAPEsIF----NCVYTFESDVWS 228
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 221 LGCVLYAMM-FGEGPY-----DMVFQKgdsvalAVQNQLSIPQsPRHSSA-LRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05055 229 YGILLWEIFsLGSNPYpgmpvDSKFYK------LIKEGYRMAQ-PEHAPAeIYDIMKTCWDADPLKRPTFKQIVQLIG 299
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
113-235 3.08e-07

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 51.03  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 113 LKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQ 192
Cdd:cd05586  87 LQKEGRF-SEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL----------SKADLTDNKTTNT 155
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46577677 193 RC-TISYRAPELfsvqshcVIDER-----TDVWSLGCVLYAMMFGEGPY 235
Cdd:cd05586 156 FCgTTEYLAPEV-------LLDEKgytkmVDFWSLGVLVFEMCCGWSPF 197
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
25-291 3.43e-07

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: 50.84  E-value: 3.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLveGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFKRG 104
Cdd:cd05069  19 KLGQGCFGEVWM--GTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEE-----PIYIVTEFMGKG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLwneIERLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQA 183
Cdd:cd05069  92 SL---LDFLKEgDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTLQ-DWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMMF-GEGPYDMVFQKgdSVALAVQNQLSIPQSPRH 261
Cdd:cd05069 169 AKFPiKWTAPEAALYGR----FTIKS--------DVWSFGILLTELVTkGRVPYPGMVNR--EVLEQVERGYRMPCPQGC 234
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 262 SSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05069 235 PESLHELMKLCWKKDPDERPTFEYIQSFLE 264
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
50-281 3.46e-07

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: 50.34  E-value: 3.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  50 RILCHEQQDREEAQREADMHRLFNHPNILRLvaycLRERGAKHEAWLLLPFFKRGTLWNEIERLKDkgnfLTEDQILWLL 129
Cdd:cd14115  24 KFVSKKMKKKEQAAHEAALLQHLQHPQYITL----HDTYESPTSYILVLELMDDGRLLDYLMNHDE----LMEEKVAFYI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 LGICRGLEAIHAKGYAHRDLKPTNILLgDEGQPV----LMDLGSMNQACIHvegSRQALTLQDwaaqrctISYRAPELfs 205
Cdd:cd14115  96 RDIMEALQYLHNCRVAHLDIKPENLLI-DLRIPVprvkLIDLEDAVQISGH---RHVHHLLGN-------PEFAAPEV-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 206 VQSHCViDERTDVWSLGCVLYAMMFGEGPYdMVFQKGDSVALAVQNQLSIPqsPRH----SSALRQLLNSMMTVDPHQRP 281
Cdd:cd14115 163 IQGTPV-SLATDIWSIGVLTYVMLSGVSPF-LDESKEETCINVCRVDFSFP--DEYfgdvSQAARDFINVILQEDPRRRP 238
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
138-281 3.51e-07

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 50.31  E-value: 3.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 138 AIHAKGYAHRDLKPTNILLG-DEGQPVLMDLGSmnqacihvegsrqALTLQDWAAQ--RCTISYRAPELFSvqsHCVIDE 214
Cdd:cd14005 122 HCHQRGVLHRDIKDENLLINlRTGEVKLIDFGC-------------GALLKDSVYTdfDGTRVYSPPEWIR---HGRYHG 185
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 215 RT-DVWSLGCVLYAMMFGEGPYdmvFQKGDSVALAVQNQlsipqsPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14005 186 RPaTVWSLGILLYDMLCGDIPF---ENDEQILRGNVLFR------PRLSKECCDLISRCLQFDPSKRP 244
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
18-235 3.55e-07

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 50.30  E-value: 3.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakHEAWLL 97
Cdd:cd14110   3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPR---HLVLIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERlkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacihv 177
Cdd:cd14110  79 ELCSGPELLYNLAER-----NSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNA------- 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 178 egsrQALTlQDWA--AQRCT--ISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14110 147 ----QPFN-QGKVlmTDKKGdyVETMAPELLEGQG---AGPQTDIWAIGVTAFIMLSADYPV 200
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
132-236 3.66e-07

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 50.85  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQaciHVEGSRQALTLqdwaaqrC-TISYRAPELFSVQSHc 210
Cdd:cd05587 106 IAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKE---GIFGGKTTRTF-------CgTPDYIAPEIIAYQPY- 174
                        90       100
                ....*....|....*....|....*.
gi 46577677 211 viDERTDVWSLGCVLYAMMFGEGPYD 236
Cdd:cd05587 175 --GKSVDWWAYGVLLYEMLAGQPPFD 198
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
74-281 4.76e-07

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: 50.40  E-value: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  74 HPNILRLVAYCLRERgaKHEAWLLLPFFkrGTLWNEIERLKD--------KGNFLTEDQILWLLLGICRGLEAIH-AKGY 144
Cdd:cd14011  61 HPRILTVQHPLEESR--ESLAFATEPVF--ASLANVLGERDNmpspppelQDYKLYDVEIKYGLLQISEALSFLHnDVKL 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 145 AHRDLKPTNILLGDEGQPVLMDLGSmnqaCIHVEG-SRQALTLQDWAAQR---CTIS--YRAPELFSVQSHcviDERTDV 218
Cdd:cd14011 137 VHGNICPESVVINSNGEWKLAGFDF----CISSEQaTDQFPYFREYDPNLpplAQPNlnYLAPEYILSKTC---DPASDM 209
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 219 WSLGCVLYAMmFGEG--PYDMVfQKGDS--VALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14011 210 FSLGVLIYAI-YNKGkpLFDCV-NNLLSykKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP 274
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
26-225 5.27e-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: 49.95  E-value: 5.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheawLLLPFFKRGT 105
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLN----FITEYIKGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LWNEIERLKDKGNFlteDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnQACIHVEGSRQALT 185
Cdd:cd14221  77 LRGIIKSMDSHYPW---SQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFG---LARLMVDEKTQPEG 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 46577677 186 LQDWAA----QRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVL 225
Cdd:cd14221 151 LRSLKKpdrkKRYTVVgnpyWMAPEMINGRSY---DEKVDVFSFGIVL 195
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
132-285 5.51e-07

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 49.73  E-value: 5.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMdLGSMNQACIhVEGSRQALtlqdWAAQRCTiSYRAPELFSVQSHcV 211
Cdd:cd13976  93 IASAVAHCHRNGIVLRDLKLRKFVFADEERTKLR-LESLEDAVI-LEGEDDSL----SDKHGCP-AYVSPEILNSGAT-Y 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 212 IDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSVALAV---QNQLSIPQSprHSSALRQLLNSMMTVDPHQRP---HIPL 285
Cdd:cd13976 165 SGKAADVWSLGVILYTMLVGRYP----FHDSEPASLFAkirRGQFAIPET--LSPRARCLIRSLLRREPSERLtaeDILL 238
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
17-232 5.53e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 50.27  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  17 NKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALK----------------RIL-CHEQQDREEAQREADMHRL--FNH--- 74
Cdd:cd14136   9 NGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKvvksaqhyteaaldeiKLLkCVREADPKDPGREHVVQLLddFKHtgp 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  75 -------------PNILRLVAYClRERGakheawLLLPFFKRgtlwneIERlkdkgnfltedQILwlllgicRGLEAIHA 141
Cdd:cd14136  89 ngthvcmvfevlgPNLLKLIKRY-NYRG------IPLPLVKK------IAR-----------QVL-------QGLDYLHT 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 142 K-GYAHRDLKPTNILLG-DEGQPVLMDLGSmnqAC-IHVEGSRQALTLQdwaaqrctisYRAPElfsvqshcVI-----D 213
Cdd:cd14136 138 KcGIIHTDIKPENVLLCiSKIEVKIADLGN---ACwTDKHFTEDIQTRQ----------YRSPE--------VIlgagyG 196
                       250
                ....*....|....*....
gi 46577677 214 ERTDVWSLGCVLYAMMFGE 232
Cdd:cd14136 197 TPADIWSTACMAFELATGD 215
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
22-291 5.55e-07

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: 50.07  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSyvDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFF 101
Cdd:cd05070  13 LIKRLGNGQFG--EVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEE-----PIYIVTEYM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLwneIERLKD-KGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGS 180
Cdd:cd05070  86 SKGSL---LDFLKDgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 181 RQALTLQ-DWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMMF-GEGPYDMVFQKgdSVALAVQNQLSIPQS 258
Cdd:cd05070 163 RQGAKFPiKWTAPEAALYGR----FTIKS--------DVWSFGILLTELVTkGRVPYPGMNNR--EVLEQVERGYRMPCP 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 46577677 259 PRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05070 229 QDCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
22-235 6.60e-07

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 50.00  E-value: 6.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFY--ALKRI--LCHEQQDREEAQREADMHRLFNHPNILRLVAYClRERGAKHEAWLL 97
Cdd:cd05089   6 FEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLkeFASENDHRDFAGELEVLCKLGHHPNIINLLGAC-ENRGYLYIAIEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPF-----FKRGTLWNEIE----RLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd05089  85 APYgnlldFLRKSRVLETDpafaKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFG 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 169 SMNQACIHVEGSRQALTLQdWAAqrctisyrapelFSVQSHCVIDERTDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05089 165 LSRGEEVYVKKTMGRLPVR-WMA------------IESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPY 219
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
128-231 6.75e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 50.03  E-value: 6.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 128 LLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPV---LMDLGSMNqaciHVEGSRQALTLQdwaaqrcTISYRAPEL 203
Cdd:cd14229 107 ILQQVATALKKLKSLGLIHADLKPENIMLVDPvRQPYrvkVIDFGSAS----HVSKTVCSTYLQ-------SRYYRAPEI 175
                        90       100
                ....*....|....*....|....*...
gi 46577677 204 FSVQSHCvidERTDVWSLGCVLYAMMFG 231
Cdd:cd14229 176 ILGLPFC---EAIDMWSLGCVIAELFLG 200
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
56-235 7.19e-07

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 49.62  E-value: 7.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  56 QQDREEA----QREADMHRLFNHPNILRLVAYCLRergAKHEAwLLLPFFKRGTLWNEIerlKDKGNFLTEDQILWLLLG 131
Cdd:cd14153  33 ERDNEEQlkafKREVMAYRQTRHENVVLFMGACMS---PPHLA-IITSLCKGRTLYSVV---RDAKVVLDVNKTRQIAQE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLgDEGQPVLMDLGSMNQACIHVEGSRQ-ALTLQD-WaaqrctISYRAPELF----- 204
Cdd:cd14153 106 IVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLFTISGVLQAGRREdKLRIQSgW------LCHLAPEIIrqlsp 178
                       170       180       190
                ....*....|....*....|....*....|..
gi 46577677 205 -SVQSHCVIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14153 179 eTEEDKLPFSKHSDVFAFGTIWYELHAREWPF 210
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
20-281 8.09e-07

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: 49.50  E-value: 8.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQdREEAQREADMHRLFNHPNILRLvaycLRERGAKHEAWLLLP 99
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSST-RARAFQERDILARLSHRRLTCL----LDQFETRKTLILILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLwneIERLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLgdegqpvlmdlgsmnqacihVEG 179
Cdd:cd14107  79 LCSSEEL---LDRLFLKGV-VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM--------------------VSP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 180 SRQALTLQDWA-AQRCTIS------YRAPELFS--VQSHCVIDERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAL--A 248
Cdd:cd14107 135 TREDIKICDFGfAQEITPSehqfskYGSPEFVApeIVHQEPVSAATDIWALGVIAYLSLTCHSPF---AGENDRATLlnV 211
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46577677 249 VQNQLS--IPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14107 212 AEGVVSwdTPEITHLSEDAKDFIKRVLQPDPEKRP 246
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
61-234 8.86e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 49.19  E-value: 8.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  61 EAQREADMHRLFNHPNILRLVAYCLrergakHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLG--ICRGLEA 138
Cdd:cd14067  56 EFRQEASMLHSLQHPCIVYLIGISI------HPLCFALELAPLGSLNTVLEENHKGSSFMPLGHMLTFKIAyqIAAGLAY 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 139 IHAKGYAHRDLKPTNILLG--DEGQPV---LMDLG----SMNQACIHVEGsrqaltlqdwaaqrcTISYRAPElfsVQSH 209
Cdd:cd14067 130 LHKKNIIFCDLKSDNILVWslDVQEHInikLSDYGisrqSFHEGALGVEG---------------TPGYQAPE---IRPR 191
                       170       180
                ....*....|....*....|....*
gi 46577677 210 CVIDERTDVWSLGCVLYAMMFGEGP 234
Cdd:cd14067 192 IVYDEKVDMFSYGMVLYELLSGQRP 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
136-236 1.04e-06

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 49.41  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqacihvEGSRQALTLQDWAAqrcTISYRAPELFSVQSHcviDER 215
Cdd:cd05591 109 LMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCK------EGILNGKTTTTFCG---TPDYIAPEILQELEY---GPS 176
                        90       100
                ....*....|....*....|.
gi 46577677 216 TDVWSLGCVLYAMMFGEGPYD 236
Cdd:cd05591 177 VDWWALGVLMYEMMAGQPPFE 197
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
70-281 1.05e-06

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 49.42  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  70 RLFNHPNILRLV-AYC--------------------LRERGAKHEAWLLL-----PFFKRGTLWNeierlkdkgNFLTED 123
Cdd:cd14018  68 LLAPHPNIIRVQrAFTdsvpllpgaiedypdvlparLNPSGLGHNRTLFLvmknyPCTLRQYLWV---------NTPSYR 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 124 QILWLLLGICRGLEAIHAKGYAHRDLKPTNILL--GDEGQPVLM--DLGsmnqACIHVEGSRQALTLQDWAAQR----CT 195
Cdd:cd14018 139 LARVMILQLLEGVDHLVRHGIAHRDLKSDNILLelDFDGCPWLViaDFG----CCLADDSIGLQLPFSSWYVDRggnaCL 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 196 IsyrAPELFSVQ--SHCVID-ERTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVALAVQNQLS-IPQSPRHSS-ALRQLLN 270
Cdd:cd14018 215 M---APEVSTAVpgPGVVINySKADAWAVGAIAYEIFGLSNPF---YGLGDTMLESRSYQESqLPALPSAVPpDVRQVVK 288
                       250
                ....*....|.
gi 46577677 271 SMMTVDPHQRP 281
Cdd:cd14018 289 DLLQRDPNKRV 299
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
25-291 1.12e-06

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: 48.92  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSyvDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFKRG 104
Cdd:cd05071  16 KLGQGCFG--EVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEE-----PIYIVTEYMSKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 105 TLwneIERLKDK-GNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQA 183
Cdd:cd05071  89 SL---LDFLKGEmGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 184 LTLQ-DWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMMF-GEGPYDMVFQKgdSVALAVQNQLSIPQSPRH 261
Cdd:cd05071 166 AKFPiKWTAPEAALYGR----FTIKS--------DVWSFGILLTELTTkGRVPYPGMVNR--EVLDQVERGYRMPCPPEC 231
                       250       260       270
                ....*....|....*....|....*....|
gi 46577677 262 SSALRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05071 232 PESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
14-238 1.24e-06

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 49.10  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  14 IIDNkRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADmhrlfnhpnILRLvaycLRERGAKHE 93
Cdd:cd14134   9 LLTN-RYKILRLLGEGTFGKVLECWDRKRKRYVAVK-IIRNVEKYREAAKIEID---------VLET----LAEKDPNGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  94 AWL--LLPFFkrgtLWN-------EI------ERLKdKGNFL--TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL 156
Cdd:cd14134  74 SHCvqLRDWF----DYRghmcivfELlgpslyDFLK-KNNYGpfPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 --------------GDEGQPV-----LMDLGSmnqACIHVEgsrqaltlqDWAAQRCTISYRAPElfsvqshcVI----- 212
Cdd:cd14134 149 vdsdyvkvynpkkkRQIRVPKstdikLIDFGS---ATFDDE---------YHSSIVSTRHYRAPE--------VIlglgw 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 46577677 213 DERTDVWSLGCVLY------------------AMM---FGEGPYDMV 238
Cdd:cd14134 209 SYPCDVWSIGCILVelytgellfqthdnlehlAMMeriLGPLPKRMI 255
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
22-235 1.34e-06

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 48.91  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVdlveglHDGHFYALKRILC------------HEQQDREEAQREADMHRLFNHPNILRLVAYCLRErg 89
Cdd:cd05048   9 FLEELGEGAFGKV------YKGELLGPSSEESaisvaiktlkenASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 akHEAWLLLPFFKRGTLwNEI-------------ERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL 156
Cdd:cd05048  81 --QPQCMLFEYMAHGDL-HEFlvrhsphsdvgvsSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 157 GDEGQPVLMDLG---SMNQACIHVEGSRQALTLQdWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMM-FGE 232
Cdd:cd05048 158 GDGLTVKISDFGlsrDIYSSDYYRVQSKSLLPVR-WMPPEAILYGK----FTTES--------DVWSFGVVLWEIFsYGL 224

                ...
gi 46577677 233 GPY 235
Cdd:cd05048 225 QPY 227
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
75-293 1.64e-06

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 48.48  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  75 PNILRLVAYCLRErgAKHEAWLLLPFfkrGTLWNEIErlKDKGNFLTEDQILWLLlGICRGLEAIHAKGYAHRDLKPTNI 154
Cdd:cd05109  69 PYVCRLLGICLTS--TVQLVTQLMPY---GCLLDYVR--ENKDRIGSQDLLNWCV-QIAKGMSYLEEVRLVHRDLAARNV 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 155 LLGDEGQPVLMDLG-----SMNQACIHVEGSRQALTlqdWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAMM 229
Cdd:cd05109 141 LVKSPNHVKITDFGlarllDIDETEYHADGGKVPIK---WMALESILHRR----FTHQS--------DVWSYGVTVWELM 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 230 -FGEGPYDMVfqKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05109 206 tFGAKPYDGI--PAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRM 268
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
61-293 1.71e-06

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 48.52  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  61 EAQREADMHRLFNHPNILRLVAYCLRErgakhEAWLLLPFFKRGTLWNEIERLKDkgNFLTEDQILWLLlGICRGLEAIH 140
Cdd:cd05110  55 EFMDEALIMASMDHPHLVRLLGVCLSP-----TIQLVTQLMPHGCLLDYVHEHKD--NIGSQLLLNWCV-QIAKGMMYLE 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 141 AKGYAHRDLKPTNILLGDEGQPVLMDLG-----SMNQACIHVEGSRQALTlqdWAAQRCtISYRApelFSVQShcvider 215
Cdd:cd05110 127 ERRLVHRDLAARNVLVKSPNHVKITDFGlarllEGDEKEYNADGGKMPIK---WMALEC-IHYRK---FTHQS------- 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 216 tDVWSLGCVLYAMM-FGEGPYDMVFQKgdSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd05110 193 -DVWSYGVTIWELMtFGGKPYDGIPTR--EIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRM 268
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
130-170 1.86e-06

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 48.93  E-value: 1.86e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 46577677 130 LGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:COG4248 128 RNLAAAVAALHAAGYVHGDVNPSNILVSDTALVTLIDTDSF 168
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
15-298 2.12e-06

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB 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 TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 48.50  E-value: 2.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLVEGLH-----DGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRerg 89
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVE--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 aKHEAWLLLPFFKRGTLwNEIER-------LKDKGN---FLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDE 159
Cdd:cd05093  79 -GDPLIMVFEYMKHGDL-NKFLRahgpdavLMAEGNrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 160 GQPVLMDLGsMNQACIHVE----GSRQALTLQdWAAQRcTISYRApelFSVQShcvidertDVWSLGCVLYAMM-FGEGP 234
Cdd:cd05093 157 LLVKIGDFG-MSRDVYSTDyyrvGGHTMLPIR-WMPPE-SIMYRK---FTTES--------DVWSLGVVLWEIFtYGKQP 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46577677 235 YdmvFQKGDSVALAVQNQLSIPQSPRH-SSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAP 298
Cdd:cd05093 223 W---YQLSNNEVIECITQGRVLQRPRTcPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASP 284
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
75-280 2.14e-06

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: 48.31  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  75 PNILRLVAYCLRErgakHEAWLLLPFFKRGTLWN---------EIERLKDKGN---------FLTEDQILWLLLGICRGL 136
Cdd:cd05576  51 PNMVCLRKYIISE----ESVFLVLQHAEGGKLWSylskflndkEIHQLFADLDerlaaasrfYIPEECIQRWAAEMVVAL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 137 EAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQacihVEGSRQALTLQDWaaqrctisYRAPELFSVQSHCvidERT 216
Cdd:cd05576 127 DALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE----VEDSCDSDAIENM--------YCAPEVGGISEET---EAC 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 217 DVWSLGCVLYAMMFGegpydMVFQKGDSVALAVQNQLSIPQSPrhSSALRQLLNSMMTVDPHQR 280
Cdd:cd05576 192 DWWSLGALLFELLTG-----KALVECHPAGINTHTTLNIPEWV--SEEARSLLQQLLQFNPTER 248
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
109-236 2.30e-06

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: 47.01  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    109 EIERLKDKGnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGqpvlmdlgsmnqacihvegsrqALTLQD 188
Cdd:smart00750   5 DILEVRGRP--LNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKLDG----------------------SVAFKT 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 46577677    189 WAAQRCTISYRAPELFSVQSHcviDERTDVWSLGCVLYAMMFGEGPYD 236
Cdd:smart00750  61 PEQSRPDPYFMAPEVIQGQSY---TEKADIYSLGITLYEALDYELPYN 105
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
26-225 2.79e-06

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: 48.02  E-value: 2.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKheawLLLPFFKRGT 105
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLN----LLTEFIEGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LwneIERLKDKGNFlTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG-------SMNQACIHVE 178
Cdd:cd14222  77 L---KDFLRADDPF-PWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGlsrliveEKKKPPPDKP 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 46577677 179 GSRQALTLQDWAAQRCTIS----YRAPELFSVQSHcviDERTDVWSLGCVL 225
Cdd:cd14222 153 TTKKRTLRKNDRKKRYTVVgnpyWMAPEMLNGKSY---DEKVDIFSFGIVL 200
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
28-231 2.99e-06

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: 47.91  E-value: 2.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  28 EGGFSyvDLVEGLHDGHFYALKRIlcheqqDREEAQREADMHRLFN----------HPNILRLVAYCLrergAKHEAWLL 97
Cdd:cd14157   3 EGTFA--DIYKGYRHGKQYVIKRL------KETECESPKSTERFFQtevqicfrccHPNILPLLGFCV----ESDCHCLI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERlKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACIHV 177
Cdd:cd14157  71 YPYMPNGSLQDRLQQ-QGGSHPLPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSG----LRLCP 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46577677 178 EGSRQALTLQDWAAQRCTISYrAPELFSvqSHCVIDERTDVWSLGCVLYAMMFG 231
Cdd:cd14157 146 VDKKSVYTMMKTKVLQISLAY-LPEDFV--RHGQLTEKVDIFSCGVVLAEILTG 196
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
22-235 3.06e-06

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 48.07  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDGHFY--ALKRILCHEQQD--REEAQREADMHRLFNHPNILRLVAYClrergaKHEAWLL 97
Cdd:cd05088  11 FQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDdhRDFAGELEVLCKLGHHPNIINLLGAC------EHRGYLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LP--FFKRGTLWNEIERLK------------DKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV 163
Cdd:cd05088  85 LAieYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46577677 164 LMDLGSMNQACIHVEGSRQALTLQdWAAqrctisyrapelFSVQSHCVIDERTDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05088 165 IADFGLSRGQEVYVKKTMGRLPVR-WMA------------IESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPY 224
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
124-231 3.31e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 47.83  E-value: 3.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 124 QILWLLLGIcRGLEAIHAkgyahrDLKPTNILLGDEG-QPV---LMDLGSmnqACiHVEGSRQALTLQdwaaqrcTISYR 199
Cdd:cd14211 109 QVLTALLKL-KSLGLIHA------DLKPENIMLVDPVrQPYrvkVIDFGS---AS-HVSKAVCSTYLQ-------SRYYR 170
                        90       100       110
                ....*....|....*....|....*....|..
gi 46577677 200 APELFSVQSHCvidERTDVWSLGCVLYAMMFG 231
Cdd:cd14211 171 APEIILGLPFC---EAIDMWSLGCVIAELFLG 199
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
64-235 3.76e-06

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 47.51  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRLV-AYCLRERgakheAWLLLPFFKRGTLWNEIERLKDKGnFLTEDQILWLLLGICRGLEAIHAK 142
Cdd:cd14109  45 REVDIHNSLDHPNIVQMHdAYDDEKL-----AVTVIDNLASTIELVRDNLLPGKD-YYTERQVAVFVRQLLLALKHMHDL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 143 GYAHRDLKPTNILLGDEgQPVLMDLGsmnqacihvegsrQALTLQDwaAQRCTISYRAPELFSVQshcVIDER-----TD 217
Cdd:cd14109 119 GIAHLDLRPEDILLQDD-KLKLADFG-------------QSRRLLR--GKLTTLIYGSPEFVSPE---IVNSYpvtlaTD 179
                       170
                ....*....|....*...
gi 46577677 218 VWSLGCVLYAMMFGEGPY 235
Cdd:cd14109 180 MWSVGVLTYVLLGGISPF 197
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
58-293 3.76e-06

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 47.51  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  58 DREEAQREADMHRLFNHPNILRLVAYCLRErgakHEAWLLLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLE 137
Cdd:cd14156  31 DQHKIVREISLLQKLSHPNIVRYLGICVKD----EKLHPILEYVSGGCL---EELLAREELPLSWREKVELACDISRGMV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 138 AIHAKGYAHRDLKPTNILL-----GDEGqpVLMDLGSMNQ-ACIHVEGSRQALTLQDWAAqrctisYRAPELFSVQSHcv 211
Cdd:cd14156 104 YLHSKNIYHRDLNSKNCLIrvtprGREA--VVTDFGLAREvGEMPANDPERKLSLVGSAF------WMAPEMLRGEPY-- 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 212 iDERTDVWSLGCVLYAMMfGEGPYD-MVFQKGDSVALAVQN-QLSIPQSPRHssaLRQLLNSMMTVDPHQRPHIPLLLSQ 289
Cdd:cd14156 174 -DRKVDVFSFGIVLCEIL-ARIPADpEVLPRTGDFGLDVQAfKEMVPGCPEP---FLDLAASCCRMDAFKRPSFAELLDE 248

                ....
gi 46577677 290 LEAL 293
Cdd:cd14156 249 LEDI 252
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
20-239 4.40e-06

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 47.63  E-value: 4.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLFN-------HPNILRLVAYCLrergakH 92
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVK-VLKNKPAYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFM------H 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  93 EAWLLLPFFKRG-TLWNEIERLKDKGNFLTEDQILwlLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGS 169
Cdd:cd14212  74 HGHLCIVFELLGvNLYELLKQNQFRGLSLQLIRKF--LQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEikLIDFGS 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 170 mnqACIhvEGSrqalTLQDWAAQRctiSYRAPE-LFSVQSHCVIdertDVWSLGCVLyAMMF-------GEGPYDMVF 239
Cdd:cd14212 152 ---ACF--ENY----TLYTYIQSR---FYRSPEvLLGLPYSTAI----DMWSLGCIA-AELFlglplfpGNSEYNQLS 212
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
132-280 4.70e-06

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: 47.35  E-value: 4.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGsmnqACihvegsRQALTLQDWAAQRC-TISYRAPELF--SVQS 208
Cdd:cd05571 104 IVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFG----LC------KEEISYGATTKTFCgTPEYLAPEVLedNDYG 173
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 209 HCVidertDVWSLGCVLYAMMFGEGP-----YDMVFQkgdsvaLAVQNQLSIPqsPRHSSALRQLLNSMMTVDPHQR 280
Cdd:cd05571 174 RAV-----DWWGLGVVMYEMMCGRLPfynrdHEVLFE------LILMEEVRFP--STLSPEAKSLLAGLLKKDPKKR 237
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
58-235 4.90e-06

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: 46.99  E-value: 4.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  58 DREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKdkgnfLTEDQIL--WlLLGICRG 135
Cdd:cd14032  43 ERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGKRCIVLVTELMTSGTLKTYLKRFK-----VMKPKVLrsW-CRQILKG 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAIHAKG--YAHRDLKPTNILL-GDEGQPVLMDLGsmnqacihvegsrqALTLQDWAAQRCTI---SYRAPELFsvQSH 209
Cdd:cd14032 117 LLFLHTRTppIIHRDLKCDNIFItGPTGSVKIGDLG--------------LATLKRASFAKSVIgtpEFMAPEMY--EEH 180
                       170       180
                ....*....|....*....|....*.
gi 46577677 210 cvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14032 181 --YDESVDVYAFGMCMLEMATSEYPY 204
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
47-287 4.97e-06

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: 47.02  E-value: 4.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  47 ALKRIlchEQQDREEAQ---READMHRLFNHPNILRLVayclrerGAKHEAWLLLPFFKR---GTL-------WNEIERL 113
Cdd:cd06624  37 AIKEI---PERDSREVQplhEEIALHSRLSHKNIVQYL-------GSVSEDGFFKIFMEQvpgGSLsallrskWGPLKDN 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 114 KDKGNFLTEdQILwlllgicRGLEAIHAKGYAHRDLKPTNILLGD-EGQPVLMDLG-SMNQACIHVEGSRQALTLQdwaa 191
Cdd:cd06624 107 ENTIGYYTK-QIL-------EGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGtSKRLAGINPCTETFTGTLQ---- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 192 qrctisYRAPElfsvqshcVIDE-------RTDVWSLGCVLYAMMFGEGPYdmvFQKGDSVAlAV------QNQLSIPQS 258
Cdd:cd06624 175 ------YMAPE--------VIDKgqrgygpPADIWSLGCTIIEMATGKPPF---IELGEPQA-AMfkvgmfKIHPEIPES 236
                       250       260
                ....*....|....*....|....*....
gi 46577677 259 prHSSALRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd06624 237 --LSEEAKSFILRCFEPDPDKRATASDLL 263
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
26-168 6.32e-06

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 45.13  E-value: 6.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREAD-MHRLFNH-PNILRLVAYCLRERgakhEAWLLLPFFKR 103
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDiLRRLKGLeLNIPKVLVTEDVDG----PNILLMELVKG 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46577677 104 GTLWNEI-ERLKDKGnfLTEdQILWLLLgicRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd13968  77 GTLIAYTqEEELDEK--DVE-SIMYQLA---ECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
43-297 6.72e-06

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 47.53  E-value: 6.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677     43 GHFYALK--RILcHEQQDREEA--QREADMHRLFNHPNILRLVayclrERGaKHEAWLLLPFFKRGTLWNEIERLKDKGN 118
Cdd:TIGR03903    3 GHEVAIKllRTD-APEEEHQRArfRRETALCARLYHPNIVALL-----DSG-EAPPGLLFAVFEYVPGRTLREVLAADGA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    119 FLTEDQILwLLLGICRGLEAIHAKGYAHRDLKPTNILL---GDEGQPVLMDLGsmnqACIHVEGSRQALTLQDWAAQRC- 194
Cdd:TIGR03903   76 LPAGETGR-LMLQVLDALACAHNQGIVHRDLKPQNIMVsqtGVRPHAKVLDFG----IGTLLPGVRDADVATLTRTTEVl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677    195 -TISYRAPELFSVQShcvIDERTDVWSLGCVLYAMMFGEgpydmVFQKGDSVALAVQNQLS-----IPQSPRhSSALRQL 268
Cdd:TIGR03903  151 gTPTYCAPEQLRGEP---VTPNSDLYAWGLIFLECLTGQ-----RVVQGASVAEILYQQLSpvdvsLPPWIA-GHPLGQV 221
                          250       260       270
                   ....*....|....*....|....*....|
gi 46577677    269 LNSMMTVDPHQRP-HIPLLLSQLEALQPPA 297
Cdd:TIGR03903  222 LRKALNKDPRQRAaSAPALAERFRALELCA 251
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
23-235 7.58e-06

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK 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: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 46.61  E-value: 7.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  23 IQKLGEGGFS--YVDLVEGLHDGHF---YALKRI--LCHEQqDREEAQREADMHRLFNHPNILRLVAYCLRergaKHEAW 95
Cdd:cd05036  11 IRALGQGAFGevYEGTVSGMPGDPSplqVAVKTLpeLCSEQ-DEMDFLMEALIMSKFNHPNIVRCIGVCFQ----RLPRF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWN---EIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMN- 171
Cdd:cd05036  86 ILLELMAGGDLKSflrENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKIGDFGm 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 -----QACIHVEGSRQALtlqdwaaqrcTISYRAPELFsvqSHCVIDERTDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05036 166 ardiyRADYYRKGGKAML----------PVKWMPPEAF---LDGIFTSKTDVWSFGVLLWEIFsLGYMPY 222
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
26-281 8.13e-06

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 46.50  E-value: 8.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVDLVEGLHDGHFYALKrilcHEQQDREEAQREAdmhrlfnhPNILR--LVAYCLRERGAKHEAWL-LLPFFK 102
Cdd:cd14100   8 LGSGGFGSVYSGIRVADGAPVAIK----HVEKDRVSEWGEL--------PNGTRvpMEIVLLKKVGSGFRGVIrLLDWFE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 103 RG----TLWNEIERLKDKGNFLTEDQILWLLLG---ICRGLEAI---HAKGYAHRDLKPTNILLG-DEGQPVLMDLGSmn 171
Cdd:cd14100  76 RPdsfvLVLERPEPVQDLFDFITERGALPEELArsfFRQVLEAVrhcHNCGVLHRDIKDENILIDlNTGELKLIDFGS-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 qacihveGSRQALTL-QDWAAQRCtisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPydmvFQKGDSValaVQ 250
Cdd:cd14100 154 -------GALLKDTVyTDFDGTRV---YSPPEW--IRFHRYHGRSAAVWSLGILLYDMVCGDIP----FEHDEEI---IR 214
                       250       260       270
                ....*....|....*....|....*....|.
gi 46577677 251 NQLSIPQspRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14100 215 GQVFFRQ--RVSSECQHLIKWCLALRPSDRP 243
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
55-235 9.59e-06

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: 46.25  E-value: 9.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  55 EQQDRE----EAQR---EADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKdkgnfLTEDQIL- 126
Cdd:cd14031  42 ELQDRKltkaEQQRfkeEAEMLKGLQHPNIVRFYDSWESVLKGKKCIVLVTELMTSGTLKTYLKRFK-----VMKPKVLr 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 127 -WlLLGICRGLEAIHAKG--YAHRDLKPTNILL-GDEGQPVLMDLGsmnqacihvegsrqALTLQDWAAQRCTI---SYR 199
Cdd:cd14031 117 sW-CRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVKIGDLG--------------LATLMRTSFAKSVIgtpEFM 181
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 46577677 200 APELFsvQSHcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14031 182 APEMY--EEH--YDESVDVYAFGMCMLEMATSEYPY 213
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
24-235 9.99e-06

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: 46.26  E-value: 9.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGgfSYVDLVEGLHDGH--FYALKrILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd05052  12 HKLGGG--QYGEVYEGVWKKYnlTVAVK-TLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREP----PFYIITEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLWNEIeRLKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSR 181
Cdd:cd05052  85 PYGNLLDYL-RECNREE-LNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGL----------SR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46577677 182 --QALTLQDWAAQRCTISYRAPE-----LFSVQShcvidertDVWSLGCVLYAM-MFGEGPY 235
Cdd:cd05052 153 lmTGDTYTAHAGAKFPIKWTAPEslaynKFSIKS--------DVWAFGVLLWEIaTYGMSPY 206
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
59-168 1.01e-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: 46.19  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  59 REEAQ--READMHR--LFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICR 134
Cdd:cd14220  29 TEEASwfRETEIYQtvLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFL-----KCTTLDTRALLKLAYSAAC 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 46577677 135 GLEAIHAKGY--------AHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd14220 104 GLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLG 145
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
18-281 1.05e-05

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 46.41  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDR---EEAQREADMHRLFNHPNILRLVaYCLRergAKHEA 94
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKnmvHQVQAERDALALSKSPFIVHLY-YSLQ---SANNV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGtlwnEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG----SM 170
Cdd:cd05610  80 YLVMEYLIGG----DVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGlskvTL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 171 NQ-------------ACIHVEGSR---QALTLQDW-----------------AAQRC-------TISYRAPELFSVQSHc 210
Cdd:cd05610 156 NRelnmmdilttpsmAKPKNDYSRtpgQVLSLISSlgfntptpyrtpksvrrGAARVegerilgTPDYLAPELLLGKPH- 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 211 viDERTDVWSLGCVLYAMMFGEGPYDmvfqkGDSVALAVQNQLS--IPQsPRHSSAL----RQLLNSMMTVDPHQRP 281
Cdd:cd05610 235 --GPAVDWWALGVCLFEFLTGIPPFN-----DETPQQVFQNILNrdIPW-PEGEEELsvnaQNAIEILLTMDPTKRA 303
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
120-296 1.08e-05

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 45.80  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 120 LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQpVLMDLGSMNQACIhVEGSRQALTLQdwaaQRCTiSYR 199
Cdd:cd14022  81 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER-TRVKLESLEDAYI-LRGHDDSLSDK----HGCP-AYV 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELFSVqSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVfQKGDSVALAVQNQLSIPQ--SPRHSSALRQLLNSmmtvDP 277
Cdd:cd14022 154 SPEILNT-SGSYSGKAADVWSLGVMLYTMLVGRYPFHDI-EPSSLFSKIRRGQFNIPEtlSPKAKCLIRSILRR----EP 227
                       170
                ....*....|....*....
gi 46577677 278 HQRphipllLSQLEALQPP 296
Cdd:cd14022 228 SER------LTSQEILDHP 240
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
92-290 1.21e-05

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 46.15  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLPFFKRGTLWNEIERLKDKGNF----LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL 167
Cdd:cd14207 145 SESFASSGFQEDKSLSDVEEEEEDSGDFykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDF 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 168 GSMNQACIHVEGSRQALTlqdwaaqRCTISYRAPE-LFSVqshcVIDERTDVWSLGCVLYAMM-FGEGPYDMVfQKGDSV 245
Cdd:cd14207 225 GLARDIYKNPDYVRKGDA-------RLPLKWMAPEsIFDK----IYSTKSDVWSYGVLLWEIFsLGASPYPGV-QIDEDF 292
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 46577677 246 ALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQL 290
Cdd:cd14207 293 CSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVERL 337
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
128-231 1.32e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 46.24  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 128 LLLGICRGLEAIHAKGYAHRDLKPTNILLGDEG-QPV---LMDLGSMNqaciHVEGSRQALTLQdwaaqrcTISYRAPEL 203
Cdd:cd14227 122 ILQQVATALMKLKSLGLIHADLKPENIMLVDPSrQPYrvkVIDFGSAS----HVSKAVCSTYLQ-------SRYYRAPEI 190
                        90       100
                ....*....|....*....|....*...
gi 46577677 204 FSVQSHCvidERTDVWSLGCVLYAMMFG 231
Cdd:cd14227 191 ILGLPFC---EAIDMWSLGCVIAELFLG 215
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
20-235 1.34e-05

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 46.19  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  20 YLFIQKLGEGGFSYVDLVEGLHDGHFYALKR-----ILCHEQQDREEAQReaDMHRLFNHPNILRLVaYCLRErgaKHEA 94
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTlrkkdVLLRNQVAHVKAER--DILAEADNEWVVRLY-YSFQD---KDNL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  95 WLLLPFFKRGTLWNEIERLkdkgNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG------ 168
Cdd:cd05625  77 YFVMDYIPGGDMMSLLIRM----GVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfr 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 -----SMNQACIHV--------------EGSRQALTLQ--DWAA----QRC-------TISYRAPELFSVQSHCvidERT 216
Cdd:cd05625 153 wthdsKYYQSGDHLrqdsmdfsnewgdpENCRCGDRLKplERRAarqhQRClahslvgTPNYIAPEVLLRTGYT---QLC 229
                       250
                ....*....|....*....
gi 46577677 217 DVWSLGCVLYAMMFGEGPY 235
Cdd:cd05625 230 DWWSVGVILFEMLVGQPPF 248
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
132-231 1.43e-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: 46.00  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 ICRGLEAIHAKGYAHRDLKPTNILLGDEGQPV--LMDLGSmnqACIHVE------GSRqaltlqdwaaqrctiSYRAPEl 203
Cdd:cd14210 125 ILQALQFLHKLNIIHCDLKPENILLKQPSKSSikVIDFGS---SCFEGEkvytyiQSR---------------FYRAPE- 185
                        90       100       110
                ....*....|....*....|....*....|...
gi 46577677 204 fsvqshcVI-----DERTDVWSLGCVLYAMMFG 231
Cdd:cd14210 186 -------VIlglpyDTAIDMWSLGCILAELYTG 211
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
65-264 1.46e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 46.04  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   65 EADMHRLFNHPNILRLvaycLRERGAKHEAWLLLPFFkRGTLWNEIERlkdKGNFLTEDQILWLLLGICRGLEAIHAKGY 144
Cdd:PHA03211 210 EARLLRRLSHPAVLAL----LDVRVVGGLTCLVLPKY-RSDLYTYLGA---RLRPLGLAQVTAVARQLLSAIDYIHGEGI 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  145 AHRDLKPTNILLGDEGQPVLMDLGSmnqACIhVEGSRQALTLQDWAAqrcTISYRAPELFSVQSHCvidERTDVWSLGCV 224
Cdd:PHA03211 282 IHRDIKTENVLVNGPEDICLGDFGA---ACF-ARGSWSTPFHYGIAG---TVDTNAPEVLAGDPYT---PSVDIWSAGLV 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46577677  225 LY------AMMFG------EGPYDMVFQKgdsvaLAVQNQLSIPQSPRHSSA 264
Cdd:PHA03211 352 IFeaavhtASLFSasrgdeRRPYDAQILR-----IIRQAQVHVDEFPQHAGS 398
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
70-280 1.61e-05

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 45.25  E-value: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  70 RLFNHPNILRLVAYCLRERgakheawLLLPFFKR--GTLWNEIERLKDkgnfLTEDQILWLLLGICRGLEAIHAKGYAHR 147
Cdd:cd14024  40 RLGPHEGVCSVLEVVIGQD-------RAYAFFSRhyGDMHSHVRRRRR----LSEDEARGLFTQMARAVAHCHQHGVILR 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 148 DLKPTNILLGDEGQPVLMdLGSMNQACIhVEGSRQALtlqdWAAQRCTiSYRAPELFSvQSHCVIDERTDVWSLGCVLYA 227
Cdd:cd14024 109 DLKLRRFVFTDELRTKLV-LVNLEDSCP-LNGDDDSL----TDKHGCP-AYVGPEILS-SRRSYSGKAADVWSLGVCLYT 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 228 MMFGEGPydmvFQKGDSVALAV---QNQLSIPQ--SPRhssaLRQLLNSMMTVDPHQR 280
Cdd:cd14024 181 MLLGRYP----FQDTEPAALFAkirRGAFSLPAwlSPG----ARCLVSCMLRRSPAER 230
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
22-290 1.80e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 45.33  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVEGLHDghfYALKRILCHEQQ------DREEAQREADMHRLFNHPNILRLVAYCLRERgakhEAW 95
Cdd:cd14206   1 YLQEIGNGWFGKVILGEIFSD---YTPAQVVVKELRvsagplEQRKFISEAQPYRSLQHPNILQCLGLCTETI----PFL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  96 LLLPFFKRGTLWNEIeRLKDKGNFLTED-------QILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG 168
Cdd:cd14206  74 LIMEFCQLGDLKRYL-RAQRKADGMTPDlptrdlrTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 ---SMNQACIHVEGSRQALTLQdWAAQRCTISYRAPELFSVQShcvidERTDVWSLGCVLYAMM-FGEGPYDMVFQKgDS 244
Cdd:cd14206 153 lshNNYKEDYYLTPDRLWIPLR-WVAPELLDELHGNLIVVDQS-----KESNVWSLGVTIWELFeFGAQPYRHLSDE-EV 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 46577677 245 VALAVQNQLSIPQSPR----HSSALRQLLNSMMtVDPHQRPHIPLLLSQL 290
Cdd:cd14206 226 LTFVVREQQMKLAKPRlklpYADYWYEIMQSCW-LPPSQRPSVEELHLQL 274
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
43-280 1.85e-05

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 45.40  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  43 GHFYALKRILCHE-QQDREEAQREADMHRLFNHPNILRLV-AYCLRErgakhEAWLllpFFKRGTLWNEIERLKDKGnFL 120
Cdd:cd14088  26 GKLYTCKKFLKRDgRKVRKAAKNEINILKMVKHPNILQLVdVFETRK-----EYFI---FLELATGREVFDWILDQG-YY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 121 TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLgdegqpvlmdLGSMNQACIHVEGSRQALTLQDWAAQRC-TISYR 199
Cdd:cd14088  97 SERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVY----------YNRLKNSKIVISDFHLAKLENGLIKEPCgTPEYL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 200 APELFSVQSHcviDERTDVWSLGCVLYAMMFGEGP-YDMV----FQKGDS----VALAVQNQLSIPQSPRHSSALRQLLN 270
Cdd:cd14088 167 APEVVGRQRY---GRPVDCWAIGVIMYILLSGNPPfYDEAeeddYENHDKnlfrKILAGDYEFDSPYWDDISQAAKDLVT 243
                       250
                ....*....|
gi 46577677 271 SMMTVDPHQR 280
Cdd:cd14088 244 RLMEVEQDQR 253
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
136-287 2.18e-05

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 44.84  E-value: 2.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 136 LEAI---HAKGYAHRDLKPTNILLG-DEGQPVLMDLGSmnQACIHVEgsrqalTLQDWAAQRCtisYRAPELFSVQSHCV 211
Cdd:cd14101 118 VEAVqhcHSKGVVHRDIKDENILVDlRTGDIKLIDFGS--GATLKDS------MYTDFDGTRV---YSPPEWILYHQYHA 186
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 212 IDerTDVWSLGCVLYAMMFGEGPYDMvfqkgDSVALAVQnqlsiPQSPRHSSA-LRQLLNSMMTVDPHQRPHIPLLL 287
Cdd:cd14101 187 LP--ATVWSLGILLYDMVCGDIPFER-----DTDILKAK-----PSFNKRVSNdCRSLIRSCLAYNPSDRPSLEQIL 251
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-281 2.20e-05

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 45.35  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  18 KRYLFIQKLGEGGFSYVDLVEGLHDGHFYAL-------KRILCHEQQDREEAQREAD---------MHRLfNHPNILRLV 81
Cdd:cd05097   5 QQLRLKEKLGEGQFGEVHLCEAEGLAEFLGEgapefdgQPVLVAVKMLRADVTKTARndflkeikiMSRL-KNPNIIRLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  82 AYCLRErgakHEAWLLLPFFKRGTL-----WNEIERLKDKGNFL---TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTN 153
Cdd:cd05097  84 GVCVSD----DPLCMITEYMENGDLnqflsQREIESTFTHANNIpsvSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 154 ILLGDEGQPVLMDLG-SMNQAC---IHVEGsRQALTLQdWAAQRCTISYRapelFSVQShcvidertDVWSLGCVLYAM- 228
Cdd:cd05097 160 CLVGNHYTIKIADFGmSRNLYSgdyYRIQG-RAVLPIR-WMAWESILLGK----FTTAS--------DVWAFGVTLWEMf 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46577677 229 -MFGEGPYDM-----VFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd05097 226 tLCKEQPYSLlsdeqVIENTGEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRP 284
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
26-281 2.44e-05

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 44.94  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  26 LGEGGFSYVdlVEGLHDGHFYALKrILCHEQQDREEAQREADMHRLfNHPNILRLVAYCLRERGakheawLLLPFFKRGT 105
Cdd:cd14068   2 LGDGGFGSV--YRAVYRGEDVAVK-IFNKHTSFRLLRQELVVLSHL-HHPSLVALLAAGTAPRM------LVMELAPKGS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 106 LwneiERL--KDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL-----GDEGQPVLMDLGsMNQACIHVe 178
Cdd:cd14068  72 L----DALlqQDNAS-LTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYG-IAQYCCRM- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 179 GSRQAltlqdwaaqRCTISYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMF-GEGPYDMVFQKGDSVALAVQNQLSIPQ 257
Cdd:cd14068 145 GIKTS---------EGTPGFRAPEV--ARGNVIYNQQADVYSFGLLLYDILTcGERIVEGLKFPNEFDELAIQGKLPDPV 213
                       250       260
                ....*....|....*....|....*..
gi 46577677 258 SPRHSS---ALRQLLNSMMTVDPHQRP 281
Cdd:cd14068 214 KEYGCApwpGVEALIKDCLKENPQCRP 240
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
25-189 2.48e-05

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 45.04  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  25 KLGEGGFSYVDLVEGL---HDGHFYALKrilcheqqdreeAQREAD----------MHRLFNHPNILRLVAYCLRERGaK 91
Cdd:cd13981   7 ELGEGGYASVYLAKDDdeqSDGSLVALK------------VEKPPSiwefyicdqlHSRLKNSRLRESISGAHSAHLF-Q 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLPFFKRGTLWNEIERLKDKGNF-LTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSM 170
Cdd:cd13981  74 DESILVMDYSSQGTLLDVVNKMKNKTGGgMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICADWPGEGEN 153
                       170
                ....*....|....*....
gi 46577677 171 NqacihveGSRQALTLQDW 189
Cdd:cd13981 154 G-------WLSKGLKLIDF 165
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
130-240 2.61e-05

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: 44.87  E-value: 2.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 LGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQAltlqdwaaqrcTISYRAPELFSVQSH 209
Cdd:cd06619 102 VAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVG-----------TNAYMAPERISGEQY 170
                        90       100       110
                ....*....|....*....|....*....|.
gi 46577677 210 CVideRTDVWSLGCVLYAMMFGEGPYDMVFQ 240
Cdd:cd06619 171 GI---HSDVWSLGISFMELALGRFPYPQIQK 198
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
97-281 2.69e-05

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 44.56  E-value: 2.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLW----NEIERLKDKGNFLTEDQIL--WLLLGICRG-LEAI---HAKGYAHRDLKPTNILLG-DEGQPVLM 165
Cdd:cd14102  69 LLDWYERPDGFlivmERPEPVKDLFDFITEKGALdeDTARGFFRQvLEAVrhcYSCGVVHRDIKDENLLVDlRTGELKLI 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 166 DLGSmnqacihveGSRQALTL-QDWAAQRCtisYRAPELfsVQSHCVIDERTDVWSLGCVLYAMMFGEGPydmvFQKGDS 244
Cdd:cd14102 149 DFGS---------GALLKDTVyTDFDGTRV---YSPPEW--IRYHRYHGRSATVWSLGVLLYDMVCGDIP----FEQDEE 210
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 46577677 245 ValaVQNQLSIPQspRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14102 211 I---LRGRLYFRR--RVSPECQQLIKWCLSLRPSDRP 242
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
22-288 2.73e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 44.98  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFSYVDLVE---GLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYClrergAKHEAWLL- 97
Cdd:cd05087   1 YLKEIGHGWFGKVFLGEvnsGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQC-----AEVTPYLLv 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  98 LPFFKRGTLWNEIERLKDKGNFLTEDQILW-LLLGICRGLEAIHAKGYAHRDLKPTNILLGDEgqpVLMDLGSMNQACIH 176
Cdd:cd05087  76 MEFCPLGDLKGYLRSCRAAESMAPDPLTLQrMACEVACGLLHLHRNNFVHSDLALRNCLLTAD---LTVKIGDYGLSHCK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 177 VEGSRQALTLQDWAAQRctisYRAPELF-SVQSHCVIDERT---DVWSLGCVLYAMM-FGEGPYDmvfQKGDSVALAV-- 249
Cdd:cd05087 153 YKEDYFVTADQLWVPLR----WIAPELVdEVHGNLLVVDQTkqsNVWSLGVTIWELFeLGNQPYR---HYSDRQVLTYtv 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 46577677 250 -QNQLSIPQsPRHSSALRQLLNSMMT---VDPHQRP---HIPLLLS 288
Cdd:cd05087 226 rEQQLKLPK-PQLKLSLAERWYEVMQfcwLQPEQRPtaeEVHLLLS 270
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
128-231 2.87e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 45.08  E-value: 2.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 128 LLLGICRGLEAIHAKGYAHRDLKPTNILLGDE-GQPV---LMDLGSMNqaciHVEGSRQALTLQdwaaqrcTISYRAPEL 203
Cdd:cd14228 122 ILQQVATALMKLKSLGLIHADLKPENIMLVDPvRQPYrvkVIDFGSAS----HVSKAVCSTYLQ-------SRYYRAPEI 190
                        90       100
                ....*....|....*....|....*...
gi 46577677 204 FSVQSHCvidERTDVWSLGCVLYAMMFG 231
Cdd:cd14228 191 ILGLPFC---EAIDMWSLGCVIAELFLG 215
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
130-234 3.55e-05

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: 44.66  E-value: 3.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 130 LGICRGLEAIHAK-GYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQAltlqdwaaqrcTISYRAPELFSVQS 208
Cdd:cd06650 110 IAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVG-----------TRSYMSPERLQGTH 178
                        90       100
                ....*....|....*....|....*.
gi 46577677 209 HCVideRTDVWSLGCVLYAMMFGEGP 234
Cdd:cd06650 179 YSV---QSDIWSMGLSLVEMAVGRYP 201
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
24-228 3.64e-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: 44.39  E-value: 3.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLveGLHDGHFYALKRILCHEqqdreEAQ--READMHR--LFNHPNILRLVAYCLRERGAKHEAWLLLP 99
Cdd:cd14144   1 RSVGKGRYGEVWK--GKWRGEKVAVKIFFTTE-----EASwfRETEIYQtvLMRHENILGFIAADIKGTGSWTQLYLITD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLWNEIerlkdKGNFLTEDQILWLLLGICRGLEAIHAKGY--------AHRDLKPTNILLGDEGQPVLMDLGsmn 171
Cdd:cd14144  74 YHENGSLYDFL-----RGNTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLG--- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 172 QACIHVEGSRQALTLQDwaAQRCTISYRAPELFSVQ---SHCVIDERTDVWSLGCVLYAM 228
Cdd:cd14144 146 LAVKFISETNEVDLPPN--TRVGTKRYMAPEVLDESlnrNHFDAYKMADMYSFGLVLWEI 203
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
57-235 3.73e-05

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 44.56  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  57 QDREEAQ--READMHRL----FNHPNILRLVAYClreRGAKHEawLLLPFFKRGTLWNEIERLKDKgnfLTEDQILWLLL 130
Cdd:cd05111  45 QDRSGRQsfQAVTDHMLaigsLDHAYIVRLLGIC---PGASLQ--LVTQLLPLGSLLDHVRQHRGS---LGPQLLLNWCV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 131 GICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqACIHVEGSRQALtlqdWAAQRCTISYRAPE--LFSVQS 208
Cdd:cd05111 117 QIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGV---ADLLYPDDKKYF----YSEAKTPIKWMALEsiHFGKYT 189
                       170       180
                ....*....|....*....|....*...
gi 46577677 209 HcvideRTDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05111 190 H-----QSDVWSYGVTVWEMMtFGAEPY 212
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
15-298 3.87e-05

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: 44.62  E-value: 3.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  15 IDNKRYLFIQKLGEGGFSYVDLVEGLH-----DGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYClrerG 89
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVFLAECYNlsptkDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVC----G 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 AKHEAWLLLPFFKRGTLwNEIER--------------LKDKGNfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNIL 155
Cdd:cd05094  78 DGDPLIMVFEYMKHGDL-NKFLRahgpdamilvdgqpRQAKGE-LGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 156 LGDEGQPVLMDLG---SMNQACIHVEGSRQALTLQdWAAQRcTISYRApelFSVQShcvidertDVWSLGCVLYAMM-FG 231
Cdd:cd05094 156 VGANLLVKIGDFGmsrDVYSTDYYRVGGHTMLPIR-WMPPE-SIMYRK---FTTES--------DVWSFGVILWEIFtYG 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 232 EGPYdmvFQKGDSVALAVQNQLSIPQSPRHSSalRQLLNSMMTV---DPHQRPHIPLLLSQLEALQPPAP 298
Cdd:cd05094 223 KQPW---FQLSNTEVIECITQGRVLERPRVCP--KEVYDIMLGCwqrEPQQRLNIKEIYKILHALGKATP 287
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
56-235 4.19e-05

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: 44.22  E-value: 4.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  56 QQDREEAQREADMHRLFNHPNILRLV-AYCLRERGAKHEAwLLLPFFKRGTLWNEIERLKD-KGNFLTE--DQILwlllg 131
Cdd:cd14033  41 KGERQRFSEEVEMLKGLQHPNIVRFYdSWKSTVRGHKCII-LVTELMTSGTLKTYLKRFREmKLKLLQRwsRQIL----- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 132 icRGLEAIHAKG--YAHRDLKPTNILL-GDEGQPVLMDLGsmnqacihvegsrqALTLQDWAAQRCTI---SYRAPELFS 205
Cdd:cd14033 115 --KGLHFLHSRCppILHRDLKCDNIFItGPTGSVKIGDLG--------------LATLKRASFAKSVIgtpEFMAPEMYE 178
                       170       180       190
                ....*....|....*....|....*....|
gi 46577677 206 VQshcvIDERTDVWSLGCVLYAMMFGEGPY 235
Cdd:cd14033 179 EK----YDEAVDVYAFGMCILEMATSEYPY 204
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
24-235 4.65e-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: 43.87  E-value: 4.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDG--HFYALKRILCHEQQDREEAQ----READ-MHRLfNHPNILRLVAYCLrergaKHEAWL 96
Cdd:cd05040   1 EKLGDGSFGVVRRGEWTTPSgkVIQVAVKCLKSDVLSQPNAMddflKEVNaMHSL-DHPNLIRLYGVVL-----SSPLMM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  97 LLPFFKRGTLwneIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMnqacih 176
Cdd:cd05040  75 VTELAPLGSL---LDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLM------ 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46577677 177 vegsrQALTLQD--------------WAAQRCtISYRApelFSVQShcvidertDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05040 146 -----RALPQNEdhyvmqehrkvpfaWCAPES-LKTRK---FSHAS--------DVWMFGVTLWEMFtYGEEPW 202
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
64-231 5.41e-05

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 44.11  E-value: 5.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  64 READMHRLFNHPNILRLVAYClrerGAKHEAWLLLPFFKRGTLWNEIERLKDKGNfLTEDQILWLLLGICRGLEAIHAK- 142
Cdd:cd14160  41 SELEVLLLFQHPNILELAAYF----TETEKFCLVYPYMQNGTLFDRLQCHGVTKP-LSWHERINILIGIAKAIHYLHNSq 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 143 --GYAHRDLKPTNILLGDEGQPVLMDLGsMNQACIHVEgsRQALTLQDWAAQRCTISYrAPELFSVQSHCVIdeRTDVWS 220
Cdd:cd14160 116 pcTVICGNISSANILLDDQMQPKLTDFA-LAHFRPHLE--DQSCTINMTTALHKHLWY-MPEEYIRQGKLSV--KTDVYS 189
                       170
                ....*....|.
gi 46577677 221 LGCVLYAMMFG 231
Cdd:cd14160 190 FGIVIMEVLTG 200
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
19-291 5.93e-05

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 43.85  E-value: 5.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  19 RYLFIQKLGEGGFSYVDLVE--GLHDGHFYALKRILCH------EQQDREEAQREADMHRLF-NHPNILRLVAYCLRErg 89
Cdd:cd05098  14 RLVLGKPLGEGCFGQVVLAEaiGLDKDKPNRVTKVAVKmlksdaTEKDLSDLISEMEMMKMIgKHKNIINLLGACTQD-- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  90 akHEAWLLLPFFKRGTLWNEIERLKDKG------------NFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLG 157
Cdd:cd05098  92 --GPLYVIVEYASKGNLREYLQARRPPGmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 158 DEGQPVLMDLGsMNQACIHVEGSRQALTlqdwaaQRCTISYRAPE-LFS-VQSHcvideRTDVWSLGCVLYAMM-FGEGP 234
Cdd:cd05098 170 EDNVMKIADFG-LARDIHHIDYYKKTTN------GRLPVKWMAPEaLFDrIYTH-----QSDVWSFGVLLWEIFtLGGSP 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46577677 235 YDMVFQKGDSVALAVQNQLSIPQSPRHSsaLRQLLNSMMTVDPHQRPHIPLLLSQLE 291
Cdd:cd05098 238 YPGVPVEELFKLLKEGHRMDKPSNCTNE--LYMMMRDCWHAVPSQRPTFKQLVEDLD 292
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
146-234 6.83e-05

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: 43.58  E-value: 6.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 146 HRDLKPTNILLGDEGQPVLMDLGSMNQacihvegsrqaltLQDWAAQRC--TISYRAPEL-----FSVQShcvidertDV 218
Cdd:cd06615 123 HRDVKPSNILVNSRGEIKLCDFGVSGQ-------------LIDSMANSFvgTRSYMSPERlqgthYTVQS--------DI 181
                        90
                ....*....|....*.
gi 46577677 219 WSLGCVLYAMMFGEGP 234
Cdd:cd06615 182 WSLGLSLVEMAIGRYP 197
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
92-293 7.55e-05

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 43.68  E-value: 7.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  92 HEAWLLLPFFKRG-TLWNEIERLKDKgnfLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILL--GDEGQPVLMDLG 168
Cdd:cd14124  93 HDSYRFLVFPSLGqSLQSALDEGKGV---LSEKAVLQLACRLLDALEFIHENEYVHGDITAENIFVdpEDQSEVYLAGYG 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 169 SMNQAC------IHVEGSRqalTLQDWAAqrctisyrapELFSVQSH--CVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ 240
Cdd:cd14124 170 FAFRYCpggkhvEYREGSR---SPHEGDI----------EFISLDSHkgAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLH 236
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46577677 241 KGDSVALAVQNQLSIP--------QSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEAL 293
Cdd:cd14124 237 NTEDIMKQKERFMDDVpgflgpcfHQKKVSEALQKYLKVVMALQYEEKPDYAMLRNGLSAA 297
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
65-235 8.36e-05

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 43.21  E-value: 8.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  65 EADMHRLFNHPNILRLVAYCLRERGAkheAWLLLPFFKRGTL--WNEIERLKDKGNF--LTEDQILWLLLGICRGLEAIH 140
Cdd:cd05043  57 ESSLLYGLSHQNLLPILHVCIEDGEK---PMVLYPYMNWGNLklFLQQCRLSEANNPqaLSTQQLVHMALQIACGMSYLH 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 141 AKGYAHRDLKPTNILLGDEGQPVLM------DLGSMNQACIhveGSRQALTLQdWAAqrctISYRAPELFSVQShcvide 214
Cdd:cd05043 134 RRGVIHKDIAARNCVIDDELQVKITdnalsrDLFPMDYHCL---GDNENRPIK-WMS----LESLVNKEYSSAS------ 199
                       170       180
                ....*....|....*....|..
gi 46577677 215 rtDVWSLGCVLYAMM-FGEGPY 235
Cdd:cd05043 200 --DVWSFGVLLWELMtLGQTPY 219
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
2-226 8.55e-05

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 43.46  E-value: 8.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677   2 GHalCVCSRGTVIidNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREAdmhrlfnhpNILRLV 81
Cdd:cd14214   1 GH--LVCRIGDWL--QERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEI---------NVLKKI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  82 AYclRERGAKHEAWLLLPFFK-RGTLWNEIERL-KDKGNFLTED--------QILWLLLGICRGLEAIHAKGYAHRDLKP 151
Cdd:cd14214  68 KE--KDKENKFLCVLMSDWFNfHGHMCIAFELLgKNTFEFLKENnfqpyplpHIRHMAYQLCHALKFLHENQLTHTDLKP 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 152 TNILLGDEGQPVLMDlgsMNQACIHVEGSRQALTLQDWAAQR----------CTISYRAPElfsvqshcVIDE-----RT 216
Cdd:cd14214 146 ENILFVNSEFDTLYN---ESKSCEEKSVKNTSIRVADFGSATfdhehhttivATRHYRPPE--------VILElgwaqPC 214
                       250
                ....*....|
gi 46577677 217 DVWSLGCVLY 226
Cdd:cd14214 215 DVWSLGCILF 224
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
118-293 1.02e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 43.43  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 118 NFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSmnqacihvegSRQALTLQDWAAQ---RC 194
Cdd:cd05103 174 DFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGL----------ARDIYKDPDYVRKgdaRL 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 195 TISYRAPE-----LFSVQShcvidertDVWSLGCVLYAMM-FGEGPYDMVfqKGDSVALAVQNQLSIPQSPRHSSAlrQL 268
Cdd:cd05103 244 PLKWMAPEtifdrVYTIQS--------DVWSFGVLLWEIFsLGASPYPGV--KIDEEFCRRLKEGTRMRAPDYTTP--EM 311
                       170       180
                ....*....|....*....|....*...
gi 46577677 269 LNSMMTV---DPHQRPHIPLLLSQLEAL 293
Cdd:cd05103 312 YQTMLDCwhgEPSQRPTFSELVEHLGNL 339
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
22-237 1.03e-04

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: 43.15  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  22 FIQKLGEGGFsyvDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFnHPNILRLVAYCLRERgakhEAWLLLPFF 101
Cdd:cd13992   7 ASSHTGEPKY---VKKVGVYGGRTVAIKHITFSRTEKRTILQELNQLKELV-HDNLNKFIGICINPP----NIAVVTEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 102 KRGTLwNEIerLKDKGNFLTEDQILWLLLGICRGLEAIH-AKGYAHRDLKPTNILLGDEGQPVLMDLGSMNqaCIHVEGS 180
Cdd:cd13992  79 TRGSL-QDV--LLNREIKMDWMFKSSFIKDIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRN--LLEEQTN 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46577677 181 RQALTLQDWAAQRCTisyrAPELFSVQSHCV-IDERTDVWSLGCVLYAMMFGEGPYDM 237
Cdd:cd13992 154 HQLDEDAQHKKLLWT----APELLRGSLLEVrGTQKGDVYSFAIILYEILFRSDPFAL 207
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
24-281 1.23e-04

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: 42.87  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  24 QKLGEGGFSYVDLVEGLHDGHFYALK---RILCHEQQDREEAQREADMHRL-FNHpnILRLVAYClrergaKHEAWLLLP 99
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKcppSLHVDDSERMELLEEAKKMEMAkFRH--ILPVYGIC------SEPVGLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 100 FFKRGTLwneierlkdkGNFLTEDQILW-----LLLGICRGLEAIH--AKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQ 172
Cdd:cd14025  74 YMETGSL----------EKLLASEPLPWelrfrIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAKW 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 173 AcihvEGSRQALTLQDwaAQRCTISYRAPELFSVQSHCvIDERTDVWSLGCVLYAMMFGEGPYD------MVFQKgdsVA 246
Cdd:cd14025 144 N----GLSHSHDLSRD--GLRGTIAYLPPERFKEKNRC-PDTKHDVYSFAIVIWGILTQKKPFAgennilHIMVK---VV 213
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 46577677 247 LAVQNQLSI--PQSPRHSSALRQLLNSMMTVDPHQRP 281
Cdd:cd14025 214 KGHRPSLSPipRQRPSECQQMICLMKRCWDQDPRKRP 250
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
73-293 1.37e-04

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 42.64  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677  73 NHPNILRLVAYCLRErgakHEAWLLLPFFKRGTL--------------------WNEIERLKDKGNFLTEDQILWLLLGI 132
Cdd:cd05045  61 NHPHVIKLYGACSQD----GPLLLIVEYAKYGSLrsflresrkvgpsylgsdgnRNSSYLDNPDERALTMGDLISFAWQI 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 133 CRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLG---SMNQACIHVEGSRqaltlqdwaaQRCTISYRAPElfSVQSH 209
Cdd:cd05045 137 SRGMQYLAEMKLVHRDLAARNVLVAEGRKMKISDFGlsrDVYEEDSYVKRSK----------GRIPVKWMAIE--SLFDH 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46577677 210 cVIDERTDVWSLGCVLYAMM-FGEGPYDMVFQKGDSVALAVQNQLSIPQSPrhSSALRQLLNSMMTVDPHQRPHIPLLLS 288
Cdd:cd05045 205 -IYTTQSDVWSFGVLLWEIVtLGGNPYPGIAPERLFNLLKTGYRMERPENC--SEEMYNLMLTCWKQEPDKRPTFADISK 281

                ....*
gi 46577677 289 QLEAL 293
Cdd:cd05045 282 ELEKM 286
 
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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