NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|594150345|ref|NP_001277304|]
View 

calcium/calmodulin-dependent protein kinase type 1D isoform c [Mus musculus]

Protein Classification

calcium/calmodulin-dependent protein kinase type 1D( domain architecture ID 10197682)

calcium/calmodulin-dependent protein kinase type 1D is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is stimulated by calcium and calmodulin (CaM)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-312 0e+00

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: 603.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14168    1 WKKQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKM 171
Cdd:cd14168   81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDS 251
Cdd:cd14168  161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNFAKSKWRQAFNA 312
Cdd:cd14168  241 AKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQAFNA 301
 
Name Accession Description Interval E-value
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-312 0e+00

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: 603.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14168    1 WKKQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKM 171
Cdd:cd14168   81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDS 251
Cdd:cd14168  161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNFAKSKWRQAFNA 312
Cdd:cd14168  241 AKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQAFNA 301
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-279 4.53e-123

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 354.53  E-value: 4.53e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFEQILKAEYEFDSPYWdDISDSAKDFIRNLME 261
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPgDDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 594150345   262 KDPNKRYTCEQAARHPWI 279
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
23-279 1.71e-80

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 244.85  E-value: 1.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYylhrmgivhrdlkpenllyysqdeeskimisdfglskmegKGDVMSTA 181
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLE----------------------------------------SGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPyWDDISDSAKDFIRNLME 261
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 594150345  262 KDPNKRYTCEQAARHPWI 279
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-275 8.32e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 205.25  E-value: 8.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEarERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV--M 178
Cdd:COG0515   89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL---TPDGRVKLIDFGIARALGGATLtqT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                        250
                 ....*....|....*...
gi 594150345 259 LMEKDPNKRY-TCEQAAR 275
Cdd:COG0515  246 ALAKDPEERYqSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
7-281 8.05e-61

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 198.50  E-value: 8.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   7 ESSSSWKKQAedikkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKA-LKGKE-SSIENEIAVLRKIKHENIVAL 84
Cdd:PTZ00263  10 PDTSSWKLSD------FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQvQHVAQEKSILMELSHPFIVNM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  85 EDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:PTZ00263  84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMegKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPY 244
Cdd:PTZ00263 161 DFGFAKK--VPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF--PN 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 245 WDDisDSAKDFIRNLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:PTZ00263 237 WFD--GRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFHG 276
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
27-268 4.59e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 100.25  E-value: 4.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIpkkalkgKESSIENEIAVLR---------KIKHENIVALEDIYESPNHLYLV 97
Cdd:NF033483  13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL-------RPDLARDPEFVARfrreaqsaaSLSHPNIVSVYDVGEDGGIPYIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMisDFGLSK------M 171
Cdd:NF033483  86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKDGRVKVT--DFGIARalssttM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMstacGTPGYVAPEvlaQKPYSKA---VDCWSIGVIAYILLCGYPPFydENDS------KLFEQILKAEYEFDs 242
Cdd:NF033483 163 TQTNSVL----GTVHYLSPE---QARGGTVdarSDIYSLGIVLYEMLTGRPPF--DGDSpvsvayKHVQEDPPPPSELN- 232
                        250       260
                 ....*....|....*....|....*.
gi 594150345 243 pywDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:NF033483 233 ---PGIPQSLDAVVLKATAKDPDDRY 255
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
69-278 4.65e-23

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: 101.07  E-value: 4.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    69 EIAVLRKIKHENIVALEDIYES-PNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKP 147
Cdd:TIGR03903   28 ETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   148 ENLLYYSQDEESKIMISDFGLSKM-EGKGDVMSTAC-------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP 219
Cdd:TIGR03903  108 QNIMVSQTGVRPHAKVLDFGIGTLlPGVRDADVATLtrttevlGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQR 187
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345   220 PFYDENDSKLFEQILKAEyEFDSPYWDDiSDSAKDFIRNLMEKDPNKRytcEQAARHPW 278
Cdd:TIGR03903  188 VVQGASVAEILYQQLSPV-DVSLPPWIA-GHPLGQVLRKALNKDPRQR---AASAPALA 241
 
Name Accession Description Interval E-value
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
12-312 0e+00

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: 603.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14168    1 WKKQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKM 171
Cdd:cd14168   81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDS 251
Cdd:cd14168  161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNFAKSKWRQAFNA 312
Cdd:cd14168  241 AKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQAFNA 301
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-278 0e+00

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: 594.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14083    1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGdVM 178
Cdd:cd14083   81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSKMEDSG-VM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14083  160 STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIRH 239
                        250       260
                 ....*....|....*....|
gi 594150345 259 LMEKDPNKRYTCEQAARHPW 278
Cdd:cd14083  240 LMEKDPNKRYTCEQALEHPW 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-281 0e+00

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: 549.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14167    1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd14167   81 QLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGSVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14167  161 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQH 240
                        250       260
                 ....*....|....*....|...
gi 594150345 259 LMEKDPNKRYTCEQAARHPWIAG 281
Cdd:cd14167  241 LMEKDPEKRFTCEQALQHPWIAG 263
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-305 0e+00

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: 529.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14166    1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLS-RDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGdVM 178
Cdd:cd14166   80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSKMEQNG-IM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14166  159 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRH 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 259 LMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNFAKSK 305
Cdd:cd14166  239 LLEKNPSKRYTCEKALSHPWIIGNTALHRDIYPSVSEQIQKNFAKSK 285
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-296 2.19e-179

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: 498.26  E-value: 2.19e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14169    1 INSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGdVM 178
Cdd:cd14169   81 ELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLSKIEAQG-ML 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14169  160 STACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIRH 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 259 LMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQ 296
Cdd:cd14169  240 LLERDPEKRFTCEQALQHPWISGDTALDRDIHGSVSEQ 277
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-278 1.55e-154

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: 434.60  E-value: 1.55e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKsEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd05117   82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLME 261
Cdd:cd05117  162 CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLLV 241
                        250
                 ....*....|....*..
gi 594150345 262 KDPNKRYTCEQAARHPW 278
Cdd:cd05117  242 VDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-279 4.53e-123

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 354.53  E-value: 4.53e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFEQILKAEYEFDSPYWdDISDSAKDFIRNLME 261
Cdd:smart00220 158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPgDDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLIRKLLV 236
                          250
                   ....*....|....*...
gi 594150345   262 KDPNKRYTCEQAARHPWI 279
Cdd:smart00220 237 KDPEKRLTAEEALQHPFF 254
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
23-278 5.05e-111

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: 324.28  E-value: 5.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY-SQDEESKIMISDFGLSkMEGKgDVMSTA 181
Cdd:cd14095   82 GGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVeHEDGSKSLKLADFGLA-TEVK-EPLFTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK--LFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd14095  160 CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQeeLFDLILAGEFEFLSPYWDNISDSAKDLISRM 239
                        250
                 ....*....|....*....
gi 594150345 260 MEKDPNKRYTCEQAARHPW 278
Cdd:cd14095  240 LVVDPEKRYSAGQVLDHPW 258
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-312 2.14e-109

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: 321.39  E-value: 2.14e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgkeSSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14085    1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDK---KIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd14085   78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN-DSKLFEQILKAEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd14085  158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERgDQYMFKRILNCDYDFVSPWWDDVSLNAKDLVK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWIAGDTAlSKNIHESVSAQIRKNFAKSKWRQAFNA 312
Cdd:cd14085  238 KLIVLDPKKRLTTQQALQHPWVTGKAA-NFAHMDTAQKKLQEFNARRKLKAAVKA 291
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
23-278 2.83e-108

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: 317.15  E-value: 2.83e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEkIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14003   82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---DKNGNLKIIDFGLSNEFRGGSLLKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLM 260
Cdd:cd14003  159 CGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPI--PSH--LSPDARDLIRRML 234
                        250
                 ....*....|....*...
gi 594150345 261 EKDPNKRYTCEQAARHPW 278
Cdd:cd14003  235 VVDPSKRITIEEILNHPW 252
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
23-279 9.34e-107

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: 313.70  E-value: 9.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC-RGREV-CESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGD--VMST 180
Cdd:cd14087   81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGPncLMKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd14087  161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLL 240
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14087  241 TVNPGERLSATQALKHPWI 259
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-309 9.72e-99

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: 294.33  E-value: 9.72e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14086    3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDhQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLS-KMEGKGDVMST 180
Cdd:cd14086   83 TGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAiEVQGDQQAWFG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd14086  163 FAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQML 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 261 EKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSAQIRKNF-AKSKWRQA 309
Cdd:cd14086  243 TVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFnARRKLKGA 292
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
23-279 1.11e-98

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: 293.08  E-value: 1.11e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14088    3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEgkGDVMSTAC 182
Cdd:cd14088   83 GREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKLE--NGLIKEPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE--------NDSKLFEQILKAEYEFDSPYWDDISDSAKD 254
Cdd:cd14088  161 GTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEaeeddyenHDKNLFRKILAGDYEFDSPYWDDISQAAKD 240
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14088  241 LVTRLMEVEQDQRITAEEAISHEWI 265
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
17-279 1.14e-96

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: 288.52  E-value: 1.14e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKG-------KESSIENEIAVLRKIKHENIVALEDIYE 89
Cdd:cd14084    2 KELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIgsrreinKPRNIETEIEILKKLSHPCIIKIEDFFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  90 SPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLS 169
Cdd:cd14084   82 AEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDVMSTACGTPGYVAPEVLA---QKPYSKAVDCWSIGVIAYILLCGYPPFYDEN-DSKLFEQILKAEYEFDSPYW 245
Cdd:cd14084  162 KILGETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYtQMSLKEQILSGKYTFIPKAW 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 594150345 246 DDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14084  242 KNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-279 1.09e-92

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: 278.94  E-value: 1.09e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLA-EEKATGKLFAVKCIPKK-----ALKGKES-SIENEIAVLRKIKHENIVALEDIYESPNHLY 95
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKAdlssdNLKGSSRaNILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL-------------YYSQDEESK-- 160
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklRKADDDETKvd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 161 ---------------IMISDFGLSKMEGKGDVMsTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN 225
Cdd:cd14096  163 egefipgvggggigiVKLADFGLSKQVWDSNTK-TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDES 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 226 DSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14096  242 IETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
29-279 1.71e-92

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: 276.80  E-value: 1.71e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDRED-VRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFY-TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeSKIMISDFGLS-KMEGKGDVMsTACGTPG 186
Cdd:cd14103   80 RVVDDDFElTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTG-NQIKIIDFGLArKYDPDKKLK-VLFGTPE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNK 266
Cdd:cd14103  158 FVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRK 237
                        250
                 ....*....|...
gi 594150345 267 RYTCEQAARHPWI 279
Cdd:cd14103  238 RMSAAQCLQHPWL 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
29-278 4.57e-92

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: 275.69  E-value: 4.57e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD--KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeSKIMISDFGLSKMEGKGDVMSTACGTPGYV 188
Cdd:cd14006   79 RLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPS-PQIKIIDFGLARKLNPGEELKEIFGTPEFV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 189 APEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:cd14006  158 APEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEPRKRP 237
                        250
                 ....*....|
gi 594150345 269 TCEQAARHPW 278
Cdd:cd14006  238 TAQEALQHPW 247
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
23-278 1.72e-90

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: 272.29  E-value: 1.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESK-IMISDFGLSK-MEGKgdvMST 180
Cdd:cd14184   83 GGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKsLKLGDFGLATvVEGP---LYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND--SKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14184  160 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSPYWDNITDSAKELISH 239
                        250       260
                 ....*....|....*....|
gi 594150345 259 LMEKDPNKRYTCEQAARHPW 278
Cdd:cd14184  240 MLQVNVEARYTAEQILSHPW 259
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
23-279 1.15e-87

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: 264.72  E-value: 1.15e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQksGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEGKGDVMST 180
Cdd:cd14007   82 APNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILL---GSNGELKLADFGWSV-HAPSNRRKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdspyWDDISDSAKDFIRNLM 260
Cdd:cd14007  158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKF----PSSVSPEAKDLISKLL 233
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14007  234 QKDPSKRLSLEQVLNHPWI 252
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
29-278 1.89e-87

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: 263.99  E-value: 1.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIikRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM-EGKGDVMSTACGTP 185
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL---DSDGHIKLTDFGLAKElSSDGDRTYTFCGTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKDFIRNLMEKDPN 265
Cdd:cd05123  158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFP----EYVSPEAKSLISGLLQKDPT 233
                        250
                 ....*....|....*.
gi 594150345 266 KRYTCEQAA---RHPW 278
Cdd:cd05123  234 KRLGSGGAEeikAHPF 249
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
23-278 2.26e-87

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: 264.60  E-value: 2.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIE-------NEIAVLRKI-KHENIVALEDIYESPNHL 94
Cdd:cd14093    5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEelreatrREIEILRQVsGHPNIIELHDVFESPTFI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGK 174
Cdd:cd14093   85 FLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL---DDNLNVKISDFGFATRLDE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLA------QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDI 248
Cdd:cd14093  162 GEKLRELCGTPGYLAPEVLKcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSPEWDDI 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 249 SDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14093  242 SDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
23-288 5.48e-87

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: 264.11  E-value: 5.48e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalkGKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKS---KRDPSEEIEI-LLRYGQHPNIITLRDVYDDGNSVYLVTELLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY--SQDEESkIMISDFGLSKM--EGKGDVM 178
Cdd:cd14091   78 GGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYAdeSGDPES-LRICDFGFAKQlrAENGLLM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 sTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF-YDENDSKlfEQILK----AEYEFDSPYWDDISDSAK 253
Cdd:cd14091  157 -TPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFaSGPNDTP--EVILArigsGKIDLSGGNWDHVSDSAK 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKN 288
Cdd:cd14091  234 DLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQR 268
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
23-278 2.62e-86

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: 261.42  E-value: 2.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLY-YSQDEESKIMISDFGLSKMEGKGdvMSTA 181
Cdd:cd14185   82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqHNPDKSTTLKLADFGLAKYVTGP--IFTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY--DENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd14185  160 CGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRspERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLISRL 239
                        250
                 ....*....|....*....
gi 594150345 260 MEKDPNKRYTCEQAARHPW 278
Cdd:cd14185  240 LVVDPEKRYTAKQVLQHPW 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
23-278 7.08e-85

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: 258.17  E-value: 7.08e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIE---NEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQlfqREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMISDFGLSKMEGKGDVMS 179
Cdd:cd14098   82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENIL-ITQDDPVIVKISDFGLAKVIHTGTFLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKP------YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd14098  161 TFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNISEEAI 240
                        250       260
                 ....*....|....*....|....*
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14098  241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
19-282 2.18e-84

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: 256.85  E-value: 2.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14183    4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYS-QDEESKIMISDFGLSKM-EGKgd 176
Cdd:cd14183   84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhQDGSKSLKLGDFGLATVvDGP-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK--LFEQILKAEYEFDSPYWDDISDSAKD 254
Cdd:cd14183  162 -LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQevLFDQILMGQVDFPSPYWDNVSDSAKE 240
                        250       260
                 ....*....|....*....|....*...
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWIAGD 282
Cdd:cd14183  241 LITMMLQVDVDQRYSALQVLEHPWVNDD 268
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
28-279 3.53e-84

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: 255.64  E-value: 3.53e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14081    8 TLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLskESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGTP 185
Cdd:cd14081   88 LFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL---DEKNNIKIADFGMASLQPEGSLLETSCGSP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPY--SKAvDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPywDDISDSAKDFIRNLMEKD 263
Cdd:cd14081  165 HYACPEVIKGEKYdgRKA-DIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHI--P--HFISPDAQDLLRRMLEVN 239
                        250
                 ....*....|....*.
gi 594150345 264 PNKRYTCEQAARHPWI 279
Cdd:cd14081  240 PEKRITIEEIKKHPWF 255
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
17-279 4.03e-84

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: 256.26  E-value: 4.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK-----ESSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14105    1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvsREDIEREVSILRQVLHPNIITLHDVFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSK 170
Cdd:cd14105   81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIpRIKLIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISD 250
Cdd:cd14105  161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14105  241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-313 7.42e-83

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: 254.53  E-value: 7.42e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKEssieneIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14092   12 EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSRE------VQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTP 185
Cdd:cd14092   86 LLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFARLKPENQPLKTPCFTL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPF----YDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd14092  166 PYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDGEEWKNVSSEAKSLIQ 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWIAGDTALSKN------IHESVSAQIRKNFakskwRQAFNAT 313
Cdd:cd14092  246 GLLTVDPSKRLTMSELRNHPWLQGSSSPSSTplmtpgVLSSSAAAVSTAL-----RATFDAF 302
Pkinase pfam00069
Protein kinase domain;
23-279 1.71e-80

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 244.85  E-value: 1.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYylhrmgivhrdlkpenllyysqdeeskimisdfglskmegKGDVMSTA 181
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGLE----------------------------------------SGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPyWDDISDSAKDFIRNLME 261
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLK 199
                         250
                  ....*....|....*...
gi 594150345  262 KDPNKRYTCEQAARHPWI 279
Cdd:pfam00069 200 KDPSKRLTATQALQHPWF 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-278 8.75e-80

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: 244.62  E-value: 8.75e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAreGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGDVM 178
Cdd:cd14663   82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLL---DEDGNLKISDFGLSALseQFRQDGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 -STACGTPGYVAPEVLAQKPYSKA-VDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFI 256
Cdd:cd14663  159 lHTTCGTPNYVAPEVLARRGYDGAkADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEY--PRW--FSPGAKSLI 234
                        250       260
                 ....*....|....*....|..
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14663  235 KRILDPNPSTRITVEQIMASPW 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
29-279 4.02e-79

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: 243.23  E-value: 4.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK-------------ESSIENEIAVLRKIKHENIVALEDIYESP--NH 93
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRregkndrgkiknaLDDVRREIAIMKKLDHPNIVRLYEVIDDPesDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM 171
Cdd:cd14008   81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLL---TADGTVKISDFGVSEM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 -EGKGDVMSTACGTPGYVAPEVLA--QKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPywDD 247
Cdd:cd14008  158 fEDGNDTLQKTAGTPAFLAPELCDgdSKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIP--PE 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 248 ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14008  236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
26-278 4.27e-79

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: 242.96  E-value: 4.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGkessiENEIAV-LRKIKHENIVALEDIYESPNH----LYLVMQL 100
Cdd:cd14089    6 KQVLGLGINGKVLECFHKKTGEKFALK-VLRDNPKA-----RREVELhWRASGCPHIVRIIDVYENTYQgrkcLLVVMEC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd14089   80 MEGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLF----EQILKAEYEFDSPYWDDISDSAKD 254
Cdd:cd14089  160 QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkKRIRNGQYEFPNPEWSNVSEEAKD 239
                        250       260
                 ....*....|....*....|....
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14089  240 LIRGLLKTDPSERLTIEEVMNHPW 263
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
19-279 5.89e-78

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: 239.98  E-value: 5.89e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14078    1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKME-GKGD 176
Cdd:cd14078   81 EYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL---DEDQNLKLIDFGLcAKPKgGMDH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPY--SKAvDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEfdSPYWddISDSAKD 254
Cdd:cd14078  158 HLETCCGSPAYAAPELIQGKPYigSEA-DVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYE--EPEW--LSPSSKL 232
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14078  233 LLDQMLQVDPKKRITVKELLNHPWV 257
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
27-278 3.79e-76

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: 235.24  E-value: 3.79e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd14079    8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEekIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGT 184
Cdd:cd14079   88 ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL---DSNMNVKIADFGLSNIMRDGEFLKTSCGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKD 263
Cdd:cd14079  165 PNYAAPEVISGKLYAgPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPS----HLSPGARDLIKRMLVVD 240
                        250
                 ....*....|....*
gi 594150345 264 PNKRYTCEQAARHPW 278
Cdd:cd14079  241 PLKRITIPEIRQHPW 255
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
21-279 5.33e-76

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: 235.52  E-value: 5.33e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14097    1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINReKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESK----IMISDFGLS--KMEG 173
Cdd:cd14097   81 LCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLSvqKYGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd14097  161 GEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAK 240
                        250       260
                 ....*....|....*....|....*.
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14097  241 NVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
17-279 2.41e-75

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: 233.76  E-value: 2.41e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK------GKESsIENEIAVLRKIKHENIVALEDIYES 90
Cdd:cd14194    1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKssrrgvSRED-IEREVSILKEIQHPNVITLHEVYEN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQD-EESKIMISDFGLS 169
Cdd:cd14194   80 KTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvPKPRIKIIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDIS 249
Cdd:cd14194  160 HKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTS 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14194  240 ALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
23-279 5.61e-74

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: 229.58  E-value: 5.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMvrIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL---DQNGNAKIADFGLSNLYSKDKLLQT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEY-EFDSPywddiSDsAKDFIRN 258
Cdd:cd14073  160 FCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYrEPTQP-----SD-ASGLIRW 233
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14073  234 MLTVNPKRRATIEDIANHWWV 254
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
16-278 3.01e-73

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: 228.70  E-value: 3.01e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  16 AEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCI---PKK----ALKGKESSIENEIAVLRKIK-HENIVALEDI 87
Cdd:cd14181    5 AKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIevtAERlspeQLEEVRSSTLKEIHILRQVSgHPSIITLIDS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd14181   85 YESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLHIKLSDFG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKMEGKGDVMSTACGTPGYVAPEVL------AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFD 241
Cdd:cd14181  162 FSCHLEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFS 241
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 594150345 242 SPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14181  242 SPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
17-279 3.04e-73

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: 228.39  E-value: 3.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKET-LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESS--IENEIAVLRKIK-HENIVALEDIYESPN 92
Cdd:cd14106    3 ENINEVYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFL-RKRRRGQDCRneILHEIAVLELCKdCPRVVNLHEVYETRS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKME 172
Cdd:cd14106   82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSA 252
Cdd:cd14106  162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLA 241
                        250       260
                 ....*....|....*....|....*..
gi 594150345 253 KDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14106  242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
17-279 3.98e-73

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: 228.30  E-value: 3.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-----SSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14196    1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrgvsrEEIEREVSILRQVLHPNIITLHDVYENR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEE-SKIMISDFGLSK 170
Cdd:cd14196   81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPiPHIKLIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISD 250
Cdd:cd14196  161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14196  241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
27-279 3.59e-72

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: 226.53  E-value: 3.59e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlKGKESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14090    8 ELLGEGAYASVQTCINLYTGKEYAVKIIEKHP-GHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGL-SKMEGKGDVMS----- 179
Cdd:cd14090   87 LLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLgSGIKLSSTSMTpvttp 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 ---TACGTPGYVAPEVL------AQKpYSKAVDCWSIGVIAYILLCGYPPFYDENDSK---------------LFEQILK 235
Cdd:cd14090  167 ellTPVGSAEYMAPEVVdafvgeALS-YDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqdcqelLFHSIQE 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 594150345 236 AEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14090  246 GEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
17-279 1.93e-71

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: 223.73  E-value: 1.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-----SSIENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd14195    1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrgvsrEEIEREVNILREIQHPNIITLHDIFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSK 170
Cdd:cd14195   81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNpRIKLIDFGIAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISD 250
Cdd:cd14195  161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14195  241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
21-279 3.00e-71

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: 222.81  E-value: 3.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-KGK-ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKqREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDV 177
Cdd:cd14099   81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL---DENMNVKIGDFGLAaRLEYDGER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLA-QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWDDISDSAKDFI 256
Cdd:cd14099  158 KKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSF--PSHLSISDEAKDLI 235
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14099  236 RSMLQPDPTKRPSLDEILSHPFF 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
23-279 5.79e-71

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: 222.44  E-value: 5.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEK--ATGKLFAVKCIPKKalKGKESSIEN----EIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKK--KAPKDFLEKflprELEILRKLRHPNIIQVYSIFERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGK 174
Cdd:cd14080   80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL---DSNNNVKLSDFGFARLcpDDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMS-TACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWdDISDSA 252
Cdd:cd14080  157 GDVLSkTFCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVK-KLSPEC 235
                        250       260
                 ....*....|....*....|....*..
gi 594150345 253 KDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14080  236 KDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
27-279 8.77e-71

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: 221.63  E-value: 8.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKES-SIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELeALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMS---TAC 182
Cdd:cd06606   86 LASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILV---DSDGVVKLADFGCAKRLAEIATGEgtkSLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFDSPywDDISDSAKDFIRNLME 261
Cdd:cd06606  163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVaALFKIGSSGEPPPIP--EHLSEEAKDFLRKCLQ 240
                        250
                 ....*....|....*...
gi 594150345 262 KDPNKRYTCEQAARHPWI 279
Cdd:cd06606  241 RDPKKRPTADELLQHPFL 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
25-279 1.75e-70

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: 221.95  E-value: 1.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLFAVKCIpkkaLKGKESSIENEIAVlRKIKHENIVALEDIY----------ESPNHL 94
Cdd:cd14171   10 WTQKLGTGISGPVRVCVKKSTGERFALKIL----LDRPKARTEVRLHM-MCSGHPNIVQIYDVYansvqfpgesSPRARL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEgK 174
Cdd:cd14171   85 LIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGFAKVD-Q 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMsTACGTPGYVAPEVL-AQK----------------PYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-----LFEQ 232
Cdd:cd14171  164 GDLM-TPQFTPYYVAPQVLeAQRrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRtitkdMKRK 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 233 ILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14171  243 IMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
23-289 4.58e-70

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: 220.91  E-value: 4.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIikLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMegKGDVMST 180
Cdd:cd05580   83 VPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL---DSDGHIKITDFGFAKR--VKDRTYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYwddiSDSAKDFIRNLM 260
Cdd:cd05580  158 LCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFF----DPDAKDLIKRLL 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 594150345 261 EKDPNKRYTC-----EQAARHPWIAG---DTALSKNI 289
Cdd:cd05580  234 VVDLTKRLGNlkngvEDIKNHPWFAGidwDALLQRKI 270
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
20-279 7.78e-70

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: 219.49  E-value: 7.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14191    1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd14191   80 MVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTKIKLIDFGLARRLENAGSL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd14191  159 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 238
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14191  239 LLKKDMKARLTCTQCLQHPWL 259
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
23-278 7.38e-69

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: 217.47  E-value: 7.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIikEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG------- 173
Cdd:cd05581   83 APNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILL---DEDMHIKITDFGTAKVLGpdsspes 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 -KGDVMSTA----------CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDs 242
Cdd:cd05581  160 tKGDADSQIaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFP- 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 243 pywDDISDSAKDFIRNLMEKDPNKRYTC------EQAARHPW 278
Cdd:cd05581  239 ---ENFPPDAKDLIQKLLVLDPSKRLGVnenggyDELKAHPF 277
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
23-288 2.44e-68

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: 216.80  E-value: 2.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK---RDPSEEIEI-LLRYGQHPNIITLKDVYDDGKFVYLVMELMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY--SQDEESkIMISDFGLSK-MEGKGDVMS 179
Cdd:cd14178   81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMdeSGNPES-IRICDFGFAKqLRAENGLLM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY---DENDSKLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd14178  160 TPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDAAKDIV 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWIAGDTALSKN 288
Cdd:cd14178  240 SKMLHVDPHQRLTAPQVLRHPWIVNREYLSQN 271
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
23-278 2.64e-68

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: 215.93  E-value: 2.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKGKESSIEnEIAVLRKIK-HENIVALEDIYESPN 92
Cdd:cd14182    5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIditgggsfsPEEVQELREATLK-EIDILRKVSgHPNIIQLKDTYETNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME 172
Cdd:cd14182   84 FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL---DDDMNIKLTDFGFSCQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTACGTPGYVAPEVLA------QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWD 246
Cdd:cd14182  161 DPGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWD 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 247 DISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14182  241 DRSDTVKDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
26-279 2.69e-68

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: 215.62  E-value: 2.69e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKlfavKCIPKKALKGKESSIENEIAVlRKIKHENIVALEDIYESPNH----LYLVMQLV 101
Cdd:cd14172    9 KQVLGLGVNGKVLECFHRRTGQ----KCALKLLYDSPKARREVEHHW-RASGGPHIVHILDVYENMHHgkrcLLIIMECM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKG--FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMS 179
Cdd:cd14172   84 EGGELFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQNALQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLF----EQILKAEYEFDSPYWDDISDSAKDF 255
Cdd:cd14172  164 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGFPNPEWAEVSEEAKQL 243
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14172  244 IRHLLKTDPTERMTITQFMNHPWI 267
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
26-288 1.38e-67

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: 214.89  E-value: 1.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14175    6 KETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK---RDPSEEIEI-LLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY--SQDEESkIMISDFGLSK-MEGKGDVMSTAC 182
Cdd:cd14175   82 LLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVdeSGNPES-LRICDFGFAKqLRAENGLLMTPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD---ENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd14175  161 YTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKM 240
                        250       260
                 ....*....|....*....|....*....
gi 594150345 260 MEKDPNKRYTCEQAARHPWIAGDTALSKN 288
Cdd:cd14175  241 LHVDPHQRLTAKQVLQHPWITQKDKLPQS 269
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
23-275 1.79e-67

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: 213.22  E-value: 1.79e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIE---NEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIK-VLRPELAEDEEFRErflREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMS 179
Cdd:cd14014   81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL---TEDGRVKLTDFGIARALGDSGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 T--ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd14014  158 TgsVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIIL 237
                        250
                 ....*....|....*....
gi 594150345 258 NLMEKDPNKRY-TCEQAAR 275
Cdd:cd14014  238 RALAKDPEERPqSAAELLA 256
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
27-279 2.70e-67

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: 212.85  E-value: 2.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14193   10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEE-VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKGDVMSTACGTP 185
Cdd:cd14193   89 FDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSR-EANQVKIIDFGLARRYKPREKLRVNFGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPN 265
Cdd:cd14193  168 EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKS 247
                        250
                 ....*....|....
gi 594150345 266 KRYTCEQAARHPWI 279
Cdd:cd14193  248 WRMSASEALKHPWL 261
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
32-281 2.92e-67

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: 213.23  E-value: 2.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDR 109
Cdd:cd05579    4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNqvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 110 IVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGDVMS-------- 179
Cdd:cd05579   84 LENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILI---DANGHLKLTDFGLSKVglVRRQIKLSiqkksnga 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 ------TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWDDISDSAK 253
Cdd:cd05579  161 pekedrRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEW--PEDPEVSDEAK 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAA---RHPWIAG 281
Cdd:cd05579  239 DLISKLLTPDPEKRLGAKGIEeikNHPFFKG 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
22-279 3.30e-67

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: 212.45  E-value: 3.30e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKE-KKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd05122   80 SGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILL---TSDGEVKLIDFGLSAQLSDGKTRNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK-AEYEFDSPYWddISDSAKDFIRNL 259
Cdd:cd05122  157 FVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATnGPPGLRNPKK--WSKEFKDFLKKC 234
                        250       260
                 ....*....|....*....|
gi 594150345 260 MEKDPNKRYTCEQAARHPWI 279
Cdd:cd05122  235 LQKDPEKRPTAEQLLKHPFI 254
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
22-280 2.19e-66

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 211.80  E-value: 2.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14177    5 VYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK---RDPSEEIEI-LMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSK-MEGKGDVMS 179
Cdd:cd14177   81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFAKqLRGENGLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDS--KLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd14177  161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANgPNDTpeEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                        250       260
                 ....*....|....*....|....
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd14177  241 SHMLHVDPHQRYTAEQVLKHSWIA 264
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
29-278 5.77e-66

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: 209.00  E-value: 5.77e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK-ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGY 187
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSPLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd14009  161 MAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
                        250
                 ....*....|.
gi 594150345 268 YTCEQAARHPW 278
Cdd:cd14009  241 ISFEEFFAHPF 251
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
29-277 6.22e-65

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: 205.20  E-value: 6.22e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEK-GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKGDVMSTACG--T 184
Cdd:cd00180   81 LLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKdLDSDDSLLKTTGGttP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILlcgyppfydendsklfeqilkaeyefdspywddisDSAKDFIRNLMEKDP 264
Cdd:cd00180  158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDP 202
                        250
                 ....*....|...
gi 594150345 265 NKRYTCEQAARHP 277
Cdd:cd00180  203 KKRPSAKELLEHL 215
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
29-281 1.32e-64

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: 205.92  E-value: 1.32e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIvqTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGTPG 186
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL---DSNGYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY--DENDSKLFEQILKAEYEFDSPywDDISDSAKDFIRNLMEKDP 264
Cdd:cd05572  158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKGIDKIEFP--KYIDKNAKNLIKQLLRRNP 235
                        250       260
                 ....*....|....*....|..
gi 594150345 265 NKRYTCEQAA-----RHPWIAG 281
Cdd:cd05572  236 EERLGYLKGGirdikKHKWFEG 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-288 2.02e-64

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: 207.20  E-value: 2.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgkESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRM----EANTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGELL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGD-VMSTACGTPG 186
Cdd:cd14179   91 ERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPDNqPLKTPCFTLH 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS-------KLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd14179  171 YAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQGL 250
                        250       260
                 ....*....|....*....|....*....
gi 594150345 260 MEKDPNKRYTCEQAARHPWIAGDTALSKN 288
Cdd:cd14179  251 LTVDPNKRIKMSGLRYNEWLQDGSQLSSN 279
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
23-279 3.58e-64

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: 207.57  E-value: 3.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY--SQDEESkIMISDFGLSK-MEGKGDVMS 179
Cdd:cd14176   97 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdeSGNPES-IRICDFGFAKqLRAENGLLM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY---DENDSKLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd14176  176 TPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLV 255
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14176  256 SKMLHVDPHQRLTAALVLRHPWI 278
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
19-279 6.34e-64

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: 204.18  E-value: 6.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKG-KESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd14074    1 IAGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDvSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIV--EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKImiSDFGLSKMEGKG 175
Cdd:cd14074   81 LELGDGGDMYDYIMkhENGL-NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKL--TDFGFSNKFQPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKD 254
Cdd:cd14074  158 EKLETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP----AHVSPECKD 233
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14074  234 LIRRMLIRDPKKRASLEEIENHPWL 258
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
26-279 7.20e-64

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: 204.00  E-value: 7.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14190    9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVL-LEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFY-TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEEsKIMISDFGLSKMEGKGDVMSTACGT 184
Cdd:cd14190   88 LFERIVDEDYHlTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH-QVKIIDFGLARRYNPREKLKVNFGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDP 264
Cdd:cd14190  167 PEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKER 246
                        250
                 ....*....|....*
gi 594150345 265 NKRYTCEQAARHPWI 279
Cdd:cd14190  247 SARMSATQCLKHPWL 261
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
29-280 8.20e-64

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: 206.05  E-value: 8.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKEssienEIA-------VLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKD-----EVAhtltenrVLQNTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGK-GDVMST 180
Cdd:cd05571   78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFGLCKEEISyGATTKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLM 260
Cdd:cd05571  155 FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS----TLSPEAKSLLAGLL 230
                        250       260
                 ....*....|....*....|....*
gi 594150345 261 EKDPNKRY-----TCEQAARHPWIA 280
Cdd:cd05571  231 KKDPKKRLgggprDAKEIMEHPFFA 255
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-279 2.42e-63

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: 203.06  E-value: 2.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP--------KKALKGKESSIENEIAVLRK------IKHENIVALEDIY 88
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkKEREKRLEKEISRDIRTIREaalsslLNHPHICRLRDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL 168
Cdd:cd14077   83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILI---SKSGNIKIIDFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 SKMEGKGDVMSTACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWdd 247
Cdd:cd14077  160 SNLYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEY--PSY-- 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 248 ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14077  236 LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
27-279 8.97e-63

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: 201.34  E-value: 8.97e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREE-VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFY-TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKGDVMSTACGTP 185
Cdd:cd14192   89 FDRITDESYQlTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNS-TGNQIKIIDFGLARRYKPREKLKVNFGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPN 265
Cdd:cd14192  168 EFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKS 247
                        250
                 ....*....|....
gi 594150345 266 KRYTCEQAARHPWI 279
Cdd:cd14192  248 CRMSATQCLKHEWL 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
23-279 1.29e-62

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: 200.89  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKET-VRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14114   83 GGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTK-RSNEVKLIDFGLATHLDPKESVKVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLME 261
Cdd:cd14114  162 TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLLL 241
                        250
                 ....*....|....*...
gi 594150345 262 KDPNKRYTCEQAARHPWI 279
Cdd:cd14114  242 ADPNKRMTIHQALEHPWL 259
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
23-279 2.23e-62

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: 200.00  E-value: 2.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKErEEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRI----VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKGD 176
Cdd:cd08215   82 DGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFL---TKDGVVKLGDFGISKvLESTTD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE-FDSPYwddiSDSAKDF 255
Cdd:cd08215  159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQY----SSELRDL 234
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08215  235 VNSMLQKDPEKRPSANEILSSPFI 258
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
27-279 4.96e-62

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: 200.65  E-value: 4.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneiavLRKIKHENIVALEDIYE----SPNHLYLVMQLVS 102
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELH-----WRASQCPHIVRIVDVYEnlyaGRKCLLIVMECLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKG--FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd14170   83 GGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN----DSKLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd14170  163 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPEWSEVSEEVKMLI 242
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14170  243 RNLLKTEPTQRMTITEFMNHPWI 265
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
22-309 5.23e-62

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: 200.46  E-value: 5.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE----SSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd14094    4 VYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEK---GF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEG 173
Cdd:cd14094   84 FEFMDGADLCFEIVKRadaGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDeNDSKLFEQILKAEYEFDSPYWDDISDSA 252
Cdd:cd14094  164 ESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESA 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 253 KDFIRNLMEKDPNKRYTCEQAARHPWIAG--DTALSKNIHESVSaQIRKNFAKSKWRQA 309
Cdd:cd14094  243 KDLVRRMLMLDPAERITVYEALNHPWIKErdRYAYRIHLPETVE-QLRKFNARRKLKGA 300
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
23-275 8.32e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 205.25  E-value: 8.32e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEarERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV--M 178
Cdd:COG0515   89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL---TPDGRVKLIDFGIARALGGATLtqT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                        250
                 ....*....|....*...
gi 594150345 259 LMEKDPNKRY-TCEQAAR 275
Cdd:COG0515  246 ALAKDPEERYqSAAELAA 263
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
23-281 1.43e-61

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: 199.17  E-value: 1.43e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKqKVVKLKQvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKgdvMS 179
Cdd:cd14209   83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI---DQQGYIKVTDFGFAKrVKGR---TW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYwddiSDSAKDFIRNL 259
Cdd:cd14209  157 TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHF----SSDLKDLLRNL 232
                        250       260
                 ....*....|....*....|....*..
gi 594150345 260 MEKDPNKRYTCEQAA-----RHPWIAG 281
Cdd:cd14209  233 LQVDLTKRFGNLKNGvndikNHKWFAT 259
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
27-278 1.47e-61

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: 197.94  E-value: 1.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14069    7 QTLGEGAFGEVFLAVNRNTEEAVAVKFVDmKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM---EGKGDVMSTAC 182
Cdd:cd14069   87 LFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLL---DENDNLKISDFGLATVfryKGKERLLNKMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPfYDE--NDSKLFEQILKAEYEFDSPyWDDISDSAKDFIRNL 259
Cdd:cd14069  164 GTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELP-WDQpsDSCQEYSDWKENKKTYLTP-WKKIDTAALSLLRKI 241
                        250
                 ....*....|....*....
gi 594150345 260 MEKDPNKRYTCEQAARHPW 278
Cdd:cd14069  242 LTENPNKRITIEDIKKHPW 260
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-286 3.80e-61

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: 198.56  E-value: 3.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgkESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRM----EANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDV-MSTACGTPG 186
Cdd:cd14180   90 DRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARLRPQGSRpLQTPCFTLQ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND-------SKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd14180  170 YAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGkmfhnhaADIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGL 249
                        250       260
                 ....*....|....*....|....*..
gi 594150345 260 MEKDPNKRYTCEQAARHPWIAGDTALS 286
Cdd:cd14180  250 LTVDPAKRLKLSELRESDWLQGGSALS 276
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
7-281 8.05e-61

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 198.50  E-value: 8.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   7 ESSSSWKKQAedikkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKA-LKGKE-SSIENEIAVLRKIKHENIVAL 84
Cdd:PTZ00263  10 PDTSSWKLSD------FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQvQHVAQEKSILMELSHPFIVNM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  85 EDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:PTZ00263  84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMegKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPY 244
Cdd:PTZ00263 161 DFGFAKK--VPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF--PN 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 245 WDDisDSAKDFIRNLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:PTZ00263 237 WFD--GRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFHG 276
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
29-279 1.74e-60

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: 195.54  E-value: 1.74e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlKGKESSIE--NEIAVLrKIKHEN--IVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRR-KGQDCRMEiiHEIAVL-ELAQANpwVINLHEVYETASEMILVLEYAAGG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIV---EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14197   95 EIFNQCVadrEEAF-KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLME 261
Cdd:cd14197  174 MGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTLLI 253
                        250
                 ....*....|....*...
gi 594150345 262 KDPNKRYTCEQAARHPWI 279
Cdd:cd14197  254 KKPENRATAEDCLKHPWL 271
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
23-279 3.54e-60

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: 194.15  E-value: 3.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLdEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14071   82 SNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL---DANMNIKIADFGFSNFFKPGELLKTW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaEYEFDSPYWddISDSAKDFIRNLM 260
Cdd:cd14071  159 CGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVL--SGRFRIPFF--MSTDCEHLIRRML 234
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14071  235 VLDPSKRLTIEQIKKHKWM 253
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
29-270 1.22e-59

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: 195.13  E-value: 1.22e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipkkALKgKESSIENE----IAVLRKI-----KHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIK-----VLK-KEVIIEDDdvecTMTEKRVlalanRHPFLTGLHACFQTEDRLYFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDV 177
Cdd:cd05570   77 YVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL---DAEGHIKIADFGMCK-EGiwGGNT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIR 257
Cdd:cd05570  153 TSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLY--PRW--LSREAVSILK 228
                        250
                 ....*....|...
gi 594150345 258 NLMEKDPNKRYTC 270
Cdd:cd05570  229 GLLTKDPARRLGC 241
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
23-295 3.60e-59

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: 194.81  E-value: 3.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMlkREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDVMS 179
Cdd:cd05573   83 MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL---DADGHIKLADFGLCtKMNKSGDRES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 -----------------------------TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLF 230
Cdd:cd05573  160 ylndsvntlfqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETY 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 231 EQILKAEYEFDSPYWDDISDSAKDFIRNLMeKDPNKRYTC-EQAARHPWIAGDTAlsKNIHESVSA 295
Cdd:cd05573  240 SKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGSaEEIKAHPFFKGIDW--ENLRESPPP 302
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
27-278 4.84e-59

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 191.47  E-value: 4.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK-ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGgE 105
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKqESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG-D 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIV--EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACG 183
Cdd:cd14082   88 MLEMILssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKlfEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKD 263
Cdd:cd14082  168 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIN--DQIQNAAFMYPPNPWKEISPDAIDLINNLLQVK 245
                        250
                 ....*....|....*
gi 594150345 264 PNKRYTCEQAARHPW 278
Cdd:cd14082  246 MRKRYSVDKSLSHPW 260
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
26-279 7.40e-59

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: 191.67  E-value: 7.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKE--SSIENEIAVLRKIKHE-NIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14198   13 SKELGRGKFAVVRQCISKSTGQEYAAKFL-KKRRRGQDcrAEILHEIAVLELAKSNpRVVNLHEVYETTSEIILILEYAA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIV--EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd14198   92 GGEIFNLCVpdLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd14198  172 IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFIQKLL 251
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14198  252 VKNPEKRPTAEICLSHSWL 270
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
19-279 5.49e-58

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: 188.62  E-value: 5.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKaTGKLFAVKCIPKKALKGKES--SIENEIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd14161    1 LKHRYEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDllHIRREIEIMSSLNHPHIISVYEVFENSSKIVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGD 176
Cdd:cd14161   80 VMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL---DANGNIKIADFGLSNLYNQDK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDdisdsAKDF 255
Cdd:cd14161  157 FLQTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSD-----ACGL 231
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14161  232 IRWLLMVNPERRATLEDVASHWWV 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
28-279 7.27e-58

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: 188.49  E-value: 7.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKESS-----IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14070    9 KLGEGSFAKVREGLHAVTGEKVAIKVIDKK--KAKKDSyvtknLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS---KMEGKGDVMS 179
Cdd:cd14070   87 GGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL---DENDNIKLIDFGLSncaGILGYSDPFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE--NDSKLFEQILKAEYefdSPYWDDISDSAKDFIR 257
Cdd:cd14070  164 TQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEM---NPLPTDLSPGAISFLR 240
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14070  241 SLLEPDPLKRPNIKQALANRWL 262
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
23-279 7.71e-58

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: 188.11  E-value: 7.71e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNpSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL---DADMNIKIADFGFSNEFTPGNKLDTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLM 260
Cdd:cd14072  159 CGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRI--PFY--MSTDCENLLKKFL 234
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14072  235 VLNPSKRGTLEQIMKDRWM 253
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
23-279 2.22e-57

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: 187.76  E-value: 2.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKG--ADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14104   80 GVDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTR-RGSYIKIIEFGQSRQLKPGDKFRLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLME 261
Cdd:cd14104  159 YTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLV 238
                        250
                 ....*....|....*...
gi 594150345 262 KDPNKRYTCEQAARHPWI 279
Cdd:cd14104  239 KERKSRMTAQEALNHPWL 256
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
27-279 4.22e-57

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: 186.30  E-value: 4.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGgE 105
Cdd:cd14002    7 ELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKElRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG-E 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSK-MEGKGDVMSTACGT 184
Cdd:cd14002   86 LFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG---GVVKLCDFGFARaMSCNTLVLTSIKGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyefDSPYWDDISDSAKDFIRNLMEKDP 264
Cdd:cd14002  163 PLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKD----PVKWPSNMSPEFKSFLQGLLNKDP 238
                        250
                 ....*....|....*
gi 594150345 265 NKRYTCEQAARHPWI 279
Cdd:cd14002  239 SKRLSWPDLLEHPFV 253
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
28-267 5.49e-57

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: 188.29  E-value: 5.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKATGKLFAVKCIPKKA-LKGKESS-IENEIAVLRK-IKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAiLKRNEVKhIMAERNVLLKnVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGkGDVMSTAC 182
Cdd:cd05575   82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL---DSQGHVVLTDFGLCKegIEP-SDTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKDFIRNLMEK 262
Cdd:cd05575  158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLR----TNVSPSARDLLEGLLQK 233

                 ....*
gi 594150345 263 DPNKR 267
Cdd:cd05575  234 DRTKR 238
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
28-279 7.77e-56

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: 183.84  E-value: 7.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKAT-----GKLFAVKCIPKKALKG--KESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14076    8 TLGEGEFGKVKLGWPLPKanhrsGVQVAIKLIRRDTQQEncQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGDVM 178
Cdd:cd14076   88 VSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL---DKNRNLVITDFGFANTfdHFNGDLM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPE-VLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYD-------ENDSKLFEQILKAEYEFDspywDDIS 249
Cdd:cd14076  165 STSCGSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDdphnpngDNVPRLYRYICNTPLIFP----EYVT 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14076  241 PKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
22-278 1.21e-55

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: 182.78  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIavLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14107    3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDI--LARLSHRRLTCLLDQFETRKTLILILELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESkIMISDFGLSKMEGKGDVMSTA 181
Cdd:cd14107   81 SSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRED-IKICDFGFAQEITPSEHQFSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLME 261
Cdd:cd14107  160 YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQ 239
                        250
                 ....*....|....*..
gi 594150345 262 KDPNKRYTCEQAARHPW 278
Cdd:cd14107  240 PDPEKRPSASECLSHEW 256
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
27-279 2.91e-55

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: 182.92  E-value: 2.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKeSSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSR-SRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLskmeGKG---------- 175
Cdd:cd14174   87 ILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDL----GSGvklnsactpi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 --DVMSTACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPF---------YDEND------SKLFEQI 233
Cdd:cd14174  163 ttPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgWDRGEvcrvcqNKLFESI 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 594150345 234 LKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14174  243 QEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
29-267 3.22e-55

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: 183.67  E-value: 3.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDevAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDVMSTACGT 184
Cdd:cd05595   83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCK-EGitDGATMKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKDP 264
Cdd:cd05595  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPR----TLSPEAKSLLAGLLKKDP 234

                 ...
gi 594150345 265 NKR 267
Cdd:cd05595  235 KQR 237
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
23-279 5.02e-55

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: 180.88  E-value: 5.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd06627    2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKimISDFGLS-KMEGKGDVMST 180
Cdd:cd06627   82 ENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL-TTKDGLVK--LADFGVAtKLNEVEKDENS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND-SKLFeQILKAEYefdSPYWDDISDSAKDFIRNL 259
Cdd:cd06627  159 VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPmAALF-RIVQDDH---PPLPENISPELRDFLLQC 234
                        250       260
                 ....*....|....*....|
gi 594150345 260 MEKDPNKRYTCEQAARHPWI 279
Cdd:cd06627  235 FQKDPTLRPSAKELLKHPWL 254
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
23-278 5.97e-55

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: 180.96  E-value: 5.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKESSIEN----EIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKK--KAPEDYLQKflprEIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM-----EG 173
Cdd:cd14162   80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL---DKNNNLKITDFGFARGvmktkDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKaEYEFdsPYWDDISDSA 252
Cdd:cd14162  157 KPKLSETYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVF--PKNPTVSEEC 233
                        250       260
                 ....*....|....*....|....*.
gi 594150345 253 KDFIRNLMEKDPnKRYTCEQAARHPW 278
Cdd:cd14162  234 KDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-278 7.42e-55

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: 181.86  E-value: 7.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVK--CIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKvmAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMegKGDVMST 180
Cdd:cd05612   83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL---DKEGHIKLTDFGFAKK--LRDRTWT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWDDIsdSAKDFIRNLM 260
Cdd:cd05612  158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEF--PRHLDL--YAKDLIKKLL 233
                        250       260
                 ....*....|....*....|...
gi 594150345 261 EKDPNKRYTC-----EQAARHPW 278
Cdd:cd05612  234 VVDRTRRLGNmkngaDDVKNHRW 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
22-280 8.66e-54

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: 177.79  E-value: 8.66e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKM--RLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFY-TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYySQDEESKImiSDFG----LSKMEGKgd 176
Cdd:cd06614   79 DGGSLTDIITQNPVRmNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL-SKDGSVKL--ADFGfaaqLTKEKSK-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI-LKAEYEFDSPywDDISDSAKDF 255
Cdd:cd06614  154 -RNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLItTKGIPPLKNP--EKWSPEFKDF 230
                        250       260
                 ....*....|....*....|....*
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd06614  231 LNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
23-267 2.48e-53

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: 179.44  E-value: 2.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRK-IKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAIlkKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTTDKLYFVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGKGdV 177
Cdd:cd05602   89 YINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL---DSQGHIVLTDFGLCKenIEPNG-T 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIR 257
Cdd:cd05602  165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKP----NITNSARHLLE 240
                        250
                 ....*....|
gi 594150345 258 NLMEKDPNKR 267
Cdd:cd05602  241 GLLQKDRTKR 250
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-278 4.23e-53

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: 176.11  E-value: 4.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKkALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIER-GLKIDEN-VQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd14662   80 GGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAPRLKICDFGYSKSSVLHSQPKSTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLF----EQILKAEYEFdsPYWDDISDSAKDFIR 257
Cdd:cd14662  159 GTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKI--PDYVRVSQDCRHLLS 236
                        250       260
                 ....*....|....*....|.
gi 594150345 258 NLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14662  237 RIFVANPAKRITIPEIKNHPW 257
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
26-279 6.82e-53

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: 176.76  E-value: 6.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKeSSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd14173    7 EEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSR-SRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLS---KMEGKGDVMS-- 179
Cdd:cd14173   86 SILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGsgiKLNSDCSPIStp 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 ---TACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPF---------YDEND------SKLFEQILKA 236
Cdd:cd14173  166 ellTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgWDRGEacpacqNMLFESIQEG 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 594150345 237 EYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14173  246 KYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
29-267 1.28e-52

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: 177.08  E-value: 1.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKA-LKGKESS-IENEIAVLRK-IKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTiLKKKEQNhIMAERNVLLKnLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGKgDVMSTACG 183
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DCQGHVVLTDFGLCKegMEPE-ETTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYwddiSDSAKDFIRNLMEKD 263
Cdd:cd05603  159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGK----TVAACDLLQGLLHKD 234

                 ....
gi 594150345 264 PNKR 267
Cdd:cd05603  235 QRRR 238
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
27-278 2.57e-52

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: 174.01  E-value: 2.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGK-LFAVKCIPKKALKgkESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGAReVVAVKCVSKSSLN--KASTENlltEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESkIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd14121   79 GGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPV-LKLADFGFAQHLKPNDEAHSLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEyEFDSPYWDDISDSAKDFIRNLMEK 262
Cdd:cd14121  158 GSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSK-PIEIPTRPELSADCRDLLLRLLQR 236
                        250
                 ....*....|....*.
gi 594150345 263 DPNKRYTCEQAARHPW 278
Cdd:cd14121  237 DPDRRISFEEFFAHPF 252
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
29-279 5.21e-52

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: 173.29  E-value: 5.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEN-EIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSrEISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGELY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGKGDVMSTACGTPGY 187
Cdd:cd14075   90 TKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS---NNCVKVGDFGFSTHAKRGETLNTFCGSPPY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKA-VDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLMEKDPNK 266
Cdd:cd14075  167 AAPELFKDEHYIGIyVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTI--PSY--VSEPCQELIRGILQPVPSD 242
                        250
                 ....*....|...
gi 594150345 267 RYTCEQAARHPWI 279
Cdd:cd14075  243 RYSIDEIKNSEWL 255
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
29-277 5.78e-52

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: 173.32  E-value: 5.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKA-TGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESK-------IMISDFGLSKMEGKGDVMST 180
Cdd:cd14120   81 DYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNIL-LSHNSGRKpspndirLKIADFGFARFLQDGMMAAT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdsklfEQILKAEYEFDSPYWDDI----SDSAKDFI 256
Cdd:cd14120  160 LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQT-----PQELKAFYEKNANLRPNIpsgtSPALKDLL 234
                        250       260
                 ....*....|....*....|.
gi 594150345 257 RNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14120  235 LGLLKRNPKDRIDFEDFFSHP 255
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
27-278 6.47e-52

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: 173.25  E-value: 6.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalkgKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14010    6 DEIGRGKHSVVYKGRRKGTIEFVAIKCVDKS----KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG------------- 173
Cdd:cd14010   82 ETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSDFGLARREGeilkelfgqfsde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 ----KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDD-I 248
Cdd:cd14010  159 gnvnKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSSkP 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 249 SDSAKDFIRNLMEKDPNKRYTCEQAARHP-W 278
Cdd:cd14010  239 SPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
29-281 8.22e-52

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: 173.16  E-value: 8.22e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLAD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRM-GIVHRDLKPENLLYYSQDEeskIMISDFGLSK-MEGKGDVMSTACGTPG 186
Cdd:cd06623   89 LLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE---VKIADFGISKvLENTLDQCNTFVGTVT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEqILKAEYEFDSPYWDD--ISDSAKDFIRNLMEKDP 264
Cdd:cd06623  166 YMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFE-LMQAICDGPPPSLPAeeFSPEFRDFISACLQKDP 244
                        250
                 ....*....|....*..
gi 594150345 265 NKRYTCEQAARHPWIAG 281
Cdd:cd06623  245 KKRPSAAELLQHPFIKK 261
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
29-279 9.26e-52

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: 173.31  E-value: 9.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKES----------------------SIENEIAVLRKIKHENIVALED 86
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGffrrppprrkpgalgkpldpldRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  87 IYESPN--HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:cd14118   82 VLDDPNedNLYMVFELVDKGAVMEVPTDNPL-SEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLL---GDDGHVKIA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLS-KMEGKGDVMSTACGTPGYVAPEVLA--QKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEF 240
Cdd:cd14118  158 DFGVSnEFEGDDALLSSTAGTPAFMAPEALSesRKKFSgKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVF 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 594150345 241 -DSPYwddISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14118  238 pDDPV---VSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
29-267 1.67e-51

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: 174.00  E-value: 1.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRK-IKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVIlnRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDVMSTACG 183
Cdd:cd05604   84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL---DSQGHIVLTDFGLCK-EGisNSDTTTTFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKD 263
Cdd:cd05604  160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRP----GISLTAWSILEELLEKD 235

                 ....
gi 594150345 264 PNKR 267
Cdd:cd05604  236 RQLR 239
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
29-267 3.43e-51

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: 172.95  E-value: 3.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIENEIaVLRKI-----KHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKAL-KKDVVLEDDDVECTM-IERRVlalasQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVM-STAC 182
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADFGMCKENIYGENKaSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLMEK 262
Cdd:cd05592  158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHY--PRW--LTKEAASCLSLLLER 233

                 ....*
gi 594150345 263 DPNKR 267
Cdd:cd05592  234 NPEKR 238
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
29-278 3.54e-51

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: 170.90  E-value: 3.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALK---GKESSIENEIAVLRKIKHENIVALEDIYESPNH--LYLVMQLVSG 103
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRripNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEYCVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 G--ELFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKimISDFGLSKMEGK---GDVM 178
Cdd:cd14119   81 GlqEMLDSAPDKRLPIWQ-AHGYFVQLIDGLEYLHSQGIIHKDIKPGNLL-LTTDGTLK--ISDFGVAEALDLfaeDDTC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLA-QKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPywDDISDSAKDFI 256
Cdd:cd14119  157 TTSQGSPAFQPPEIANgQDSFSgFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTI--P--DDVDPDLQDLL 232
                        250       260
                 ....*....|....*....|..
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14119  233 RGMLEKDPEKRFTIEQIRQHPW 254
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
23-279 3.55e-51

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: 171.29  E-value: 3.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKA--LKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKciEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd05578   82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNIATKLTDGTLATS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPfYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd05578  159 TSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRP-YEIHSRTSIEEIRAKFETASVLYPAGWSEEAIDLINKLL 237
                        250       260
                 ....*....|....*....|
gi 594150345 261 EKDPNKRYTC-EQAARHPWI 279
Cdd:cd05578  238 ERDPQKRLGDlSDLKNHPYF 257
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
28-279 3.91e-51

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: 171.12  E-value: 3.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYE-SPNHLYLVMQLVSGG 104
Cdd:cd14165    8 NLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfvEKFLPRELEILARLNHKSIIKTYEIFEtSDGKVYIVMELGVQG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK---MEGKGDVM--S 179
Cdd:cd14165   88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKrclRDENGRIVlsK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWDDISDSAKDFIRN 258
Cdd:cd14165  165 TFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRF--PRSKNLTSECKDLIYR 242
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14165  243 LLQPDVSQRLCIDEVLSHPWL 263
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
29-278 4.16e-51

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: 172.97  E-value: 4.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKAT---GKLFAVKCIpKKAlkgkeSSIEN---------EIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd05584    4 LGKGGYGKVFQVRKTTGsdkGKIFAMKVL-KKA-----SIVRNqkdtahtkaERNILEAVKHPFIVDLHYAFQTGGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGD 176
Cdd:cd05584   78 ILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL---DAQGHVKLTDFGLCKESIHDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMS-TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdSPYwddISDSAKDF 255
Cdd:cd05584  155 TVThTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNL-PPY---LTNEARDL 230
                        250       260
                 ....*....|....*....|....*...
gi 594150345 256 IRNLMEKDPNKRY-----TCEQAARHPW 278
Cdd:cd05584  231 LKKLLKRNVSSRLgsgpgDAEEIKAHPF 258
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
29-279 4.23e-51

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 171.31  E-value: 4.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMK--RDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYV 188
Cdd:cd14113   93 YVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTYYIHQLLGSPEFA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 189 APEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:cd14113  173 APEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFVCFLLQMDPAKRP 252
                        250
                 ....*....|.
gi 594150345 269 TCEQAARHPWI 279
Cdd:cd14113  253 SAALCLQEQWL 263
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
29-278 5.01e-51

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: 170.53  E-value: 5.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKaLKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK-MKKKEQ-AAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMSTACGTPGYV 188
Cdd:cd14115   79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 189 APEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:cd14115  159 APEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRP 238
                        250
                 ....*....|
gi 594150345 269 TCEQAARHPW 278
Cdd:cd14115  239 TAATCLQHPW 248
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
23-281 7.08e-51

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: 173.34  E-value: 7.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEN--EIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05593   17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEGKGD--VM 178
Cdd:cd05593   97 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCK-EGITDaaTM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRN 258
Cdd:cd05593  173 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSADAKSLLSG 248
                        250       260
                 ....*....|....*....|....*...
gi 594150345 259 LMEKDPNKRY-----TCEQAARHPWIAG 281
Cdd:cd05593  249 LLIKDPNKRLgggpdDAKEIMRHSFFTG 276
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-281 7.38e-51

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: 170.65  E-value: 7.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEE---KATGKLFAVKCIPKKALKGKESSIEN---EIAVLRKIKHEN-IVALEDIYESPNHLYLVMQLV 101
Cdd:cd05583    2 LGTGAYGKVFLVRKvggHDAGKLYAMKVLKKATIVQKAKTAEHtmtERQVLEAVRQSPfLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGKGDVMS 179
Cdd:cd05583   82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSEGHVVLTDFGLSKefLPGENDRAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKP--YSKAVDCWSIGVIAYILLCGYPPFYDE----NDSKLFEQILKAEyefdSPYWDDISDSAK 253
Cdd:cd05583  159 SFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFTVDgernSQSEISKRILKSH----PPIPKTFSAEAK 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 594150345 254 DFIRNLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:cd05583  235 DFILKLLEKDPKKRLGAgprgaHEIKEHPFFKG 267
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-278 2.25e-50

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: 169.01  E-value: 2.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERG--EKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd14665   80 GGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAPRLKICDFGYSKSSVLHSQPKSTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLF----EQILKAEYEFdsPYWDDISDSAKDFIR 257
Cdd:cd14665  159 GTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFrktiQRILSVQYSI--PDYVHISPECRHLIS 236
                        250       260
                 ....*....|....*....|.
gi 594150345 258 NLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14665  237 RIFVADPATRITIPEIRNHEW 257
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
18-281 2.37e-50

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: 170.88  E-value: 2.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEfketLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLY 95
Cdd:cd05574    2 HFKKIKL----LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMikRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFdRIVEK---GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIMISDFGLSKME 172
Cdd:cd05574   78 FVMDYCPGGELF-RLLQKqpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLH---ESGHIMLTDFDLSKQS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVM-----------------------------STAC-GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY 222
Cdd:cd05574  154 SVTPPPvrkslrkgsrrssvksieketfvaepsarSNSFvGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFK 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594150345 223 DENDSKLFEQILKAEYEFdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAA----RHPWIAG 281
Cdd:cd05574  234 GSNRDETFSNILKKELTF--PESPPVSSEAKDLIRKLLVKDPSKRLGSKRGAseikRHPFFRG 294
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
29-267 5.11e-50

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: 167.71  E-value: 5.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKatGKLFAVKCIPKKALKG-KESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDeLLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTekDASTLIRQVLD---AVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKGDVMSTACG 183
Cdd:cd13999   79 DLLHKKKIPL--SWSLRLKIALDiarGMNYLHSPPIIHRDLKSLNILL---DENFTVKIADFGLSRiKNSTTEKMTGVVG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsklFEQILKAEYEFDSPYwddISDSAKDFIRNLMEK- 262
Cdd:cd13999  154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSP---IQIAAAVVQKGLRPP---IPPDCPPELSKLIKRc 227

                 ....*...
gi 594150345 263 ---DPNKR 267
Cdd:cd13999  228 wneDPEKR 235
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
29-267 5.37e-50

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: 169.67  E-value: 5.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIENEIA---VLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTI-RKAHIVSRSEVTHTLAertVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME-GKGDVMSTACGT 184
Cdd:cd05585   81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL---DYTGHIALCDFGLCKLNmKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKDFIRNLMEKDP 264
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGLLNRDP 233

                 ...
gi 594150345 265 NKR 267
Cdd:cd05585  234 TKR 236
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
27-279 1.26e-49

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: 167.18  E-value: 1.26e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-------KGKESSIENEIAV---LRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd14004    6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwvrDRKLGTVPLEIHIldtLNKRSHPNIVKLLDFFEDDEFYYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLV-SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EG 173
Cdd:cd14004   86 VMEKHgSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL---DGNGTIKLIDFGSAAYikSG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMstaCGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDendsklFEQILKAEYEFdsPYwdDISDSA 252
Cdd:cd14004  163 PFDTF---VGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN------IEEILEADLRI--PY--AVSEDL 229
                        250       260
                 ....*....|....*....|....*..
gi 594150345 253 KDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14004  230 IDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
23-281 1.44e-49

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: 168.95  E-value: 1.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMleKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMST 180
Cdd:cd05599   83 LPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLL---DARGHIKLSDFGLCTGLKKSHLAYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd05599  160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIERLL 239
                        250       260
                 ....*....|....*....|....
gi 594150345 261 eKDPNKR---YTCEQAARHPWIAG 281
Cdd:cd05599  240 -CDAEHRlgaNGVEEIKSHPFFKG 262
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
23-279 2.19e-49

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: 166.67  E-value: 2.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEkaGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSkMEGKGDVMST 180
Cdd:cd14116   87 APLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGE---LKIADFGWS-VHAPSSRRTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEfdspYWDDISDSAKDFIRNLM 260
Cdd:cd14116  163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFT----FPDFVTEGARDLISRLL 238
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd14116  239 KHNPSQRPMLREVLEHPWI 257
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
17-279 3.58e-49

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: 165.76  E-value: 3.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEfkETLGTGAFSEVVLAEEKATGKLFAVKcipkkaLKGKESSIENEIAVLRKIKHENIVALEDIYESPN-HLY 95
Cdd:cd14109    2 RELYEIGE--EDEKRAAQGAPFHVTERSTGRNFLAQ------LRYGDPFLMREVDIHNSLDHPNIVQMHDAYDDEKlAVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELF--DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEesKIMISDFGLSKMEG 173
Cdd:cd14109   74 VIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL--QDD--KLKLADFGQSRRLL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd14109  150 RGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDAR 229
                        250       260
                 ....*....|....*....|....*.
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14109  230 DFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
23-279 4.64e-49

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: 165.55  E-value: 4.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkGKESSIEN----EIAVLRKIKHENIVALEDIYESPN-HLYLV 97
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSG--GPEEFIQRflprELQIVERLDHKNIIHVYEMLESADgKIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeeskIMISDFGLSKMEGKG-- 175
Cdd:cd14163   80 MELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLPKGgr 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyeFDSPYWDDISDSAKD 254
Cdd:cd14163  156 ELSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG---VSLPGHLGVSRTCQD 232
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14163  233 LLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
23-267 1.22e-48

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: 167.51  E-value: 1.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEN--EIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDV 177
Cdd:cd05594  107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLCK-EGikDGAT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIR 257
Cdd:cd05594  183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLSPEAKSLLS 258
                        250
                 ....*....|
gi 594150345 258 NLMEKDPNKR 267
Cdd:cd05594  259 GLLKKDPKQR 268
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
23-270 2.79e-48

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: 165.56  E-value: 2.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIENEIAVLRKI----KHENIVALEDIYESPNHLYLVM 98
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVK-ILKKDVVIQDDDVECTMVEKRVLalsgKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEGKGDVM 178
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML---DSEGHIKIADFGMCK-ENIWDGV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STA--CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaeyEFDSPYWDDISDSAKDFI 256
Cdd:cd05616  157 TTKtfCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIM----EHNVAYPKSMSKEAVAIC 232
                        250
                 ....*....|....
gi 594150345 257 RNLMEKDPNKRYTC 270
Cdd:cd05616  233 KGLMTKHPGKRLGC 246
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
29-281 3.17e-48

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: 165.47  E-value: 3.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIENEIAVLRKI----KHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVL-KKDVILQDDDVECTMTEKRILslarNHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDVMSTAC 182
Cdd:cd05590   82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCK-EGifNGKTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLMEK 262
Cdd:cd05590  158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVY--PTW--LSQDAVDILKAFMTK 233
                        250       260
                 ....*....|....*....|....*
gi 594150345 263 DPNKRYTC-----EQA-ARHPWIAG 281
Cdd:cd05590  234 NPTMRLGSltlggEEAiLRHPFFKE 258
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
23-278 4.81e-48

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: 163.15  E-value: 4.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14108    4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRA-KKKTSARR-ELALLAELDHKSIVRFHDAFEKRRVVIIVTELCH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEEsKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd14108   82 E-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTD-QVRICDFGNAQELTPNEPQYCKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEK 262
Cdd:cd14108  160 GTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVS 239
                        250
                 ....*....|....*.
gi 594150345 263 DpNKRYTCEQAARHPW 278
Cdd:cd14108  240 D-RLRPDAEETLEHPW 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
32-280 5.37e-48

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: 163.04  E-value: 5.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLR-KIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd05611    7 GAFGSVYLAKKRSTGDYFAIKVLKKSDMiaKNQVTNVKAERAIMMiQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGTPGYV 188
Cdd:cd05611   87 LIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFGLSRNGLEKRHNKKFVGTPDYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 189 APEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:cd05611  164 APETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKRL 243
                        250
                 ....*....|....*
gi 594150345 269 TC---EQAARHPWIA 280
Cdd:cd05611  244 GAngyQEIKSHPFFK 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
23-274 5.85e-48

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: 162.90  E-value: 5.85e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEN------EIAVLRKI-KHENIVALEDIYESPNHLY 95
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQklpqlrEIDLHRRVsRHPNIITLHDVFETEVAIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYteKDASTLIR----QVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESkIMISDFGLSKM 171
Cdd:cd13993   82 IVLEYCPNGDLFEAITENRIY--VGKTELIKnvflQLIDAVKHCHSLGIYHRDIKPENIL-LSQDEGT-VKLCDFGLATT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGdvMSTACGTPGYVAPEVLAQKP------YSKAVDCWSIGVIAYILLCGYPPFY--DENDSKLFEQILKAEYEFDSp 243
Cdd:cd13993  158 EKIS--MDFGVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFDV- 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 244 yWDDISDSAKDFIRNLMEKDPNKRYTCEQAA 274
Cdd:cd13993  235 -ILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
29-279 8.82e-48

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: 162.48  E-value: 8.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEK--ATGKLFAVKCIPKKALKGKE----SSIENEIAVLRKIKHENIVALEDIYESPNHLY-LVMQLV 101
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRkdyvKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS---KMEGKGDVM 178
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL---DEDGVLKLTDFGTAevfGMPAEKESP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STA--CGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPF----YDENDSKLFEQILKAEYEFDSPYWDDISDS 251
Cdd:cd13994  158 MSAglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIENLLPSE 237
                        250       260
                 ....*....|....*....|....*...
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd13994  238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
29-270 9.58e-48

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: 164.10  E-value: 9.58e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE----SSIENEIAVLRKiKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDdvecTMVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMS-TACG 183
Cdd:cd05587   83 DLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAEGHIKIADFGMCKEGIFGGKTTrTFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaeyEFDSPYWDDISDSAKDFIRNLMEKD 263
Cdd:cd05587  160 TPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM----EHNVSYPKSLSKEAVSICKGLLTKH 235

                 ....*..
gi 594150345 264 PNKRYTC 270
Cdd:cd05587  236 PAKRLGC 242
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
23-279 2.63e-47

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: 161.18  E-value: 2.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLA-EEKATGKLfAVKCIPKKalKGKESSIEN----EIAVLRKIKHENIVALEDIYESPN-HLYL 96
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLAtSQKYCCKV-AIKIVDRR--RASPDFVQKflprELSILRRVNHPNIVQMFECIEVANgRLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQlVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKimISDFGLSK-MEGKG 175
Cdd:cd14164   79 VME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRKIK--IADFGFARfVEDYP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYefdsPYWDDISDSAKD 254
Cdd:cd14164  156 ELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLY----PSGVALEEPCRA 231
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14164  232 LIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
23-279 3.28e-47

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: 161.33  E-value: 3.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEF--KETLGTGAFSEVVLAEEKATGKL-FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14202    2 FEFsrKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPEN-LLYYSQDEES-----KIMISDFGLSKMEG 173
Cdd:cd14202   82 YCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNiLLSYSGGRKSnpnniRIKIADFGFARYLQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdsklfEQILKAEYEFDSPYWDDI----S 249
Cdd:cd14202  162 NNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASS-----PQDLRLFYEKNKSLSPNIpretS 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14202  237 SHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
29-270 4.26e-47

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: 161.16  E-value: 4.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKkgETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGT 184
Cdd:cd05577   81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---DDHGHVRISDLGLAVEFKGGKKIKGRVGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQK-PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKD 263
Cdd:cd05577  158 HGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKD 237

                 ....*..
gi 594150345 264 PNKRYTC 270
Cdd:cd05577  238 PERRLGC 244
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
29-279 5.15e-47

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: 160.60  E-value: 5.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIP----KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQVEidpiNTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyysQDEESKIMISDFGLSK-----MEGKGdvMS 179
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL---RDSNGNVKLGDFGASKrlqtiCSSTG--MK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFeQILKAEYEFDSPywDDISDSAKDFIRN 258
Cdd:cd06625  163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMAAIF-KIATQPTNPQLP--PHVSEDARDFLSL 239
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06625  240 IFVRNKKQRPSAEELLSHSFV 260
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
29-278 8.64e-47

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: 161.51  E-value: 8.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE----SSIENEIAVLRKiKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDdvdcTMTEKRILALAA-KHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDVMSTAC 182
Cdd:cd05591   82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL---DAEGHCKLADFGMCK-EGilNGKTTTTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLMEK 262
Cdd:cd05591  158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILKAFMTK 233
                        250       260
                 ....*....|....*....|...
gi 594150345 263 DPNKRYTC------EQAAR-HPW 278
Cdd:cd05591  234 NPAKRLGCvasqggEDAIRqHPF 256
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-278 9.17e-47

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: 160.94  E-value: 9.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKA---TGKLFAVKCIPKKALKGKESSIEN---EIAVLRKIKHEN-IVALEDIYESPNHLY 95
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKAKTAEHtrtERQVLEHIRQSPfLVTLHYAFQTDTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEG 173
Cdd:cd05613   82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSSGHVVLTDFGLSKefLLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVL--AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDS 251
Cdd:cd05613  159 ENERAYSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSAL 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 252 AKDFIRNLMEKDPNKRYTC-----EQAARHPW 278
Cdd:cd05613  239 AKDIIQRLLMKDPKKRLGCgpngaDEIKKHPF 270
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
27-279 2.72e-46

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: 158.33  E-value: 2.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIP--KKALKGKESS--IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvDDDKKSRESVkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd06632   86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADFGMAKHVEAFSFAKSFK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQK--PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPywDDISDSAKDFIRNLM 260
Cdd:cd06632  163 GSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIP--DHLSPDAKDFIRLCL 240
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd06632  241 QRDPEDRPTASQLLEHPFV 259
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
23-279 2.96e-46

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: 159.36  E-value: 2.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-------------------------KGKESSIENEIAVLRKIK 77
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprgaraapegctqpRGPIERVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  78 HENIVALEDIYESPN--HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysq 155
Cdd:cd14199   84 HPNVVKLVEVLDDPSedHLYMVFELVKQGPVMEVPTLKPL-SEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 156 DEESKIMISDFGLS-KMEGKGDVMSTACGTPGYVAPEVLAQ--KPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFE 231
Cdd:cd14199  160 GEDGHIKIADFGVSnEFEGSDALLTNTVGTPAFMAPETLSEtrKIFSgKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 232 QILKAEYEFdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14199  240 KIKTQPLEF--PDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
23-272 3.25e-46

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: 160.93  E-value: 3.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIENEIAVLRKIKHEN----IVALEDIYESPNHLYLVM 98
Cdd:cd05615   12 FNFLMVLGKGSFGKVMLAERKGSDELYAIK-ILKKDVVIQDDDVECTMVEKRVLALQDkppfLTQLHSCFQTVDRLYFVM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK---MEGKg 175
Cdd:cd05615   91 EYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML---DSEGHIKIADFGMCKehmVEGV- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 dVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaeyEFDSPYWDDISDSAKDF 255
Cdd:cd05615  167 -TTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM----EHNVSYPKSLSKEAVSI 241
                        250
                 ....*....|....*..
gi 594150345 256 IRNLMEKDPNKRYTCEQ 272
Cdd:cd05615  242 CKGLMTKHPAKRLGCGP 258
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-275 7.07e-46

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: 157.84  E-value: 7.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd13996    8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYT---EKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKimISDFGLSKMEGKGDV-- 177
Cdd:cd13996   88 GGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVK--IGDFGLATSIGNQKRel 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 -------------MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCgypPFydendSKLFE--QILKA--EYEF 240
Cdd:cd13996  166 nnlnnnnngntsnNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PF-----KTAMErsTILTDlrNGIL 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594150345 241 dSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAAR 275
Cdd:cd13996  238 -PESFKAKHPKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
21-279 8.95e-46

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: 157.04  E-value: 8.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPkkaLKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVP---VEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFD--RIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDV 177
Cdd:cd06612   80 CGAGSVSDimKITNKTL-TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL---NEEGQAKLADFGVSgQLTDTMAK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFDSPywDDISDSAKDFI 256
Cdd:cd06612  156 RNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRaIFMIPNKPPPTLSDP--EKWSPEFNDFV 233
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06612  234 KKCLVKDPEERPSAIQLLQHPFI 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
29-279 1.23e-45

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: 156.63  E-value: 1.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKIK----HENIVALEDIYESP--NHLYLVMQLVs 102
Cdd:cd05118    7 IGEGAFGTVWLARDKVTGEKVAIKKI--KNDFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFEHRggNHLCLVFELM- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdEESKIMISDFGLSKmEGKGDVMSTA 181
Cdd:cd05118   84 GMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINL--ELGQLKLADFGLAR-SFTSPPYTPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsklFEQILKAEyefdspywdDI--SDSAKDFIRN 258
Cdd:cd05118  161 VATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSE---VDQLAKIV---------RLlgTPEALDLLSK 228
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd05118  229 MLKYDPAKRITASQALAHPYF 249
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
23-281 1.82e-45

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: 158.24  E-value: 1.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsfFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELF---DRivEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGD 176
Cdd:cd05601   83 HPGGDLLsllSR--YDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGSAaKLSSDKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMST-ACGTPGYVAPEVL------AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDIS 249
Cdd:cd05601  158 VTSKmPVGTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVS 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 250 DSAKDFIRNLMEkDPNKRYTCEQAARHPWIAG 281
Cdd:cd05601  238 ESAVDLIKGLLT-DAKERLGYEGLCCHPFFSG 268
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-293 4.04e-45

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: 158.31  E-value: 4.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  10 SSWKKQAEDikkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSI---ENEIAVlrkikHEN---IV 82
Cdd:cd05596   19 TKLRMNAED----FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfEMIKRSDSAFfweERDIMA-----HANsewIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  83 ALEDIYESPNHLYLVMQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIM 162
Cdd:cd05596   90 QLHYAFQDDKYLYMVMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL---DASGHLK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 ISDFGLS-KMEGKGDVMS-TACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA 236
Cdd:cd05596  166 LADFGTCmKMDKDGLVRSdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNH 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 237 EYEFDSPYWDDISDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAGDTALSKNIHESV 293
Cdd:cd05596  246 KNSLQFPDDVEISKDAKSLICAFLTDREVRlgRNGIEEIKAHPFFKNDQWTWDNIRETV 304
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-303 4.52e-45

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: 157.39  E-value: 4.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKA---TGKLFAVKCIPKKALKGKESSIEN---EIAVLRKIKHEN-IVALEDIYESPNHLY 95
Cdd:cd05614    2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAKTVEHtrtERNVLEHVRQSPfLVTLHYAFQTDAKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEG 173
Cdd:cd05614   82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL---DSEGHVVLTDFGLSKefLTE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSA 252
Cdd:cd05614  159 EKERTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVA 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150345 253 KDFIRNLMEKDPNKR-----YTCEQAARHPWIAGD--TALS-KNIHESVSAQIR-----KNFAK 303
Cdd:cd05614  239 RDLLQKLLCKDPKKRlgagpQGAQEIKEHPFFKGLdwEALAlRKVNPPFRPSIRseldvGNFAE 302
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
23-279 4.59e-45

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: 155.55  E-value: 4.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEF--KETLGTGAFSEVVLAEE-KATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14201    6 FEYsrKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPEN-LLYYSQDEES-----KIMISDFGLSKMEG 173
Cdd:cd14201   86 YCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNiLLSYASRKKSsvsgiRIKIADFGFARYLQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdsklfEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd14201  166 SNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANS-----PQDLRMFYEKNKNLQPSIPRETS 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 254 DFIRN----LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14201  241 PYLADlllgLLQRNQKDRMDFEAFFSHPFL 270
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
23-267 5.93e-45

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 157.08  E-value: 5.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkkALKGKESSIENEIAVL---RKI-------KHENIVALEDIYESPN 92
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIK-----ALKKGDIIARDEVESLmceKRIfetvnsaRHPFLVNLFACFQTPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-- 170
Cdd:cd05589   76 HVCFVMEYAAGGDLMMHIHEDVF-SEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLL---DTEGYVKIADFGLCKeg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MeGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISD 250
Cdd:cd05589  152 M-GFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRY--PRF--LST 226
                        250
                 ....*....|....*..
gi 594150345 251 SAKDFIRNLMEKDPNKR 267
Cdd:cd05589  227 EAISIMRRLLRKNPERR 243
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
23-267 1.00e-44

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: 154.87  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgkessIENEIA---VLRKIKH--EN--IVALEDIYESPNHLY 95
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLI-----LRNQIQqvfVERDILTfaENpfVVSMYCSFETKRHLC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKM---- 171
Cdd:cd05609   77 MVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSKIglms 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 ------EGKGDVMST------ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE 239
Cdd:cd05609  154 lttnlyEGHIEKDTRefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIE 233
                        250       260
                 ....*....|....*....|....*....
gi 594150345 240 FdsPYWDD-ISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05609  234 W--PEGDDaLPDDAQDLITRLLQQNPLER 260
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
29-280 1.21e-44

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: 156.19  E-value: 1.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSI----ENEIAVLRKIKHEN-IVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAhtigERNILVRTALDESPfIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME-GKGDVMSTAC 182
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL---DANGHIALCDFGLSKADlTDNKTTNTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLA-QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywDDISDSAKDFIRNLME 261
Cdd:cd05586  158 GTTEYLAPEVLLdEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPK---DVLSDEGRSFVKGLLN 234
                        250       260
                 ....*....|....*....|...
gi 594150345 262 KDPNKRYTC----EQAARHPWIA 280
Cdd:cd05586  235 RNPKHRLGAhddaVELKEHPFFA 257
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
23-279 3.28e-44

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: 153.09  E-value: 3.28e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQkaGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGL-SKMEGKGDVM 178
Cdd:cd14186   83 CHNGEMSRYLKNrKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR---NMNIKIADFGLaTQLKMPHEKH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKDFIRN 258
Cdd:cd14186  160 FTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMP----AFLSREAQDLIHQ 235
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14186  236 LLRKNPADRLSLSSVLDHPFM 256
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
27-267 7.35e-44

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: 153.95  E-value: 7.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIENEIAVLR--KIKHEN--IVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKAL-KKDVVLIDDDVECTMVEKRvlALAWENpfLTHLYCTFQTKEHLFFVMEFLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGD-VMSTA 181
Cdd:cd05620   80 GGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGMCKENVFGDnRASTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIlkaeyEFDSPYWDD-ISDSAKDFIRNLM 260
Cdd:cd05620  157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-----RVDTPHYPRwITKESKDILEKLF 231

                 ....*..
gi 594150345 261 EKDPNKR 267
Cdd:cd05620  232 ERDPTRR 238
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
23-283 3.08e-43

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: 150.79  E-value: 3.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIekEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSkMEGKGDVMST 180
Cdd:cd14117   88 APRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE---LKIADFGWS-VHAPSLRRRT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLM 260
Cdd:cd14117  164 MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPP----FLSDGSRDLISKLL 239
                        250       260
                 ....*....|....*....|...
gi 594150345 261 EKDPNKRYTCEQAARHPWIAGDT 283
Cdd:cd14117  240 RYHPSERLPLKGVMEHPWVKANS 262
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
29-281 1.59e-42

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: 150.24  E-value: 1.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEE---KATGKLFAVKCIPKKALKGKE---SSIENEIavLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05582    3 LGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDrvrTKMERDI--LADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGKGDVMST 180
Cdd:cd05582   81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEDGHIKLTDFGLSKesIDHEKKAYSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 aCGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEY---EFDSPywddisdSAKDFIR 257
Cdd:cd05582  158 -CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLgmpQFLSP-------EAQSLLR 229
                        250       260
                 ....*....|....*....|....*....
gi 594150345 258 NLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:cd05582  230 ALFKRNPANRLGAgpdgvEEIKRHPFFAT 258
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
23-281 1.89e-42

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: 150.55  E-value: 1.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKK-ALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05598    3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKdVLKRNQVAhVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-----KMEGKG 175
Cdd:cd05598   83 IPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCtgfrwTHDSKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDF 255
Cdd:cd05598  160 YLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPEAKDL 239
                        250       260
                 ....*....|....*....|....*....
gi 594150345 256 IRNLMeKDPNKRYTCEQAA---RHPWIAG 281
Cdd:cd05598  240 ILRLC-CDAEDRLGRNGADeikAHPFFAG 267
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
29-278 2.39e-42

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: 149.04  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05605    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIV---EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACG 183
Cdd:cd05605   88 KFHIYnmgNPGF-EEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRISDLGLAVEIPEGETIRGRVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKD 263
Cdd:cd05605  164 TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKD 243
                        250       260
                 ....*....|....*....|
gi 594150345 264 PNKRYTC-----EQAARHPW 278
Cdd:cd05605  244 PKTRLGCrgegaEDVKSHPF 263
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
23-278 4.32e-42

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: 148.49  E-value: 4.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI----PKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgeRKEAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSG---GELFDRIVekgFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGK- 174
Cdd:cd07841   82 EFMETdleKVIKDKSI---VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLI---ASDGVLKLADFGLARSFGSp 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND----SKLFEQI-------------LKA 236
Cdd:cd07841  156 NRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDidqlGKIFEALgtpteenwpgvtsLPD 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 594150345 237 EYEFDS---PYWDDI----SDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07841  236 YVEFKPfppTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
29-278 5.19e-42

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: 148.25  E-value: 5.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESSIEN----EIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVsG 103
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALK---KVALRKLEGGIPNqalrEIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYM-L 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRI--VEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKM--EGKGDVMS 179
Cdd:cd07832   84 SSLSEVLrdEERPL-TEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV---LKIADFGLARLfsEEDPRLYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVL--AQKpYSKAVDCWSIGVIAYILLCGYPPFYDEND--------SKLFEQILKAEYEFDS------- 242
Cdd:cd07832  160 HQVATRWYRAPELLygSRK-YDEGVDLWAVGCIFAELLNGSPLFPGENDieqlaivlRTLGTPNEKTWPELTSlpdynki 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 243 --PY-----WDDI----SDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07832  239 tfPEskgirLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
20-279 5.71e-42

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: 147.28  E-value: 5.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14111    2 QKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQA--EEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSKMEGKGDV-- 177
Cdd:cd14111   80 FCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLN---AIKIVDFGSAQSFNPLSLrq 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEfDSPYWDDISDSAKDFIR 257
Cdd:cd14111  157 LGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLK 235
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14111  236 KVLSSYPWSRPTTKDCFAHAWL 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
23-279 7.94e-42

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: 147.79  E-value: 7.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL------------KGKESS-------------IENEIAVLRKIK 77
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrpppRGSKAAqgeqakplaplerVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  78 HENIVALEDIYESP--NHLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysq 155
Cdd:cd14200   82 HVNIVKLIEVLDDPaeDNLYMVFDLLRKGPVMEVPSDKPF-SEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLL--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 156 DEESKIMISDFGLS-KMEGKGDVMSTACGTPGYVAPEVLAQKPYS---KAVDCWSIGVIAYILLCGYPPFYDENDSKLFE 231
Cdd:cd14200  158 GDDGHVKIADFGVSnQFEGNDALLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPFIDEFILALHN 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 232 QILKAEYEFdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14200  238 KIKNKPVEF--PEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
23-278 8.63e-42

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: 147.46  E-value: 8.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkkALKGKESS------IENEIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK-----KFKESEDDedvkktALREVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVsGGELFDRIVEKGFYTEKDA-STLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EG 173
Cdd:cd07833   78 VFEYV-ERTLLELLEASPGGLPPDAvRSYIWQLLQAIAYCHSHNIIHRDIKPENILV---SESGVLKLCDFGFARAltAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA--------EYEFDS-- 242
Cdd:cd07833  154 PASPLTDYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKClgplppshQELFSSnp 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 243 -------P-----------YWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07833  234 rfagvafPepsqpeslerrYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
23-279 1.01e-41

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: 147.24  E-value: 1.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKE----SSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI--RLDNEEEgipsTALR-EISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSggelFD--RIVEKGFY--TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmegk 174
Cdd:cd07829   78 EYCD----QDlkKYLDKRPGplPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLI---NRDGVLKLADFGLAR---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 gdvmstACGTPG-----------YVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFE--QIL----- 234
Cdd:cd07829  147 ------AFGIPLrtythevvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPgDSEIDQLFKifQILgtpte 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150345 235 --------KAEYEFDSPYWD---------DISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07829  221 eswpgvtkLPDYKPTFPKWPkndlekvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
20-267 1.34e-41

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: 146.97  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKeTLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS----IENEIavLRKIKHENIVALEDIYESPNHLY 95
Cdd:cd05607    2 KYFYEFR-VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEkmalLEKEI--LEKVNSPFIVSLAYAFETKTHLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKG----------FYTEkdastlirQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISD 165
Cdd:cd05607   79 LVMSLMNGGDLKYHIYNVGergiemerviFYSA--------QITCGILHLHSLKIVYRDMKPENVLL---DDNGNCRLSD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD--ENDSK--LFEQILKAEYEFD 241
Cdd:cd05607  148 LGLAVEVKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDhkEKVSKeeLKRRTLEDEVKFE 227
                        250       260
                 ....*....|....*....|....*.
gi 594150345 242 SPYWDdisDSAKDFIRNLMEKDPNKR 267
Cdd:cd05607  228 HQNFT---EEAKDICRLFLAKKPENR 250
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
23-281 1.89e-41

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: 147.88  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05597    3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKwEMLKRAETAcFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELF-------DRIVEK--GFYtekdastlIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-K 170
Cdd:cd05597   83 YCGGDLLtllskfeDRLPEEmaRFY--------LAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHIRLADFGSClK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMS-TACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSP- 243
Cdd:cd05597  152 LREDGTVQSsVAVGTPDYISPEILqamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPd 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 594150345 244 YWDDISDSAKDFIRNLMeKDPNKRY---TCEQAARHPWIAG 281
Cdd:cd05597  232 DEDDVSEEAKDLIRRLI-CSRERRLgqnGIDDFKKHPFFEG 271
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
29-269 2.25e-41

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: 145.85  E-value: 2.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlkPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKMEGKGDVMSTACGTP 185
Cdd:cd14187   95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFL---NDDMEVKIGDFGLaTKVEYDGERKKTLCGTP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKDPN 265
Cdd:cd14187  172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDPT 247

                 ....
gi 594150345 266 KRYT 269
Cdd:cd14187  248 ARPT 251
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
23-278 2.49e-41

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: 145.46  E-value: 2.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKeSSIEN------EIAVLRKI---KHENIVALEDIYESPNH 93
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEW-AMINGpvpvplEIALLLKAskpGVPGVIRLLDWYERPDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGE-LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMisDFGLSKME 172
Cdd:cd14005   81 FLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLI--DFGCGALL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGdVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDEndsklfEQILKAEYEFdspyWDDISDS 251
Cdd:cd14005  159 KDS-VYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLF----RPRLSKE 227
                        250       260
                 ....*....|....*....|....*..
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14005  228 CCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
23-277 2.68e-41

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: 146.29  E-value: 2.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd05631   82 MNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIPEGETV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRN 258
Cdd:cd05631  159 RGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRM 238
                        250       260
                 ....*....|....*....|....
gi 594150345 259 LMEKDPNKRYTC--EQAA---RHP 277
Cdd:cd05631  239 LLTKNPKERLGCrgNGAAgvkQHP 262
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
23-279 5.79e-41

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: 144.81  E-value: 5.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkkALKGKESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRI---DLEKCQTSMDElrkEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFD---RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGD 176
Cdd:cd06610   80 LLSGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL---GEDGSVKIADFGVSASLATGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMS-----TACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK---AEYEFDSPYwDD 247
Cdd:cd06610  157 DRTrkvrkTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQndpPSLETGADY-KK 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 248 ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06610  236 YSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
32-281 5.84e-41

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: 146.95  E-value: 5.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDR 109
Cdd:cd05610   15 GAFGKVYLGRKKNNSKLYAVKVVKKADMINKNmvHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 110 IVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGK--------------- 174
Cdd:cd05610   95 LHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISN---EGHIKLTDFGLSKVTLNrelnmmdilttpsma 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 ----------GDVMSTAC-----------------------------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05610  172 kpkndysrtpGQVLSLISslgfntptpyrtpksvrrgaarvegerilGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFL 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 216 CGYPPFYDENDSKLFEQILKAEYEFdsPYWDD-ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAG 281
Cdd:cd05610  252 TGIPPFNDETPQQVFQNILNRDIPW--PEGEEeLSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHG 316
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
32-279 7.60e-41

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 144.61  E-value: 7.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKALkgkeSSIENEIAVLRKiKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIV 111
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNF----NAIEPMVHQLMK-DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 112 EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqDEESKIMISDFGLSKMEGkgdVMSTACGTPGYVAPE 191
Cdd:PHA03390 102 KEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYD--RAKDRIYLCDYGLCKIIG---TPSCYDGTLDYFSPE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 192 VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKR-YTC 270
Cdd:PHA03390 177 KIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLPFIKNVSKNANDFVQSMLKYNINYRlTNY 256

                 ....*....
gi 594150345 271 EQAARHPWI 279
Cdd:PHA03390 257 NEIIKHPFL 265
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-267 9.49e-41

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: 144.18  E-value: 9.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATG-KLFAVKCIP------KKALKGKESS---IENEIAVLR-KIKHENIVALEDIYESP 91
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINmtnpafGRTEQERDKSvgdIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSG---GELFDRIVEK-GFYTEKDASTLIRQVLDAVYYLHR-MGIVHRDLKPENLLYysqDEESKIMISDF 166
Cdd:cd08528   82 DRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIML---GEDDKVTITDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSKMEGKGDV-MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEfdsPYW 245
Cdd:cd08528  159 GLAKQKGPESSkMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE---PLP 235
                        250       260
                 ....*....|....*....|...
gi 594150345 246 DDI-SDSAKDFIRNLMEKDPNKR 267
Cdd:cd08528  236 EGMySDDITFVIRSCLTPDPEAR 258
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
18-279 1.03e-40

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: 143.91  E-value: 1.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYESPN 92
Cdd:cd06647    4 DPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLVGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKM 171
Cdd:cd06647   78 ELWVVMEYLAGGSLTDVVTETCM-DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsklfeqiLKAEY--------EFDSP 243
Cdd:cd06647  154 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP-------LRALYliatngtpELQNP 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 244 ywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06647  227 --EKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
23-280 1.05e-40

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: 145.75  E-value: 1.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP---------KKALKgkessienEIAVLRKIKHENIVALEDIYESP-- 91
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISnvfddlidaKRILR--------EIKILRHLKHENIIGLLDILRPPsp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 ---NHLYLVMqlvsggELFD----RIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMI 163
Cdd:cd07834   74 eefNDVYIVT------ELMEtdlhKVIKsPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV---NSNCDLKI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLSKM---EGKGDVMStacgtpGYV------APEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF----YDENDSKL 229
Cdd:cd07834  145 CDFGLARGvdpDEDKGFLT------EYVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFpgrdYIDQLNLI 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 230 FEQIlkaeyefDSPYWDDI----SDSAKDFIRNLMEK--------------------------DPNKRYTCEQAARHPWI 279
Cdd:cd07834  219 VEVL-------GTPSEEDLkfisSEKARNYLKSLPKKpkkplsevfpgaspeaidllekmlvfNPKKRITADEALAHPYL 291

                 .
gi 594150345 280 A 280
Cdd:cd07834  292 A 292
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
29-276 1.44e-40

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: 143.53  E-value: 1.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKK--ALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHSrvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDVMSTACGTP 185
Cdd:cd14189   89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFI---NENMELKVGDFGLAaRLEPPEQRKKTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKDPN 265
Cdd:cd14189  166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA----SLSLPARHLLAGILKRNPG 241
                        250
                 ....*....|.
gi 594150345 266 KRYTCEQAARH 276
Cdd:cd14189  242 DRLTLDQILEH 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-279 1.53e-40

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: 143.45  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALED-IYESPNH-LYLVMQ 99
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEkQQLVSEVNILRELKHPNIVRYYDrIVDRANTtLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRI----VEKGFYTEKDASTLIRQVLDAVYYLHR-----MGIVHRDLKPENLLYysqDEESKIMISDFGLSK 170
Cdd:cd08217   82 YCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFL---DSDNNVKLGDFGLAR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVM-STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEF-DSPYwddi 248
Cdd:cd08217  159 VLSHDSSFaKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRiPSRY---- 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 249 SDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08217  235 SSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
20-290 1.92e-40

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: 144.73  E-value: 1.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd05632    1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRkgESMALNEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKG 175
Cdd:cd05632   81 LTIMNGGDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISDLGLAVKIPEG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDF 255
Cdd:cd05632  158 ESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSI 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 594150345 256 IRNLMEKDPNKRYTCE-----QAARHPWIagdtalsKNIH 290
Cdd:cd05632  238 CKMLLTKDPKQRLGCQeegagEVKRHPFF-------RNMN 270
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
23-277 2.23e-40

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: 142.92  E-value: 2.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLsqKEREDSV-NEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVE----KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMeGKGD 176
Cdd:cd08530   81 APFGDLSKLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL---VKIGDLGISKV-LKKN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSP-YWDDISdsakDF 255
Cdd:cd08530  157 LAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPvYSQDLQ----QI 232
                        250       260
                 ....*....|....*....|..
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd08530  233 IRSLLQVNPKKRPSCDKLLQSP 254
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
23-277 2.47e-40

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: 143.63  E-value: 2.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRkgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIV---EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd05630   82 MNGGDLKFHIYhmgQAGF-PEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVPEGQT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd05630  158 IKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCS 237
                        250       260
                 ....*....|....*....|....*
gi 594150345 258 NLMEKDPNKRYTCE-----QAARHP 277
Cdd:cd05630  238 MLLCKDPAERLGCRgggarEVKEHP 262
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
17-280 3.75e-40

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: 142.96  E-value: 3.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgkESSIEN---EIAVLRKIKHENIVALEDIYESPNH 93
Cdd:cd06611    1 VNPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIES----EEELEDfmvEIDILSECKHPNIVGLYEAYFYENK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELfDRIV---EKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLS- 169
Cdd:cd06611   77 LWILIEFCDGGAL-DSIMlelERGL-TEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTL---DGDVKLADFGVSa 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEY-EFDSP 243
Cdd:cd06611  152 KNKSTLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPpTLDQP 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 244 Y-WddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd06611  232 SkW---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
29-280 1.01e-39

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: 141.43  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKgKESSIE---NEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVK---KMDLR-KQQRREllfNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGKgDV--MSTACG 183
Cdd:cd06648   91 LTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGFCAQVSK-EVprRKSLVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdSPYWDDISDSAKDFIRNLMEKD 263
Cdd:cd06648  166 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPK-LKNLHKVSPRLRSFLDRMLVRD 244
                        250
                 ....*....|....*..
gi 594150345 264 PNKRYTCEQAARHPWIA 280
Cdd:cd06648  245 PAQRATAAELLNHPFLA 261
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
29-279 1.22e-39

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: 141.52  E-value: 1.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKC--IPKKALKGKE------SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQveLPSVSAENKDrkksmlDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDVMS 179
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV---DNKGGIKISDFGISkKLEANSLSTK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPG------YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsklFEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd06628  165 NNGARPSlqgsvfWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIFKIGENASPTIPSNISSEAR 241
                        250       260
                 ....*....|....*....|....*.
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06628  242 DFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
29-281 1.78e-39

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: 144.02  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFklNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGDF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK---------------- 170
Cdd:cd05600   99 RTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLI---DSSGHIKLTDFGLASgtlspkkiesmkirle 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 -----------MEGKGDVMST-----------ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK 228
Cdd:cd05600  176 evkntafleltAKERRNIYRAmrkedqnyansVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNE 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 229 LFEQILKAEYEFDSPYWDD------ISDSAKDFIRNLMEkDPNKRY-TCEQAARHPWIAG 281
Cdd:cd05600  256 TWANLYHWKKTLQRPVYTDpdlefnLSDEAWDLITKLIT-DPQDRLqSPEQIKNHPFFKN 314
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
21-279 2.07e-39

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: 140.84  E-value: 2.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPkkaLKGKESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID---LEEAEDEIEDiqqEIQFLSQCDSPYITKYYGSFLKGSKLWII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGD 176
Cdd:cd06609   78 MEYCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL---SEEGDVKLADFGVSgQLTSTMS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEyefdSPYWDD--ISDSAKD 254
Cdd:cd06609  154 KRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNN----PPSLEGnkFSKPFKD 229
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06609  230 FVELCLNKDPKERPSAKELLKHKFI 254
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
21-279 4.73e-39

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: 139.67  E-value: 4.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14110    3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYK--PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV-MS 179
Cdd:cd14110   81 CSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMII---TEKNLLKIVDLGNAQPFNQGKVlMT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTpgYV---APEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYwDDISDSAKDFI 256
Cdd:cd14110  158 DKKGD--YVetmAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCY-AGLSGGAVNFL 234
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14110  235 KSTLCAKPWGRPTASECLQNPWL 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
23-278 4.80e-38

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: 137.67  E-value: 4.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkkALKGKESSIE-----NEIAVLRKIK-HENIVALEDIYESPNHLYL 96
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIK-----KMKKKFYSWEecmnlREVKSLRKLNeHPNIVKLKEVFRENDELYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGgELFDRIV--EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSK-MEG 173
Cdd:cd07830   76 VFEYMEG-NLYQLMKdrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAReIRS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KgDVMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDD----- 247
Cdd:cd07830  152 R-PPYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEgykla 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 248 ---------------------ISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07830  231 sklgfrfpqfaptslhqlipnASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
23-267 1.24e-37

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: 137.75  E-value: 1.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIENEIAVLRKI----KHENIVALEDIYESPNHLYLVM 98
Cdd:cd05619    7 FVLHKMLGKGSFGKVFLAELKGTNQFFAIKAL-KKDVVLMDDDVECTMVEKRVLslawEHPFLTHLFCTFQTKENLFFVM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV- 177
Cdd:cd05619   86 EYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHIKIADFGMCKENMLGDAk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIlkaeyEFDSPYWDD-ISDSAKDFI 256
Cdd:cd05619  163 TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-----RMDNPFYPRwLEKEAKDIL 237
                        250
                 ....*....|.
gi 594150345 257 RNLMEKDPNKR 267
Cdd:cd05619  238 VKLFVREPERR 248
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
29-278 1.87e-37

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: 135.91  E-value: 1.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKC---IPKKALKGKESSIE---NEIAVLRKIKHENIVALEDIYESPNHLYL-VMQLV 101
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKIhqlNKDWSEEKKQNYIKhalREYEIHKSLDHPRIVKLYDVFEIDTDSFCtVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYL--HRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKM-------E 172
Cdd:cd13990   88 DGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKImddesynS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVIAYILLCGYPPF-YDENDSKLFEQ--ILKAEyEFDSPYW 245
Cdd:cd13990  168 DGMELTSQGAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEEntILKAT-EVEFPSK 246
                        250       260       270
                 ....*....|....*....|....*....|...
gi 594150345 246 DDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd13990  247 PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
18-286 3.30e-37

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: 135.62  E-value: 3.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYESPN 92
Cdd:cd06655   16 DPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQInlqkqPKKEL------IINEILVMKELKNPNIVNFLDSFLVGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKM 171
Cdd:cd06655   90 ELFVVMEYLAGGSLTDVVTETCM-DEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL---GMDGSVKLTDFGFcAQI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFDSPywDDISD 250
Cdd:cd06655  166 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLSP 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALS 286
Cdd:cd06655  244 IFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLS 279
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
30-279 6.38e-37

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: 133.97  E-value: 6.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  30 GTGAFSEVVLAEEKATGKLFAVKCIP-----KKALKgkesSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEIRfqdndPKTIK----EIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDrIVEkgfYTEKDASTLIR----QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVM-- 178
Cdd:cd06626   85 TLEE-LLR---HGRILDEAVIRvytlQLLEGLAYLHENGIVHRDIKPANIFL---DSNGLIKLGDFGSAVKLKNNTTTma 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 ----STACGTPGYVAPEVL---AQKPYSKAVDCWSIGVIAYILLCGYPP--FYDENDSKLFEQILKAEYEFdsPYWDDIS 249
Cdd:cd06626  158 pgevNSLVGTPAYMAPEVItgnKGEGHGRAADIWSLGCVVLEMATGKRPwsELDNEWAIMYHVGMGHKPPI--PDSLQLS 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06626  236 PEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
29-278 8.09e-37

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: 134.33  E-value: 8.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpkkALKGKES----SIENEIAVLRKIK---HENIVALEDI-----YESPNHLYL 96
Cdd:cd07838    7 IGEGAYGTVYKARDLQDGRFVALKKV---RVPLSEEgiplSTIREIALLKQLEsfeHPNVVRLLDVchgprTDRELKLTL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSG--GELFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEGK 174
Cdd:cd07838   84 VFEHVDQdlATYLDKCPKPGLPPET-IKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ---VKLADFGLARIYSF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND----SKLFEQI-LKAEYEF--DSPY-WD 246
Cdd:cd07838  160 EMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIgLPSEEEWprNSALpRS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 247 ---------------DISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07838  240 sfpsytprpfksfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
23-281 8.85e-37

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: 136.52  E-value: 8.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05629    3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDqlAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK---------- 170
Cdd:cd05629   83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI---DRGGHIKLSDFGLSTgfhkqhdsay 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 ----MEGKG-----------------------DVMST-----------ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY 212
Cdd:cd05629  160 yqklLQGKSnknridnrnsvavdsinltmsskDQIATwkknrrlmaysTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594150345 213 ILLCGYPPFYDENDSKLFEQILKAEYEFDSPywDDI--SDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAG 281
Cdd:cd05629  240 ECLIGWPPFCSENSHETYRKIINWRETLYFP--DDIhlSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFRG 310
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
24-267 1.15e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 133.04  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    24 EFKETLGTGAFSEVVLAE----EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   100 LVSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVM 178
Cdd:smart00219  82 YMEGGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV---GENLVVKISDFGLSRDLYDDDYY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   179 STAcGTPGYV---APEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQiLKAEYEFDSPywddisDSAKD 254
Cdd:smart00219 159 RKR-GGKLPIrwmAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEY-LKNGYRLPQP------PNCPP 230
                          250
                   ....*....|....*..
gi 594150345   255 FIRNLMEK----DPNKR 267
Cdd:smart00219 231 ELYDLMLQcwaeDPEDR 247
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
24-267 2.14e-36

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: 132.29  E-value: 2.14e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    24 EFKETLGTGAFSEVVLAEEKATGKLF----AVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   100 LVSGGEL--FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:smart00221  82 YMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV---GENLVVKISDFGLSRDLYDDDY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   178 MSTACGT-PgyV---APEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAEYEfdspywdDISDSA 252
Cdd:smart00221 159 YKVKGGKlP--IrwmAPESLKEGKFTSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKGYRL-------PKPPNC 229
                          250
                   ....*....|....*....
gi 594150345   253 KDFIRNLMEK----DPNKR 267
Cdd:smart00221 230 PPELYKLMLQcwaeDPEDR 248
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-221 3.53e-36

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: 132.96  E-value: 3.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVK-CipKKALKGKESSIE---NEIAVLRKIKHENIVALEDIYE-----SPNHL-YLVM 98
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkC--RQELSPSDKNRErwcLEVQIMKKLNHPNVVSARDVPPeleklSPNDLpLLAM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGEL---FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKIM--ISDFGLSKMEG 173
Cdd:cd13989   79 EYCSGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVL--QQGGGRVIykLIDLGYAKELD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd13989  157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
29-294 5.28e-36

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: 132.07  E-value: 5.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgkESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTKS----EEELEDymvEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGKG-DVMSTACG 183
Cdd:cd06643   89 VDAVMLElERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTL---DGDIKLADFGVSAKNTRTlQRRDSFIG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAE-YEFDSPY-WddiSDSAKDFI 256
Cdd:cd06643  166 TPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpPTLAQPSrW---SPEFKDFL 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWIAGDTAlSKNIHESVS 294
Cdd:cd06643  243 RKCLEKNVDARWTTSQLLQHPFVSVLVS-NKPLRELIA 279
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
29-279 5.49e-36

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: 131.39  E-value: 5.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd08220    8 VGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMtKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKG--FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKImiSDFGLSKMEGKGDVMSTACGTP 185
Cdd:cd08220   88 EYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKI--GDFGISKILSSKSKAYTVVGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYefdSPYWDDISDSAKDFIRNLMEKDPN 265
Cdd:cd08220  166 CYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTF---APISDRYSEELRHLILSMLHLDPN 242
                        250
                 ....*....|....
gi 594150345 266 KRYTCEQAARHPWI 279
Cdd:cd08220  243 KRPTLSEIMAQPII 256
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
22-279 5.76e-36

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: 131.66  E-value: 5.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkGKESSIENEIAVLRKI-KHENIVALEDIYESPNH------L 94
Cdd:cd06608    7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIE--DEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPpggddqL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGG---ELFDRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK 170
Cdd:cd06608   85 WLVMEYCGGGsvtDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL---TEEAEVKLVDFGVSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 M----EGKGDvmsTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyefD 241
Cdd:cd06608  162 QldstLGRRN---TFIGTPYWMAPEVIAcdQQPdasYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRN----P 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 594150345 242 SP------YWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06608  235 PPtlkspeKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
29-281 6.70e-36

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: 131.93  E-value: 6.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALK---GKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05608    9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKkrkGYEGAMV-EKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIV----EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--MEGKGDVMS 179
Cdd:cd05608   88 LRYHIYnvdeENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAVelKDGQTKTKG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd05608  165 YA-GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEAL 243
                        250       260
                 ....*....|....*....|....*..
gi 594150345 260 MEKDPNKRY-----TCEQAARHPWIAG 281
Cdd:cd05608  244 LAKDPEKRLgfrdgNCDGLRTHPFFRD 270
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
23-279 7.57e-36

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: 131.24  E-value: 7.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIeNEIAVLRKIK------HENIVALEDIYESPNHLYL 96
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNNKDYLDQSL-DEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGG--ELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeESKIMISDFGLSKMEgk 174
Cdd:cd14133   79 VFELLSQNlyEFLKQNKFQYL-SLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYS-RCQIKIIDFGSSCFL-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDSKlFEQILKAEYEFDSPYWDDISDSA-- 252
Cdd:cd14133  155 TQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLF--PGASE-VDQLARIIGTIGIPPAHMLDQGKad 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 253 ----KDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14133  232 delfVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
23-277 7.67e-36

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: 130.99  E-value: 7.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI--PKKALKGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIdiSRMSRKMREEAI-DEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRI--VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG-KGDV 177
Cdd:cd08529   81 AENGDLHSLIksQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL---DKGDNVKIGDLGVAKILSdTTNF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE-FDSPYWDDISdsakDFI 256
Cdd:cd08529  158 AQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLS----QLI 233
                        250       260
                 ....*....|....*....|.
gi 594150345 257 RNLMEKDPNKRYTCEQAARHP 277
Cdd:cd08529  234 DSCLTKDYRQRPDTTELLRNP 254
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
22-279 1.10e-35

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: 130.50  E-value: 1.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPkkaLKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIK---LEPGDdfEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEGKgdVMS 179
Cdd:cd06613   78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGD---VKLADFGVSAQLTA--TIA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 ---TACGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYefDSPYWDD---ISD 250
Cdd:cd06613  153 krkSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNF--DPPKLKDkekWSP 230
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06613  231 DFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
18-286 1.15e-35

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: 131.77  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYESPN 92
Cdd:cd06656   16 DPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLVGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKM 171
Cdd:cd06656   90 ELWVVMEYLAGGSLTDVVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFDSPywDDISD 250
Cdd:cd06656  166 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--ERLSA 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALS 286
Cdd:cd06656  244 VFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLS 279
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
23-277 1.23e-35

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: 130.20  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVK-CIPKKALKGKESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQL 100
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKkSKKPFRGPKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGEL---FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKMEGKGD 176
Cdd:cd13997   82 CENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI---SNKGTCKIGDFGLaTRLETSGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMStacGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYP-PFYDENDSKLFEQILKAEYEfdspywDDISDSAKD 254
Cdd:cd13997  159 VEE---GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQLRQGKLPLPPG------LVLSQELTR 229
                        250       260
                 ....*....|....*....|...
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd13997  230 LLKVMLDPDPTRRPTADQLLAHD 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
27-276 1.37e-35

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: 130.52  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIP--KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPhsRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDVMSTACG 183
Cdd:cd14188   87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFI---NENMELKVGDFGLAaRLEPLEHRRRTICG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKD 263
Cdd:cd14188  164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPS----SLLAPAKHLIASMLSKN 239
                        250
                 ....*....|...
gi 594150345 264 PNKRYTCEQAARH 276
Cdd:cd14188  240 PEDRPSLDEIIRH 252
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
23-260 1.64e-35

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: 133.98  E-value: 1.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05624   74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKwEMLKRAETAcFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDY 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELF-------DRIVE--KGFYtekdastlIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-K 170
Cdd:cd05624  154 YVGGDLLtllskfeDKLPEdmARFY--------IGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHIRLADFGSClK 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMST-ACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSP- 243
Cdd:cd05624  223 MNDDGTVQSSvAVGTPDYISPEILqamedGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPs 302
                        250
                 ....*....|....*..
gi 594150345 244 YWDDISDSAKDFIRNLM 260
Cdd:cd05624  303 HVTDVSEEAKDLIQRLI 319
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
14-280 4.23e-35

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: 131.26  E-value: 4.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  14 KQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKESSIE-----NEIAVLRKIKHENIVALEDIY 88
Cdd:cd07851    8 KTVWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIK----KLSRPFQSAIHakrtyRELRLLKHMKHENVIGLLDVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPNHL------YLVMQLVsGGELfDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyySQDEESKIM 162
Cdd:cd07851   84 TPASSLedfqdvYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNL---AVNEDCELK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 ISDFGLSKMegKGDVMSTACGTPGYVAPEVLAQK-PYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFD 241
Cdd:cd07851  159 ILDFGLARH--TDDEMTGYVATRWYRAPEIMLNWmHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPD 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 242 SPYWDDI-SDSAKDFIR----------------------NLMEK----DPNKRYTCEQAARHPWIA 280
Cdd:cd07851  237 EELLKKIsSESARNYIQslpqmpkkdfkevfsganplaiDLLEKmlvlDPDKRITAAEALAHPYLA 302
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
3-332 4.44e-35

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 131.26  E-value: 4.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   3 RENGESSSSWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATG-KLFAVKCIPK-KALKGKE-SSIENEIAVLRKIKHE 79
Cdd:PTZ00426  12 KKDSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKsKIIKQKQvDHVFSERKILNYINHP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  80 NIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEES 159
Cdd:PTZ00426  92 FCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL---DKDG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 160 KIMISDFGLSKMEGKGDVmsTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE 239
Cdd:PTZ00426 169 FIKMTDFGFAKVVDTRTY--TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 240 FdsPYWDDisDSAKDFIRNLMEKDPNKRY-----TCEQAARHPWIaGDTALSKNIHESVSAQIrknfaKSKWRQAFNATA 314
Cdd:PTZ00426 247 F--PKFLD--NNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWF-GNIDWVSLLHKNVEVPY-----KPKYKNVFDSSN 316
                        330
                 ....*....|....*...
gi 594150345 315 VVRHMRRLQLGSSLDSSN 332
Cdd:PTZ00426 317 FERVQEDLTIADKITNEN 334
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
21-277 1.12e-34

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: 127.72  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKAT-------GKLFAVKCI-----PKKalkgkessIENEIAVLRKIK-HENIVALEDI 87
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIyptssPSR--------ILNELECLERLGgSNNVSGLITA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMqlvsggELFDRIVEKGFYTE---KDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEesKIMIS 164
Cdd:cd14019   73 FRNEDQVVAVL------PYIEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETG--KGVLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSK-MEGKGDVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCG-YPPFYDENDSKLFEQILKaeyefd 241
Cdd:cd14019  145 DFGLAQrEEDRPEQRAPRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGrFPFFFSSDDIDALAEIAT------ 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 242 spywddI--SDSAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14019  219 ------IfgSDEAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
18-279 1.53e-34

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: 128.56  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06659   18 DPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRREL-LFNEVVIMRDYQHPNVVEMYKSYLVGEELWVL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKgDV 177
Cdd:cd06659   97 MEYLQGGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILL---TLDGRVKLSDFGFCAQISK-DV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 --MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaeyefDSP-----YWDDISD 250
Cdd:cd06659  172 pkRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLR------DSPppklkNSHKASP 245
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06659  246 VLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
29-279 1.90e-34

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: 127.52  E-value: 1.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQP-LHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEK-----------GFYTekdastliRQVLDAVYYLHRMGIVHRDLKPENLLY--YSqdeeSKIMISDFGLSK-MEGK 174
Cdd:cd06624   95 LLRSKwgplkdnentiGYYT--------KQILEGLKYLHDNKIVHRDIKGDNVLVntYS----GVVKISDFGTSKrLAGI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKP--YSKAVDCWSIGVIAYILLCGYPPFYDENDSKlfEQILK-AEYEFDSPYWDDISDS 251
Cdd:cd06624  163 NPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFIELGEPQ--AAMFKvGMFKIHPEIPESLSEE 240
                        250       260
                 ....*....|....*....|....*...
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06624  241 AKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
29-279 2.89e-34

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: 127.06  E-value: 2.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIP----KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH--LYLVMQLVS 102
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVPfdpdSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyysQDEESKIMISDFGLSK------MEGKGd 176
Cdd:cd06653   90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKriqticMSGTG- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFydeNDSKLFEQILKAEYEFDSPYW-DDISDSAKDF 255
Cdd:cd06653  166 -IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW---AEYEAMAAIFKIATQPTKPQLpDGVSDACRDF 241
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDpNKRYTCEQAARHPWI 279
Cdd:cd06653  242 LRQIFVEE-KRRPTAEFLLRHPFV 264
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
23-276 3.11e-34

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: 127.49  E-value: 3.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVA-----LEDIYespnhLYLV 97
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRyyqawIERAN-----LYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME----- 172
Cdd:cd14046   83 MEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL---DSNGNVKIGDFGLATSNklnve 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 --------------GKGDVMSTACGTPGYVAPEVLAQKP--YSKAVDCWSIGVIaYILLCgYPPFYDENDSKLFEQILKA 236
Cdd:cd14046  160 latqdinkstsaalGSSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGII-FFEMC-YPFSTGMERVQILTALRSV 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 594150345 237 EYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14046  238 SIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
18-286 3.32e-34

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: 127.92  E-value: 3.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYESPN 92
Cdd:cd06654   17 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLVGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKM 171
Cdd:cd06654   91 ELWVVMEYLAGGSLTDVVTETCM-DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFDSPywDDISD 250
Cdd:cd06654  167 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRaLYLIATNGTPELQNP--EKLSA 244
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALS 286
Cdd:cd06654  245 IFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLS 280
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
27-279 3.91e-34

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: 126.73  E-value: 3.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKC--IPKKA-------LKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQveLPKTSsdradsrQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGK--G 175
Cdd:cd06629   87 LEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV---DLEGICKISDFGISKKSDDiyG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTAC-GTPGYVAPEVL--AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEndsklfEQIlKAEYEFDS-----PYWDD 247
Cdd:cd06629  164 NNGATSMqGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDD------EAI-AAMFKLGNkrsapPVPED 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 594150345 248 --ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06629  237 vnLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
18-294 5.01e-34

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: 127.07  E-value: 5.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgkESSIEN---EIAVLRKIKHENIVALEDIYESPNHL 94
Cdd:cd06644    9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKS----EEELEDymvEIEILATCNHPYIVKLLGAFYWDGKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGELFDRIVE--KGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME 172
Cdd:cd06644   85 WIMIEFCPGGAVDAIMLEldRGL-TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLL---TLDGDIKLADFGVSAKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKG-DVMSTACGTPGYVAPEV-----LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE-FDSPY- 244
Cdd:cd06644  161 VKTlQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPtLSQPSk 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 245 WddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTAlSKNIHESVS 294
Cdd:cd06644  241 W---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTS-NRPLRELVA 286
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
29-281 6.48e-34

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: 126.40  E-value: 6.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHEN----IVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTGGdcpfIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL----SKMEGKGDVm 178
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLacdfSKKKPHASV- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 stacGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd05606  158 ----GTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPF-RQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLE 232
                        250       260
                 ....*....|....*....|....*....
gi 594150345 258 NLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:cd05606  233 GLLQRDVSKRLGClgrgaTEVKEHPFFKG 261
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
23-281 6.79e-34

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: 128.64  E-value: 6.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05627    4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEqvAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL------------ 168
Cdd:cd05627   84 LPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLL---DAKGHVKLSDFGLctglkkahrtef 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 ------------------SKMEG------KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE 224
Cdd:cd05627  161 yrnlthnppsdfsfqnmnSKRKAetwkknRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 225 NDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAG 281
Cdd:cd05627  241 TPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCTDAENRigSNGVEEIKSHPFFEG 299
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
23-279 1.04e-33

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: 125.34  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKA--TGKLFAVKCIPkkaLKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAVDSTteTDAHCAVKIFE---VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLSKMEGKgDVMST 180
Cdd:cd14112   82 LQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRAQKVSK-LGKVP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND--SKLFEQILKAEYEFDSPYwDDISDSAKDFIR 257
Cdd:cd14112  159 VDGDTDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDdeEETKENVIFVKCRPNLIF-VEATQEALRFAT 237
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14112  238 WALKKSPTRRMRTDEALEHRWL 259
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
2-270 1.44e-33

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: 127.84  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   2 ARENGESSSSWKKQAEDIKKIfefketLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIK-H 78
Cdd:cd05618    7 SRESGKASSSLGLQDFDLLRV------IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIdwVQTEKHVFEQASnH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  79 ENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEE 158
Cdd:cd05618   81 PFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL---DSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 SKIMISDFGLSKME-GKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF--------YDEN-DSK 228
Cdd:cd05618  158 GHIKLTDYGMCKEGlRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNtEDY 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 229 LFEQILKAEYEFDSpywdDISDSAKDFIRNLMEKDPNKRYTC 270
Cdd:cd05618  238 LFQVILEKQIRIPR----SLSVKAASVLKSFLNKDPKERLGC 275
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
27-259 2.75e-33

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: 127.44  E-value: 2.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVlnRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL---------SKMEGKG 175
Cdd:cd05626   87 DMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLctgfrwthnSKYYQKG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 ---------------DVMSTAC------------------------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLC 216
Cdd:cd05626  164 shirqdsmepsdlwdDVSNCRCgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 594150345 217 GYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd05626  244 GQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKL 286
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
23-267 3.10e-33

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: 124.15  E-value: 3.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   23 FEFKETLGTGAFSEVVLAEEKATGKLF----AVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   99 QLVSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:pfam07714  81 EYMPGGDLLDFLRKhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLV---SENLVVKISDFGLSRDIYDDDY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  178 MSTACGTPG---YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQIlKAEYEFDSPywDDISDSAK 253
Cdd:pfam07714 158 YRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEFL-EDGYRLPQP--ENCPDELY 234
                         250
                  ....*....|....
gi 594150345  254 DFIRNLMEKDPNKR 267
Cdd:pfam07714 235 DLMKQCWAYDPEDR 248
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
29-280 3.29e-33

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: 125.14  E-value: 3.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREL-LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 rIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKMEGKGDVMSTACGTPGY 187
Cdd:cd06657  107 -IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILL---THDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIlKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd06657  183 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
                        250
                 ....*....|...
gi 594150345 268 YTCEQAARHPWIA 280
Cdd:cd06657  262 ATAAELLKHPFLA 274
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
21-277 4.13e-33

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: 124.25  E-value: 4.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEV--VLAEEKatgKLFAVKCIpkkALKGKESSI----ENEIAVLRKIKHE-NIVALED--IYESP 91
Cdd:cd14131    1 KPYEILKQLGKGGSSKVykVLNPKK---KIYALKRV---DLEGADEQTlqsyKNEIELLKKLKGSdRIIQLYDyeVTDED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLvsgGEL-FDRIVEKGFYTEKDaSTLIR----QVLDAVYYLHRMGIVHRDLKPENLLYYsqdeESKIMISDF 166
Cdd:cd14131   75 DYLYMVMEC---GEIdLATILKKKRPKPID-PNFIRyywkQMLEAVHTIHEEGIVHSDLKPANFLLV----KGRLKLIDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSKMEGKGD---VMSTACGTPGYVAPEVLAQ-------KPYSK---AVDCWSIGVIAYILLCGYPPFYD--ENDSKLfE 231
Cdd:cd14131  147 GIAKAIQNDTtsiVRDSQVGTLNYMSPEAIKDtsasgegKPKSKigrPSDVWSLGCILYQMVYGKTPFQHitNPIAKL-Q 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 232 QILKAEYEFDSPywdDISD-SAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14131  226 AIIDPNHEIEFP---DIPNpDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
23-275 4.72e-33

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: 126.69  E-value: 4.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKES--SIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05628    3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL------------ 168
Cdd:cd05628   83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL---DSKGHVKLSDFGLctglkkahrtef 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 --------------SKMEGKGDVMS----------TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE 224
Cdd:cd05628  160 yrnlnhslpsdftfQNMNSKRKAETwkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 225 NDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRnlmekdpnkRYTCEQAAR 275
Cdd:cd05628  240 TPQETYKKVMNWKETLIFPPEVPISEKAKDLIL---------RFCCEWEHR 281
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
29-279 6.35e-33

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: 123.42  E-value: 6.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKG-----KESSIENEIAVLRKI----KHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd14101    8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklpGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 L-VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMisDFGlSKMEGKGDVM 178
Cdd:cd14101   88 RpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGDIKLI--DFG-SGATLKDSMY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDsklfEQILKAEYEFDSPywddISDSAKDFIR 257
Cdd:cd14101  165 TDFDGTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPF--ERD----TDILKAKPSFNKR----VSNDCRSLIR 234
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14101  235 SCLAYNPSDRPSLEQILLHPWM 256
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
29-279 8.19e-33

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: 123.99  E-value: 8.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREL-LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 rIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGL-SKMEGKGDVMSTACGTPGY 187
Cdd:cd06658  109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFcAQVSKEVPKRKSLVGTPYW 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEyefdSPYWDD---ISDSAKDFIRNLMEKDP 264
Cdd:cd06658  185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNL----PPRVKDshkVSSVLRGFLDLMLVREP 260
                        250
                 ....*....|....*
gi 594150345 265 NKRYTCEQAARHPWI 279
Cdd:cd06658  261 SQRATAQELLQHPFL 275
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
27-279 9.76e-33

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: 122.61  E-value: 9.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd08218    6 KKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKErEESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRI-VEKGFYTEKDastlirQVLD-------AVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKGD 176
Cdd:cd08218   86 LYKRInAQRGVLFPED------QILDwfvqlclALKHVHDRKILHRDIKSQNIFL---TKDGIIKLGDFGIARvLNSTVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWddiSDSAKDFI 256
Cdd:cd08218  157 LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYPPVPSRY---SYDLRSLV 233
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08218  234 SQLFKRNPRDRPSINSILEKPFI 256
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-221 1.60e-32

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: 123.10  E-value: 1.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVK-CIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHL-----YLVMQLVS 102
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKsCRLELSVKNKDRWCH-EIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELfDRIVEK-----GFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKIM--ISDFGLSKMEGKG 175
Cdd:cd14039   80 GGDL-RKLLNKpenccGL-KESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVL--QEINGKIVhkIIDLGYAKDLDQG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14039  156 SLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
15-294 1.73e-32

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: 125.11  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  15 QAEDikkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSI-ENEIAVLRKIKHENIVALEDIYESPN 92
Cdd:cd05621   50 KAED----YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfEMIKRSDSAFfWEERDIMAFANSPWVVQLFCAFQDDK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KM 171
Cdd:cd05621  126 YLYMVMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADFGTCmKM 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDV-MSTACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWD 246
Cdd:cd05621  202 DETGMVhCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDV 281
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 247 DISDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAGDTALSKNIHESVS 294
Cdd:cd05621  282 EISKHAKNLICAFLTDREVRlgRNGVEEIKQHPFFRNDQWNWDNIRETAA 331
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
14-281 1.78e-32

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: 125.51  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  14 KQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESS-IENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd05623   65 KQMRLHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwEMLKRAETAcFREERDVLVNGDSQWITTLHYAFQDD 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyysQDEESKIMISDFG--L 168
Cdd:cd05623  145 NNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNIL---MDMNGHIRLADFGscL 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 SKMEGKGDVMSTACGTPGYVAPEVL-----AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSP 243
Cdd:cd05623  222 KLMEDGTVQSSVAVGTPDYISPEILqamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFP 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 594150345 244 YW-DDISDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAG 281
Cdd:cd05623  302 TQvTDVSENAKDLIRRLICSREHRlgQNGIEDFKNHPFFVG 342
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
27-278 1.81e-32

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: 122.97  E-value: 1.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG-- 104
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKDlk 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEG-KGDVMSTACG 183
Cdd:cd07836   86 KYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE---LKLADFGLARAFGiPVNTFSNEVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAK--------- 253
Cdd:cd07836  163 TLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEykptfpryp 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 594150345 254 ----------------DFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07836  243 pqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-279 2.50e-32

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: 121.60  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI--PKKALKGKESSiENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIdlTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRI-VEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKImiSDFGLSK-MEGKGDV 177
Cdd:cd08225   81 CDGGDLMKRInRQRGvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKL--GDFGIARqLNDSMEL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWddiSDSAKDFIR 257
Cdd:cd08225  159 AYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFAPISPNF---SRDLRSLIS 235
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08225  236 QLFKVSPRDRPSITSILKRPFL 257
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
13-294 5.75e-32

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: 123.96  E-value: 5.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  13 KKQAEDikkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIENEIAVLRKIKHEN-IVALEDIYES 90
Cdd:cd05622   69 RMKAED----YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQD 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS- 169
Cdd:cd05622  145 DRYLYMVMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCm 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDVM-STACGTPGYVAPEVLAQKP----YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPY 244
Cdd:cd05622  221 KMNKEGMVRcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPD 300
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 245 WDDISDSAKDFIRNLMEKDPNK--RYTCEQAARHPWIAGDTALSKNIHESVS 294
Cdd:cd05622  301 DNDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFKNDQWAWETLRDTVA 352
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
25-279 6.26e-32

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: 120.61  E-value: 6.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKES-SIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd08221    4 PVRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERrDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKG--FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSK-MEGKGDVMST 180
Cdd:cd08221   84 GNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKvLDSESSMAES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPywdDISDSAKDFIRNLM 260
Cdd:cd08221  161 IVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDE---QYSEEIIQLVHDCL 237
                        250
                 ....*....|....*....
gi 594150345 261 EKDPNKRYTCEQAARHPWI 279
Cdd:cd08221  238 HQDPEDRPTAEELLERPLL 256
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-279 6.79e-32

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: 120.62  E-value: 6.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPN-HLYLVMQL 100
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNlKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVE-KGFYTEKdastliRQVLD-------AVYYLHRMGIVHRDLKPENLLYysqdEESKIM-ISDFGLSK- 170
Cdd:cd08223   82 CEGGDLYTRLKEqKGVLLEE------RQVVEwfvqiamALQYMHERNILHRDLKTQNIFL----TKSNIIkVGDLGIARv 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYefdSPYWDDISD 250
Cdd:cd08223  152 LESSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKL---PPMPKQYSP 228
                        250       260
                 ....*....|....*....|....*....
gi 594150345 251 SAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08223  229 ELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
29-278 8.53e-32

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: 120.12  E-value: 8.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK----ESSIENEIAVlrkikHENIVALEDIY-ESPNHLYLVMQLVSG 103
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKdflrEYNISLELSV-----HPHIIKTYDVAfETEDYYVFAQEYAPY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeESKIMISDFGLSKMegKGDVMSTACG 183
Cdd:cd13987   76 GDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKD-CRRVKLCDFGLTRR--VGSTVKRVSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVLAQKPYSK-----AVDCWSIGVIAYILLCGYPP---------FYDEndsklFEQILKAEYEFDSPYWDDIS 249
Cdd:cd13987  153 TIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLTGNFPwekadsddqFYEE-----FVRWQKRKNTAVPSQWRRFT 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAAR---HPW 278
Cdd:cd13987  228 PKALRMFKKLLAPEPERRCSIKEVFKylgDRW 259
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
22-279 9.95e-32

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: 120.06  E-value: 9.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKK------ALKGkeSSIENEIAVLRKIKH--ENIVALEDIYESPNH 93
Cdd:cd14102    1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKErvtewgTLNG--VMVPLEIVLLKKVGSgfRGVIKLLDWYERPDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQ---LVSggELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMisDFGlSK 170
Cdd:cd14102   79 FLIVMErpePVK--DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELKLI--DFG-SG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDsklfEQILKAEYEFDSpywdDIS 249
Cdd:cd14102  154 ALLKDTVYTDFDGTRVYSPPEwIRYHRYHGRSATVWSLGVLLYDMVCGDIPF--EQD----EEILRGRLYFRR----RVS 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 250 DSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14102  224 PECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
29-279 1.07e-31

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: 120.15  E-value: 1.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCI---PKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNH--LYLVMQLVS 102
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVqfdPESPETSKEvNALECEIQLLKNLLHERIVQYYGCLRDPQErtLSIFMEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyysQDEESKIMISDFGLSK------MEGKGd 176
Cdd:cd06652   90 GGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL---RDSVGNVKLGDFGASKrlqticLSGTG- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 vMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDendsklFE---QILKAEYEFDSPYWD-DISDSA 252
Cdd:cd06652  166 -MKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAE------FEamaAIFKIATQPTNPQLPaHVSDHC 238
                        250       260
                 ....*....|....*....|....*..
gi 594150345 253 KDFIRNLMeKDPNKRYTCEQAARHPWI 279
Cdd:cd06652  239 RDFLKRIF-VEAKLRPSADELLRHTFV 264
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
19-280 2.12e-31

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: 121.13  E-value: 2.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkkalkgkESSIEN---------EIAVLRKIK-HENIVALEDIY 88
Cdd:cd07852    5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKI--------FDAFRNatdaqrtfrEIMFLQELNdHPNIIKLLNVI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPNH--LYLVmqlvsggelFDrivekgfYTEKDASTLIR--------------QVLDAVYYLHRMGIVHRDLKPENLLY 152
Cdd:cd07852   77 RAENDkdIYLV---------FE-------YMETDLHAVIRaniledihkqyimyQLLKALKYLHSGGVIHRDLKPSNILL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 153 ysqDEESKIMISDFGLSKM------EGKGDVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFydEN 225
Cdd:cd07852  141 ---NSDCRVKLADFGLARSlsqleeDDENPVLTDYVATRWYRAPEILlGSTRYTKGVDMWSVGCILGEMLLGKPLF--PG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 226 DSKL--FEQIL-------KAEYE-FDSPYWDDI-------------------SDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd07852  216 TSTLnqLEKIIevigrpsAEDIEsIQSPFAATMleslppsrpksldelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRH 295

                 ....
gi 594150345 277 PWIA 280
Cdd:cd07852  296 PYVA 299
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
23-271 2.16e-31

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: 121.67  E-value: 2.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS--IENEIAVLRKIKHEN-IVALEDIYESPNHLYLVMQ 99
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIdwVQTEKHVFEQASSNPfLVGLHSCFQTTSRLFLVIE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME-GKGDVM 178
Cdd:cd05617   97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMCKEGlGPGDTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF---YDENDSKLFEQILKAEYEFDSPYWDDISDSAKDF 255
Cdd:cd05617  174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHV 253
                        250
                 ....*....|....*.
gi 594150345 256 IRNLMEKDPNKRYTCE 271
Cdd:cd05617  254 LKGFLNKDPKERLGCQ 269
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
29-270 2.54e-31

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: 120.60  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSI---ENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVI-KKELVNDDEDIdwvQTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmEG--KGDVMSTAC 182
Cdd:cd05588   82 DLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL---DSEGHIKLTDYGMCK-EGlrPGDTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF--------YDEN-DSKLFEQILkaEYEFDSPywDDISDSAK 253
Cdd:cd05588  158 GTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNtEDYLFQVIL--EKPIRIP--RSLSVKAA 233
                        250
                 ....*....|....*..
gi 594150345 254 DFIRNLMEKDPNKRYTC 270
Cdd:cd05588  234 SVLKGFLNKNPAERLGC 250
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
27-279 2.54e-31

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 119.50  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKH---ENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd06917    7 ELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELfDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGKGDV-MSTAC 182
Cdd:cd06917   87 GSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTN---TGNVKLCDFGVAASLNQNSSkRSTFV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEyefdSPYWDD--ISDSAKDFIRNL 259
Cdd:cd06917  163 GTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK----PPRLEGngYSPLLKEFVAAC 238
                        250       260
                 ....*....|....*....|
gi 594150345 260 MEKDPNKRYTCEQAARHPWI 279
Cdd:cd06917  239 LDEEPKDRLSADELLKSKWI 258
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
23-281 3.69e-31

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: 120.55  E-value: 3.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP---------KKALKgkessienEIAVLRKIKHENIVALEDIYESP-- 91
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPnafdvvttaKRTLR--------ELKILRHFKHDNIIAIRDILRPKvp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 ----NHLYLVMQLVSGgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd07855   79 yadfKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLV---NENCELKIGDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 L-----SKMEGKGDVMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVI---------------------AYILLCGYPP 220
Cdd:cd07855  155 MarglcTSPEEHKYFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIfaemlgrrqlfpgknyvhqlqLILTVLGTPS 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 221 --FYDENDS----KLFEQI-LKAEYEFDSPYwDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAG 281
Cdd:cd07855  235 qaVINAIGAdrvrRYIQNLpNKQPVPWETLY-PKADQQALDLLSQMLRFDPSERITVAEALQHPFLAK 301
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
29-253 3.70e-31

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: 119.30  E-value: 3.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVK-CIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYE-----SPNHL-YLVMQLV 101
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKqCRQELSPKNRERWCL-EIQIMKRLNHPNVVAARDVPEglqklAPNDLpLLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGEL---FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKIM--ISDFGLSKMEGKGD 176
Cdd:cd14038   81 QGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVL--QQGEQRLIhkIIDLGYAKELDQGS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAK 253
Cdd:cd14038  159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHGKVRQKSNEDIVVYEDLTGAVK 235
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
27-272 4.17e-31

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: 118.41  E-value: 4.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAE---EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKGFY---------TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGK 174
Cdd:cd00192   81 GDLLDFLRKSRPVfpspepstlSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLV---GEDLVVKISDFGLSRDIYD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYV---APEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSPywddisD 250
Cdd:cd00192  158 DDYYRKKTGGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKG-YRLPKP------E 230
                        250       260
                 ....*....|....*....|....*.
gi 594150345 251 SAKDFIRNLMEK----DPNKRYTCEQ 272
Cdd:cd00192  231 NCPDELYELMLScwqlDPEDRPTFSE 256
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
27-279 7.91e-31

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: 117.92  E-value: 7.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEeKATGKLFAVKCI------PKKALKGKESsIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd06631    7 NVLGKGAYGTVYCGL-TSTGQLIAVKQVeldtsdKEKAEKEYEK-LQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSK-------MEG 173
Cdd:cd06631   85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV---IKLIDFGCAKrlcinlsSGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP----------FYDENDSKLFEQIlkaeyefdsP 243
Cdd:cd06631  162 QSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSGRKPVPRL---------P 232
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 244 ywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06631  233 --DKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
27-259 7.99e-31

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: 120.54  E-value: 7.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKK--ALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKdvLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL---------SKMEGKG 175
Cdd:cd05625   87 DMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwthdSKYYQSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 D---------------------------------------VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLC 216
Cdd:cd05625  164 DhlrqdsmdfsnewgdpencrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLV 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 594150345 217 GYPPFYDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFIRNL 259
Cdd:cd05625  244 GQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKL 286
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-267 9.75e-31

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: 117.38  E-value: 9.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI--PKKAlkgkeSSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlPKSS-----SAVEDsrkEAVLLAKMKHPNIVAFKESFEADGHLYIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRI-VEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENlLYYSQDeeSKIMISDFGLSKMegKG 175
Cdd:cd08219   77 MEYCDGGDLMQKIkLQRGkLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKN-IFLTQN--GKVKLGDFGSARL--LT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTAC---GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYefdSPYWDDISDSA 252
Cdd:cd08219  152 SPGAYACtyvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSY---KPLPSHYSYEL 228
                        250
                 ....*....|....*
gi 594150345 253 KDFIRNLMEKDPNKR 267
Cdd:cd08219  229 RSLIKQMFKRNPRSR 243
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
68-272 1.00e-30

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 121.66  E-value: 1.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  68 NEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF----DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHR 143
Cdd:PTZ00267 114 SELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNkqikQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHR 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 144 DLKPENLLYYSQdeeSKIMISDFGLSKMEGKG---DVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 220
Cdd:PTZ00267 194 DLKSANIFLMPT---GIIKLGDFGFSKQYSDSvslDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRP 270
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 221 FYDENDSKLFEQILKAEYEfdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:PTZ00267 271 FKGPSQREIMQQVLYGKYD---PFPCPVSSGMKALLDPLLSKNPALRPTTQQ 319
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
69-277 1.02e-30

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: 117.76  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  69 EIAVLRKI-KHENIVALEDIYESPNHLYLVMQL--VSGGELFD--RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHR 143
Cdd:cd13982   44 EVQLLRESdEHPNVIRYFCTEKDRQFLYIALELcaASLQDLVEspRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 144 DLKPENLL--YYSQDEESKIMISDFGLSKmegKGDVM-------STACGTPGYVAPEVLAQKPY---SKAVDCWSIG-VI 210
Cdd:cd13982  124 DLKPQNILisTPNAHGNVRAMISDFGLCK---KLDVGrssfsrrSGVAGTSGWIAPEMLSGSTKrrqTRAVDIFSLGcVF 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 211 AYILLCGYPPFydenDSKLFEQ--ILKAEYEFDSPYwDDISDS--AKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd13982  201 YYVLSGGSHPF----GDKLEREanILKGKYSLDKLL-SLGEHGpeAQDLIERMIDFDPEKRPSAEEVLNHP 266
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-279 2.09e-30

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: 118.03  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkkalKGKESS---IENEIAVLRKIKH------ENIVALEDIYESPNH 93
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-----RNKKRFhqqALVEVKILKHLNDndpddkHNIVRYKDSFIFRGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGG--ELFDRIVEKGFytekdASTLIR----QVLDAVYYLHRMGIVHRDLKPENLLYySQDEESKIMISDFG 167
Cdd:cd14210   90 LCIVFELLSINlyELLKSNNFQGL-----SLSLIRkfakQILQALQFLHKLNIIHCDLKPENILL-KQPSKSSIKVIDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKMEGKgdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIL------------- 234
Cdd:cd14210  164 SSCFEGE--KVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMevlgvppkslidk 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 235 --KAEYEFDSPYW-DDISDSAK----------------------DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14210  242 asRRKKFFDSNGKpRPTTNSKGkkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
15-267 2.91e-30

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 120.74  E-value: 2.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  15 QAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL-KGKESSIENEIAVLRKIKHENIVAL-ED-IYESP 91
Cdd:PTZ00283  26 TAKEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMsEADKNRAQAEVCCLLNCDFFSIVKChEDfAKKDP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NH------LYLVMQLVSGGELFDRIVEKG----FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKI 161
Cdd:PTZ00283 106 RNpenvlmIALVLDYANAGDLRQEIKSRAktnrTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSN---GLV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 162 MISDFGLSKMEG---KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEY 238
Cdd:PTZ00283 183 KLGDFGFSKMYAatvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRY 262
                        250       260
                 ....*....|....*....|....*....
gi 594150345 239 EfdsPYWDDISDSAKDFIRNLMEKDPNKR 267
Cdd:PTZ00283 263 D---PLPPSISPEMQEIVTALLSSDPKRR 288
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
110-276 6.64e-30

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: 115.97  E-value: 6.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 110 IVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEesKIMISDFGLSK-MEGKGDVMSTACGTPGYV 188
Cdd:cd13974  124 IREKRL-SEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR--KITITNFCLGKhLVSEDDLLKDQRGSPAYI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 189 APEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEF--DSPywddISDSAKDFIRNLMEKDPN 265
Cdd:cd13974  201 SPDVLSGKPYLgKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIpeDGR----VSENTVCLIRKLLVLNPQ 276
                        170
                 ....*....|.
gi 594150345 266 KRYTCEQAARH 276
Cdd:cd13974  277 KRLTASEVLDS 287
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
32-279 7.16e-30

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: 116.17  E-value: 7.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIpkKALKGKE----SSIEnEIAVLRKIKHENIVALEDIY--ESPNHLYLVMQLVSGgE 105
Cdd:cd07843   16 GTYGVVYRARDKKTGEIVALKKL--KMEKEKEgfpiTSLR-EINILLKLQHPNIVTVKEVVvgSNLDKIYMVMEYVEH-D 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLS-KMEGKGDVMSTACG 183
Cdd:cd07843   92 LKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI---LKICDFGLArEYGSPLKPYTQLVV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA----------EYE----------FDS 242
Cdd:cd07843  169 TLWYRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLlgtptekiwpGFSelpgakkktfTKY 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 594150345 243 PYW--------DDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07843  249 PYNqlrkkfpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
23-278 7.79e-30

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: 115.47  E-value: 7.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKgkessienEIAVLRKIKHENIVALEDIYESPNH 93
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIrletedegvPSTAIR--------EISLLKELNHPNIVRLLDVVHSENK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLV-----------MQLVSGGELFDRIVEKGFYtekdastlirQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIM 162
Cdd:cd07835   73 LYLVfefldldlkkyMDSSPLTGLDPPLIKSYLY----------QLLQGIAFCHSHRVLHRDLKPQNLLI---DTEGALK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 ISDFGLSKmegkgdvmstACGTP-----------GYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDSKlF 230
Cdd:cd07835  140 LADFGLAR----------AFGVPvrtythevvtlWYRAPEIlLGSKHYSTPVDIWSVGCIFAEMVTRRPLF--PGDSE-I 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 231 EQILK-------------------AEYEFDSPYW--DDISD-------SAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07835  207 DQLFRifrtlgtpdedvwpgvtslPDYKPTFPKWarQDLSKvvpsldeDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
23-278 1.00e-29

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: 115.35  E-value: 1.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKE----SSIEnEIAVLRKIKHENIVALEDIYESPNH----- 93
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRME--NEKEgfpiTAIR-EIKLLQKLDHPNVVRLKEIVTSKGSakykg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 -LYLVmqlvsggelFDrivekgfYTEKDASTLIR----------------QVLDAVYYLHRMGIVHRDLKPENLLYysqD 156
Cdd:cd07840   78 sIYMV---------FE-------YMDHDLTGLLDnpevkftesqikcymkQLLEGLQYLHSNGILHRDIKGSNILI---N 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 157 EESKIMISDFGLS-KMEGKGDVMSTA-CGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI 233
Cdd:cd07840  139 NDGVLKLADFGLArPYTKENNADYTNrVITLWYRPPELLlGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKI 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150345 234 LKA---------EYEFDSPYWDD------------------ISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07840  219 FELcgspteenwPGVSDLPWFENlkpkkpykrrlrevfknvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
22-278 1.26e-29

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 115.85  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKA--TGKLFAVKCI--PKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd07842    1 KYEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKFkgDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHADKSVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MqlvsggeLFDrivekgfYTEKDASTLIR--------------------QVLDAVYYLHRMGIVHRDLKPENLLYYSQDE 157
Cdd:cd07842   81 L-------LFD-------YAEHDLWQIIKfhrqakrvsippsmvksllwQILNGIHYLHSNWVLHRDLKPANILVMGEGP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ES-KIMISDFGLSKM---------EGKGDVMstacgTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DEN 225
Cdd:cd07842  147 ERgVVKIGDLGLARLfnaplkplaDLDPVVV-----TIWYRAPELlLGARHYTKAIDIWAIGCIFAELLTLEPIFKgREA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 226 DSKL--------FEQILKA---------EYEFDSPYWDDISDSAK------------------------DFIRNLMEKDP 264
Cdd:cd07842  222 KIKKsnpfqrdqLERIFEVlgtptekdwPDIKKMPEYDTLKSDTKastypnsllakwmhkhkkpdsqgfDLLRKLLEYDP 301
                        330
                 ....*....|....
gi 594150345 265 NKRYTCEQAARHPW 278
Cdd:cd07842  302 TKRITAEEALEHPY 315
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
23-279 1.26e-29

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: 114.76  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd06645   13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVI--KLEPGEDfAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KMEGKGDVMST 180
Cdd:cd06645   91 GGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILL---TDNGHVKLADFGVSaQITATIAKRKS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLA---QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFeqILKAEYEFDSPYWDD---ISDSAKD 254
Cdd:cd06645  168 FIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRAL--FLMTKSNFQPPKLKDkmkWSNSFHH 245
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06645  246 FVKMALTKNPKKRPTAEKLLQHPFV 270
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
17-278 1.55e-29

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: 116.13  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESS-IEneIAVLRKIKHE------NIVALEDIYE 89
Cdd:cd14134    8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKII-RNVEKYREAAkIE--IDVLETLAEKdpngksHCVQLRDWFD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  90 SPNHLYLVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESK------- 160
Cdd:cd14134   85 YRGHMCIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVynpkkkr 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 161 ---------IMISDFGLS--KMEGKGDVMSTAcgtpGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYpPFYDENDSK- 228
Cdd:cd14134  164 qirvpkstdIKLIDFGSAtfDDEYHSSIVSTR----HYRAPEVILGLGWSYPCDVWSIGCILVELYTGE-LLFQTHDNLe 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 229 ---LFEQIL--------------KAEYEFDSPY--WDDISDSAK------------------------DFIRNLMEKDPN 265
Cdd:cd14134  239 hlaMMERILgplpkrmirrakkgAKYFYFYHGRldWPEGSSSGRsikrvckplkrlmllvdpehrllfDLIRKMLEYDPS 318
                        330
                 ....*....|...
gi 594150345 266 KRYTCEQAARHPW 278
Cdd:cd14134  319 KRITAKEALKHPF 331
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
29-267 2.27e-29

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: 113.97  E-value: 2.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKES--SIENEIAVLRKI-KHENIVALED---IYESPNHLYLVMQLVS 102
Cdd:cd13985    8 LGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQlrVAIKEIEIMKRLcGHPNIVQYYDsaiLSSEGRKEVLLLMEYC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRI--VEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVM 178
Cdd:cd13985   85 PGSLVDILekSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILF---SNTGRFKLCDFGSATTEHYPLER 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACG----------TPGYVAPEVL---AQKPYSKAVDCWSIGVIAYILLCGYPPFydENDSKLfeQILKAEYefDSPYW 245
Cdd:cd13985  162 AEEVNiieeeiqkntTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF--DESSKL--AIVAGKY--SIPEQ 235
                        250       260
                 ....*....|....*....|..
gi 594150345 246 DDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd13985  236 PRYSPELHDLIRHMLTPDPAER 257
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
23-277 2.31e-29

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: 114.52  E-value: 2.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIeneiavLRKIKHENIVALEDIY----ESPNHLYL- 96
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQdKRYKNRELQI------MRRLKHPNIVKLKYFFyssgEKKDEVYLn 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 -VMQLVSGgELFDRIVE----KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIM-ISDFGLSK 170
Cdd:cd14137   80 lVMEYMPE-TLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV---DPETGVLkLCDFGSAK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDV-MSTACgTPGYVAPEVL--AQKpYSKAVDCWSIG-VIAYiLLCGYPPFYDENDSKLFEQILK----------- 235
Cdd:cd14137  156 RLVPGEPnVSYIC-SRYYRAPELIfgATD-YTTAIDIWSAGcVLAE-LLLGQPLFPGESSVDQLVEIIKvlgtptreqik 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 236 ------AEYEFD---SPYWDDI-----SDSAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14137  233 amnpnyTEFKFPqikPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
5-284 6.66e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 114.54  E-value: 6.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   5 NGESSSSWKKQAEDIKKIFEFKE---TLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENI 81
Cdd:PLN00034  55 SSSSSSSASGSAPSAAKSLSELErvnRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQICREIEILRDVNHPNV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  82 VALEDIYESPNHLYLVMQLVSGGELFDRIVEKgfytEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKI 161
Cdd:PLN00034 135 VKCHDMFDHNGEIQVLLEFMDGGSLEGTHIAD----EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI---NSAKNV 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 162 MISDFGLSKMEGKG-DVMSTACGTPGYVAPEV----LAQKPYSK-AVDCWSIGVIAYILLCGYPPFY--DEND------- 226
Cdd:PLN00034 208 KIADFGVSRILAQTmDPCNSSVGTIAYMSPERintdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGvgRQGDwaslmca 287
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 227 ---SKLFEQILKAEYEFdspywddisdsaKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTA 284
Cdd:PLN00034 288 icmSQPPEAPATASREF------------RHFISCCLQREPAKRWSAMQLLQHPFILRAQP 336
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
23-279 7.76e-29

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: 112.44  E-value: 7.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd06605    3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKmEGKGDVMSTA 181
Cdd:cd06605   83 GGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQ---VKLCDFGVSG-QLVDSLAKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG-YP-PFYDENDSKLFEQILKAEYEFDSPYW--DDISDSAKDFIR 257
Cdd:cd06605  159 VGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrFPyPPPNAKPSMMIFELLSYIVDEPPPLLpsGKFSPDFQDFVS 238
                        250       260
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06605  239 QCLQKDPTERPSYKELMEHPFI 260
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
23-277 9.34e-29

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: 112.78  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI--PKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkdSEENEEVKETTLR-ELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGG--ELFDRIvEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSK--MEGKGD 176
Cdd:cd07848   82 VEKNmlELLEEM-PNGVPPEK-VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHND---VLKLCDFGFARnlSEGSNA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND-SKLF-----------EQiLKAEYE----- 239
Cdd:cd07848  157 NYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLFtiqkvlgplpaEQ-MKLFYSnprfh 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 240 ------------FDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd07848  236 glrfpavnhpqsLERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
29-277 1.28e-28

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: 112.14  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIP--KKALKGKES---SIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEvveAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEesKIMISDFGL-----SKMEGKGDVM 178
Cdd:cd06630   88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQ--RLRIADFGAaarlaSKGTGAGEFQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK-AEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd06630  166 GQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKiASATTPPPIPEHLSPGLRDVTL 245
                        250       260
                 ....*....|....*....|
gi 594150345 258 NLMEKDPNKRYTCEQAARHP 277
Cdd:cd06630  246 RCLELQPEDRPPARELLKHP 265
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
18-279 1.48e-28

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: 112.07  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06640    1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd06640   81 MEYLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL---SEQGDVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 M-STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKaeyeFDSPYW-DDISDSAKDF 255
Cdd:cd06640  157 KrNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPK----NNPPTLvGDFSKPFKEF 232
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06640  233 IDACLNKDPSFRPTAKELLKHKFI 256
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
29-278 1.95e-28

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: 111.71  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCI---PKKALKGKE-SSIENEIAVLRKIKHENIV----ALEDIYESPnhLYLVMQL 100
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVqfdPESPETSKEvSALECEIQLLKNLQHERIVqyygCLRDRAEKT--LTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyysQDEESKIMISDFGLSK------MEGK 174
Cdd:cd06651   93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKrlqticMSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEqilKAEYEFDSPYWDDISDSAK 253
Cdd:cd06651  170 G--IRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEyEAMAAIFK---IATQPTNPQLPSHISEHAR 244
                        250       260
                 ....*....|....*....|....*
gi 594150345 254 DFIRNLMeKDPNKRYTCEQAARHPW 278
Cdd:cd06651  245 DFLGCIF-VEARHRPSAEELLRHPF 268
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
29-278 2.08e-28

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: 111.59  E-value: 2.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCipkkaLKGKESSIE-----NEIAVLRKIK-HENIVALEDIY--ESPNHLYLVMQL 100
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKC-----MKKHFKSLEqvnnlREIQALRRLSpHPNILRLIEVLfdRKTGRLALVFEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGgELFDRIV-EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKImiSDFGLSKmegkgdvms 179
Cdd:cd07831   82 MDM-NLYELIKgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI--KDDILKL--ADFGSCR--------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYV---------APE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND------------------SKLFE 231
Cdd:cd07831  148 GIYSKPPYTeyistrwyrAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiakihdvlgtpdaevLKKFR 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 232 QILKAEYEFDS-------PYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07831  228 KSRHMNYNFPSkkgtglrKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
23-270 2.28e-28

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: 112.45  E-value: 2.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHEN---IVALEDIYESPNHLYLV 97
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTGDcpfIVCMSYAFHTPDKLSFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd14223   82 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGLACDFSKKKP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTAcGTPGYVAPEVLAQK-PYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd14223  159 HASV-GTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLL 236
                        250
                 ....*....|....
gi 594150345 257 RNLMEKDPNKRYTC 270
Cdd:cd14223  237 EGLLQRDVNRRLGC 250
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
22-278 2.36e-28

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: 111.83  E-value: 2.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKA-LKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTeTEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGG--ELFDRIVEKGFYTEKDASTLIrQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKmegkgdvm 178
Cdd:cd07860   81 LHQDlkKFMDASALTGIPLPLIKSYLF-QLLQGLAFCHSHRVLHRDLKPQNLLI---NTEGAIKLADFGLAR-------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 stACGTP-----------GYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFeQILKA--------- 236
Cdd:cd07860  149 --AFGVPvrtythevvtlWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPgDSEIDQLF-RIFRTlgtpdevvw 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 237 -------EYEFDSPYW--DDISD-------SAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07860  226 pgvtsmpDYKPSFPKWarQDFSKvvppldeDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
78-278 2.42e-28

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 110.52  E-value: 2.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  78 HENIVALEDIYESPNHLYLVMQlVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYySQDE 157
Cdd:cd14023   44 HRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF-SDEE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSK-MEGKGDVMSTACGTPGYVAPEVL-AQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIL 234
Cdd:cd14023  122 RTQLRLESLEDTHiMKGEDDALSDKHGCPAYVSPEILnTTGTYSgKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 594150345 235 KAEYEFDspywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14023  202 RGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
29-279 2.95e-28

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: 110.98  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEE---KATGKLFAVKCIPKKALKGKESSIEN-EIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd08222    8 LGSGNFGTVYLVSDlkaTADEELKVLKEISVGELQPDETVDANrEAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVE----KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqdEESKIMISDFGLSK-MEGKGDVMS 179
Cdd:cd08222   88 DLDDKISEykksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISRiLMGTSDLAT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkaeyEFDSPYWDDISDSA-KDFIRN 258
Cdd:cd08222  164 TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIV----EGETPSLPDKYSKElNAIYSR 239
                        250       260
                 ....*....|....*....|.
gi 594150345 259 LMEKDPNKRYTCEQAARHPWI 279
Cdd:cd08222  240 MLNKDPALRPSAAEILKIPFI 260
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
17-280 5.16e-28

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: 112.01  E-value: 5.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkkalkgKESSIEN---------EIAVLRKIKHENIVALEDI 87
Cdd:cd07849    1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK---------KISPFEHqtyclrtlrEIKILLRFKHENIIGILDI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 -----YESPNHLYLVMqlvsggELFDRIVEKGFYTEK----DASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEE 158
Cdd:cd07849   72 qrpptFESFKDVYIVQ------ELMETDLYKLIKTQHlsndHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL---NTN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 SKIMISDFGLSKM----EGKGDVMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF--YDENDS-KLF 230
Cdd:cd07849  143 CDLKICDFGLARIadpeHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFpgKDYLHQlNLI 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 231 EQILkaeyefDSPYWDD----ISDSAKDFIR----------------------NLMEK----DPNKRYTCEQAARHPWIA 280
Cdd:cd07849  223 LGIL------GTPSQEDlnciISLKARNYIKslpfkpkvpwnklfpnadpkalDLLDKmltfNPHKRITVEEALAHPYLE 296
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
23-280 5.24e-28

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: 111.73  E-value: 5.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKAT--GKLFAVKCIP---------KKALKgkessienEIAVLRKIK-HENIVALEDI--- 87
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITnvfskkilaKRALR--------ELKLLRHFRgHKNITCLYDMdiv 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 -YESPNHLYLVMQLVSGGelFDRIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISD 165
Cdd:cd07857   74 fPGNFNELYLYEELMEAD--LHQIIRSGQpLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA---DCELKICD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FGLSK--MEGKGDV---MSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA--- 236
Cdd:cd07857  149 FGLARgfSENPGENagfMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVlgt 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 237 ---------------EYEFDSPY---------WDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd07857  229 pdeetlsrigspkaqNYIRSLPNipkkpfesiFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-279 5.27e-28

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 112.10  E-value: 5.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEI-AVLRKIKHE---NIVALEDIYESPNHLYLVM 98
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKIlDALRRKDRDnshNVIHMKEYFYFRNHLCITF 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVsGGELFDRIVEKGFytEKDASTLIRQ----VLDAVYYLHRMGIVHRDLKPENLLYYsQDEESKIMISDFGLSKMEGK 174
Cdd:cd14225  125 ELL-GMNLYELIKKNNF--QGFSLSLIRRfaisLLQCLRLLYRERIIHCDLKPENILLR-QRGQSSIKVIDFGSSCYEHQ 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 gdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND---------------SKLFEQILKAEYE 239
Cdd:cd14225  201 --RVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEveqlacimevlglppPELIENAQRRRLF 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594150345 240 FDS----------------PYWDDISDSAK-------DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14225  279 FDSkgnprcitnskgkkrrPNSKDLASALKtsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
23-281 5.74e-28

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: 112.08  E-value: 5.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGK--ESSIENEIAVLRKIKHEN---IVALEDIYESPNHLYLV 97
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKqgETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKLCFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd05633   87 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGLACDFSKKKP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTAcGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKAEYEFDSPYWDDISDSAKDFI 256
Cdd:cd05633  164 HASV-GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLL 241
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 257 RNLMEKDPNKRYTC-----EQAARHPWIAG 281
Cdd:cd05633  242 EGLLQRDVSKRLGChgrgaQEVKEHSFFKG 271
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
17-278 7.90e-28

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 111.39  E-value: 7.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKET-LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEN-------------EIAVLRKIKHENIV 82
Cdd:PTZ00024   4 FSISERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  83 ALEDIYESPNHLYLVMQLVSG--GELFDRiveKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEesk 160
Cdd:PTZ00024  84 GLVDVYVEGDFINLVMDIMASdlKKVVDR---KIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 161 IMISDFGLSKMEGKGDVMSTACG---------------TPGYVAPEVL--AQKpYSKAVDCWSIGVIAYILLCGYPPFYD 223
Cdd:PTZ00024 158 CKIADFGLARRYGYPPYSDTLSKdetmqrreemtskvvTLWYRAPELLmgAEK-YHFAVDMWSVGCIFAELLTGKPLFPG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 224 END----SKLFEQI---------------LKAEYEFDSP-----YWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:PTZ00024 237 ENEidqlGRIFELLgtpnednwpqakklpLYTEFTPRKPkdlktIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEY 315
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
45-279 1.01e-27

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: 109.05  E-value: 1.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  45 TGKLFAVKCIPKKALKGKESsieneiAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGgELFDRIVEKGFYTEKDASTL 124
Cdd:cd13976   17 TGEELVCKVVPVPECHAVLR------AYFRLPSHPNISGVHEVIAGETKAYVFFERDHG-DLHSYVRSRKRLREPEAARL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 125 IRQVLDAVYYLHRMGIVHRDLKPENLlYYSQDEESKIMISDF-GLSKMEGKGDVMSTACGTPGYVAPEVL-AQKPYS-KA 201
Cdd:cd13976   90 FRQIASAVAHCHRNGIVLRDLKLRKF-VFADEERTKLRLESLeDAVILEGEDDSLSDKHGCPAYVSPEILnSGATYSgKA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 202 VDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDspywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd13976  169 ADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIP----ETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
23-279 1.15e-27

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: 109.35  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII--KLEPGDDFSlIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL-SKMEGKGDVMST 180
Cdd:cd06646   89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILL---TDNGDVKLADFGVaAKITATIAKRKS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEVLAQKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFeqiLKAEYEFDSPYWDD---ISDSAK 253
Cdd:cd06646  166 FIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAELQPPMFDLHPMRaLF---LMSKSNFQPPKLKDktkWSSTFH 242
                        250       260
                 ....*....|....*....|....*.
gi 594150345 254 DFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06646  243 NFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
29-280 1.23e-27

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: 110.92  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKgkessienEIAVLRKIKHENIVALEDIYESP-----NHL 94
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIanafdnridAKRTLR--------EIKLLRHLDHENVIAIKDIMPPPhreafNDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKME-G 173
Cdd:cd07858   85 YIVYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL---NANCDLKICDFGLARTTsE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE---NDSKLFEQILKAEYEFDSPYWDdiS 249
Cdd:cd07858  161 KGDFMTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKdyvHQLKLITELLGSPSEEDLGFIR--N 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 250 DSAKDFIRN----------------------LMEK----DPNKRYTCEQAARHPWIA 280
Cdd:cd07858  239 EKARRYIRSlpytprqsfarlfphanplaidLLEKmlvfDPSKRITVEEALAHPYLA 295
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
18-279 1.26e-27

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: 109.76  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06642    1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd06642   81 MEYLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLL---SEQGDVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 M-STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK-----AEYEFDSPYwddisds 251
Cdd:cd06642  157 KrNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKnspptLEGQHSKPF------- 229
                        250       260
                 ....*....|....*....|....*...
gi 594150345 252 aKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06642  230 -KEFVEACLNKDPRFRPTAKELLKHKFI 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
23-275 1.30e-27

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: 109.28  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL---KGKESSIeNEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMmdaKARQDCL-KEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRI----VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSK-MEGK 174
Cdd:cd08224   81 LADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA---NGVVKLGDLGLGRfFSSK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS--KLFEQILKAEYEfdsPYWDDI-SDS 251
Cdd:cd08224  158 TTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYP---PLPADLySQE 234
                        250       260
                 ....*....|....*....|....*...
gi 594150345 252 AKDFIRNLMEKDPNKR----YTCEQAAR 275
Cdd:cd08224  235 LRDLVAACIQPDPEKRpdisYVLDVAKR 262
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
18-279 1.32e-27

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: 109.39  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd06641    1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDrIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd06641   81 MEYLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL---SEHGEVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyefDSPYWD-DISDSAKDF 255
Cdd:cd06641  157 KRN*fVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKN----NPPTLEgNYSKPLKEF 232
                        250       260
                 ....*....|....*....|....
gi 594150345 256 IRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06641  233 VEACLNKEPSFRPTAKELLKHKFI 256
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
29-280 1.57e-27

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: 110.90  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPK---KALKGKESSieNEIAVLRKIKHENIVALEDIY------ESPNHLYLVMQ 99
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRpfqSIIHAKRTY--RELRLLKHMKHENVIGLLDVFtparslEEFNDVYLVTH 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVsGGELfDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyySQDEESKIMISDFGLSKMegKGDVMS 179
Cdd:cd07877  103 LM-GADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNL---AVNEDCELKILDFGLARH--TDDEMT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDDI-SDSAKDFIR 257
Cdd:cd07877  176 GYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKIsSESARNYIQ 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 594150345 258 ----------------------NLMEK----DPNKRYTCEQAARHPWIA 280
Cdd:cd07877  256 sltqmpkmnfanvfiganplavDLLEKmlvlDSDKRITAAQALAHAYFA 304
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
26-279 1.95e-27

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: 110.03  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIK-------HENIVALEDIYESPNHLYLVM 98
Cdd:cd14212    4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLE--IAILTLLNtkydpedKHHIVRLLDHFMHHGHLCIVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVsGGELFDRIVE---KGFYTeKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMISDFGLSKMEGKg 175
Cdd:cd14212   82 ELL-GVNLYELLKQnqfRGLSL-QLIRKFLQQLLDALSVLKDARIIHCDLKPENIL-LVNLDSPEIKLIDFGSACFENY- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 dVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIA---------------YILLC------GYPPFY----DENDSKLF 230
Cdd:cd14212  158 -TLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAaelflglplfpgnseYNQLSriiemlGMPPDWmlekGKNTNKFF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 231 EQILKAE----YEFDSP----------------YW-----DDI-------SDSAK-------------DFIRNLMEKDPN 265
Cdd:cd14212  237 KKVAKSGgrstYRLKTPeefeaenncklepgkrYFkyktlEDIimnypmkKSKKEqidkemetrlafiDFLKGLLEYDPK 316
                        330
                 ....*....|....
gi 594150345 266 KRYTCEQAARHPWI 279
Cdd:cd14212  317 KRWTPDQALNHPFI 330
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
23-278 2.69e-27

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: 109.33  E-value: 2.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKgkessienEIAVLRKIKHENIVALED-IYE-SP 91
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKIlmhnekdgfPITALR--------EIKILKKLKHPNVVPLIDmAVErPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHL-----------YLVMQLVsgGELFDRIVEkgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESK 160
Cdd:cd07866   82 KSKrkrgsvymvtpYMDHDLS--GLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILI---DNQGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 161 IMISDFGL-------SKMEGKGDVMSTACGTP-----GYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS 227
Cdd:cd07866  154 LKIADFGLarpydgpPPNPKGGGGGGTRKYTNlvvtrWYRPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDI 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 228 KLFEQILKA---EYEFDSPYWDDI-----SDSAKDFIRNLMEK------------------DPNKRYTCEQAARHPW 278
Cdd:cd07866  234 DQLHLIFKLcgtPTEETWPGWRSLpgcegVHSFTNYPRTLEERfgklgpegldllskllslDPYKRLTASDALEHPY 310
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
27-278 3.97e-27

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: 108.28  E-value: 3.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG- 104
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAMKKIRlESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLSMDl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 -ELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG-KGDVMSTAC 182
Cdd:cd07861   86 kKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLI---DNKGVIKLADFGLARAFGiPVRVYTHEV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFE--QILKA-------------EYEFDSPYW 245
Cdd:cd07861  163 VTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHgDSEIDQLFRifRILGTptediwpgvtslpDYKNTFPKW 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 246 D---------DISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07861  243 KkgslrtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
78-278 4.89e-27

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: 107.04  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  78 HENIVALEDIYESPNHLYLVMQLvSGGEL--FDRIVEKgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQ 155
Cdd:cd14022   44 HSNINQITEIILGETKAYVFFER-SYGDMhsFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 156 DEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVL-AQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI 233
Cdd:cd14022  121 ERTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 594150345 234 LKAeyEFDSPywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14022  201 RRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
20-295 9.88e-27

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: 107.51  E-value: 9.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFkETLGTGAFSEVVLAEEKATGKLFAVKCI---PKKALKgkeSSIENEIAVLRKIKHENIVALEDIY--ESPNHL 94
Cdd:cd06621    1 DKIVEL-SSLGEGAGGSVTKCRLRNTKTIFALKTIttdPNPDVQ---KQILRELEINKSCASPYIVKYYGAFldEQDSSI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGELfDRIVEK-----GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS 169
Cdd:cd06621   77 GIAMEYCEGGSL-DSIYKKvkkkgGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILL---TRKGQVKLCDFGVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KmEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS-----KLFEQI-------LKAE 237
Cdd:cd06621  153 G-ELVNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIvnmpnpeLKDE 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 238 YEfDSPYWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALSKNIHESVSA 295
Cdd:cd06621  232 PE-NGIKW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAKFVKQ 285
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
29-221 1.43e-26

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: 106.32  E-value: 1.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKatGKLFAVKCI---PKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKAArqdPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LfDRIVEKgfyTEKDASTLIR---QVLDAVYYLHR---MGIVHRDLKPENLL----YYSQDEESKIM-ISDFGLSKMEGK 174
Cdd:cd14061   80 L-NRVLAG---RKIPPHVLVDwaiQIARGMNYLHNeapVPIIHRDLKSSNILileaIENEDLENKTLkITDFGLAREWHK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 175 GDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14061  156 TTRMSAA-GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
23-267 1.55e-26

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: 106.61  E-value: 1.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP-------KKALKgkessienEIAVLRKIKHENIVALED---IYESPN 92
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILchskedvKEAMR--------EIENYRLFNHPNILRLLDsqiVKEAGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 H--LYLVMQLVSGGELFDRI----VEKGFYTEKDASTLIRQVLDAVYYLH---RMGIVHRDLKPENLLYYSQDEeskIMI 163
Cdd:cd13986   74 KkeVYLLLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDE---PIL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFG---LSKMEGKG--------DVMSTACgTPGYVAPEVLAQKPYS---KAVDCWSIGVIAYILLCGYPPF---YDEND 226
Cdd:cd13986  151 MDLGsmnPARIEIEGrrealalqDWAAEHC-TMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFeriFQKGD 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 594150345 227 SkLFEQILKAEYEF--DSPYwddiSDSAKDFIRNLMEKDPNKR 267
Cdd:cd13986  230 S-LALAVLSGNYSFpdNSRY----SEELHQLVKSMLVVNPAER 267
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
4-234 2.33e-26

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 110.60  E-value: 2.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    4 ENGESSSSwkkQAEDIKKIfefketlGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIV 82
Cdd:PTZ00266    6 DDGESRLN---EYEVIKKI-------GNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREkSQLVIEVNVMRELKHKNIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   83 ALEDIY--ESPNHLYLVMQLVSGGELfDRIVEK-----GFYTEKDASTLIRQVLDAVYYLHRMG-------IVHRDLKPE 148
Cdd:PTZ00266   76 RYIDRFlnKANQKLYILMEFCDAGDL-SRNIQKcykmfGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  149 NLLYYSQDEE-SKIM-------------ISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVIAY 212
Cdd:PTZ00266  155 NIFLSTGIRHiGKITaqannlngrpiakIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHetKSYDDKSDMWALGCIIY 234
                         250       260
                  ....*....|....*....|..
gi 594150345  213 ILLCGYPPFYDENDsklFEQIL 234
Cdd:PTZ00266  235 ELCSGKTPFHKANN---FSQLI 253
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
23-210 2.78e-26

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: 105.97  E-value: 2.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEK-ATGKLFAVKCIPKKAL--KGKESSIEnEIAVLRKIK---HENIVALEDIYESPNHLYL 96
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAgaKDRLRRLE-EVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEKGFYTEKDASTL---IRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL----- 168
Cdd:cd14052   81 QTELCENGSLDVFLSELGLLGRLDEFRVwkiLVELSLGLRFIHDHHFVHLDLKPANVLI---TFEGTLKIGDFGMatvwp 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 594150345 169 --SKMEGKGDVMstacgtpgYVAPEVLAQKPYSKAVDCWSIGVI 210
Cdd:cd14052  158 liRGIEREGDRE--------YIAPEILSEHMYDKPADIFSLGLI 193
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
22-279 2.85e-26

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: 105.44  E-value: 2.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKG-----KESSIENEIAVLRKIKH--ENIVALEDIYESPNHL 94
Cdd:cd14100    1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwgelpNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSG-GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMisDFGLSKMEg 173
Cdd:cd14100   81 VLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELKLI--DFGSGALL- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDsklfEQILKAEYEFDSpywdDISDSA 252
Cdd:cd14100  158 KDTVYTDFDGTRVYSPPEwIRFHRYHGRSAAVWSLGILLYDMVCGDIPF--EHD----EEIIRGQVFFRQ----RVSSEC 227
                        250       260
                 ....*....|....*....|....*..
gi 594150345 253 KDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14100  228 QHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
29-280 4.37e-26

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: 106.50  E-value: 4.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPK---KALKGKESSieNEIAVLRKIKHENIVALEDIYESP-NHLYLVMQLVsGG 104
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKKIMKpfsTPVLAKRTY--RELKLLKHLRHENIISLSDIFISPlEDIYFVTELL-GT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELF----DRIVEKGFytekdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGdvMST 180
Cdd:cd07856   95 DLHrlltSRPLEKQF-----IQYFLYQILRGLKYVHSAGVIHRDLKPSNILV---NENCDLKICDFGLARIQDPQ--MTG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF---------------------------YDENDSKLFEQ 232
Cdd:cd07856  165 YVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitellgtppddvintiCSENTLRFVQS 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 233 ILKAEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd07856  245 LPKRERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLA 292
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
22-277 7.55e-26

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: 103.93  E-value: 7.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPkkalkgkeSSIENEIAVLRKIK----------HENIVALEDIYESP 91
Cdd:cd14050    2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVKRSR--------SRFRGEKDRKRKLEeverheklgeHPNCVRFIKAWEEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMqlvsggELFDRIVEKgfYTEKDASTLIRQV-------LDAVYYLHRMGIVHRDLKPENlLYYSQDEESKimIS 164
Cdd:cd14050   74 GILYIQT------ELCDTSLQQ--YCEETHSLPESEVwnilldlLKGLKHLHDHGLIHLDIKPAN-IFLSKDGVCK--LG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMEGKGDVMSTACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILLCG--YPPFYDendskLFEQILKAeyEFDS 242
Cdd:cd14050  143 DFGLVVELDKEDIHDAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELACNleLPSGGD-----GWHQLRQG--YLPE 214
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594150345 243 PYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14050  215 EFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
29-267 9.70e-26

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: 103.67  E-value: 9.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAeeKATGKLFAVKCIPKKALKgkeSSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14058    1 VGRGSFGVVCKA--RWRNQIVAVKIIESESEK---KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RI---VEKGFYTEKDASTLIRQVLDAVYYLHRMG---IVHRDLKPENLLYYSQDEESKimISDFGLSKmeGKGDVMSTAC 182
Cdd:cd14058   76 VLhgkEPKPIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLK--ICDFGTAC--DISTHMTNNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFeQILKAEYEFDSPywDDISDSAKDfIRNLME- 261
Cdd:cd14058  152 GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF-DHIGGPAF-RIMWAVHNGERP--PLIKNCPKP-IESLMTr 226

                 ....*....
gi 594150345 262 ---KDPNKR 267
Cdd:cd14058  227 cwsKDPEKR 235
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
29-221 2.25e-25

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: 104.11  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPN--HLYLVMQLVSGGEL 106
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTtrHKVLVMELCPCGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVE-KGFY--TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL-YYSQDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd13988   81 YTVLEEpSNAYglPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQSVYKLTDFGAARELEDDEQFVSLY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 183 GTPGYVAPE-----VL---AQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd13988  161 GTEEYLHPDmyeraVLrkdHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
29-229 2.80e-25

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: 103.12  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKaTGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIveKGFYTEKDASTLIR-----QVLDAVYYLHRMG---IVHRDLKPENLLYysqDEESKIMISDFGLSK-MEGKGDVMS 179
Cdd:cd14066   80 RL--HCHKGSPPLPWPQRlkiakGIARGLEYLHEECpppIIHGDIKSSNILL---DEDFEPKLTDFGLARlIPPSESVSK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 180 T--ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD--ENDSKL 229
Cdd:cd14066  155 TsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEnrENASRK 208
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
29-280 3.05e-25

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: 104.48  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKES--SIENEIAVLRKIKHENIVALEDIYESPNH------------- 93
Cdd:cd07854   13 LGCGSNGLVFSAVDSDCDKRVAVK---KIVLTDPQSvkHALREIKIIRRLDHDNIVKVYEVLGPSGSdltedvgslteln 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 -LYLVMQLVSGGelFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKImiSDFGLSKM- 171
Cdd:cd07854   90 sVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLKI--GDFGLARIv 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 ----EGKGdVMSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYP------------------PFYDEND-- 226
Cdd:cd07854  166 dphySHKG-YLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPlfagaheleqmqlilesvPVVREEDrn 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 227 ---SKLFEQILKAEYEFDSPYWD---DISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd07854  245 ellNVIPSFVRNDGGEPRRPLRDllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
18-279 8.45e-25

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: 102.49  E-value: 8.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKIKHENIVAL---EDIYESP--- 91
Cdd:cd06637    3 DPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTGDEEEEIKQEINMLKKYSHHRNIATyygAFIKKNPpgm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 -NHLYLVMQLVSGGELFDRIVEKGFYTEKDA--STLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL 168
Cdd:cd06637   81 dDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEwiAYICREILRGLSHLHQHKVIHRDIKGQNVLL---TENAEVKLVDFGV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 S-KMEGKGDVMSTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFD 241
Cdd:cd06637  158 SaQLDRTVGRRNTFIGTPYWMAPEVIAcdENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPAPRLK 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 242 SPYWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06637  238 SKKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
14-278 8.71e-25

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: 103.11  E-value: 8.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  14 KQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPK---KALKGKESSieNEIAVLRKIKHENIVALEDIYES 90
Cdd:cd07880    8 KTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqSELFAKRAY--RELRLLKHMKHENVIGLLDVFTP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHL------YLVMQLVsgGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyySQDEESKIMIS 164
Cdd:cd07880   86 DLSLdrfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL---AVNEDCELKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKM---EGKGDVMstacgTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEyef 240
Cdd:cd07880  161 DFGLARQtdsEMTGYVV-----TRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVT--- 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 241 DSPYWDDI----SDSAKDFIR----------------------NLMEK----DPNKRYTCEQAARHPW 278
Cdd:cd07880  233 GTPSKEFVqklqSEDAKNYVKklprfrkkdfrsllpnanplavNVLEKmlvlDAESRITAAEALAHPY 300
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
25-267 1.09e-24

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: 101.31  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKatGKLFAVKCI-PKKALKGKESSIENEIAVLRkIKHENIV---ALEDIYESPNHLYLVMQL 100
Cdd:cd13979    7 LQEPLGSGGFGSVYKATYK--GETVAVKIVrRRRKNRASRQSFWAELNAAR-LRHENIVrvlAAETGTDFASLGLIIMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIvekgfYTEKDASTLIRQVL------DAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSKMEGK 174
Cdd:cd13979   84 CGNGTLQQLI-----YEGSEPLPLAHRILisldiaRALRFCHSHGIVHLDVKPANILISEQG---VCKLCDFGCSVKLGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDV----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWDD-IS 249
Cdd:cd13979  156 GNEvgtpRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDSeFG 235
                        250
                 ....*....|....*...
gi 594150345 250 DSAKDFIRNLMEKDPNKR 267
Cdd:cd13979  236 QRLRSLISRCWSAQPAER 253
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
18-279 1.18e-24

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: 101.62  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKIKHENIVAL---EDIYESP--- 91
Cdd:cd06636   13 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKLEINMLKKYSHHRNIATyygAFIKKSPpgh 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 -NHLYLVMQLVSGGELFDRIVE-KGFYTEKDASTLI-RQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL 168
Cdd:cd06636   91 dDQLWLVMEFCGAGSVTDLVKNtKGNALKEDWIAYIcREILRGLAHLHAHKVIHRDIKGQNVLL---TENAEVKLVDFGV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 S-KMEGKGDVMSTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEFD 241
Cdd:cd06636  168 SaQLDRTVGRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPPPKLK 247
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 242 SPYWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06636  248 SKKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
23-278 1.56e-24

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: 101.35  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKESSIENEIAV-----LRKIKHENIVALEDIYESPNHLYLV 97
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIK----KFLESEDDKMVKKIAMreikmLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKimISDFGLSK-MEGKGD 176
Cdd:cd07846   79 FEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL-VSQSGVVK--LCDFGFARtLAAPGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA------------------- 236
Cdd:cd07846  156 VYTDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKClgnliprhqelfqknplfa 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 237 --------EYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07846  236 gvrlpevkEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
29-279 1.65e-24

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: 102.11  E-value: 1.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKgkessienEIAVLRKIKHENIVALEDIY------ESPNH 93
Cdd:cd07850    8 IGSGAQGIVCAAYDTVTGQNVAIKKLsrpfqnvthAKRAYR--------ELVLMKLVNHKNIIGLLNVFtpqkslEEFQD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMqlvsggELFDRIVEKGFYTEKD---ASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqDEESKIMisDFGLSK 170
Cdd:cd07850   80 VYLVM------ELMDANLCQVIQMDLDherMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS-DCTLKIL--DFGLAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF--YDEND--SKLFEQI------------- 233
Cdd:cd07850  151 TAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFpgTDHIDqwNKIIEQLgtpsdefmsrlqp 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 234 ----------LKAEYEFDSPYWDDI--SDS----------AKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07850  231 tvrnyvenrpKYAGYSFEELFPDVLfpPDSeehnklkasqARDLLSKMLVIDPEKRISVDDALQHPYI 298
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
29-227 1.67e-24

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: 100.26  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAeeKATGKLFAVKcipkKALKGKESSIENeiavLRKIKHENIVALEDI-YESPNHLyLVMQLVSGGELF 107
Cdd:cd14059    1 LGSGAQGAVFLG--KFRGEEVAVK----KVRDEKETDIKH----LRKLNHPNIIKFKGVcTQAPCYC-ILMEYCPYGQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSKMEGKGDVMSTACGTPGY 187
Cdd:cd14059   70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYND---VLKISDFGTSKELSEKSTKMSFAGTVAW 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS 227
Cdd:cd14059  147 MAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSS 186
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
29-233 2.00e-24

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: 100.61  E-value: 2.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPK-KALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG--- 104
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSsPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGslk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKdaSTLIRQVLDAVYYLHRM--GIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTAC 182
Cdd:cd13978   81 SLLEREIQDVPWSLR--FRIIHEIALGMNFLHNMdpPLLHHDLKPENILL---DNHFHVKISDFGLSKLGMKSISANRRR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 183 ------GTPGYVAPEVL--AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI 233
Cdd:cd13978  156 gtenlgGTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQI 214
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
17-282 2.18e-24

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: 101.65  E-value: 2.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESS-----IENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd06633   17 DDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIK---KMSYSGKQTNekwqdIIKEVKFLQQLKHPNTIEYKGCYLKD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQ--LVSGGELFDriVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS 169
Cdd:cd06633   94 HTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILL---TEPGQVKLADFGSA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDvmsTACGTPGYVAPEV---LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyefDSPYW- 245
Cdd:cd06633  169 SIASPAN---SFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQN----DSPTLq 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 246 -DDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGD 282
Cdd:cd06633  242 sNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVRRE 279
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
29-280 2.74e-24

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: 101.66  E-value: 2.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCI--PKKALKGKESSIEnEIAVLRKIKHENIVALEDIY------ESPNHLYLVMQL 100
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKKLsrPFQSLIHARRTYR-ELRLLKHMKHENVIGLLDVFtpatsiENFNEVYLVTNL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VsGGELfDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyySQDEESKIMISDFGLSKMegKGDVMST 180
Cdd:cd07878  102 M-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV---AVNEDCELRILDFGLARQ--ADDEMTG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF----YDENDSKLFE-------QILK------AEYEFDS 242
Cdd:cd07878  175 YVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFpgndYIDQLKRIMEvvgtpspEVLKkissehARKYIQS 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 243 -PYW--DDISDS-------AKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd07878  255 lPHMpqQDLKKIfrganplAIDLLEKMLVLDSDKRISASEALAHPYFS 302
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
23-278 2.90e-24

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: 100.90  E-value: 2.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKE------SSIEnEIAVLRKIKHENIVALEDIY--ESPNHL 94
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALK----KVRMDNErdgipiSSLR-EITLLLNLRHPNIVELKEVVvgKHLDSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSG--GELFDRIveKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKME 172
Cdd:cd07845   84 FLVMEYCEQdlASLLDNM--PTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC---LKIADFGLARTY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDV-MSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFE---QILKAEYEFDSPYWDD 247
Cdd:cd07845  159 GLPAKpMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDliiQLLGTPNESIWPGFSD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 248 -----------------------ISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07845  239 lplvgkftlpkqpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
14-278 3.78e-24

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: 100.91  E-value: 3.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  14 KQAEDIKKIfefketlGTGAFSEVVLAEEKATGKLFAVKCI---------PKKALKgkessienEIAVLRKIKHENIVAL 84
Cdd:cd07865   12 SKYEKLAKI-------GQGTFGEVFKARHRKTGQIVALKKVlmenekegfPITALR--------EIKILQLLKHENVVNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  85 EDIYESP--------NHLYLVMQLVS---GGELFDRIVEkgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYy 153
Cdd:cd07865   77 IEICRTKatpynrykGSIYLVFEFCEhdlAGLLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 154 sqDEESKIMISDFGLSK-----MEGKGDVMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIA---------------- 211
Cdd:cd07865  153 --TKDGVLKLADFGLARafslaKNSQPNRYTNRVVTLWYRPPELlLGERDYGPPIDMWGAGCIMaemwtrspimqgnteq 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 212 -----YILLCG------YP-----PFYDEndSKLFEQILKAEYEFDSPYWDDisDSAKDFIRNLMEKDPNKRYTCEQAAR 275
Cdd:cd07865  231 hqltlISQLCGsitpevWPgvdklELFKK--MELPQGQKRKVKERLKPYVKD--PYALDLIDKLLVLDPAKRIDADTALN 306

                 ...
gi 594150345 276 HPW 278
Cdd:cd07865  307 HDF 309
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
23-278 4.51e-24

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: 100.14  E-value: 4.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVK---------CIPKKALKgkessienEIAVLRKIKHENIVALEDIYESPNH 93
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKkfveseddpVIKKIALR--------EIRMLKQLKHPNLVNLIEVFRRKRK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVsggelfDRIVekgfYTEKDAST----------LIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMI 163
Cdd:cd07847   75 LHLVFEYC------DHTV----LNELEKNPrgvpehlikkIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQ---IKL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLSKMEGKGDVMSTAC-GTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND--------------- 226
Cdd:cd07847  142 CDFGFARILTGPGDDYTDYvATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDvdqlylirktlgdli 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 227 ---SKLFEQ----------------ILKAEYEfdspywdDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07847  222 prhQQIFSTnqffkglsipepetrePLESKFP-------NISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
21-279 4.56e-24

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: 99.45  E-value: 4.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESS-----IENEIAVLRKIKHENIVALEDIYESPNHLY 95
Cdd:cd06607    1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIK---KMSYSGKQSTekwqdIIKEVKFLRQLRHPNTIEYKGCYLREHTAW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQ--LVSGGELFDriVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEg 173
Cdd:cd06607   78 LVMEycLGSASDIVE--VHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILL---TEPGTVKLADFGSASLV- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 kgDVMSTACGTPGYVAPEV-LA--QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyefDSPYW--DDI 248
Cdd:cd06607  152 --CPANSFVGTPYWMAPEViLAmdEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQN----DSPTLssGEW 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 249 SDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06607  226 SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
17-279 6.43e-24

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: 100.12  E-value: 6.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESS-----IENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd06635   21 EDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIK---KMSYSGKQSNekwqdIIKEVKFLQRIKHPNSIEYKGCYLRE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQ--LVSGGELFDriVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS 169
Cdd:cd06635   98 HTAWLVMEycLGSASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILL---TEPGQVKLADFGSA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDvmsTACGTPGYVAPEV---LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEY-EFDSPYW 245
Cdd:cd06635  173 SIASPAN---SFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESpTLQSNEW 249
                        250       260       270
                 ....*....|....*....|....*....|....
gi 594150345 246 ddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06635  250 ---SDYFRNFVDSCLQKIPQDRPTSEELLKHMFV 280
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
24-282 1.34e-23

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 98.77  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd06622    4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELfDRIVEKGFYTEKDASTLIRQVLDAV-----YYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEGKgDVM 178
Cdd:cd06622   84 GSL-DKLYAGGVATEGIPEDVLRRITYAVvkglkFLKEEHNIIHRDVKPTNVLVNGNGQ---VKLCDFGVSGNLVA-SLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVL------AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQiLKAEYEFDSPYW-DDISDS 251
Cdd:cd06622  159 KTNIGCQSYMAPERIksggpnQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQ-LSAIVDGDPPTLpSGYSDD 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGD 282
Cdd:cd06622  238 AQDFVAKCLNKIPNRRPTYAQLLEHPWLVKY 268
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
15-291 1.70e-23

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 98.28  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  15 QAEDIKKIFEfketLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIY-ESPNH 93
Cdd:cd06620    3 KNQDLETLKD----LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlNENNN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELfDRIV-EKGFYTEKDASTLIRQV---LDAVYYLHRmgIVHRDLKPENLLYYSQDEeskIMISDFGLS 169
Cdd:cd06620   79 IIICMEYMDCGSL-DKILkKKGPFPEEVLGKIAVAVlegLTYLYNVHR--IIHRDIKPSNILVNSKGQ---IKLCDFGVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KmEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-----------LFEQILKaEY 238
Cdd:cd06620  153 G-ELINSIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDdgyngpmgildLLQRIVN-EP 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 239 EFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQ-AARHPWIAGDTALSKNIHE 291
Cdd:cd06620  231 PPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLlLDHDPFIQAVRASDVDLRA 284
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
18-279 1.99e-23

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: 98.16  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKIK-HENIVALEDIY-----ESP 91
Cdd:cd06638   15 DPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKIL--DPIHDIDEEIEAEYNILKALSdHPNVVKFYGMYykkdvKNG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFDRIveKGFYTEKD------ASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISD 165
Cdd:cd06638   93 DQLWLVLELCNGGSVTDLV--KGFLKRGErmeepiIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTT---EGGVKLVD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FGLS-KMEGKGDVMSTACGTPGYVAPEVLA-----QKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEY 238
Cdd:cd06638  168 FGVSaQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRaLFKIPRNPPP 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 239 EFDSP-YWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06638  248 TLHQPeLW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
27-268 4.59e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 100.25  E-value: 4.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIpkkalkgKESSIENEIAVLR---------KIKHENIVALEDIYESPNHLYLV 97
Cdd:NF033483  13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL-------RPDLARDPEFVARfrreaqsaaSLSHPNIVSVYDVGEDGGIPYIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMisDFGLSK------M 171
Cdd:NF033483  86 MEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKDGRVKVT--DFGIARalssttM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMstacGTPGYVAPEvlaQKPYSKA---VDCWSIGVIAYILLCGYPPFydENDS------KLFEQILKAEYEFDs 242
Cdd:NF033483 163 TQTNSVL----GTVHYLSPE---QARGGTVdarSDIYSLGIVLYEMLTGRPPF--DGDSpvsvayKHVQEDPPPPSELN- 232
                        250       260
                 ....*....|....*....|....*.
gi 594150345 243 pywDDISDSAKDFIRNLMEKDPNKRY 268
Cdd:NF033483 233 ---PGIPQSLDAVVLKATAKDPDDRY 255
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
69-278 4.65e-23

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: 101.07  E-value: 4.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345    69 EIAVLRKIKHENIVALEDIYES-PNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKP 147
Cdd:TIGR03903   28 ETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   148 ENLLYYSQDEESKIMISDFGLSKM-EGKGDVMSTAC-------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP 219
Cdd:TIGR03903  108 QNIMVSQTGVRPHAKVLDFGIGTLlPGVRDADVATLtrttevlGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQR 187
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345   220 PFYDENDSKLFEQILKAEyEFDSPYWDDiSDSAKDFIRNLMEKDPNKRytcEQAARHPW 278
Cdd:TIGR03903  188 VVQGASVAEILYQQLSPV-DVSLPPWIA-GHPLGQVLRKALNKDPRQR---AASAPALA 241
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
40-279 5.04e-23

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: 96.10  E-value: 5.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  40 AEEKATGKLFAVKCIPKKalkgkeSSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQlVSGGELFDRIVEKGFYTEK 119
Cdd:cd14024   12 AEHYQTEKEYTCKVLSLR------SYQECLAPYDRLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 120 DASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdEESKIMISDFGLS-KMEGKGDVMSTACGTPGYVAPEVL-AQKP 197
Cdd:cd14024   85 EARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDE-LRTKLVLVNLEDScPLNGDDDSLTDKHGCPAYVGPEILsSRRS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 198 YS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEFdsPYWddISDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14024  164 YSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSL--PAW--LSPGARCLVSCMLRRSPAERLKASEILLH 239

                 ...
gi 594150345 277 PWI 279
Cdd:cd14024  240 PWL 242
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
29-278 6.73e-23

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: 97.00  E-value: 6.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSgGELFD 108
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD-SDLKQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG-KGDVMSTACGTPG 186
Cdd:cd07871   92 YLDNCGnLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLI---NEKGELKLADFGLARAKSvPTKTYSNEVVTLW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 187 YVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF-----------------------------YDENDSKLFEQILKA 236
Cdd:cd07871  169 YRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFpgstvkeelhlifrllgtpteetwpgvtsNEEFRSYLFPQYRAQ 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 594150345 237 EYEFDSPYWDdiSDSAkDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07871  249 PLINHAPRLD--TDGI-DLLSSLLLYETKSRISAEAALRHSY 287
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
27-278 8.68e-23

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: 96.61  E-value: 8.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMqlvsggEL 106
Cdd:cd07873    8 DKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVF------EY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKgfYTEkDASTLIR---------QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG-KGD 176
Cdd:cd07873   82 LDKDLKQ--YLD-DCGNSINmhnvklflfQLLRGLAYCHRRKVLHRDLKPQNLLI---NERGELKLADFGLARAKSiPTK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF----YDENDSKLFE-----------QILKAE--- 237
Cdd:cd07873  156 TYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFpgstVEEQLHFIFRilgtpteetwpGILSNEefk 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 594150345 238 -YEFDSPYWDDISDSAK-------DFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07873  236 sYNYPKYRADALHNHAPrldsdgaDLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
32-276 1.06e-22

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: 95.46  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneiavlRKIKHENIVALED--IYESPNHLYlvMQLVSGGELFDR 109
Cdd:cd13995   15 GAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQ------ACFRHENIAELYGalLWEETVHLF--MEAGEGGSVLEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 110 IVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeeSKIMISDFGLSkMEGKGDVM--STACGTPGY 187
Cdd:cd13995   87 LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMS----TKAVLVDFGLS-VQMTEDVYvpKDLRGTEIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 188 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEfDSPYWDDISDSAKDFIRNL----MEKD 263
Cdd:cd13995  162 MSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHK-QAPPLEDIAQDCSPAMRELleaaLERN 240
                        250
                 ....*....|...
gi 594150345 264 PNKRYTCEQAARH 276
Cdd:cd13995  241 PNHRSSAAELLKH 253
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
29-279 1.13e-22

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: 96.88  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIEnEIAVLRKIKH--------ENIVALEDIYE--SPN--HLYL 96
Cdd:cd14136   18 LGWGHFSTVWLCWDLQNKRFVALK-VVKSAQHYTEAALD-EIKLLKCVREadpkdpgrEHVVQLLDDFKhtGPNgtHVCM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQlVSGGELFDRIvEKGFYTE---KDASTLIRQVLDAVYYLHRM-GIVHRDLKPENLLYYSQDEESKimISDFGlskme 172
Cdd:cd14136   96 VFE-VLGPNLLKLI-KRYNYRGiplPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIEVK--IADLG----- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 gkgdvmsTAC----------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF-------YDEND--------- 226
Cdd:cd14136  167 -------NACwtdkhftediQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphsgedYSRDEdhlaliiel 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 227 ----------------------------SKL----FEQILKAEYEFDSPYWDDISdsakDFIRNLMEKDPNKRYTCEQAA 274
Cdd:cd14136  240 lgriprsiilsgkysreffnrkgelrhiSKLkpwpLEDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEKRATAAQCL 315

                 ....*
gi 594150345 275 RHPWI 279
Cdd:cd14136  316 QHPWL 320
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
29-279 1.29e-22

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: 96.28  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIEN-------EIAVLRKIKHENIVALEDIYESPNHLY-LVMQL 100
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKG--- 175
Cdd:cd14040   93 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDsyg 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 ----DVMSTACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVIAYILLCGYPPF-YDENDSKLFEQ--ILKAEyEFDSPY 244
Cdd:cd14040  173 vdgmDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAT-EVQFPV 251
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594150345 245 WDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14040  252 KPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
29-216 1.40e-22

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: 95.25  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG---E 105
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMK---ELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGtleE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKdaSTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKM-------EGKGDVM 178
Cdd:cd14065   78 LLKSMDEQLPWSQR--VSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREmpdektkKPDRKKR 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 594150345 179 STACGTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 216
Cdd:cd14065  156 LTVVGSPYWMAPEMLRGESYDEKVDVFSFG----IVLC 189
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
29-279 2.23e-22

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: 95.41  E-value: 2.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIK---HENIVALEDIYESPN-----HLYLVMQ 99
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVRvQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCATSRtdretKVTLVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGG--ELFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKMEGKGDV 177
Cdd:cd07863   88 HVDQDlrTYLDKVPPPGLPAET-IKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKLADFGLARIYSCQMA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS----KLFEQI-LKAEYEFD----------S 242
Cdd:cd07863  164 LTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEAdqlgKIFDLIgLPPEDDWPrdvtlprgafS 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 594150345 243 P--------YWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07863  244 PrgprpvqsVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-276 3.42e-22

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: 94.48  E-value: 3.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkkALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH--------- 93
Cdd:cd14047    8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIK-----RVKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFDYdpetsssns 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 -------LYLVMQLVSGGELFDRIVEKGfYTEKD---ASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMI 163
Cdd:cd14047   83 srsktkcLFIQMEFCEKGTLESWIEKRN-GEKLDkvlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFL---VDTGKVKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGL-SKMEGKGDvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND--SKLFEQILkaeyef 240
Cdd:cd14047  159 GDFGLvTSLKNDGK-RTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKfwTDLRNGIL------ 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 594150345 241 dSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14047  232 -PDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
29-295 3.52e-22

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: 95.13  E-value: 3.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIEN-------EIAVLRKIKHENIVALEDIYE-SPNHLYLVMQL 100
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVK-IHQLNKNWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDSFCTVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH--RMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKME-----G 173
Cdd:cd14041   93 CEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMdddsyN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVM---STACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVIAYILLCGYPPF-YDENDSKLFEQ--ILKAEyEFDSP 243
Cdd:cd14041  173 SVDGMeltSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQEntILKAT-EVQFP 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 244 YWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWiagdtaLSKNIHESVSA 295
Cdd:cd14041  252 PKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPY------LLPHIRKSVST 297
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
29-278 3.63e-22

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: 95.74  E-value: 3.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVK--CIP-------KKALKgkessienEIAVLRKIKHENIVALEDIYESP------NH 93
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKVAIKklSRPfqseifaKRAYR--------ELTLLKHMQHENVIGLLDVFTSAvsgdefQD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVM-------QLVSGGELfdrivekgfyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKIMisDF 166
Cdd:cd07879   95 FYLVMpymqtdlQKIMGHPL----------SEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLA-VNEDCELKIL--DF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSK---MEGKGDVMstacgTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKA------ 236
Cdd:cd07879  162 GLARhadAEMTGYVV-----TRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVtgvpgp 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150345 237 ----------------------EYEFdSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07879  237 efvqkledkaaksyikslpkypRKDF-STLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
12-279 4.18e-22

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: 94.87  E-value: 4.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIkkiFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIY-- 88
Cdd:cd07864    1 WGKRCVDK---FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKeGFPITAIREIKILRQLNHRSVVNLKEIVtd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 --------ESPNHLYLVMQLVSG---GELFDRIVEkgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDE 157
Cdd:cd07864   78 kqdaldfkKDKGAFYLVFEYMDHdlmGLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL---NN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKMEGKGD--VMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYIL-------------------- 214
Cdd:cd07864  152 KGQIKLADFGLARLYNSEEsrPYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELftkkpifqanqelaqlelis 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 215 -LCGYP-----P-------FYDENDSKLFEQILKAEYEFdspywddISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07864  232 rLCGSPcpavwPdviklpyFNTMKPKKQYRRRLREEFSF-------IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
29-221 4.96e-22

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: 93.95  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKatGKLFAVKCI---PKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14146    2 IGVGGFGKVYRATWK--GQEVAVKAArqdPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIR---------QVLDAVYYLHRMGIV---HRDLKPENLLYYSQDEESKI-----MISDFGL 168
Cdd:cd14146   80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEHDDIcnktlKITDFGL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 169 SKMEGKGDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14146  160 AREWHRTTKMSAA-GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
24-215 5.61e-22

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: 94.11  E-value: 5.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKET--LGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH--LYLVM 98
Cdd:cd14049    7 EFEEIarLGKGGYGKVYKVRNKLDGQYYAIKKILiKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQlmLYIQM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGgELFDRIVEKG----FYTEKDA----------STLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEEskIMIS 164
Cdd:cd14049   87 QLCEL-SLWDWIVERNkrpcEEEFKSApytpvdvdvtTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH--VRIG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150345 165 DFGLS------------KMEGKGDVMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd14049  164 DFGLAcpdilqdgndstTMSRLNGLTHTSgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
36-269 6.56e-22

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: 93.19  E-value: 6.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  36 EVVLAEEKATGKlFAVKCIPKKALKGKE--SSIENEIAVLRKIKHENIVALED------IYESPNHLYLVMQLVSGGELF 107
Cdd:cd14012   14 EVVLDNSKKPGK-FLTSQEYFKTSNGKKqiQLLEKELESLKKLRHPNLVSYLAfsierrGRSDGWKVYLLTEYAPGGSLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSK------MEGKGDVMSTA 181
Cdd:cd14012   93 ELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKtlldmcSRGSLDEFKQT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CgtpgYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFydendsklfeqiLKAEYEFDSPYWDDISDSAKDFIRNLM 260
Cdd:cd14012  173 Y----WLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLDVL------------EKYTSPNPVLVSLDLSASLQDFLSKCL 236

                 ....*....
gi 594150345 261 EKDPNKRYT 269
Cdd:cd14012  237 SLDPKKRPT 245
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
23-221 6.68e-22

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 93.56  E-value: 6.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKatGKLFAVKCI---PKKALKGKESSIENEIAVLRKIKHENIVALEDI-YESPNhLYLVM 98
Cdd:cd14147    5 LRLEEVIGIGGFGKVYRGSWR--GELVAVKAArqdPDEDISVTAESVRQEARLFAMLAHPNIIALKAVcLEEPN-LCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGFYTEKDASTLIrQVLDAVYYLHRMGIV---HRDLKPENLLYY----SQDEESKIM-ISDFGLSK 170
Cdd:cd14147   82 EYAAGGPLSRALAGRRVPPHVLVNWAV-QIARGMHYLHCEALVpviHRDLKSNNILLLqpieNDDMEHKTLkITDFGLAR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 171 MEGKGDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14147  161 EWHKTTQMSAA-GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
27-278 1.45e-21

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: 92.88  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMqlvsggE 105
Cdd:cd07839    6 EKIGEGTYGTVFKAKNRETHEIVALKRVRlDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVF------E 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYT---EKDAST---LIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEG-KGDVM 178
Cdd:cd07839   80 YCDQDLKKYFDScngDIDPEIvksFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE---LKLADFGLARAFGiPVRCY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTPGYVAPEVL-AQKPYSKAVDCWSIGVI-AYILLCGYP--PFYDENDS-KLFEQILKA-------------EYEF 240
Cdd:cd07839  157 SAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIfAELANAGRPlfPGNDVDDQlKRIFRLLGTpteeswpgvsklpDYKP 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 241 DSPY-----WDDI----SDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07839  237 YPMYpattsLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
29-279 2.10e-21

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: 94.04  E-value: 2.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIP---------KKALKgkessienEIAVLRKIKHENIVALEDIYESPN-----HL 94
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKRVALKKMPnvfqnlvscKRVFR--------ELKMLCFFKHDNVLSALDILQPPHidpfeEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGK 174
Cdd:cd07853   80 YVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS---NCVLKICDFGLARVEEP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GD--VMSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVI-AYIL--------------------LCGYPPFYDEND--SK 228
Cdd:cd07853  156 DEskHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIfAELLgrrilfqaqspiqqldlitdLLGTPSLEAMRSacEG 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 229 LFEQILKAEYE---FDSPYW--DDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd07853  236 ARAHILRGPHKppsLPVLYTlsSQATHEAVHLLCRMLVFDPDKRISAADALAHPYL 291
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
12-272 2.29e-21

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: 91.97  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIKkifeFKETLGTGAFSEVVLAEEKatGKLFAVKCIPKKAlkgKESSIENEIAVLRKIKHENIVALED-IYES 90
Cdd:cd05082    1 WALNMKELK----LLQTIGKGEFGDVMLGDYR--GNKVAVKCIKNDA---TAQAFLAEASVMTQLRHSNLVQLLGvIVEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSGGELFDRIVEKGfYTEKDASTLIRQVLD---AVYYLHRMGIVHRDLKPENLLYySQDEESKImiSDFG 167
Cdd:cd05082   72 KGGLYIVTEYMAKGSLVDYLRSRG-RSVLGGDCLLKFSLDvceAMEYLEGNNFVHRDLAARNVLV-SEDNVAKV--SDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKMEGKgdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFydeNDSKLFEQILKAE--YEFDSPy 244
Cdd:cd05082  148 LTKEASS--TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWeIYSFGRVPY---PRIPLKDVVPRVEkgYKMDAP- 221
                        250       260
                 ....*....|....*....|....*...
gi 594150345 245 wDDISDSAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd05082  222 -DGCPPAVYDVMKNCWHLDAAMRPSFLQ 248
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
29-272 2.34e-21

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: 92.29  E-value: 2.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKatGKLFAVKCIPKKALKGKE--------------------SSIENEIAVLRKIKHENIVALEDIY 88
Cdd:cd14000    2 LGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFAnvpadtmlrhlratdamknfRLLRQELTVLSHLHHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPnhLYLVMQLVSGGELfDRIVEKgfYTEKDAS-------TLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKI 161
Cdd:cd14000   80 IHP--LMLVLELAPLGSL-DHLLQQ--DSRSFASlgrtlqqRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 162 M--ISDFGLSKMEGKGDVMsTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYD----ENDSKLFEQIL 234
Cdd:cd14000  155 IikIADYGISRQCCRMGAK-GSEGTPGFRAPEIArGNVIYNEKVDVFSFGMLLYEILSGGAPMVGhlkfPNEFDIHGGLR 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 235 KAEYEFDSPYWDDIsdsaKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd14000  234 PPLKQYECAPWPEV----EVLMKKCWKENPQQRPTAVT 267
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
17-279 2.65e-21

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: 92.78  E-value: 2.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESS-----IENEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd06634   11 DDPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIK---KMSYSGKQSNekwqdIIKEVKFLQKLRHPNTIEYRGCYLRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQ--LVSGGELFDriVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFgls 169
Cdd:cd06634   88 HTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILL---TEPGLVKLGDF--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 kmeGKGDVMSTA---CGTPGYVAPEV---LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYE-FDS 242
Cdd:cd06634  160 ---GSASIMAPAnsfVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPaLQS 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 594150345 243 PYWddiSDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06634  237 GHW---SEYFRNFVDSCLQKIPQDRPTSDVLLKHRFL 270
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
23-279 2.76e-21

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 93.66  E-value: 2.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKalKGKESSIENEIAVLRKIKHE------NIVALEDIYESPNHLYL 96
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNE--KRFHRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHICM 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGG--ELFDRIVEKGF---YTEKDASTLIrQVLDAvyyLHRMGIVHRDLKPENLLYySQDEESKIMISDFGLSKM 171
Cdd:cd14224  145 TFELLSMNlyELIKKNKFQGFslqLVRKFAHSIL-QCLDA---LHRNKIIHCDLKPENILL-KQQGRSGIKVIDFGSSCY 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP--PFYDEND-------------SKLFEQILKA 236
Cdd:cd14224  220 EHQR--IYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPlfPGEDEGDqlacmiellgmppQKLLETSKRA 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 237 EYEFDS--------------------------------PYWDDISDSAK--------DFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14224  298 KNFISSkgypryctvttlpdgsvvlnggrsrrgkmrgpPGSKDWVTALKgcddplflDFLKRCLEWDPAARMTPSQALRH 377

                 ...
gi 594150345 277 PWI 279
Cdd:cd14224  378 PWL 380
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
27-235 3.07e-21

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: 92.33  E-value: 3.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEG-KGDVMSTACGTP 185
Cdd:cd07870   86 QYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE---LKLADFGLARAKSiPSQTYSSEVVTL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 186 GYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFydENDSKLFEQILK 235
Cdd:cd07870  163 WYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAF--PGVSDVFEQLEK 211
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
18-279 3.42e-21

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 92.36  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNH--- 93
Cdd:cd06639   19 DPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKIL--DPISDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQyvg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 --LYLVMQLVSGG---ELFDRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFG 167
Cdd:cd06639   97 gqLWLVLELCNGGsvtELVKGLLKCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---EGGVKLVDFG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LS-KMEGKGDVMSTACGTPGYVAPEVLA---QKPYSKAVDC--WSIGVIAYILLCGYPPFYDENDSK-LFEQILKAEYEF 240
Cdd:cd06639  174 VSaQLTSARLRRNTSVGTPFWMAPEVIAceqQYDYSYDARCdvWSLGITAIELADGDPPLFDMHPVKaLFKIPRNPPPTL 253
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 594150345 241 DSPywDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06639  254 LNP--EKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-267 3.42e-21

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: 91.63  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAE---EKATGKLFAVKCIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATcllDRKPVALKKVQIFEMMDAKARQDCVK-EIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIV----EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKM-EGK 174
Cdd:cd08228   83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV---VKLGDLGLGRFfSSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE--NDSKLFEQILKAEYefdSPY-WDDISDS 251
Cdd:cd08228  160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLFSLCQKIEQCDY---PPLpTEHYSEK 236
                        250
                 ....*....|....*.
gi 594150345 252 AKDFIRNLMEKDPNKR 267
Cdd:cd08228  237 LRELVSMCIYPDPDQR 252
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
29-227 4.02e-21

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: 91.20  E-value: 4.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVV----LAEEKATGklfAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd14148    2 IGVGGFGKVYkglwRGEEVAVK---AARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKgfytEKDASTLIR---QVLDAVYYLHR---MGIVHRDLKPENLLYYSQDEESKIM-----ISDFGLSKMEG 173
Cdd:cd14148   79 ALNRALAGK----KVPPHVLVNwavQIARGMNYLHNeaiVPIIHRDLKSSNILILEPIENDDLSgktlkITDFGLAREWH 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 174 KGDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPfYDENDS 227
Cdd:cd14148  155 KTTKMSAA-GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVP-YREIDA 206
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
12-275 5.70e-21

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: 90.87  E-value: 5.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIKkifeFKETLGTGAFSEVVLAEEKatGKLFAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESP 91
Cdd:cd05039    1 WAINKKDLK----LGELIGKGEFGDVMLGDYR--GQKVAVKCL-KDDSTAAQAFLA-EASVMTTLRHPNLVQLLGVVLEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVSGGELFD--RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKimISDFGLS 169
Cdd:cd05039   73 NGLYIVTEYMAKGSLVDylRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVL-VSEDNVAK--VSDFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KME------GKGDVMSTacgtpgyvAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDS 242
Cdd:cd05039  150 KEAssnqdgGKLPIKWT--------APEALREKKFSTKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPHVEKG-YRMEA 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 594150345 243 PywddisDSAKDFIRNLM----EKDPNKRYTCEQAAR 275
Cdd:cd05039  221 P------EGCPPEVYKVMkncwELDPAKRPTFKQLRE 251
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
21-279 5.73e-21

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: 92.78  E-value: 5.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFAVK--CIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIY------ESPN 92
Cdd:cd07876   21 KRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKklSRPFQNQTHAKRAYR-ELVLLKCVNHKNIISLLNVFtpqkslEEFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGGelFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKME 172
Cdd:cd07876  100 DVYLVMELMDAN--LCQVIHMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGLARTA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY--DEND--SKLFEQILKAEYEFDS------ 242
Cdd:cd07876  174 CTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQgtDHIDqwNKVIEQLGTPSAEFMNrlqptv 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594150345 243 -------------------PYWDDISDSAKDFI-----RNLMEK----DPNKRYTCEQAARHPWI 279
Cdd:cd07876  254 rnyvenrpqypgisfeelfPDWIFPSESERDKLktsqaRDLLSKmlviDPDKRISVDEALRHPYI 318
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
23-215 6.27e-21

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: 91.09  E-value: 6.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIpkkALKGKESSIEN---EIAVLRKIKHENIVALEDIY-ESPN------ 92
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRI---RLPNNELAREKvlrEVRALAKLDHPGIVRYFNAWlERPPegwqek 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 ----HLYLVMQLVSGGELFDRIVEKGFYTEKDAST---LIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDEESKimISD 165
Cdd:cd14048   85 mdevYLYIQMQLCRKENLKDWMNRRCTMESRELFVclnIFKQIASAVEYLHSKGLIHRDLKPSNVF-FSLDDVVK--VGD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594150345 166 FGLSKMEGKGDVMSTA-------------CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd14048  162 FGLVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
23-278 6.95e-21

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: 91.25  E-value: 6.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEE-KATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIK---HENIVALEDI-----YESPN 92
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRvQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVctvsrTDRET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 HLYLVMQLVSGG--ELFDRIVEKGFYTE--KDastLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGL 168
Cdd:cd07862   83 KLTLVFEHVDQDltTYLDKVPEPGVPTEtiKD---MMFQLLRGLDFLHSHRVVHRDLKPQNILVTSS---GQIKLADFGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 169 SKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND----SKLFEQILKAEYEfDSP- 243
Cdd:cd07862  157 ARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDvdqlGKILDVIGLPGEE-DWPr 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 244 -------------------YWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07862  236 dvalprqafhsksaqpiekFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
24-230 8.38e-21

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: 90.49  E-value: 8.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAE---EKATgKLFAVKCIPKKALKgkesSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd14063    3 EIKEVIGKGRFGRVHRGRwhgDVAI-KLLNIDYLNEEQLE----AFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqdEESKIMISDFGLSKMEG------ 173
Cdd:cd14063   78 CKGRTLYSLIHErKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL----ENGRVVITDFGLFSLSGllqpgr 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 174 KGDVMSTACGTPGYVAPEVL----------AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN-DSKLF 230
Cdd:cd14063  154 REDTLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPaESIIW 221
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
29-215 1.86e-20

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: 90.13  E-value: 1.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLA----EEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP--NHLYLVMQLVS 102
Cdd:cd05038   12 LGEGHFGSVELCrydpLGDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIMEYLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELfdRIVEKGFYTEKDASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGDV 177
Cdd:cd05038   92 SGSL--RDYLQRHRDQIDLKRLLLfasQICKGMEYLGSQRYIHRDLAARNILV---ESEDLVKISDFGLAKVlpEDKEYY 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 594150345 178 MSTacgTPG-----YVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05038  167 YVK---EPGespifWYAPECLRESRFSSASDVWSFGVTLYELF 206
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
27-221 3.23e-20

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: 89.67  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMqlvsggEL 106
Cdd:cd07872   12 EKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVF------EY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEK------GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEG-KGDVMS 179
Cdd:cd07872   86 LDKDLKQymddcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLI---NERGELKLADFGLARAKSvPTKTYS 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 594150345 180 TACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd07872  163 NEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLF 205
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
25-221 3.30e-20

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 88.95  E-value: 3.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLA----EEKATGklfAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDI-YESPNhLYLVMQ 99
Cdd:cd14145   10 LEEIIGIGGFGKVYRAiwigDEVAVK---AARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVcLKEPN-LCLVME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELfDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIV---HRDLKPENLLYYSQ----DEESKIM-ISDFGLSKM 171
Cdd:cd14145   86 FARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKvengDLSNKILkITDFGLARE 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14145  165 WHRTTKMSAA-GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
24-279 4.28e-20

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: 88.78  E-value: 4.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd06619    4 QYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GEL--FDRIVEKGFytekdaSTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKmEGKGDVMSTA 181
Cdd:cd06619   84 GSLdvYRKIPEHVL------GRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTR---GQVKLCDFGVST-QLVNSIAKTY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 182 CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG---YPPFYDENDSKLFEQILKAEYEFDSPYWDD--ISDSAKDFI 256
Cdd:cd06619  154 VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGrfpYPQIQKNQGSLMPLQLLQCIVDEDPPVLPVgqFSEKFVHFI 233
                        250       260
                 ....*....|....*....|...
gi 594150345 257 RNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06619  234 TQCMRKQPKERPAPENLMDHPFI 256
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
27-268 4.96e-20

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: 88.27  E-value: 4.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVK-C-------IPKKALKGKEssieneiaVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKtCretlppdLKRKFLQEAR--------ILKQYDHPNIVKLIGVCVQKQPIMIVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGfyTEKDASTLIRQVLDA---VYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKG 175
Cdd:cd05041   73 ELVPGGSLLTFLRKKG--ARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLV---GENNVLKISDFGMSREEEDG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 dVMSTACGT---P-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQIlkaeyefDSPYWDDISD 250
Cdd:cd05041  148 -EYTVSDGLkqiPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQTREQI-------ESGYRMPAPE 219
                        250       260
                 ....*....|....*....|..
gi 594150345 251 SAKDFIRNLMEK----DPNKRY 268
Cdd:cd05041  220 LCPEAVYRLMLQcwayDPENRP 241
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
29-167 7.41e-20

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: 84.42  E-value: 7.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGKESSIENEIAVLRKIK-HE-NIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVK-IGDDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 107 FDRIVEkGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd13968   80 IAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL---SEDGNVKLIDFG 136
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
23-278 1.07e-19

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 87.95  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMqlv 101
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRlEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 sggELFDRIVEKGFYTEKDAS-------TLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKimISDFGLSKMEG- 173
Cdd:PLN00009  81 ---EYLDLDLKKHMDSSPDFAknprlikTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALK--LADFGLARAFGi 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLFE--QILKAEYE---------- 239
Cdd:PLN00009 156 PVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPgDSEIDELFKifRILGTPNEetwpgvtslp 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 240 -FDS--PYWD---------DISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:PLN00009 236 dYKSafPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
23-194 2.28e-19

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: 86.54  E-value: 2.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKgkeSSIENEIAVLRKIKHENIVA-LEDIYESPNHLYLVMQLV 101
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPK---QVLKMEVAVLKKLQGKPHFCrLIGCGRTERYNYIVMTLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 sGGELFD--RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL--YYSQDEEsKIMISDFGLSK--MEGKG 175
Cdd:cd14017   79 -GPNLAElrRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAigRGPSDER-TVYILDFGLARqyTNKDG 156
                        170
                 ....*....|....*....
gi 594150345 176 DVMSTACGTPGYVAPEVLA 194
Cdd:cd14017  157 EVERPPRNAAGFRGTVRYA 175
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
22-280 2.63e-19

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: 86.91  E-value: 2.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKETLGTGAFSEV-----VLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIK-HENIVALEDIYES----- 90
Cdd:cd14020    1 LWEVQSRLGQGSSASVyrvssGRGADQPTSALKEFQLDHQGSQESGDYGFAKERAALEQLQgHRNIVTLYGVFTNhysan 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 -PNHLYLVMQL-VSGGELFDRIVEKGFytekdASTLI----RQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMis 164
Cdd:cd14020   81 vPSRCLLLELLdVSVSELLLRSSNQGC-----SMWMIqhcaRDVLEALAFLHHEGYVHADLKPRNILWSAEDECFKLI-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMEGKGDVMSTAcgTPGYVAPEV-----LAQKPY------SKAVDCWSIGVIAYILLCGYppfydendsKLFEQI 233
Cdd:cd14020  154 DFGLSFKEGNQDVKYIQ--TDGYRAPEAelqncLAQAGLqsetecTSAVDLWSLGIVLLEMFSGM---------KLKHTV 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 234 LKAEYEFDSPYWDD-------ISDSA------KDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd14020  223 RSQEWKDNSSAIIDhifasnaVVNPAipayhlRDLIKSMLHNDPGKRATAEAALCSPFFS 282
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
29-224 2.67e-19

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: 86.16  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKatGKLFAVKCIPKKAlkgKESSIENEIAVLRKIKHENIVALEDIYESPNhlYLVMQLVSGGELfD 108
Cdd:cd14068    2 LGDGGFGSVYRAVYR--GEDVAVKIFNKHT---SFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL-D 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIV--EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIM--ISDFGLSKMEGKGDVmSTACGT 184
Cdd:cd14068   74 ALLqqDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIakIADYGIAQYCCRMGI-KTSEGT 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVL-AQKPYSKAVDCWSIGVIAY-ILLCG--------YPPFYDE 224
Cdd:cd14068  153 PGFRAPEVArGNVIYNQQADVYSFGLLLYdILTCGeriveglkFPNEFDE 202
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
4-279 2.96e-19

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: 87.79  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   4 ENGESSSSWKKQAEDIKKIFEFKETLGTGAFsEVVLAEEKATGKL---FAVKCIPKKALKgkessienEIAVLRKIKHEN 80
Cdd:cd07875   14 EIGDSTFTVLKRYQNLKPIGSGAQGIVCAAY-DAILERNVAIKKLsrpFQNQTHAKRAYR--------ELVLMKCVNHKN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  81 IVALEDIY------ESPNHLYLVMQLVSGGelFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYS 154
Cdd:cd07875   85 IIGLLNVFtpqkslEEFQDVYIVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 155 qdeESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF----YDENDSKLF 230
Cdd:cd07875  162 ---DCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFpgtdHIDQWNKVI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 231 EQI-------LK----------------AEYEFDSPYWDDI-----------SDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd07875  239 EQLgtpcpefMKklqptvrtyvenrpkyAGYSFEKLFPDVLfpadsehnklkASQARDLLSKMLVIDASKRISVDEALQH 318

                 ...
gi 594150345 277 PWI 279
Cdd:cd07875  319 PYI 321
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
23-221 3.52e-19

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: 86.67  E-value: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd07869    7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVH 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GG--ELFDRivEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEG-KGDVMS 179
Cdd:cd07869   87 TDlcQYMDK--HPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE---LKLADFGLARAKSvPSHTYS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 594150345 180 TACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd07869  162 NEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
23-238 3.64e-19

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: 87.45  E-value: 3.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIKHE-----NIVALEDIYESPNHLYLV 97
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIE--VSILARLSTEsaddyNFVRAYECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGgELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSKMEGK 174
Cdd:cd14227   95 FEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPyRVKVIDFGSASHVSK 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 175 GdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF-----YDENDSKLFEQILKAEY 238
Cdd:cd14227  174 A-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYpgaseYDQIRYISQTQGLPAEY 241
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
23-277 3.99e-19

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 86.44  E-value: 3.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKlfavKCIpKKALKG-KESSIENEIAVLRKIK-HENIVALEDI--YESPNHLYLVM 98
Cdd:cd14132   20 YEIIRKIGRGKYSEVFEGINIGNNE----KVV-IKVLKPvKKKKIKREIKILQNLRgGPNIVKLLDVvkDPQSKTPSLIF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGgELFDRIVEKgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEE-SKIMISDFGLSKMEGKGDV 177
Cdd:cd14132   95 EYVNN-TDFKTLYPT--LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI---DHEkRKLRLIDWGLAEFYHPGQE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVLAQKP-YSKAVDCWSIGVIAYILLCGYPPFYDENDSklFEQILKA----------EY-------- 238
Cdd:cd14132  169 YNVRVASRYYKGPELLVDYQyYDYSLDMWSLGCMLASMIFRKEPFFHGHDN--YDQLVKIakvlgtddlyAYldkygiel 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 239 --EFDS--------PYWDDISDS--------AKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14132  247 ppRLNDilgrhskkPWERFVNSEnqhlvtpeALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
23-219 4.76e-19

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: 86.62  E-value: 4.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIKHEN-----IVALEDIYESPNHLYLV 97
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIE--VGILARLSNENadefnFVRAYECFQHRNHTCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGgELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSKMEGK 174
Cdd:cd14229   80 FEMLEQ-NLYDFLKQNKFspLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSK 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 594150345 175 GdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP 219
Cdd:cd14229  159 T-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 202
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
23-219 5.47e-19

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: 86.73  E-value: 5.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCI---PKKALKGKessieNEIAVLRKIKHE-----NIVALEDIYESPNHL 94
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILknhPSYARQGQ-----IEVSILSRLSQEnadefNFVRAYECFQHKNHT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGgELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSKM 171
Cdd:cd14211   76 CLVFEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASH 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 172 EGKGdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYP 219
Cdd:cd14211  155 VSKA-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 201
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
29-216 5.93e-19

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: 85.26  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKAlkgKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV---DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGK-----GDVMSTAC 182
Cdd:cd14156   78 LLAREELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGEmpandPERKLSLV 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 216
Cdd:cd14156  158 GSAFWMAPEMLRGEPYDRKVDVFSFG----IVLC 187
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
23-278 5.99e-19

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 86.44  E-value: 5.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVV-LAEEKATGKLFAVKCIpKKALKGKESSiENEIAVLRKIKHEN------IVALEDIYESPNHLY 95
Cdd:cd14213   14 YEIVDTLGEGAFGKVVeCIDHKMGGMHVAVKIV-KNVDRYREAA-RSEIQVLEHLNTTDpnstfrCVQMLEWFDHHGHVC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQD----------------E 157
Cdd:cd14213   92 IVFELL-GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmkrdertlK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKMEgkGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSK----LFEQI 233
Cdd:cd14213  171 NPDIKVVDFGSATYD--DEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF-QTHDSKehlaMMERI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 234 L-------------KAEYEFDSPYWDDISDSAK------------------------DFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14213  248 LgplpkhmiqktrkRKYFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALKH 327

                 ..
gi 594150345 277 PW 278
Cdd:cd14213  328 PF 329
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
4-279 8.40e-19

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: 86.30  E-value: 8.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   4 ENGESSSSWKKQAEDIKKIfefketlGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIV 82
Cdd:cd07874    7 EVGDSTFTVLKRYQNLKPI-------GSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKrAYRELVLMKCVNHKNII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  83 ALEDIY------ESPNHLYLVMQLVSGGelFDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqd 156
Cdd:cd07874   80 SLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 157 eESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIA------YILLCGYPpfYDENDSKLF 230
Cdd:cd07874  155 -DCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvrhKILFPGRD--YIDQWNKVI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 231 EQILKAEYEF----------------------------------DSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd07874  232 EQLGTPCPEFmkklqptvrnyvenrpkyagltfpklfpdslfpaDSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQH 311

                 ...
gi 594150345 277 PWI 279
Cdd:cd07874  312 PYI 314
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
19-278 8.83e-19

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 85.84  E-value: 8.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  19 IKKIFEFKETLGTGAFSEVV-LAEEKATGKLFAVKCIpKKALKGKESSiENEIAVLRKIKHEN------IVALEDIYESP 91
Cdd:cd14215   10 LQERYEIVSTLGEGTFGRVVqCIDHRRGGARVALKII-KNVEKYKEAA-RLEINVLEKINEKDpenknlCVQMFDWFDYH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  92 NHLYLVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEE----------- 158
Cdd:cd14215   88 GHMCISFELL-GLSTFDFLKENNYlpYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYEltynlekkrde 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 -----SKIMISDFGLSKMEGKGDvmSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK---LF 230
Cdd:cd14215  167 rsvksTAIRVVDFGSATFDHEHH--STIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREhlaMM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 231 EQIL------------KAEYEFDSPY-WDDISDSAK------------------------DFIRNLMEKDPNKRYTCEQA 273
Cdd:cd14215  245 ERILgpipsrmirktrKQKYFYHGRLdWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAA 324

                 ....*
gi 594150345 274 ARHPW 278
Cdd:cd14215  325 LKHPF 329
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
25-279 9.06e-19

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: 84.58  E-value: 9.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESP--NHLYLVMQLV 101
Cdd:cd13983    5 FNEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQrFKQEIEILKSLKHPNIIKFYDSWESKskKEVIFITELM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYYSQDEESKimISDFGLSKMEgKGDVMS 179
Cdd:cd13983   85 TSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTGEVK--IGDLGLATLL-RQSFAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQKpYSKAVDCWSIGVIAYILLCG-YPpfYDE--NDSklfeQILKAEYEFDSPY-WDDISDS-AKD 254
Cdd:cd13983  162 SVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGeYP--YSEctNAA----QIYKKVTSGIKPEsLSKVKDPeLKD 234
                        250       260
                 ....*....|....*....|....*
gi 594150345 255 FIRNLMEKdPNKRYTCEQAARHPWI 279
Cdd:cd13983  235 FIEKCLKP-PDERPSARELLEHPFF 258
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
29-221 1.03e-18

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: 84.85  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEV---VLAEekatGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14664    1 IGRGGAGTVykgVMPN----GTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEK-DASTLIRQVLDA---VYYLHR---MGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGD 176
Cdd:cd14664   77 LGELLHSRPESQPPlDWETRQRIALGSargLAYLHHdcsPLIIHRDVKSNNILL---DEEFEAHVADFGLAKLmdDKDSH 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 594150345 177 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14664  154 VMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
27-267 1.11e-18

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: 84.21  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEkdASTLIRQVLDA---VYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGdVMSTACG 183
Cdd:cd05084   82 LTFLRTEGPRLK--VKELIRMVENAaagMEYLESKHCIHRDLAARNCLV---TEKNVLKISDFGMSREEEDG-VYAATGG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 184 TP----GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSPywddisDSAKDFIRN 258
Cdd:cd05084  156 MKqipvKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQG-VRLPCP------ENCPDEVYR 228
                        250
                 ....*....|...
gi 594150345 259 LMEK----DPNKR 267
Cdd:cd05084  229 LMEQcweyDPRKR 241
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
23-170 1.64e-18

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: 84.05  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcIPKKalKGKESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKK--DSKHPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVMDLL 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594150345 102 --SGGELFDRIveKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSK 170
Cdd:cd14016   79 gpSLEDLFNKC--GRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAK 147
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
17-278 1.71e-18

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: 85.06  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSiENEIAVLRKIKHEN------IVALEDIYES 90
Cdd:cd14214    9 DWLQERYEIVGDLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAA-RLEINVLKKIKEKDkenkflCVLMSDWFNF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVsGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQD-----------E 157
Cdd:cd14214   88 HGHMCIAFELL-GKNTFEFLKENNFqpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtlyneskscE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 E-----SKIMISDFGLSKMEgkGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK---L 229
Cdd:cd14214  167 EksvknTSIRVADFGSATFD--HEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREhlvM 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 230 FEQIL------------KAEYEFD-SPYWDDISDSAK------------------------DFIRNLMEKDPNKRYTCEQ 272
Cdd:cd14214  245 MEKILgpipshmihrtrKQKYFYKgSLVWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRITLKE 324

                 ....*.
gi 594150345 273 AARHPW 278
Cdd:cd14214  325 ALLHPF 330
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
18-280 2.70e-18

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: 84.09  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  18 DIKKIFEFKETLGTGAFSEVVLAEEK----ATGKLFAVKCIPKKALKgkeSSIENEIAVLRKIKHENIVALEDIYESPNH 93
Cdd:cd14158   12 DERPISVGGNKLGEGGFGVVFKGYINdknvAVKKLAAMVDISTEDLT---KQFEQEIQVMAKCQHENLVELLGYSCDGPQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELFDRIVEKgfytEKDASTLIRQVLDAVY-------YLHRMGIVHRDLKPENLLYysqDEESKIMISDF 166
Cdd:cd14158   89 LCLVYTYMPNGSLLDRLACL----NDTPPLSWHMRCKIAQgtanginYLHENNHIHRDIKSANILL---DETFVPKISDF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSKMEGKG--DVM-STACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILLCGYPPFyDEN--DSKLFEQILKAEYEFD 241
Cdd:cd14158  162 GLARASEKFsqTIMtERIVGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPPV-DENrdPQLLLDIKEEIEDEEK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 594150345 242 SPYwDDISDSAKDFIRNLMEKDPN--KRYTCEQAARHPWIA 280
Cdd:cd14158  240 TIE-DYVDKKMGDWDSTSIEAMYSvaSQCLNDKKNRRPDIA 279
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
23-278 2.74e-18

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: 84.12  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESSIEN----EIAVLRKIKHEN----IVALEDIYESPN-H 93
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK---KTRLEMEEEGVPStalrEVSLLQMLSQSIyivrLLDVEHVEENGKpL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQ-LVSGGELFDRIVEKGFYTEKDASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKIMISDFGLS 169
Cdd:cd07837   80 LYLVFEyLDTDLKKFIDSYGRGPHNPLPAKTIQSfmyQLCKGVAHCHSHGVMHRDLKPQNLLV--DKQKGLLKIADLGLG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 K---MEGKGDVMSTAcgTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFY-DENDSKLF----------EQI- 233
Cdd:cd07837  158 RaftIPIKSYTHEIV--TLWYRAPEVlLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPgDSELQQLLhifrllgtpnEEVw 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 234 -----LKAEYEFdsPYWD---------DISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07837  236 pgvskLRDWHEY--PQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
23-299 3.02e-18

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: 84.45  E-value: 3.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNH-----LYL 96
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATrILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVsGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKM---EG 173
Cdd:cd07859   82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANA---DCKLKICDFGLARVafnDT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMST-ACGTPGYVAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAeyeFDSPYWDDIS- 249
Cdd:cd07859  158 PTAIFWTdYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDL---LGTPSPETISr 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 250 ---DSAKDFIRNLMEK--------------------------DPNKRYTCEQAARHPWIAGdtaLSKNIHESVSAQIRK 299
Cdd:cd07859  235 vrnEKARRYLSSMRKKqpvpfsqkfpnadplalrllerllafDPKDRPTAEEALADPYFKG---LAKVEREPSAQPITK 310
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
27-278 3.43e-18

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: 83.58  E-value: 3.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMqlvsggEL 106
Cdd:cd07844    6 DKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVF------EY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKgfYTEKDASTL----IR----QVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEG-KGDV 177
Cdd:cd07844   80 LDTDLKQ--YMDDCGGGLsmhnVRlflfQLLRGLAYCHQRRVLHRDLKPQNLLISERGE---LKLADFGLARAKSvPSKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPF------YDENDsKLFEQI----------LKAEYEF 240
Cdd:cd07844  155 YSNEVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstdvEDQLH-KIFRVLgtpteetwpgVSSNPEF 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 241 dSPYW----------------DDISDsAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd07844  234 -KPYSfpfypprplinhaprlDRIPH-GEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
85-274 3.68e-18

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: 84.08  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  85 EDIYESPNHLYLVMQLVSggELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPEN-LLYYSQDEESKIMI 163
Cdd:cd14018  106 PSGLGHNRTLFLVMKNYP--CTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNiLLELDFDGCPWLVI 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLS--------KMEGKGDVMSTAcGTPGYVAPEVLAQKP-------YSKAvDCWSIGVIAYILLCGYPPFYDENDSK 228
Cdd:cd14018  184 ADFGCCladdsiglQLPFSSWYVDRG-GNACLMAPEVSTAVPgpgvvinYSKA-DAWAVGAIAYEIFGLSNPFYGLGDTM 261
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 229 LfeqiLKAEYEFDS--PYWDDISDSAKDFIRNLMEKDPNKRYTCEQAA 274
Cdd:cd14018  262 L----ESRSYQESQlpALPSAVPPDVRQVVKDLLQRDPNKRVSARVAA 305
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
68-234 4.15e-18

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: 82.83  E-value: 4.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  68 NEIAVLRKIKHENIVALEDIYESPNhLYLVMQLVSGGELFDRI--VEKGFytekDASTLI---RQVLDAVYYLHRMGIVH 142
Cdd:cd14062   38 NEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCEGSSLYKHLhvLETKF----EMLQLIdiaRQTAQGMDYLHAKNIIH 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 143 RDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV---MSTACGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLC 216
Cdd:cd14062  113 RDLKSNNIFL---HEDLTVKIGDFGLATVKTRWSGsqqFEQPTGSILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLT 189
                        170
                 ....*....|....*...
gi 594150345 217 GYPPFYDENDSklfEQIL 234
Cdd:cd14062  190 GQLPYSHINNR---DQIL 204
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
23-268 4.38e-18

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: 84.37  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIKHEN-----IVALEDIYESPNHLYLV 97
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIE--VSILSRLSSENadeynFVRSYECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGgELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEES-KIMISDFGLSKMEGK 174
Cdd:cd14228   95 FEMLEQ-NLYDFLKQNKFspLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASHVSK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF-----YDENDSKLFEQILKAEYEFdspywddis 249
Cdd:cd14228  174 A-VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYpgaseYDQIRYISQTQGLPAEYLL--------- 243
                        250
                 ....*....|....*....
gi 594150345 250 dSAKDFIRNLMEKDPNKRY 268
Cdd:cd14228  244 -SAGTKTSRFFNRDPNLGY 261
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
14-270 4.89e-18

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 83.91  E-value: 4.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  14 KQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIKHE------NIVALEDI 87
Cdd:cd14226    6 KNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIE--VRLLELMNKHdtenkyYIVRLKRH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMQLVSGgELFDRIVEKGFY------TEKDAstliRQVLDAVYYLHR--MGIVHRDLKPEN-LLYYSQdeE 158
Cdd:cd14226   84 FMFRNHLCLVFELLSY-NLYDLLRNTNFRgvslnlTRKFA----QQLCTALLFLSTpeLSIIHCDLKPENiLLCNPK--R 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 SKIMISDFGLSKMEGKgdVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsklFEQILKAEY 238
Cdd:cd14226  157 SAIKIIDFGSSCQLGQ--RIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANE---VDQMNKIVE 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 239 EFDSPYWDDISDSAKdfIRNLMEKDPNKRYTC 270
Cdd:cd14226  232 VLGMPPVHMLDQAPK--ARKFFEKLPDGTYYL 261
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
27-269 6.64e-18

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: 82.39  E-value: 6.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKA-TGKLF--AVKCIPKKALKGKESSIE--NEIAVLRKIKHENIVALEDIYESpNHLYLVMQLV 101
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTpSGKVIqvAVKCLKSDVLSQPNAMDDflKEVNAMHSLDHPNLIRLYGVVLS-SPLMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRIVE-KGFYTekdASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGLSKMEGKGD- 176
Cdd:cd05040   80 PLGSLLDRLRKdQGHFL---ISTLCDyavQIANGMAYLESKRFIHRDLAARNILLASKD---KVKIGDFGLMRALPQNEd 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 --VMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAEYEFDSPywDDISDSA 252
Cdd:cd05040  154 hyVMQEHRKVPfAWCAPESLKTRKFSHASDVWMFGVTLWeMFTYGEEPWLGLNGSQILEKIDKEGERLERP--DDCPQDI 231
                        250
                 ....*....|....*..
gi 594150345 253 KDFIRNLMEKDPNKRYT 269
Cdd:cd05040  232 YNVMLQCWAHKPADRPT 248
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
27-267 9.70e-18

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: 81.84  E-value: 9.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEekATGKLFAVKCIpkKALKGKESSIEnEIAVLRKIKHENIVALEDIYESpNHLYLVMQLVSGGEL 106
Cdd:cd05083   12 EIIGEGEFGAVLQGE--YMGQKVAVKNI--KCDVTAQAFLE-ETAVMTKLQHKNLVRLLGVILH-NGLYIVMELMSKGNL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLI--RQVLDAVYYLHRMGIVHRDLKPENLLYySQDEESKImiSDFGLSKMEGKGDVMSTAcgT 184
Cdd:cd05083   86 VNFLRSRGRALVPVIQLLQfsLDVAEGMEYLESKKLVHRDLAARNILV-SEDGVAKI--SDFGLAKVGSMGVDNSRL--P 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 PGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSPywDDISDSAKDFIRNLMEKD 263
Cdd:cd05083  161 VKWTAPEALKNKKFSSKSDVWSYGVLLWeVFSYGRAPYPKMSVKEVKEAVEKG-YRMEPP--EGCPPDVYSIMTSCWEAE 237

                 ....
gi 594150345 264 PNKR 267
Cdd:cd05083  238 PGKR 241
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
29-209 1.57e-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: 81.24  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEV---VLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNhLYLVMQLVSGGE 105
Cdd:cd05060    3 LGHGNFGSVrkgVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPLGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMEGKGDVMSTAcGTP 185
Cdd:cd05060   82 LLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGMSRALGAGSDYYRA-TTA 157
                        170       180
                 ....*....|....*....|....*....
gi 594150345 186 G-----YVAPEVLAQKPYSKAVDCWSIGV 209
Cdd:cd05060  158 GrwplkWYAPECINYGKFSSKSDVWSYGV 186
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
29-216 3.13e-17

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: 80.76  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKESSIEN---EIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfltEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK--ME----------- 172
Cdd:cd14222   77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI---KLDKTVVVADFGLSRliVEekkkpppdkpt 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 173 ------GKGDVMS--TACGTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 216
Cdd:cd14222  154 tkkrtlRKNDRKKryTVVGNPYWMAPEMLNGKSYDEKVDIFSFG----IVLC 201
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
29-267 3.42e-17

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: 80.25  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSienEIAVLRKIKhenIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELM---ACAGLTSPR---VVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysQDEESKIMISDFGLSKM---EGKGDVMSTACGTP 185
Cdd:cd13991   88 LIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLL--SSDGSDAFLCDFGHAECldpDGLGKSLFTGDYIP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 186 G---YVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKaeyefDSPYWDDISDSAKDF----IRN 258
Cdd:cd13991  166 GtetHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIAN-----EPPPLREIPPSCAPLtaqaIQA 240

                 ....*....
gi 594150345 259 LMEKDPNKR 267
Cdd:cd13991  241 GLRKEPVHR 249
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
27-243 4.53e-17

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: 79.66  E-value: 4.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd05085    2 ELLGKGNFGEVYKGTLKDKTPV-AVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGfyTEKDASTLIRQVLDA---VYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACG 183
Cdd:cd05085   81 LSFLRKKK--DELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLV---GENNALKISDFGMSRQEDDGVYSSSGLK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594150345 184 T-P-GYVAPEVLAQKPYSKAVDCWSIGVIAY----ILLCGYPPFYDENDSklfEQILKAeYEFDSP 243
Cdd:cd05085  156 QiPiKWTAPEALNYGRYSSESDVWSFGILLWetfsLGVCPYPGMTNQQAR---EQVEKG-YRMSAP 217
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
30-221 4.55e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 79.62  E-value: 4.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  30 GTGAFSEVVLAEEKATGKLFAVKcipkKALKgkessIENEIAVLRKIKHENIVALED-IYESPNHLyLVMQLVSGGELFD 108
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK----KLLK-----IEKEAEILSVLSHRNIIQFYGaILEAPNYG-IVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGfYTEKDASTLI---RQVLDAVYYLHR---MGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGKGDVMSTAc 182
Cdd:cd14060   72 YLNSNE-SEEMDMDQIMtwaTDIAKGMHYLHMeapVKVIHRDLKSRNVVIAA---DGVLKICDFGASRFHSHTTHMSLV- 146
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14060  147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
25-215 6.60e-17

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: 80.06  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAE----EKATGKLFAVKCIpKKALKGKESSIENEIAVLRKIKHENIVALEDIYESP--NHLYLVM 98
Cdd:cd14205    8 FLQQLGKGNFGSVEMCRydplQDNTGEVVAVKKL-QHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDrivekgfYTEK-----DASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSK 170
Cdd:cd14205   87 EYLPYGSLRD-------YLQKhkeriDHIKLLQytsQICKGMEYLGTKRYIHRDLATRNILV---ENENRVKIGDFGLTK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEGKgDVMSTACGTPG-----YVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd14205  157 VLPQ-DKEYYKVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
52-212 6.62e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 81.04  E-value: 6.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  52 KCIPKKALKGKesSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQlVSGGELFDRIVEKGFYTEKDASTLIRQVLDA 131
Cdd:PHA03207 121 KVIVKAVTGGK--TPGREIDILKTISHRAIINLIHAYRWKSTVCMVMP-KYKCDLFTYVDRSGPLPLEQAITIQRRLLEA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 132 VYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDVMSTACGTPGYV---APEVLAQKPYSKAVDCWSIG 208
Cdd:PHA03207 198 LAYLHGRGIIHRDVKTENIFL---DEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLetnSPELLALDPYCAKTDIWSAG 274

                 ....
gi 594150345 209 VIAY 212
Cdd:PHA03207 275 LVLF 278
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
28-267 8.39e-17

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: 79.62  E-value: 8.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIE-----NEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05045    7 TLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSElrdllSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGEL-----FDRIVEKGF-------------------YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqdEE 158
Cdd:cd05045   87 YGSLrsflrESRKVGPSYlgsdgnrnssyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV----AE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 SKIM-ISDFGLSK--MEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQI 233
Cdd:cd05045  163 GRKMkISDFGLSRdvYEEDSYVKRSKGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIAPERLF-NL 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 594150345 234 LKAEYEFDSPywDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05045  242 LKTGYRMERP--ENCSEEMYNLMLTCWKQEPDKR 273
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
13-305 9.12e-17

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: 79.73  E-value: 9.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  13 KKQAEDIKKIfEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKiKHE--NIVALEDIYES 90
Cdd:cd06618    8 KKYKADLNDL-ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLK-SHDcpYIVKCYGYFIT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSG--GELFDRIveKGFYTEKDASTLIRQVLDAVYYL-HRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd06618   86 DSDVFICMELMSTclDKLLKRI--QGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILL---DESGNVKLCDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSK---AVDCWSIGVIAYILLCG-YPpfYDENDSKlFEQILK-AEYEFDS 242
Cdd:cd06618  161 ISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGqFP--YRNCKTE-FEVLTKiLNEEPPS 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594150345 243 -PYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAgdtalsknIHESVSAQIRKNFAKSK 305
Cdd:cd06618  238 lPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR--------RYETAEVDVASWFQDVM 293
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-267 1.64e-16

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: 78.92  E-value: 1.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKAL---KGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd08229   26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmdaKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRI----VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKM-EGK 174
Cdd:cd08229  105 LADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITAT---GVVKLGDLGLGRFfSSK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 175 GDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE--NDSKLFEQILKAEYefdSPY-WDDISDS 251
Cdd:cd08229  182 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLYSLCKKIEQCDY---PPLpSDHYSEE 258
                        250
                 ....*....|....*.
gi 594150345 252 AKDFIRNLMEKDPNKR 267
Cdd:cd08229  259 LRQLVNMCINPDPEKR 274
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
29-216 1.96e-16

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 78.32  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLK-EVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIMISDFGLSK----------MEGKGDV 177
Cdd:cd14154   80 VLKDMArPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVR---EDKTVVVADFGLARliveerlpsgNMSPSET 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MS-----------TACGTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 216
Cdd:cd14154  157 LRhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFG----IVLC 202
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
24-267 2.08e-16

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: 78.48  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAEEKATGKLFAVKCI---PKKALKGkessIENEIAVLRKIK-HENIVAL---------EDIYEs 90
Cdd:cd14037    6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEHDLNV----CKREIEIMKRLSgHKNIVGYidssanrsgNGVYE- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 pnhLYLVMQLVSGGELFDRIVEK---GFyTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYysqDEESKIMISD 165
Cdd:cd14037   81 ---VLLLMEYCKGGGVIDLMNQRlqtGL-TESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLI---SDSGNYKLCD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FG-----LSKMEGKGDVMSTA-----CGTPGYVAPEVL---AQKPYSKAVDCWSIGVIAYiLLCGYP-PFYDENDSKlfe 231
Cdd:cd14037  154 FGsattkILPPQTKQGVTYVEedikkYTTLQYRAPEMIdlyRGKPITEKSDIWALGCLLY-KLCFYTtPFEESGQLA--- 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 232 qILKAEYEF--DSPYwddiSDSAKDFIRNLMEKDPNKR 267
Cdd:cd14037  230 -ILNGNFTFpdNSRY----SKRLHKLIRYMLEEDPEKR 262
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
88-215 2.36e-16

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: 78.75  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMQLVSGGELFDRIVEKGfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFG 167
Cdd:cd13977  104 PRSACYLWFVMEFCDGGDMNEYLLSRR-PDRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGEPILKVADFG 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKM-EGKGDV-----------MSTACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd13977  183 LSKVcSGSGLNpeepanvnkhfLSSACGSDFYMAPEVW-EGHYTAKADIFALGIIIWAMV 241
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
20-215 2.64e-16

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: 78.02  E-value: 2.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVL----AEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH-- 93
Cdd:cd05080    3 KRYLKKIRDLGEGHFGKVSLycydPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGks 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELFDrivekgfYTEKDASTL------IRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd05080   83 LQLIMEYVPLGSLRD-------YLPKHSIGLaqlllfAQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594150345 168 LSKMEGKGD----VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05080  153 LAKAVPEGHeyyrVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELL 204
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
26-233 2.88e-16

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: 77.71  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGK---LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05063   10 QKVIGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELfDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKM---EGKGDV 177
Cdd:cd05063   90 NGAL-DKYLRDhdGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLE---CKVSDFGLSRVledDPEGTY 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 178 MSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05063  166 TTSGGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAI 223
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
24-233 3.25e-16

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: 77.74  E-value: 3.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVlaEEKATGKLfAVKCIP-KKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd14153    3 EIGELIGKGRFGQVY--HGRWHGEV-AIRLIDiERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQ-VLDAVYYLHRMGIVHRDLKPENLLYysqdEESKIMISDFGLSKMEG------KG 175
Cdd:cd14153   80 GRTLYSVVRDAKVVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFTISGvlqagrRE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 176 DVMSTACGTPGYVAPEVLAQ---------KPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI 233
Cdd:cd14153  156 DKLRIQSGWLCHLAPEIIRQlspeteedkLPFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQV 222
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
15-278 3.47e-16

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: 78.56  E-value: 3.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  15 QAEDIKKIFEFKE-TLGTGAFSEVVLAEEK--ATGKLFAVKCIPKKalkGKESSIENEIAVLRKIKHENIVALEDIYES- 90
Cdd:cd07868   10 ERERVEDLFEYEGcKVGRGTYGHVYKAKRKdgKDDKDYALKQIEGT---GISMSACREIALLRELKHPNVISLQKVFLSh 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 ------------PNHLYLVMQLVSGGELFDRIVE--KGFytekdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQD 156
Cdd:cd07868   87 adrkvwllfdyaEHDLWHIIKFHRASKANKKPVQlpRGM-----VKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 157 -EESKIMISDFGLSK-----MEGKGDvMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYP---------- 219
Cdd:cd07868  162 pERGRVKIADMGFARlfnspLKPLAD-LDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPifhcrqedik 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 220 ---PFYDENDSKLFeQILKAEYEFDspyWDDI------SDSAKDFIRN----------------------------LMEK 262
Cdd:cd07868  241 tsnPYHHDQLDRIF-NVMGFPADKD---WEDIkkmpehSTLMKDFRRNtytncslikymekhkvkpdskafhllqkLLTM 316
                        330
                 ....*....|....*.
gi 594150345 263 DPNKRYTCEQAARHPW 278
Cdd:cd07868  317 DPIKRITSEQAMQDPY 332
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
64-220 4.66e-16

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: 77.31  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  64 SSIENEIAVLRKIKHENIVALEDIYESPnhLYLVMQLVSGGELFDRIVEKgfytEKDAS----------TLIRQVLDAVY 133
Cdd:cd14067   55 SEFRQEASMLHSLQHPCIVYLIGISIHP--LCFALELAPLGSLNTVLEEN----HKGSSfmplghmltfKIAYQIAAGLA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 134 YLHRMGIVHRDLKPENLLYYSQDEESKIMI--SDFGLSKMEGKGDVMSTAcGTPGYVAPEVLAQKPYSKAVDCWSIGVIA 211
Cdd:cd14067  129 YLHKKNIIFCDLKSDNILVWSLDVQEHINIklSDYGISRQSFHEGALGVE-GTPGYQAPEIRPRIVYDEKVDMFSYGMVL 207

                 ....*....
gi 594150345 212 YILLCGYPP 220
Cdd:cd14067  208 YELLSGQRP 216
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
29-267 5.99e-16

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros 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: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 76.69  E-value: 5.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEV-------VLAEEKATGKLfAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd05044    3 LGSGAFGEVfegtakdILGDGSGETKV-AVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDRI-------VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIM-ISDFGLSK--- 170
Cdd:cd05044   82 EGGDLLSYLraarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVVkIGDFGLARdiy 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 ------MEGKGDVmstacgtP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKAEYEFDS 242
Cdd:cd05044  162 kndyyrKEGEGLL-------PvRWMAPESLVDGVFTTQSDVWAFGVLMWeILTLGQQPYPARNNLEVL-HFVRAGGRLDQ 233
                        250       260
                 ....*....|....*....|....*....
gi 594150345 243 PywddisDSAKDFIRNLM----EKDPNKR 267
Cdd:cd05044  234 P------DNCPDDLYELMlrcwSTDPEER 256
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
8-210 1.02e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 78.20  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   8 SSSSWKKQAEDIKKiFEFKETLGTGAFSEVVLA--------EEKATGKLFAVKCIPK---------KALKGKESSIENEI 70
Cdd:PHA03210 136 AQAKLKHDDEFLAH-FRVIDDLPAGAFGKIFICalrasteeAEARRGVNSTNQGKPKcerliakrvKAGSRAAIQLENEI 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  71 AVLRKIKHENIVALEDIYESPNHLYLVMQLVSgGELFDRIVEKGFyTEKDASTL------IRQVLDAVYYLHRMGIVHRD 144
Cdd:PHA03210 215 LALGRLNHENILKIEEILRSEANTYMITQKYD-FDLYSFMYDEAF-DWKDRPLLkqtraiMKQLLCAVEYIHDKKLIHRD 292
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 145 LKPENLLYysqDEESKIMISDFGlSKMEGKGDVMSTACGTPGYVA---PEVLAQKPYSKAVDCWSIGVI 210
Cdd:PHA03210 293 IKLENIFL---NCDGKIVLGDFG-TAMPFEKEREAFDYGWVGTVAtnsPEILAGDGYCEITDIWSCGLI 357
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
13-272 1.39e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.84  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  13 KKQAEDIKKIFEFK--ETLGTGAFSEVVLAEEKATGKLFAVKCipkkalkGKESSIENEIAVLRKIKHENIVALEDI--- 87
Cdd:PHA03209  56 KQKAREVVASLGYTviKTLTPGSEGRVFVATKPGQPDPVVLKI-------GQKGTTLIEAMLLQNVNHPSVIRMKDTlvs 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 ----------YESPNHLYLVMqlvsggelfdrivEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDE 157
Cdd:PHA03209 129 gaitcmvlphYSSDLYTYLTK-------------RSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFI---ND 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLcGYP-PFYDENDSKLFEQILKA 236
Cdd:PHA03209 193 VDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML-AYPsTIFEDPPSTPEEYVKSC 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 237 EY--------------EFDSpywDDISDSAKDFIR-NLMEKDPNKRYTCEQ 272
Cdd:PHA03209 272 HShllkiistlkvhpeEFPR---DPGSRLVRGFIEyASLERQPYTRYPCFQ 319
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
26-267 1.85e-15

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: 75.62  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKES---SIENEIAVLRKIK-HENIVALEDIY----ESPNHL--- 94
Cdd:cd14036    5 KRVIAEGGFAFVYEAQDVGTGKEYALK----RLLSNEEEknkAIIQEINFMKKLSgHPNIVQFCSAAsigkEESDQGqae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGELFDRIVEKGFYTEKDASTLIR---QVLDAVYYLHRMG--IVHRDLKPENLLYYSQdeeSKIMISDFGLS 169
Cdd:cd14036   81 YLLLTELCKGQLVDFVKKVEAPGPFSPDTVLKifyQTCRAVQHMHKQSppIIHRDLKIENLLIGNQ---GQIKLCDFGSA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 170 KMEGKGDVMSTACG-------------TPGYVAPEVL---AQKPYSKAVDCWSIGVIAYiLLCGYP-PFydENDSKLfeQ 232
Cdd:cd14036  158 TTEAHYPDYSWSAQkrslvedeitrntTPMYRTPEMIdlySNYPIGEKQDIWALGCILY-LLCFRKhPF--EDGAKL--R 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594150345 233 ILKAEYEFdsPYWDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd14036  233 IINAKYTI--PPNDTQYTVFHDLIRSTLKVNPEER 265
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
29-215 2.04e-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: 75.74  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLA----EEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDI--YESPNHLYLVMQLVS 102
Cdd:cd05079   12 LGEGHFGKVELCrydpEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGIctEDGGNGIKLIMEFLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM----EGKGDV 177
Cdd:cd05079   92 SGSLKEYLPRnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLTKAietdKEYYTV 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 594150345 178 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05079  169 KDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELL 206
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
22-278 2.05e-15

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: 76.26  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  22 IFEFKE-TLGTGAFSEVVLAEEK--ATGKLFAVKCIPKKalkGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVM 98
Cdd:cd07867    2 LFEYEGcKVGRGTYGHVYKAKRKdgKDEKEYALKQIEGT---GISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEkgFYTEKDAS------------TLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQD-EESKIMISD 165
Cdd:cd07867   79 LFDYAEHDLWHIIK--FHRASKANkkpmqlprsmvkSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FGLSK-----MEGKGDvMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYP-------------PFYDEND 226
Cdd:cd07867  157 MGFARlfnspLKPLAD-LDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 227 SKLFeQILKAEYEFDspyWDDISDS------AKDFIRN----------------------------LMEKDPNKRYTCEQ 272
Cdd:cd07867  236 DRIF-SVMGFPADKD---WEDIRKMpeyptlQKDFRRTtyansslikymekhkvkpdskvflllqkLLTMDPTKRITSEQ 311

                 ....*.
gi 594150345 273 AARHPW 278
Cdd:cd07867  312 ALQDPY 317
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
25-243 2.46e-15

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: 74.79  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALkGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05059    8 FLKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSM-SEDDFIE-EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFD--RIVEKGFYTEKDASTLIrQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTAC 182
Cdd:cd05059   85 CLLNylRERRGKFQTEQLLEMCK-DVCEAMEYLESNGFIHRDLAARNCLV---GEQNVVKVSDFGLARYV-LDDEYTSSV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594150345 183 GTP---GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSP 243
Cdd:cd05059  160 GTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQG-YRLYRP 223
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
67-237 2.85e-15

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: 75.00  E-value: 2.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  67 ENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQ-VLDAVYYLHRMGIVHRDL 145
Cdd:cd14152   44 KKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTLYSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 146 KPENLLYysqdEESKIMISDFGLSKMEG------KGDVMSTACGTPGYVAPEVLA---------QKPYSKAVDCWSIGVI 210
Cdd:cd14152  124 KSKNVFY----DNGKVVITDFGLFGISGvvqegrRENELKLPHDWLCYLAPEIVRemtpgkdedCLPFSKAADVYAFGTI 199
                        170       180
                 ....*....|....*....|....*..
gi 594150345 211 AYILLCGYPPFYDENDSKLFEQILKAE 237
Cdd:cd14152  200 WYELQARDWPLKNQPAEALIWQIGSGE 226
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
29-210 2.86e-15

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: 74.82  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKcipKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELfD 108
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALK---MNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL-E 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVEKGFYTEkdASTLIRQVLD---AVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSK---MEGKGDVMSTAC 182
Cdd:cd14155   77 QLLDSNEPLS--WTVRVKLALDiarGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEkipDYSDGKEKLAVV 154
                        170       180
                 ....*....|....*....|....*...
gi 594150345 183 GTPGYVAPEVLAQKPYSKAVDCWSIGVI 210
Cdd:cd14155  155 GSPYWMAPEVLRGEPYNEKADVFSYGII 182
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
27-226 2.98e-15

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: 75.10  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVlaEEKATGKLfAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDiYESPNHLYLVMQLVSGGE 105
Cdd:cd14151   14 QRIGSGSFGTVY--KGKWHGDV-AVKMLNVTAPTPQQlQAFKNEVGVLRKTRHVNILLFMG-YSTKPQLAIVTQWCEGSS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDR--IVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIMISDFGLSKMEGK---GDVMST 180
Cdd:cd14151   90 LYHHlhIIETKFEMIK-LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLH---EDLTVKIGDFGLATVKSRwsgSHQFEQ 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 594150345 181 ACGTPGYVAPEVLA---QKPYSKAVDCWSIGVIAYILLCGYPPFYDEND 226
Cdd:cd14151  166 LSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINN 214
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
29-271 3.39e-15

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: 74.18  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALEDIY-ESPnhLYLVMQLVSGGELF 107
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTKV-AIKTL-KPGTMSPEAFLE-EAQIMKKLRHDKLVQLYAVVsEEP--IYIVTEFMSKGSLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DrivekgFYTEKDASTL--------IRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMegKGDVMS 179
Cdd:cd14203   78 D------FLKDGEGKYLklpqlvdmAAQIASGMAYIERMNYIHRDLRAANILV---GDNLVCKIADFGLARL--IEDNEY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGY----VAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPFYDENDSKLFEQIlkaEYEFDSPYWDDISDSAKD 254
Cdd:cd14203  147 TARQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV---ERGYRMPCPPGCPESLHE 223
                        250
                 ....*....|....*..
gi 594150345 255 FIRNLMEKDPNKRYTCE 271
Cdd:cd14203  224 LMCQCWRKDPEERPTFE 240
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
27-217 3.46e-15

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 75.34  E-value: 3.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEE-KATGKLFAVKCIPKKALKGKESsiENEIAVLRKI--------KHenIVALEDIYESPNHLYLV 97
Cdd:cd14135    6 GYLGKGVFSNVVRARDlARGNQEVAIKIIRNNELMHKAG--LKELEILKKLndadpddkKH--CIRLLRHFEHKNHLCLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  98 MQLVSGGElfdRIVEKGFYTEKDAS-TLIR----QVLDAVYYLHRMGIVHRDLKPENLLYYSQdeESKIMISDFGlSKME 172
Cdd:cd14135   82 FESLSMNL---REVLKKYGKNVGLNiKAVRsyaqQLFLALKHLKKCNILHADIKPDNILVNEK--KNTLKLCDFG-SASD 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 173 -GKGDVmstacgTPG-----YVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 217
Cdd:cd14135  156 iGENEI------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
pknD PRK13184
serine/threonine-protein kinase PknD;
29-275 6.56e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 75.96  E-value: 6.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpkkalkgKESSIENEI---AVLRKIK------HENIVALEDIYESPNHLYLVMQ 99
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKKI-------REDLSENPLlkkRFLREAKiaadliHPGIVPVYSICSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFD--------RIVEKGFYTEKDASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLY--YSQdeeskIMISDF 166
Cdd:PRK13184  83 YIEGYTLKSllksvwqkESLSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLglFGE-----VVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSKM-EGKGD------------------VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDS 227
Cdd:PRK13184 158 GAAIFkKLEEEdlldidvdernicyssmtIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 594150345 228 KL-FEQILKAEYEFdSPYwDDISDSAKDFIRNLMEKDPNKRYTCEQAAR 275
Cdd:PRK13184 238 KIsYRDVILSPIEV-APY-REIPPFLSQIAMKALAVDPAERYSSVQELK 284
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
27-226 7.44e-15

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: 73.68  E-value: 7.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPnhLYLVMQLVSGGE 105
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSErMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LfdrivEKGFYTE----KDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYysqDEESKIMISDFGLSKMEG---KGD 176
Cdd:cd14025   80 L-----EKLLASEplpwELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILL---DAHYHVKISDFGLAKWNGlshSHD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 177 V-MSTACGTPGYVAPEVLAQK--PYSKAVDCWSIGVIAYILLCGYPPFYDEND 226
Cdd:cd14025  152 LsRDGLRGTIAYLPPERFKEKnrCPDTKHDVYSFAIVIWGILTQKKPFAGENN 204
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
20-243 7.59e-15

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: 73.62  E-value: 7.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05148    5 REEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKIL-KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGEL--FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDV 177
Cdd:cd05148   83 LMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILV---GEDLVCKVADFGLARLI-KEDV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 178 MSTACGTPGY--VAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILkAEYEFDSP 243
Cdd:cd05148  159 YLSSDKKIPYkwTAPEAASHGTFSTKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQIT-AGYRMPCP 226
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
29-226 1.03e-14

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: 73.13  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVlaEEKATGKLfAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNhLYLVMQLVSGGELF 107
Cdd:cd14150    8 IGTGSFGTVF--RGKWHGDV-AVKILKVTEPTPEQlQAFKNEMQVLRKTRHVNILLFMGFMTRPN-FAIITQWCEGSSLY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 DR--IVEKGFytekDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIMISDFGLSKMEGK---GDVMS 179
Cdd:cd14150   84 RHlhVTETRF----DTMQLIdvaRQTAQGMDYLHAKNIIHRDLKSNNIFLH---EGLTVKIGDFGLATVKTRwsgSQQVE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLCGYPPFYDEND 226
Cdd:cd14150  157 QPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINN 206
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
25-233 1.24e-14

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: 73.06  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05112    8 FVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMS--EEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRI-VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTACG 183
Cdd:cd05112   85 CLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLV---GENQVVKVSDFGMTRFV-LDDQYTSSTG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 184 TP---GYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPFYDENDSKLFEQI 233
Cdd:cd05112  161 TKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI 214
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
23-215 1.90e-14

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: 72.83  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEV---VLAEEKATGKL-FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLyLVM 98
Cdd:cd05057    9 LEKGKVLGSGAFGTVykgVWIPEGEKVKIpVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ-LIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QLVSGGELFDRIVEKGfyTEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKMEGKG 175
Cdd:cd05057   88 QLMPLGCLLDYVRNHR--DNIGSQLLLnwcVQIAKGMSYLEEKRLVHRDLAARNVLVKTP---NHVKITDFGLAKLLDVD 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 594150345 176 DVMSTACG--TP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05057  163 EKEYHAEGgkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELM 205
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
21-276 2.02e-14

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: 72.34  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLA-EEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH----LY 95
Cdd:cd14033    1 RFLKFNIEIGRGSFKTVYRGlDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGEL---FDRIVEKGFYTEKDAStliRQVLDAVYYLHRMG--IVHRDLKPENLlyYSQDEESKIMISDFGLSK 170
Cdd:cd14033   81 LVTELMTSGTLktyLKRFREMKLKLLQRWS---RQILKGLHFLHSRCppILHRDLKCDNI--FITGPTGSVKIGDLGLAT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 MEgKGDVMSTACGTPGYVAPEVLAQKpYSKAVDCWSIGV-IAYILLCGYPPFYDENDSKLFEQILKAeYEFDSPYWDDIS 249
Cdd:cd14033  156 LK-RASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMcILEMATSEYPYSECQNAAQIYRKVTSG-IKPDSFYKVKVP 232
                        250       260
                 ....*....|....*....|....*..
gi 594150345 250 DsAKDFIRNLMEKDPNKRYTCEQAARH 276
Cdd:cd14033  233 E-LKEIIEGCIRTDKDERFTIQDLLEH 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
12-272 2.10e-14

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 72.84  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDIkkifEFKETLGTGAFSEVVLAEEKATGKL------FAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVAL 84
Cdd:cd05053    7 WELPRDRL----TLGKPLGEGAFGQVVKAEAVGLDNKpnevvtVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  85 EDIYESPNHLYLVMQLVSGGELFD----------------RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPE 148
Cdd:cd05053   83 LGACTQDGPLYVVVEYASKGNLREflrarrppgeeaspddPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAAR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 149 NLLYysqDEESKIMISDFGLSKmegkgDVMS-------TACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYP 219
Cdd:cd05053  163 NVLV---TEDNVMKIADFGLAR-----DIHHidyyrktTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGS 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 220 PFYDENDSKLFEqILKAEYEFDSPYwdDISDSAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd05053  235 PYPGIPVEELFK-LLKEGHRMEKPQ--NCTQELYMLMRDCWHEVPSQRPTFKQ 284
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
6-271 2.10e-14

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: 72.80  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   6 GESSSSWKKQAEDIKkifeFKETLGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALE 85
Cdd:cd05069    1 GLAKDAWEIPRESLR----LDVKLGQGCFGEVWMGTWNGTTKV-AIKTL-KPGTMMPEAFLQ-EAQIMKKLRHDKLVPLY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  86 DIYeSPNHLYLVMQLVSGGELFDrivekgFYTEKDASTL--------IRQVLDAVYYLHRMGIVHRDLKPENLLYysqDE 157
Cdd:cd05069   74 AVV-SEEPIYIVTEFMGKGSLLD------FLKEGDGKYLklpqlvdmAAQIADGMAYIERMNYIHRDLRAANILV---GD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKM-EGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPFYDENDSKLFEQIl 234
Cdd:cd05069  144 NLVCKIADFGLARLiEDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQV- 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 594150345 235 kaEYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCE 271
Cdd:cd05069  223 --ERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFE 257
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
29-215 2.18e-14

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: 72.62  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEK----ATGKLFAVKCIPKKALKgKESSIENEIAVLRKIKHENIVALEDIYESPNH--LYLVMQLVS 102
Cdd:cd05081   12 LGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPD-QQRDFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLVMEYLP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDrivekgfYTEK-----DASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKMEGK 174
Cdd:cd05081   91 SGCLRD-------FLQRhrarlDASRLLlysSQICKGMEYLGSRRCVHRDLAARNILVES---EAHVKIADFGLAKLLPL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 594150345 175 gDVMSTACGTPG-----YVAPEVLAQKPYSKAVDCWSIGVIAYILL 215
Cdd:cd05081  161 -DKDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
23-279 2.60e-14

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 72.46  E-value: 2.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAV-LRKIKHENIVALEDIYESPNHLYLVMQLV 101
Cdd:cd06617    3 LEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 --SGGELFDRIVEKGFYTEKDASTLIR-QVLDAVYYLH-RMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGKGDV 177
Cdd:cd06617   83 dtSLDKFYKKVYDKGLTIPEDILGKIAvSIVKALEYLHsKLSVIHRDVKPSNVLI---NRNGQVKLCDFGISGYLVDSVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTACGTPGYVAPE----VLAQKPYSKAVDCWSIGVIAYILLCGYPPFydENDSKLFEQiLKAEYEFDSPYW--DDISDS 251
Cdd:cd06617  160 KTIDAGCKPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPY--DSWKTPFQQ-LKQVVEEPSPQLpaEKFSPE 236
                        250       260
                 ....*....|....*....|....*...
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd06617  237 FQDFVNKCLKKNYKERPNYPELLQHPFF 264
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
26-210 2.81e-14

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: 72.07  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKEssIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05052   11 KHKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEE--FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LFDRIVEKGfYTEKDASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTAC 182
Cdd:cd05052   89 LLDYLRECN-REELNAVVLLYmatQIASAMEYLEKKNFIHRDLAARNCLV---GENHLVKVADFGLSRLM-TGDTYTAHA 163
                        170       180       190
                 ....*....|....*....|....*....|.
gi 594150345 183 GTP---GYVAPEVLAQKPYSKAVDCWSIGVI 210
Cdd:cd05052  164 GAKfpiKWTAPESLAYNKFSIKSDVWAFGVL 194
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
29-216 3.00e-14

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: 71.91  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLK-EVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 RIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM--EGKGDVMS------ 179
Cdd:cd14221   80 IIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLV---RENKSVVVADFGLARLmvDEKTQPEGlrslkk 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 594150345 180 -------TACGTPGYVAPEVLAQKPYSKAVDCWSIGviayILLC 216
Cdd:cd14221  157 pdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFG----IVLC 196
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
29-269 3.26e-14

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 71.76  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGkLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELF 107
Cdd:cd14027    1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGPNCiEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 108 dRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGL------SKM---------E 172
Cdd:cd14027   80 -HVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLasfkmwSKLtkeehneqrE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTAcGTPGYVAPEVLAQ---KPYSKAvDCWSIGVIAYILLCGYPPFYDE-NDSKLFEQILKAEyefdSPYWDDI 248
Cdd:cd14027  156 VDGTAKKNA-GTLYYMAPEHLNDvnaKPTEKS-DVYSFAIVLWAIFANKEPYENAiNEDQIIMCIKSGN----RPDVDDI 229
                        250       260
                 ....*....|....*....|....*
gi 594150345 249 SDSAKDFIRNLM----EKDPNKRYT 269
Cdd:cd14027  230 TEYCPREIIDLMklcwEANPEARPT 254
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
21-284 3.70e-14

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: 71.68  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFA-VKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYES----PNHLY 95
Cdd:cd14031   10 RFLKFDIELGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLlyYSQDEESKIMISDFGLSKMEg 173
Cdd:cd14031   90 LVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNI--FITGPTGSVKIGDLGLATLM- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEvLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEQILKAeyeFDSPYWDDISD-S 251
Cdd:cd14031  167 RTSFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTSG---IKPASFNKVTDpE 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTA 284
Cdd:cd14031  243 VKEIIEGCIRQNKSERLSIKDLLNHAFFAEDTG 275
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
29-221 6.82e-14

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: 70.64  E-value: 6.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVlaEEKATGKLFAVKCIPKKALKGKeSSIE---NEIAVLRKIKHENIVA-----LEDiyesPNHLYLVMQL 100
Cdd:cd14064    1 IGSGSFGKVY--KGRCRNKIVAIKRYRANTYCSK-SDVDmfcREVSILCRLNHPCVIQfvgacLDD----PSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRI-VEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLLYYsqdEESKIMISDFGLSKM--EGKG 175
Cdd:cd14064   74 VSGGSLFSLLhEQKRVIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLY---EDGHAVVADFGESRFlqSLDE 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 594150345 176 DVMSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPF 221
Cdd:cd14064  151 DNMTKQPGNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPF 197
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
17-241 6.96e-14

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: 71.62  E-value: 6.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEfketLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd06650    5 DDFEKISE----LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELfDRIVEK-GFYTEKDASTLIRQVLDAVYYL-HRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMegK 174
Cdd:cd06650   81 CMEHMDGGSL-DQVLKKaGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGE---IKLCDFGVSGQ--L 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 175 GDVMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQILKAEYEFD 241
Cdd:cd06650  155 IDSMANSfVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPI-PPPDAKELELMFGCQVEGD 221
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
17-280 7.29e-14

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: 71.31  E-value: 7.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEfketLGTGAFSEVVLAEEKATGKLFAVKCIP---KKALKGKessIENEIAVLRKIKHENIVALEDIYESPNH 93
Cdd:cd06615    1 DDFEKLGE----LGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAIRNQ---IIRELKVLHECNSPYIVGFYGAFYSDGE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELfDRIVEK-GFYTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKM 171
Cdd:cd06615   74 ISICMEHMDGGSL-DQVLKKaGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGE---IKLCDFGVSGQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 egKGDVMS-TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG-YP----------PFYDENDSklfEQILKAEYE 239
Cdd:cd06615  150 --LIDSMAnSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrYPipppdakeleAMFGRPVS---EGEAKESHR 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 240 FDSPYWDD--------------------------ISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIA 280
Cdd:cd06615  225 PVSGHPPDsprpmaifelldyivnepppklpsgaFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
26-267 7.53e-14

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: 70.67  E-value: 7.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKlfAVKCIPKKALKGKESSIE-----NEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05065    9 EEVIGAGEFGEVCRGRLKLPGK--REIFVAIKTLKSGYTEKQrrdflSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGEL--FDRIVEkGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSKM--EGKGD 176
Cdd:cd05065   87 MENGALdsFLRQND-GQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSN---LVCKVSDFGLSRFleDDTSD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 177 VMSTAC---GTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQIlkaEYEFDSPYWDDISDS 251
Cdd:cd05065  163 PTYTSSlggKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWDMSNQDVINAI---EQDYRLPPPMDCPTA 239
                        250
                 ....*....|....*.
gi 594150345 252 AKDFIRNLMEKDPNKR 267
Cdd:cd05065  240 LHQLMLDCWQKDRNLR 255
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
24-223 7.93e-14

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: 71.17  E-value: 7.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVV--LAEEKATGKLFAVKCI-----PKKALKgkesSIENEIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd08216    1 ELLYEIGKCFKGGGVvhLAKHKPTNTLVAVKKInlesdSKEDLK----FLQQEILTSRQLQHPNILPYVTSFVVDNDLYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGG---ELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS-KME 172
Cdd:cd08216   77 VTPLMAYGscrDLLKTHFPEGL-PELAIAFILRDVLNALEYIHSKGYIHRSVKASHILI---SGDGKVVLSGLRYAySMV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 173 GKGDVMSTACGTPGY-------VAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 223
Cdd:cd08216  153 KHGKRQRVVHDFPKSseknlpwLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSD 212
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
7-226 9.91e-14

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: 70.83  E-value: 9.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   7 ESSSSWKKQAEDIKkifeFKETLGTGAFSEVVLAE---EKATGKLFAVKCIPKKAlkgkeSSIENEIAVLRKIKHENIVA 83
Cdd:cd14149    2 DSSYYWEIEASEVM----LSTRIGSGSFGTVYKGKwhgDVAVKILKVVDPTPEQF-----QAFRNEVAVLRKTRHVNILL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  84 LEDiYESPNHLYLVMQLVSGGELFDRI-VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIM 162
Cdd:cd14149   73 FMG-YMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVK 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 ISDFGLSKMEGK---GDVMSTACGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLCGYPPFYDEND 226
Cdd:cd14149  149 IGDFGLATVKSRwsgSQQVEQPTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHINN 218
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
6-278 1.02e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 71.99  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345   6 GESSSSWKKQAEDIK----KIFEFKETLGTGAFSEVVLAEEKATGKLFAVKcipkKALKGKESSiENEIAVLRKIKHENI 81
Cdd:PTZ00036  47 GEDEDEEKMIDNDINrspnKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIK----KVLQDPQYK-NRELLIMKNLNHINI 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  82 VALEDIYES----PNHLYLVMQLVSggELFDRIVEK--GFYTEKDAST---LIR----QVLDAVYYLHRMGIVHRDLKPE 148
Cdd:PTZ00036 122 IFLKDYYYTecfkKNEKNIFLNVVM--EFIPQTVHKymKHYARNNHALplfLVKlysyQLCRALAYIHSKFICHRDLKPQ 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 149 NLLYYSQDEESKimISDFGLSK--MEGKGDVmSTACgTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEN 225
Cdd:PTZ00036 200 NLLIDPNTHTLK--LCDFGSAKnlLAGQRSV-SYIC-SRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQS 275
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 226 DSKLFEQILKA-------EYEFDSPYWDDIS------------------DSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:PTZ00036 276 SVDQLVRIIQVlgtptedQLKEMNPNYADIKfpdvkpkdlkkvfpkgtpDDAINFISQFLKYEPLKRLNPIEALADPF 353
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
29-212 1.32e-13

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: 69.99  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVV--LAEEKATGKLFAVKCIPKKAlkgKESSIENEI----AVLRKIKHENIVALEDIYESPNhLYLVMQLVS 102
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKILKNEA---NDPALKDELlreaNVMQQLDNPYIVRMIGICEAES-WMLVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESkimISDFGLSKMEGKGDVMSTAC 182
Cdd:cd05116   79 LGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAK---ISDFGLSKALRADENYYKAQ 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 594150345 183 GTP----GYVAPEVLAQKPYSKAVDCWSIGVIAY 212
Cdd:cd05116  156 THGkwpvKWYAPECMNYYKFSSKSDVWSFGVLMW 189
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
23-272 2.09e-13

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 69.59  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAeeKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHE--NIVALEDIYESPNHLYLVMQL 100
Cdd:cd13980    2 YLYDKSLGSTRFLKVARA--RHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLLElpNVLPFQKVIETDKAAYLIRQY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VsGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFglskmegkgdvmst 180
Cdd:cd13980   80 V-KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNW---VYLTDF-------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 181 ACGTPGY----------------------VAPE------VLAQKPY------SKAVDCWSIG-VIAYILLCGYPPFydeN 225
Cdd:cd13980  142 ASFKPTYlpednpadfsyffdtsrrrtcyIAPErfvdalTLDAESErrdgelTPAMDIFSLGcVIAELFTEGRPLF---D 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 594150345 226 DSKLFEqiLKAEYEFDSPYWDDISD-SAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd13980  219 LSQLLA--YRKGEFSPEQVLEKIEDpNIRELILHMIQRDPSKRLSAED 264
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
29-272 2.14e-13

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: 69.51  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK---LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05066   12 IGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LfDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQdeeSKIMISDFGLSK-MEGKGDVMSTAC 182
Cdd:cd05066   92 L-DAFLRKhdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSN---LVCKVSDFGLSRvLEDDPEAAYTTR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 183 GTP---GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSPYwdDISDSAKDFIRN 258
Cdd:cd05066  168 GGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAIEEG-YRLPAPM--DCPAALHQLMLD 244
                        250
                 ....*....|....
gi 594150345 259 LMEKDPNKRYTCEQ 272
Cdd:cd05066  245 CWQKDRNERPKFEQ 258
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
27-223 2.18e-13

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: 69.32  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGK---LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GEL--FDRIVEKGFYTEKdASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYySQDEESKImiSDFGLSK-MEGKGDVMST 180
Cdd:cd05033   90 GSLdkFLRENDGKFTVTQ-LVGMLRGIASGMKYLSEMNYVHRDLAARNILV-NSDLVCKV--SDFGLSRrLEDSEATYTT 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 594150345 181 ACG-TP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYD 223
Cdd:cd05033  166 KGGkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSYGERPYWD 211
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
24-231 2.68e-13

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They 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 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 69.67  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAE----------------EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDI 87
Cdd:cd05051    8 EFVEKLGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMQLVSGGE----LFDRIVEKGFYTEKDASTLIRQVLdaVY----------YLHRMGIVHRDLKPENLLYy 153
Cdd:cd05051   88 CTRDEPLCMIVEYMENGDlnqfLQKHEAETQGASATNSKTLSYGTL--LYmatqiasgmkYLESLNFVHRDLATRNCLV- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 154 sqDEESKIMISDFGLS---------KMEGKGDV----MSTACgtpgyvapeVLAQKpYSKAVDCWSIGVIAY-IL-LCGY 218
Cdd:cd05051  165 --GPNYTIKIADFGMSrnlysgdyyRIEGRAVLpirwMAWES---------ILLGK-FTTKSDVWAFGVTLWeILtLCKE 232
                        250
                 ....*....|...
gi 594150345 219 PPFYDENDSKLFE 231
Cdd:cd05051  233 QPYEHLTDEQVIE 245
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
29-243 3.09e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 69.66  E-value: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK-------LFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05101   32 LGEGCFGQVVMAEAVGIDKdkpkeavTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEY 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGEL---------------FD--RIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqdEESKIM- 162
Cdd:cd05101  112 ASKGNLreylrarrppgmeysYDinRVPEEQM-TFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV----TENNVMk 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 ISDFGLSKMEGKGDVM--STACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKAEY 238
Cdd:cd05101  187 IADFGLARDINNIDYYkkTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLMWeIFTLGGSPYPGIPVEELF-KLLKEGH 265

                 ....*
gi 594150345 239 EFDSP 243
Cdd:cd05101  266 RMDKP 270
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
29-272 4.47e-13

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: 68.89  E-value: 4.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK-------LFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05098   21 LGEGCFGQVVLAEAIGLDKdkpnrvtKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRI----------------VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:cd05098  101 ASKGNLREYLqarrppgmeycynpshNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLV---TEDNVMKIA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMEGKGDVM--STACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKAEYEF 240
Cdd:cd05098  178 DFGLARDIHHIDYYkkTTNGRLPvKWMAPEALFDRIYTHQSDVWSFGVLLWeIFTLGGSPYPGVPVEELF-KLLKEGHRM 256
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 241 DSPywDDISDSAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd05098  257 DKP--SNCTNELYMMMRDCWHAVPSQRPTFKQ 286
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
61-212 4.78e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 69.92  E-value: 4.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  61 GKESSIENEIAVLRKIKHENIVALEDI-------------YESPNHLYLVMQLVSGGELfdrivekgfytekDASTLIRQ 127
Cdd:PHA03211 202 GWYASSVHEARLLRRLSHPAVLALLDVrvvggltclvlpkYRSDLYTYLGARLRPLGLA-------------QVTAVARQ 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 128 VLDAVYYLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMeGKGDVMSTA----CGTPGYVAPEVLAQKPYSKAVD 203
Cdd:PHA03211 269 LLSAIDYIHGEGIIHRDIKTENVLVNGPED---ICLGDFGAACF-ARGSWSTPFhygiAGTVDTNAPEVLAGDPYTPSVD 344

                 ....*....
gi 594150345 204 CWSIGVIAY 212
Cdd:PHA03211 345 IWSAGLVIF 353
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
20-240 4.93e-13

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) 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 DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 68.87  E-value: 4.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEVVLAE----EKATGK------------LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVA 83
Cdd:cd05095    4 RKLLTFKEKLGEGQFGEVHLCEaegmEKFMDKdfalevsenqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  84 LEDIYESPNHLYLVMQLVSGGELFDRI----VEKGFYTEKDAST--------LIRQVLDAVYYLHRMGIVHRDLKPENLL 151
Cdd:cd05095   84 LLAVCITDDPLCMITEYMENGDLNQFLsrqqPEGQLALPSNALTvsysdlrfMAAQIASGMKYLSSLNFVHRDLATRNCL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 152 YysqDEESKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY--ILLCGYPPFYDEND 226
Cdd:cd05095  164 V---GKNYTIKIADFGMSRNLYSGDyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetLTFCREQPYSQLSD 240
                        250
                 ....*....|....
gi 594150345 227 sklfEQILKAEYEF 240
Cdd:cd05095  241 ----EQVIENTGEF 250
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
21-284 5.22e-13

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: 68.18  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLAEEKATGKLFA-VKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH----LY 95
Cdd:cd14032    1 RFLKFDIELGRGSFKTVYKGLDTETWVEVAwCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLlyYSQDEESKIMISDFGLSKMEg 173
Cdd:cd14032   81 LVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNI--FITGPTGSVKIGDLGLATLK- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEvLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEQILKAeyeFDSPYWDDISD-S 251
Cdd:cd14032  158 RASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRKVTCG---IKPASFEKVTDpE 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTA 284
Cdd:cd14032  234 IKEIIGECICKNKEERYEIKDLLSHAFFAEDTG 266
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
23-271 5.58e-13

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: 68.56  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALEDIYeSPNHLYLVMQLVS 102
Cdd:cd05070   11 LQLIKRLGNGQFGEVWMGTWNGNTKV-AIKTL-KPGTMSPESFLE-EAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGELFDRIVEKGFYTEK--DASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM-EGKGDVMS 179
Cdd:cd05070   87 KGSLLDFLKDGEGRALKlpNLVDMAAQVAAGMAYIERMNYIHRDLRSANILV---GNGLICKIADFGLARLiEDNEYTAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 180 TACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPFYDENDSKLFEQIlkaEYEFDSPYWDDISDSAKDFIR 257
Cdd:cd05070  164 QGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV---ERGYRMPCPQDCPISLHELMI 240
                        250
                 ....*....|....
gi 594150345 258 NLMEKDPNKRYTCE 271
Cdd:cd05070  241 HCWKKDPEERPTFE 254
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
49-225 6.01e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 69.25  E-value: 6.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  49 FAVKCIPKKALK------GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGgELFDRIVEKGFYTEKDAS 122
Cdd:PHA03212 107 FAFACIDNKTCEhvvikaGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDIL 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 123 TLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLS--KMEGKGDVMSTACGTPGYVAPEVLAQKPYSK 200
Cdd:PHA03212 186 AIERSVLRAIQYLHENRIIHRDIKAENIFI---NHPGDVCLGDFGAAcfPVDINANKYYGWAGTIATNAPELLARDPYGP 262
                        170       180
                 ....*....|....*....|....*
gi 594150345 201 AVDCWSIGVIAYILLCGYPPFYDEN 225
Cdd:PHA03212 263 AVDIWSAGIVLFEMATCHDSLFEKD 287
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
24-272 6.04e-13

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: 68.67  E-value: 6.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEiAVLRKIK-------HENIVALEDIYESPNHLYL 96
Cdd:cd05055   38 SFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSERE-ALMSELKimshlgnHENIVNLLGACTIGGPILV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqdEESKIM-ISDFGLSK--M 171
Cdd:cd05055  117 ITEYCCYGDLLNFLRRKreSFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL----THGKIVkICDFGLARdiM 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 172 EGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAEYEFDSPYWddis 249
Cdd:cd05055  193 NDSNYVVKGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWeIFSLGSNPYPGMPVDSKFYKLIKEGYRMAQPEH---- 268
                        250       260
                 ....*....|....*....|....*..
gi 594150345 250 dsAKDFIRNLMEK----DPNKRYTCEQ 272
Cdd:cd05055  269 --APAEIYDIMKTcwdaDPLKRPTFKQ 293
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
25-233 8.33e-13

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: 67.58  E-value: 8.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALKgKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05114    8 FMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMS-EEDFIE-EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKGFYTEKDAS-TLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTACG 183
Cdd:cd05114   85 CLLNYLRQRRGKLSRDMLlSMCQDVCEGMEYLERNNFIHRDLAARNCLV---NDTGVVKVSDFGMTRYV-LDDQYTSSSG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 184 TP---GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05114  161 AKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMV 214
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
20-237 9.40e-13

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: 67.45  E-value: 9.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFSEV---VLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESpNHLYL 96
Cdd:cd05056    5 REDITLGRCIGEGQFGDVyqgVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITE-NPVWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELfdrivekGFYTEK-----DASTLIR---QVLDAVYYLHRMGIVHRDLKPENLLYYSQDeesKIMISDFGL 168
Cdd:cd05056   84 VMELAPLGEL-------RSYLQVnkyslDLASLILyayQLSTALAYLESKRFVHRDIAARNVLVSSPD---CVKLGDFGL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594150345 169 SK-MEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAE 237
Cdd:cd05056  154 SRyMEDESYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIENGE 225
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
29-243 1.20e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 67.68  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK-------LFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05099   20 LGEGCFGQVVRAEAYGIDKsrpdqtvTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGEL---------------FDRI-VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:cd05099  100 AAKGNLreflrarrppgpdytFDITkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLV---TEDNVMKIA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKmeGKGDVMSTACGTPG-----YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKAEY 238
Cdd:cd05099  177 DFGLAR--GVHDIDYYKKTSNGrlpvkWMAPEALFDRVYTHQSDVWSFGILMWeIFTLGGSPYPGIPVEELF-KLLREGH 253

                 ....*
gi 594150345 239 EFDSP 243
Cdd:cd05099  254 RMDKP 258
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
27-267 1.21e-12

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: 67.37  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKATGKLF--AVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFD-----RIVEK--GFYTEKD-ASTLIRQ--------VLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFG 167
Cdd:cd05047   81 GNLLDflrksRVLETdpAFAIANStASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIADFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 168 LSKMEgKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQiLKAEYEFDSPYw 245
Cdd:cd05047  158 LSRGQ-EVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEK-LPQGYRLEKPL- 234
                        250       260
                 ....*....|....*....|..
gi 594150345 246 dDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05047  235 -NCDDEVYDLMRQCWREKPYER 255
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
43-278 1.52e-12

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: 67.35  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  43 KATGK-----LFAVKCIPKKALKGKESSIE---NEIAVLRKIKHENIVALEDIY-ESPNHLYLVMQLV------------ 101
Cdd:cd14011   18 KSTKQevsvfVFEKKQLEEYSKRDREQILEllkRGVKQLTRLRHPRILTVQHPLeESRESLAFATEPVfaslanvlgerd 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 ---------SGGELFDRIVEKGFYtekdastlirQVLDAVYYLH-RMGIVHRDLKPENLLYYSQDEeSKIMISDFGLSK- 170
Cdd:cd14011   98 nmpspppelQDYKLYDVEIKYGLL----------QISEALSFLHnDVKLVHGNICPESVVINSNGE-WKLAGFDFCISSe 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 ---------MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAEYEF 240
Cdd:cd14011  167 qatdqfpyfREYDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYaIYNKGKPLFDCVNNLLSYKKNSNQLRQL 246
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 241 DSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14011  247 SLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
29-243 2.51e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 66.97  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK-------LFAVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05100   20 LGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGEL---------------FD--RIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMI 163
Cdd:cd05100  100 ASKGNLreylrarrppgmdysFDtcKLPEEQL-TFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV---TEDNVMKI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLSKMEGKGDVM--STACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQILKAEYE 239
Cdd:cd05100  176 ADFGLARDVHNIDYYkkTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPYPGIPVEELF-KLLKEGHR 254

                 ....
gi 594150345 240 FDSP 243
Cdd:cd05100  255 MDKP 258
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
17-267 3.12e-12

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: 66.56  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKkifeFKETLGTGAFSEVVLAEEKATGKLF--AVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNH 93
Cdd:cd05089    2 EDIK----FEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELFD-----RIVEK--GFYTEK-DASTLIRQVL--------DAVYYLHRMGIVHRDLKPENLLYysqDE 157
Cdd:cd05089   78 LYIAIEYAPYGNLLDflrksRVLETdpAFAKEHgTASTLTSQQLlqfasdvaKGMQYLSEKQFIHRDLAARNVLV---GE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKMEgKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQiLK 235
Cdd:cd05089  155 NLVSKIADFGLSRGE-EVYVKKTMGRLPvRWMAIESLNYSVYTTKSDVWSFGVLLWeIVSLGGTPYCGMTCAELYEK-LP 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 236 AEYEFDSPywDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05089  233 QGYRMEKP--RNCDDEVYELMRQCWRDRPYER 262
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
25-240 4.40e-12

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: 66.15  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGK--------------LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYES 90
Cdd:cd05097    9 LKEKLGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSGGELFDRIVEKGFYTE------------KDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEE 158
Cdd:cd05097   89 DDPLCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLV---GNH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 159 SKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY--ILLCGYPPFYDENDsklfEQI 233
Cdd:cd05097  166 YTIKIADFGMSRNLYSGDyyrIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWemFTLCKEQPYSLLSD----EQV 241

                 ....*..
gi 594150345 234 LKAEYEF 240
Cdd:cd05097  242 IENTGEF 248
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
25-240 4.65e-12

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) 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 DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 66.11  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAE----------------EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIY 88
Cdd:cd05096    9 FKEKLGEGQFGEVHLCEvvnpqdlptlqfpfnvRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPNHLYLVM---------QLVSGGELFDRIVEKGFYTEKDA-------STLIR---QVLDAVYYLHRMGIVHRDLKPEN 149
Cdd:cd05096   89 VDEDPLCMITeymengdlnQFLSSHHLDDKEENGNDAVPPAHclpaisySSLLHvalQIASGMKYLSSLNFVHRDLATRN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 150 LLYysqDEESKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY--ILLCGYPPFYDE 224
Cdd:cd05096  169 CLV---GENLTIKIADFGMSRNLYAGDyyrIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWeiLMLCKEQPYGEL 245
                        250
                 ....*....|....*.
gi 594150345 225 NDsklfEQILKAEYEF 240
Cdd:cd05096  246 TD----EQVIENAGEF 257
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
21-283 6.81e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 65.46  E-value: 6.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  21 KIFEFKETLGTGAFSEVVLA-EEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNH----LY 95
Cdd:cd14030   25 RFLKFDIEIGRGSFKTVYKGlDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDLKPENLlyYSQDEESKIMISDFGLSKMEg 173
Cdd:cd14030  105 LVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNI--FITGPTGSVKIGDLGLATLK- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 174 KGDVMSTACGTPGYVAPEVLAQKpYSKAVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEQILKAeyeFDSPYWDDIS-DS 251
Cdd:cd14030  182 RASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRRVTSG---VKPASFDKVAiPE 257
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 252 AKDFIRNLMEKDPNKRYTCEQAARHPWIAGDT 283
Cdd:cd14030  258 VKEIIEGCIRQNKDERYAIKDLLNHAFFQEET 289
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
29-223 8.50e-12

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: 64.94  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGK---LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGE 105
Cdd:cd05064   13 LGTGRFGELCRGCLKLPSKrelPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 106 LfDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqDEESKimISDFGLSKMEGKGDVMSTACG 183
Cdd:cd05064   93 L-DSFLRKheGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNS-DLVCK--ISGFRRLQEDKSEAIYTTMSG 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 594150345 184 TPG--YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYD 223
Cdd:cd05064  169 KSPvlWAAPEAIQYHHFSSASDVWSFGIVMWeVMSYGERPYWD 211
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
28-233 8.74e-12

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: 64.79  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  28 TLGTGAFSEVVLA-----EEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd05046   12 TLGRGEFGEVFLAkakgiEEEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYTD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GGEL--FDRIVEKGFYTEKDASTLIRQVLDAVY-------YLHRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKmeg 173
Cdd:cd05046   92 LGDLkqFLRATKSKDEKLKPPPLSTKQKVALCTqialgmdHLSNARFVHRDLAARNCLVSSQRE---VKVSLLSLSK--- 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 174 kgDVMST-------ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05046  166 --DVYNSeyyklrnALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWeVFTQGELPFYGLSDEEVLNRL 231
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
11-269 1.06e-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: 64.68  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  11 SWKKQAEDIKKIfefkETLGTGAFSEVVLAEEKATGKLfAVKcipkkALKGKESSIE---NEIAVLRKIKHENIVALEDI 87
Cdd:cd05072    1 AWEIPRESIKLV----KKLGAGQFGEVWMGYYNNSTKV-AVK-----TLKPGTMSVQaflEEANLMKTLQHDKLVRLYAV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPNHLYLVMQLVSGGELFDrivekgFYTEKDASTLI--------RQVLDAVYYLHRMGIVHRDLKPENLLYysqDEES 159
Cdd:cd05072   71 VTKEEPIYIITEYMAKGSLLD------FLKSDEGGKVLlpklidfsAQIAEGMAYIERKNYIHRDLRAANVLV---SESL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 160 KIMISDFGLSK-MEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKA 236
Cdd:cd05072  142 MCKIADFGLARvIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRG 221
                        250       260       270
                 ....*....|....*....|....*....|...
gi 594150345 237 eyeFDSPYWDDISDSAKDFIRNLMEKDPNKRYT 269
Cdd:cd05072  222 ---YRMPRMENCPDELYDIMKTCWKEKAEERPT 251
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
25-220 1.27e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 64.34  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKL----FAVKCIPKKALKGKESSIEN----EIAVLRKIKHENIVALEDIYESPN-HLY 95
Cdd:cd14001    3 FMKKLGYGTGVNVYLMKRSPRGGSsrspWAVKKINSKCDKGQRSLYQErlkeEAKILKSLNHPNIVGFRAFTKSEDgSLC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLvSGGELFDRIvEKGFYTEKD---ASTLIR---QVLDAVYYLHR-MGIVHRDLKPENLLyYSQDEESkIMISDFGL 168
Cdd:cd14001   83 LAMEY-GGKSLNDLI-EERYEAGLGpfpAATILKvalSIARALEYLHNeKKILHGDIKSGNVL-IKGDFES-VKLCDFGV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594150345 169 S-----KMEGKGDVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPP 220
Cdd:cd14001  159 SlplteNLEVDSDPKAQYVGTEPWKAKEALeEGGVITDKADIFAYGLVLWEMMTLSVP 216
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
128-267 1.72e-11

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 63.66  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 128 VLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEGkgdVMS-TACGTPGYVAPEVLAQKpYSKAVDCWS 206
Cdd:cd13975  111 VVEGIRFLHSQGLVHRDIKLKNVLL---DKKNRAKITDLGFCKPEA---MMSgSIVGTPIHMAPELFSGK-YDNSVDVYA 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 207 IGVIAYILLCGY---PPFYDENDSK--LFEQILKAEYEFDSPYWDDISdsakdfiRNLMEK----DPNKR 267
Cdd:cd13975  184 FGILFWYLCAGHvklPEAFEQCASKdhLWNNVRKGVRPERLPVFDEEC-------WNLMEAcwsgDPSQR 246
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
17-234 2.10e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 64.30  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDIKKIFEfketLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYL 96
Cdd:cd06649    5 DDFERISE----LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYL-HRMGIVHRDLKPENLLYYSQDEeskIMISDFGLSKMegKG 175
Cdd:cd06649   81 CMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGE---IKLCDFGVSGQ--LI 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 176 DVMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFyDENDSKLFEQIL 234
Cdd:cd06649  156 DSMANSfVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPI-PPPDAKELEAIF 214
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
32-267 3.13e-11

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: 62.95  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  32 GAFSEVVLAEEKATGKLFAVKCIPKKALKGKESsieneiavLRKIKH--ENIVALEDIYESPNHLYLVMQLVSGGELFDR 109
Cdd:cd05576   10 GVIDKVLLVMDTRTQETFILKGLRKSSEYSRER--------KTIIPRcvPNMVCLRKYIISEESVFLVLQHAEGGKLWSY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 110 IVEkgFYTEKDASTLIRQ------------------------VLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISD 165
Cdd:cd05576   82 LSK--FLNDKEIHQLFADlderlaaasrfyipeeciqrwaaeMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLTY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FG-LSKMEGK--GDVMSTAcgtpgYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPfydendSKLFEQILKAEYEFDS 242
Cdd:cd05576  157 FSrWSEVEDScdSDAIENM-----YCAPEVGGISEETEACDWWSLGALLFELLTGKAL------VECHPAGINTHTTLNI 225
                        250       260
                 ....*....|....*....|....*
gi 594150345 243 PYWddISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05576  226 PEW--VSEEARSLLQQLLQFNPTER 248
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
24-277 3.60e-11

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: 62.81  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKE--TLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGK--ESSIENEI---AVLRKikHENIVALEDIYESPNHLYL 96
Cdd:cd14051    1 EFHEveKIGSGEFGSVYKCINRLDGCVYAIK-KSKKPVAGSvdEQNALNEVyahAVLGK--HPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQLVSGGELFDRIVEK----GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLL-----------------YYSQ 155
Cdd:cd14051   78 QNEYCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFisrtpnpvsseeeeedfEGEE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 156 DEESKIMIsdfgLSKMEGKGDVMSTAC-----GTPGYVAPEVLaQKPYS---KAvDCWSIGVIAYILLCGYP-PfydEND 226
Cdd:cd14051  158 DNPESNEV----TYKIGDLGHVTSISNpqveeGDCRFLANEIL-QENYShlpKA-DIFALALTVYEAAGGGPlP---KNG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 227 SKlFEQILKAEYefdsPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14051  229 DE-WHEIRQGNL----PPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
29-209 4.52e-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: 62.66  E-value: 4.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCipkKALK-GKESSIENEIAVLRKIKHE----NIVALEDIYESPNhLYLVMQLVSG 103
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKQIDVAI---KVLKqGNEKAVRDEMMREAQIMHQldnpYIVRMIGVCEAEA-LMLVMEMASG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELFDRIV-EKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESkimISDFGLSKMEGKGDVMSTAc 182
Cdd:cd05115   88 GPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAK---ISDFGLSKALGADDSYYKA- 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 594150345 183 GTPG-----YVAPEVLAQKPYSKAVDCWSIGV 209
Cdd:cd05115  164 RSAGkwplkWYAPECINFRKFSSRSDVWSYGV 195
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
29-279 5.32e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 63.13  E-value: 5.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIEnEIAVLRKIKH--------ENIVALEDIYE----SPNHLYL 96
Cdd:cd14216   18 LGWGHFSTVWLSWDIQGKRFVAMKVV-KSAEHYTETALD-EIKLLKSVRNsdpndpnrEMVVQLLDDFKisgvNGTHICM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  97 VMQlVSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYYSQD----------------- 156
Cdd:cd14216   96 VFE-VLGHHLLKWIIKSNYqgLPLPCVKKIIRQVLQGLDYLHtKCRIIHTDIKPENILLSVNEqyirrlaaeatewqrnf 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 157 ----------EESKIMISDFGLSKMEGKGdvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG---YPPFYD 223
Cdd:cd14216  175 lvnplepknaEKLKVKIADLGNACWVHKH--FTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGdylFEPHSG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 224 ENDSK----------------------------------------------LFEqILKAEYEFDspywDDISDSAKDFIR 257
Cdd:cd14216  253 EDYSRdedhialiiellgkvprklivagkyskefftkkgdlkhitklkpwgLFE-VLVEKYEWS----QEEAAGFTDFLL 327
                        330       340
                 ....*....|....*....|..
gi 594150345 258 NLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14216  328 PMLELIPEKRATAAECLRHPWL 349
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
29-271 5.84e-11

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: 62.40  E-value: 5.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALEDIYeSPNHLYLVMQLVSGGELFD 108
Cdd:cd05071   17 LGQGCFGEVWMGTWNGTTRV-AIKTL-KPGTMSPEAFLQ-EAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSKGSLLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 rivekgfYTEKDASTLIR---------QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKM-EGKGDVM 178
Cdd:cd05071   93 -------FLKGEMGKYLRlpqlvdmaaQIASGMAYVERMNYVHRDLRAANILV---GENLVCKVADFGLARLiEDNEYTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 179 STACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPFYDENDSKLFEQIlkaEYEFDSPYWDDISDSAKDFI 256
Cdd:cd05071  163 RQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQV---ERGYRMPCPPECPESLHDLM 239
                        250
                 ....*....|....*
gi 594150345 257 RNLMEKDPNKRYTCE 271
Cdd:cd05071  240 CQCWRKEPEERPTFE 254
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
123-278 6.83e-11

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 62.46  E-value: 6.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 123 TLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMisDFGLSK--MEGKGDVMSTACGTPGYVAPE--VLAQ--- 195
Cdd:cd14013  124 SIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQFKII--DLGAAAdlRIGINYIPKEFLLDPRYAPPEqyIMSTqtp 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 196 KPYSKAV-----------------DCWSIGVIayILLCGYPPFYDENDSKLFEQILKaEYEFDSPYWD------------ 246
Cdd:cd14013  202 SAPPAPVaaalspvlwqmnlpdrfDMYSAGVI--LLQMAFPNLRSDSNLIAFNRQLK-QCDYDLNAWRmlveprasadlr 278
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 594150345 247 ------DISDSAK-DFIRNLMEKDPNKRYTCEQAARHPW 278
Cdd:cd14013  279 egfeilDLDDGAGwDLVTKLIRYKPRGRLSASAALAHPY 317
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
25-233 8.18e-11

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: 62.10  E-value: 8.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAE-----EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05049    9 LKRELGEGAFGKVFLGEcynlePEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGEL--FDRI------------VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISD 165
Cdd:cd05049   89 YMEHGDLnkFLRShgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLV---GTNLVVKIGD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594150345 166 FGLSKmegkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05049  166 FGMSR-----DIYSTDYYRVGghtmlpirWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQLSNTEVIECI 237
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
25-267 1.14e-10

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: 61.52  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAE-----EKATGKLFAVKCIpKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05092    9 LKWELGEGAFGKVFLAEchnllPEQDKMLVAVKAL-KEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGEL--FDR-------IVEKGFYTEKDASTLIR------QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:cd05092   88 YMRHGDLnrFLRshgpdakILDGGEGQAPGQLTLGQmlqiasQIASGMVYLASLHFVHRDLATRNCLV---GQGLVVKIG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKmegkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILK 235
Cdd:cd05092  165 DFGMSR-----DIYSTDYYRVGgrtmlpirWMPPESILYRKFTTESDIWSFGVVLWeIFTYGKQPWYQLSNTEAIECITQ 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 594150345 236 AEyEFDSPywDDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd05092  240 GR-ELERP--RTCPPEVYAIMQGCWQREPQQR 268
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
25-233 1.15e-10

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: 61.43  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGG 104
Cdd:cd05113    8 FLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSMS--EDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 105 ELFDRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTACG 183
Cdd:cd05113   85 CLLNYLREMRkRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLV---NDQGVVKVSDFGLSRYV-LDDEYTSSVG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 594150345 184 TPGYV---APEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05113  161 SKFPVrwsPPEVLMYSKFSSKSDVWAFGVLMWeVYSLGKMPYERFTNSETVEHV 214
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
20-237 1.41e-10

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: 61.47  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKETLGTGAFS---EVVLAEEKATGKLFAVKCIpkKALKGKESSIEN---EIAVLRKIKHENIVALEDIY---ES 90
Cdd:cd05074    8 EQQFTLGRMLGKGEFGsvrEAQLKSEDGSFQKVAVKML--KADIFSSSDIEEflrEAACMKEFDHPNVIKLIGVSlrsRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHL---YLVMQLVSGGEL-----FDRIVEKGFYTEKdaSTLIRQVLD---AVYYLHRMGIVHRDLKPENLLYysqDEES 159
Cdd:cd05074   86 KGRLpipMVILPFMKHGDLhtfllMSRIGEEPFTLPL--QTLVRFMIDiasGMEYLSSKNFIHRDLAARNCML---NENM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 160 KIMISDFGLSKMEGKGDVMSTACGTP---GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILK 235
Cdd:cd05074  161 TVCVADFGLSKKIYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWeIMTRGQTPYAGVENSEIYNYLIK 240

                 ..
gi 594150345 236 AE 237
Cdd:cd05074  241 GN 242
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
24-235 3.11e-10

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: 60.65  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTG--AFSEVVLAEEKATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd08226    1 ELQVELGKGfcNLTSVYLARHTPTGTLVTVKITNLDNCSEEHlKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELfdRIVEKGFYTEKDASTLIRQVL----DAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDF-GLSKMEGKG 175
Cdd:cd08226   81 MAYGSA--RGLLKTYFPEGMNEALIGNILygaiKALNYLHQNGCIHRSVKASHILI---SGDGLVSLSGLsHLYSMVTNG 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 176 DVMSTACGTPGY-------VAPEVLAQKPYSKAV--DCWSIGVIAYILLCGYPPFYDENDSKLFEQILK 235
Cdd:cd08226  156 QRSKVVYDFPQFstsvlpwLSPELLRQDLHGYNVksDIYSVGITACELARGQVPFQDMRRTQMLLQKLK 224
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
29-271 3.80e-10

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: 59.60  E-value: 3.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLfAVKCIpKKALKGKESSIEnEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFD 108
Cdd:cd05034    3 LGAGQFGEVWMGVWNGTTKV-AVKTL-KPGTMSPEAFLQ-EAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 109 --RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDFGLSKMEgKGDVMSTACGT-- 184
Cdd:cd05034   80 ylRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILV---GENNVCKVADFGLARLI-EDDEYTAREGAkf 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 185 P-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAeYEFDSPywDDISDSAKDFIRNLMEK 262
Cdd:cd05034  156 PiKWTAPEAALYGRFTIKSDVWSFGILLYeIVTYGRVPYPGMTNREVLEQVERG-YRMPKP--PGCPDELYDIMLQCWKK 232

                 ....*....
gi 594150345 263 DPNKRYTCE 271
Cdd:cd05034  233 EPEERPTFE 241
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
24-272 4.22e-10

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: 60.01  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAEEKATGKLF--AVKCIPKKALKGKESSIENEIAVLRKI-KHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05088   10 KFQDVIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFD-----RIVEKG---FYTEKDASTLIRQ--------VLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMIS 164
Cdd:cd05088   90 APHGNLLDflrksRVLETDpafAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV---GENYVAKIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKMEgKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQiLKAEYEFDS 242
Cdd:cd05088  167 DFGLSRGQ-EVYVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWeIVSLGGTPYCGMTCAELYEK-LPQGYRLEK 244
                        250       260       270
                 ....*....|....*....|....*....|
gi 594150345 243 PYwdDISDSAKDFIRNLMEKDPNKRYTCEQ 272
Cdd:cd05088  245 PL--NCDDEVYDLMRQCWREKPYERPSFAQ 272
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
29-223 4.48e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 59.93  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKC--IPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 106
Cdd:cd14026    5 LSRGAFGTVSRARHADWRVTVAIKClkLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 107 FDRIVEKGFYTEKDASTLIR---QVLDAVYYLHRMG--IVHRDLKPENLLYysqDEESKIMISDFGLSK------MEGKG 175
Cdd:cd14026   85 NELLHEKDIYPDVAWPLRLRilyEIALGVNYLHNMSppLLHHDLKTQNILL---DGEFHVKIADFGLSKwrqlsiSQSRS 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 594150345 176 DVMSTACGTPGYVAPEVLAQKPYSKAV---DCWSIGVIAYILLCGYPPFYD 223
Cdd:cd14026  162 SKSAPEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPFEE 212
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
25-236 5.34e-10

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: 59.67  E-value: 5.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAE-----EKATGKLFAVKCIpKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 99
Cdd:cd05093    9 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGEL--FDR--------IVEKGFYTEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISDF 166
Cdd:cd05093   88 YMKHGDLnkFLRahgpdavlMAEGNRPAELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDF 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 167 GLSKmegkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKA 236
Cdd:cd05093  165 GMSR-----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 238
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
23-277 6.26e-10

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: 59.27  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEVVLAEEKATGKLFAVKcIPKKALKGkesSIENEIAvLRKI-------KHENIVALEDIYESPNHLY 95
Cdd:cd14138    7 FHELEKIGSGEFGSVFKCVKRLDGCIYAIK-RSKKPLAG---SVDEQNA-LREVyahavlgQHSHVVRYYSAWAEDDHML 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  96 LVMQLVSGGELFDRIVEK----GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYY--------SQDEESKIMI 163
Cdd:cd14138   82 IQNEYCNGGSLADAISENyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaSEEGDEDEWA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLSKMEGKGDVMSTAC-----GTPGYVAPEVLaQKPYS---KAvdcwSIGVIAYILLC--GYPPFYDENDS------ 227
Cdd:cd14138  162 SNKVIFKIGDLGHVTRVSSpqveeGDSRFLANEVL-QENYThlpKA----DIFALALTVVCaaGAEPLPTNGDQwheirq 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 228 -KL--FEQILKAEYefdspywddisdsaKDFIRNLMEKDPNKRYTCEQAARHP 277
Cdd:cd14138  237 gKLprIPQVLSQEF--------------LDLLKVMIHPDPERRPSAVALVKHS 275
PTZ00284 PTZ00284
protein kinase; Provisional
17-279 9.24e-10

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 59.98  E-value: 9.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  17 EDI---KKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALKGKESSIEneIAVLRKIKHEN------IVALEDI 87
Cdd:PTZ00284 122 EDIdvsTQRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIE--IQFMEKVRQADpadrfpLMKIQRY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  88 YESPN-HLYLVMQLVsGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYYSQD--------- 156
Cdd:PTZ00284 200 FQNETgHMCIVMPKY-GPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHtELHLMHTDLKPENILMETSDtvvdpvtnr 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 157 ----EESKIMISDFG--LSKMEGKGDVMSTAcgtpGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGyPPFYDENDS--- 227
Cdd:PTZ00284 279 alppDPCRVRICDLGgcCDERHSRTAIVSTR----HYRSPEVVLGLGWMYSTDMWSMGCIIYELYTG-KLLYDTHDNleh 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 228 -KLFEQIL--------------KAEYEFDS--------------------PYWDDISDSAK-DFIRNLMEKDPNKRYTCE 271
Cdd:PTZ00284 354 lHLMEKTLgrlpsewagrcgteEARLLYNSagqlrpctdpkhlariararPVREVIRDDLLcDLIYGLLHYDRQKRLNAR 433

                 ....*...
gi 594150345 272 QAARHPWI 279
Cdd:PTZ00284 434 QMTTHPYV 441
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
26-267 1.42e-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: 58.53  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  26 KETLGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESS---IENEiAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 102
Cdd:cd06616   11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRI-RSTVDEKEQKrllMDLD-VVMRSSDCPYIVKFYGALFREGDCWICMELMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 103 GG-ELFDRIV---EKGFYTEKDASTLIRQVLDAVYYLHR-MGIVHRDLKPENLLYysqDEESKIMISDFGLSkmeGKgDV 177
Cdd:cd06616   89 ISlDKFYKYVyevLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILL---DRNGNIKLCDFGIS---GQ-LV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 178 MSTA----CGTPGYVAPEVL----AQKPYSKAVDCWSIGVIAYILLCGYPPfYDENDSkLFEQILKAEY----EFDSPYW 245
Cdd:cd06616  162 DSIAktrdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFP-YPKWNS-VFDQLTQVVKgdppILSNSEE 239
                        250       260
                 ....*....|....*....|..
gi 594150345 246 DDISDSAKDFIRNLMEKDPNKR 267
Cdd:cd06616  240 REFSPSFVNFVNLCLIKDESKR 261
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
25-237 1.54e-09

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 58.10  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKETLGTGAFSEVVLAEEKATG----KLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 100
Cdd:cd05090    9 FMEELGECAFGKIYKGHLYLPGmdhaQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 101 VSGGELFDRIVEKGFYTE----KDASTLIRQVLDAVYYLHrMGI--------------VHRDLKPENLLYysqDEESKIM 162
Cdd:cd05090   89 MNQGDLHEFLIMRSPHSDvgcsSDEDGTVKSSLDHGDFLH-IAIqiaagmeylsshffVHKDLAARNILV---GEQLHVK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594150345 163 ISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKAE 237
Cdd:cd05090  165 ISDLGLSREIYSSDyyrVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRKRQ 243
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
27-224 1.85e-09

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: 57.83  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKatGKLFAVKCIPkkaLKGKESSI-ENEIAVLRKIKHENIVALEDIYESPNH----LYLVMQLV 101
Cdd:cd13998    1 EVIGKGRFGEVWKASLK--NEPVAVKIFS---SRDKQSWFrEKEIYRTPMLKHENILQFIAADERDTAlrteLWLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 102 SGGELFDrivekgfYTEKDAST---LIRQVLDA---VYYLH---------RMGIVHRDLKPENLLYYSqdeESKIMISDF 166
Cdd:cd13998   76 PNGSL*D-------YLSLHTIDwvsLCRLALSVargLAHLHseipgctqgKPAIAHRDLKSKNILVKN---DGTCCIADF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 167 GLSKM----EGKGDVM-STACGTPGYVAPEVLA-----QKPYS-KAVDCWSIGVIAY-------ILLCGY----PPFYDE 224
Cdd:cd13998  146 GLAVRlspsTGEEDNAnNGQVGTKRYMAPEVLEgainlRDFESfKRVDIYAMGLVLWemasrctDLFGIVeeykPPFYSE 225
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
23-243 2.20e-09

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: 57.85  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  23 FEFKETLGTGAFSEV---VLAEEKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENI-----VALEDiYESPNHL 94
Cdd:cd05043    8 VTLSDLLQEGTFGRIfhgILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLlpilhVCIED-GEKPMVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQlVSGGELFDRIVEkgfYTEKDASTLIR---------QVLDAVYYLHRMGIVHRDLKPENLLYysqDEESKIMISD 165
Cdd:cd05043   87 YPYMN-WGNLKLFLQQCR---LSEANNPQALStqqlvhmalQIACGMSYLHRRGVIHKDIAARNCVI---DDELQVKITD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 166 FGLSKmegkgDV--MSTACGTPG------YVAPEVLAQKPYSKAVDCWSIGVIAYIL--LCGYPpfYDENDSKLFEQILK 235
Cdd:cd05043  160 NALSR-----DLfpMDYHCLGDNenrpikWMSLESLVNKEYSSASDVWSFGVLLWELmtLGQTP--YVEIDPFEMAAYLK 232

                 ....*...
gi 594150345 236 AEYEFDSP 243
Cdd:cd05043  233 DGYRLAQP 240
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
24-233 3.12e-09

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: 57.39  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  24 EFKETLGTGAFSEVVLAE-----EKATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDI--YESPN---- 92
Cdd:cd05048    8 RFLEELGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVctKEQPQcmlf 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  93 --------HLYLVMQ-------LVSGGELFDRIVEKGfytekDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdE 157
Cdd:cd05048   88 eymahgdlHEFLVRHsphsdvgVSSDDDGTASSLDQS-----DFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVG---D 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 158 ESKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQI 233
Cdd:cd05048  160 GLTVKISDFGLSRDIYSSDyyrVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWeIFSYGLQPYYGYSNQEVIEMI 239
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
29-221 7.10e-09

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: 56.24  E-value: 7.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEV----VLAEEKATGKL-FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 103
Cdd:cd05036   14 LGQGAFGEVyegtVSGMPGDPSPLqVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 104 GELfdriveKGFYTE-------------KDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSK 170
Cdd:cd05036   94 GDL------KSFLREnrprpeqpssltmLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKIGDFGMAR 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 171 megkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 221
Cdd:cd05036  168 -----DIYRADYYRKGgkamlpvkWMPPEAFLDGIFTSKTDVWSFGVLLWeIFSLGYMPY 222
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
12-271 9.04e-09

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: 55.80  E-value: 9.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  12 WKKQAEDI-KKIFEFKETLGTGAFSEVVLAEEKATGKLfAVKCIPKKALKgkESSIENEIAVLRKIKHENIVALEDIYeS 90
Cdd:cd05073    1 WEKDAWEIpRESLKLEKKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSMS--VEAFLAEANVMKTLQHDKLVKLHAVV-T 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  91 PNHLYLVMQLVSGGELFDRI-VEKGfyTEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYysqdeeSKIM---I 163
Cdd:cd05073   77 KEPIYIITEFMAKGSLLDFLkSDEG--SKQPLPKLIdfsAQIAEGMAFIEQRNYIHRDLRAANILV------SASLvckI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 164 SDFGLSK-MEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGV-IAYILLCGYPPFYDENDSklfEQILKAEYEF 240
Cdd:cd05073  149 ADFGLARvIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPYPGMSNP---EVIRALERGY 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 594150345 241 DSPYWDDISDSAKDFIRNLMEKDPNKRYTCE 271
Cdd:cd05073  226 RMPRPENCPEELYNIMMRCWKNRPEERPTFE 256
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
29-279 1.19e-08

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 56.18  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  29 LGTGAFSEVVLAEEKATGKLFAVKCIpKKALKGKESSIEnEIAVLRKI--------KHENIVALEDIYE--SPNHLYLVM 98
Cdd:cd14218   18 LGWGHFSTVWLCWDIQRKRFVALKVV-KSAVHYTETAVD-EIKLLKCVrdsdpsdpKRETIVQLIDDFKisGVNGVHVCM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  99 QL-VSGGELFDRIVEKGF--YTEKDASTLIRQVLDAVYYLH-RMGIVHRDLKPENLLYYSQD-------EESKIM----- 162
Cdd:cd14218   96 VLeVLGHQLLKWIIKSNYqgLPLPCVKSILRQVLQGLDYLHtKCKIIHTDIKPENILMCVDEgyvrrlaAEATIWqqaga 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 163 -----------ISDFGLSKMEGK-GDVMS-------TAC----------GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYI 213
Cdd:cd14218  176 pppsgssvsfgASDFLVNPLEPQnADKIRvkiadlgNACwvhkhftediQTRQYRALEVLIGAEYGTPADIWSTACMAFE 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 214 LLCG---YPPFYDENDSK----------------------------------------------LFEqILKAEYEfdspy 244
Cdd:cd14218  256 LATGdylFEPHSGEDYTRdedhiahivellgdipphfalsgrysreyfnrrgelrhiknlkhwgLYE-VLVEKYE----- 329
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 594150345 245 WD-DISDSAKDFIRNLMEKDPNKRYTCEQAARHPWI 279
Cdd:cd14218  330 WPlEQAAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
15-212 1.23e-08

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: 55.49  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  15 QAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLfAVKCI------PKKALKgkessienEIAVLRKIKHENIVALEDIY 88
Cdd:cd05068    2 QWEIDRKSLKLLRKLGSGQFGEVWEGLWNNTTPV-AVKTLkpgtmdPEDFLR--------EAQIMKKLRHPKLIQLYAVC 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  89 ESPNHLYLVMQLVSGGELFDrivekgfYTEKDASTL-IRQVLD-------AVYYLHRMGIVHRDLKPENLLYysqDEESK 160
Cdd:cd05068   73 TLEEPIYIITELMKHGSLLE-------YLQGKGRSLqLPQLIDmaaqvasGMAYLESQNYIHRDLAARNVLV---GENNI 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 594150345 161 IMISDFGLSKMEGKGDVMSTACGTP---GYVAPEVLAQKPYSKAVDCWSIGVIAY 212
Cdd:cd05068  143 CKVADFGLARVIKVEDEYEAREGAKfpiKWTAPEAANYNRFSIKSDVWSFGILLT 197
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
25-221 1.40e-08

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 55.35  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  25 FKET-------LGTGAFSEV---VLAEEKATGKL-FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNh 93
Cdd:cd05111    4 FKETelrklkvLGSGVFGTVhkgIWIPEGDSIKIpVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGAS- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  94 LYLVMQLVSGGELFDRIVE-KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSqdeESKIMISDFGLSKM- 171
Cdd:cd05111   83 LQLVTQLLPLGSLLDHVRQhRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKS---PSQVQVADFGVADLl 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 172 --EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLC-GYPPF 221
Cdd:cd05111  160 ypDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPY 212
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
27-210 1.93e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 54.97  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  27 ETLGTGAFSEVVLAEEKatGKLFAVKCIPKKalkgKESSIENE--IAVLRKIKHENI---VAlEDIY--ESPNHLYLVMQ 99
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSR----DEDSWFREteIYQTVMLRHENIlgfIA-ADIKstGSWTQLWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 100 LVSGGELFDRIVekgfYTEKDASTLIRQVLDAV---YYLH--------RMGIVHRDLKPENLLYYSqdeESKIMISDFGL 168
Cdd:cd14056   74 YHEHGSLYDYLQ----RNTLDTEEALRLAYSAAsglAHLHteivgtqgKPAIAHRDLKSKNILVKR---DGTCCIADLGL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 594150345 169 S--KMEGKGDV---MSTACGTPGYVAPEVLAQK--PYS----KAVDCWSIGVI 210
Cdd:cd14056  147 AvrYDSDTNTIdipPNPRVGTKRYMAPEVLDDSinPKSfesfKMADIYSFGLV 199
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
37-223 2.35e-08

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: 54.95  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  37 VVLAEEKATGKLFAVKCIPKKALKGKESS-IENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGF 115
Cdd:cd08227   16 VNLARYKPTGEYVTVRRINLEACTNEMVTfLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 116 --YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyYSQDeeSKIMISDF-GLSKMEGKGDVMSTACGTPGY----- 187
Cdd:cd08227   96 dgMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL-ISVD--GKVYLSGLrSNLSMINHGQRLRVVHDFPKYsvkvl 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 594150345 188 --VAPEVLAQ--KPYSKAVDCWSIGVIAYILLCGYPPFYD 223
Cdd:cd08227  173 pwLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFKD 212
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
20-269 2.82e-08

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 54.59  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  20 KKIFEFKEtLGTGAFSEVV--LAEEKATGKL---FAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHL 94
Cdd:cd05061    6 EKITLLRE-LGQGSFGMVYegNARDIIKGEAetrVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345  95 YLVMQLVSGGEL--FDRIVE--------KGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYsqdEESKIMIS 164
Cdd:cd05061   85 LVVMELMAHGDLksYLRSLRpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVA---HDFTVKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150345 165 DFGLSKmegkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDsklfEQILK 235
Cdd:cd05061  162 DFGMTR-----DIYETDYYRKGgkgllpvrWMAPESLKDGVFTTSSDMWSFGVVLWeITSLAEQPYQGLSN----EQVLK 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 594150345 236 aeYEFDSPYWDDiSDSAKDFIRNLM----EKDPNKRYT 269
Cdd:cd05061  233 --FVMDGGYLDQ-PDNCPERVTDLMrmcwQFNPKMRPT 267
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH