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Conserved domains on  [gi|38787904|ref|NP_060063|]
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BMP-2-inducible protein kinase isoform b [Homo sapiens]

Protein Classification

Ark/Prk/Nak family serine/threonine-protein kinase( domain architecture ID 10197152)

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

CATH:  1.10.510.10
EC:  2.7.11.-
Gene Ontology:  GO:0004674|GO:0006468|GO:0005524
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
47-320 0e+00

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: 554.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  47 GRHQVTLEESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWE 125
Cdd:cd14037   1 GSHHVTIEKYLAEGGFAHVYLVKTSnGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSANRSGNGVYE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd14037  81 VLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQK-DGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-QVAICDGNFTIPDN 283
Cdd:cd14037 161 ILPPQTkQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPFEESgQLAILNGNFTFPDN 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd14037 241 SRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELAG 277
 
Name Accession Description Interval E-value
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
47-320 0e+00

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: 554.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  47 GRHQVTLEESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWE 125
Cdd:cd14037   1 GSHHVTIEKYLAEGGFAHVYLVKTSnGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSANRSGNGVYE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd14037  81 VLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQK-DGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-QVAICDGNFTIPDN 283
Cdd:cd14037 161 ILPPQTkQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPFEESgQLAILNGNFTFPDN 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd14037 241 SRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELAG 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
52-311 1.36e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 184.27  E-value: 1.36e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904     52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMP-DLNVCKREITIMKELsGHKNIVGYLDCAVNSisDNVWevlIL 129
Cdd:smart00220   2 EILEKLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKkDRERILREIKILKKL-KHPNIVRLYDVFEDE--DKLY---LV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    130 MEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNP 209
Cdd:smart00220  76 MEYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLADFGLA--RQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    210 qkdgvnvvEEEIKKYT-TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVA-----ICDGNFTIP- 281
Cdd:smart00220 150 --------GEKLTTFVgTPEYMAPEVLL---GKGYGKAVDIWSLGVILYELLTGKPPFpGDDQLLelfkkIGKPKPPFPp 218
                          250       260       270
                   ....*....|....*....|....*....|
gi 38787904    282 DNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:smart00220 219 PEWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
52-415 1.94e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.15  E-value: 1.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKR---EITIMKELSgHKNIVGYLDCAVNSisDNVWevl 127
Cdd:COG0515  10 RILRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARERfrrEARALARLN-HPNIVRVYDVGEED--GRPY--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAG---QVVNQmnkklQTGFTEPEVLQIFCDTCEAVARLHQCktPIIHRDLKVENILLNDGGNYVLCDFGSATn 204
Cdd:COG0515  84 LVMEYVEGEslaDLLRR-----RGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDFGIAR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpQKDGVNVVEEEIKKYtTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICDGNFTIP-- 281
Cdd:COG0515 156 -----ALGGATLTQTGTVVG-TPGYMAPEQAR---GEPVDPRSDVYSLGVTLYELLTGRPPFdGDSPAELLRAHLREPpp 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 282 ----DNSRYSRNIHCLIRFMLEPDPEHRPDifqvSYFAFKFAKKDCPVSNINNSSIPSALPEPMTASEAAARKSQIKARI 357
Cdd:COG0515 227 ppseLRPDLPPALDAIVLRALAKDPEERYQ----SAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 302
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 358 TDTIGPTETSIAPRQRPKANSATTATPSVLTIQSSATPVKVLAPGEFGNHRPKGALRP 415
Cdd:COG0515 303 AAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAA 360
Pkinase pfam00069
Protein kinase domain;
52-311 1.27e-23

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 99.63  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    52 TLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPD--LNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWevlI 128
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKaKHRDTGKIVAIKKIKKEKIKKkkDKNILREIKILKKLN-HPNIVRLYDAFEDK--DNLY---L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   129 LMEYCRAGQVvnqmNKKLQ--TGFTEPEVLQIFCDTCEAVARLHQCKTPIIhrdlkvenillndggnyvlcdfgsatnkf 206
Cdd:pfam00069  76 VLEYVEGGSL----FDLLSekGAFSEREAKFIMKQILEGLESGSSLTTFVG----------------------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   207 lnpqkdgvnvveeeikkytTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPFGES------QVAICDGNFTI 280
Cdd:pfam00069 123 -------------------TPWYMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFPGIngneiyELIIDQPYAFP 180
                         250       260       270
                  ....*....|....*....|....*....|.
gi 38787904   281 PDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:pfam00069 181 ELPSNLSEEAKDLLKKLLKKDPSKRLTATQA 211
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
95-310 1.69e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 83.63  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    95 EITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYCRAGQVVNQMNK--KLQTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:PTZ00266   62 EVNVMRELK-HKNIVRYIDRFLNKANQKLY---ILMEFCDAGDLSRNIQKcyKMFGKIEEHAIVDITRQLLHALAYCHNL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   173 K-----TPIIHRDLKVENILLNDGGNYV-----------------LCDFGSATNkflnpqkdgVNVVEEEIKKYTTLSYR 230
Cdd:PTZ00266  138 KdgpngERVLHRDLKPQNIFLSTGIRHIgkitaqannlngrpiakIGDFGLSKN---------IGIESMAHSCVGTPYYW 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   231 APEMInLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQvaicdgNFT-----------IPDNSRySRNIHCLIRFMLE 299
Cdd:PTZ00266  209 SPELL-LHETKSYDDKSDMWALGCIIYELCSGKTPFHKAN------NFSqliselkrgpdLPIKGK-SKELNILIKNLLN 280
                         250
                  ....*....|.
gi 38787904   300 PDPEHRPDIFQ 310
Cdd:PTZ00266  281 LSAKERPSALQ 291
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
47-273 2.46e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 66.74  E-value: 2.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   47 GRHQvtLEESLAEGGFSTVFLVR-THGGIRCALKRMYvnnmPDLnvC---------KREITIMKELSgHKNIVgyldcav 116
Cdd:NF033483   7 GRYE--IGERIGRGGMAEVYLAKdTRLDRDVAVKVLR----PDL--ArdpefvarfRREAQSAASLS-HPNIV------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  117 nSISDnVWE----VLILMEYcragqvVNQMNKK--LQTG--FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL 188
Cdd:NF033483  71 -SVYD-VGEdggiPYIVMEY------VDGRTLKdyIREHgpLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  189 NDGGNYVLCDFGSA----------TNKFLnpqkdGvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYK 258
Cdd:NF033483 141 TKDGRVKVTDFGIAralssttmtqTNSVL-----G------------TVHYLSPEQAR---GGTVDARSDIYSLGIVLYE 200
                        250
                 ....*....|....*.
gi 38787904  259 LCFFTLPF-GESQVAI 273
Cdd:NF033483 201 MLTGRPPFdGDSPVSV 216
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
127-200 9.01e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 37.96  E-value: 9.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904   127 LILMEYCRaGQVVNQMnkklqtgfTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLcDFG 200
Cdd:TIGR03724  73 TIVMEYIE-GKPLKDV--------IEENGDELAREIGRLVGKLH--KAGIVHGDLTTSNIIVRDDKVYLI-DFG 134
 
Name Accession Description Interval E-value
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
47-320 0e+00

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: 554.97  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  47 GRHQVTLEESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWE 125
Cdd:cd14037   1 GSHHVTIEKYLAEGGFAHVYLVKTSnGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSANRSGNGVYE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd14037  81 VLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLISDSGNYKLCDFGSATTK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQK-DGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-QVAICDGNFTIPDN 283
Cdd:cd14037 161 ILPPQTkQGVTYVEEDIKKYTTLQYRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPFEESgQLAILNGNFTFPDN 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd14037 241 SRYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAFELAG 277
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
48-320 2.38e-147

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: 428.29  E-value: 2.38e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEesLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISdNVWEV 126
Cdd:cd13985   1 RYQVTKQ--LGEGGFSYVYLAHDVNtGRRYALKRMYFNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSAILSSE-GRKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRaGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATN-- 204
Cdd:cd13985  78 LLLMEYCP-GSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRFKLCDFGSATTeh 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPQKDgVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-QVAICDGNFTIPDN 283
Cdd:cd13985 157 YPLERAEE-VNIIEEEIQKNTTPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESsKLAIVAGKYSIPEQ 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd13985 236 PRYSPELHDLIRHMLTPDPAERPDIFQVINIITKDTK 272
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
57-311 1.37e-68

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: 225.47  E-value: 1.37e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYldCAVNSISDNVW-----EVLILM 130
Cdd:cd14036   8 IAEGGFAFVYEAQDVGtGKEYALKRLLSNEEEKNKAIIQEINFMKKLSGHPNIVQF--CSAASIGKEESdqgqaEYLLLT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRaGQVVNQMNKKLQTGFTEPE-VLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNP 209
Cdd:cd14036  86 ELCK-GQLVDFVKKVEAPGPFSPDtVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 ------QKDGVnvVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-QVAICDGNFTIPD 282
Cdd:cd14036 165 dyswsaQKRSL--VEDEITRNTTPMYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGaKLRIINAKYTIPP 242
                       250       260
                ....*....|....*....|....*....
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14036 243 NDTQYTVFHDLIRSTLKVNPEERLSITEI 271
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
57-311 2.03e-54

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: 186.51  E-value: 2.03e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDCavnSISDNVweVLILMEYC 133
Cdd:cd08215   8 IGKGSFGSAYLVRrKSDGKLYVLKEIDLSNMSekEREEALNEVKLLSKLK-HPNIVKYYES---FEENGK--LCIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAG---QVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQ 210
Cdd:cd08215  82 DGGdlaQKIKKQKKK-GQPFPEEQILDWFVQICLALKYLHSRK--ILHRDLKTQNIFLTKDGVVKLGDFGIS--KVLEST 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 KDGVN-VVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQ----VAICDGNFTiPDNS 284
Cdd:cd08215 157 TDLAKtVV-------GTPYYLSPELCE---NKPYNYKSDIWALGCVLYELCTLKHPFeANNLpalvYKIVKGQYP-PIPS 225
                       250       260
                ....*....|....*....|....*..
gi 38787904 285 RYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08215 226 QYSSELRDLVNSMLQKDPEKRPSANEI 252
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
52-311 4.20e-54

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: 186.73  E-value: 4.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITiMKELSGHKNIVGYLDCAVNSISDNVWEVLILM 130
Cdd:cd13986   3 RIQRLLGEGGFSFVYLVEdLSTGRLYALKKILCHSKEDVKEAMREIE-NYRLFNHPNILRLLDSQIVKEAGGKKEVYLLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQCKT-PIIHRDLKVENILLNDGGNYVLCDFGSAT--NK 205
Cdd:cd13986  82 PYYKRGSLQDEIERRLVKGtfFPEDRILHIFLGICRGLKAMHEPELvPYAHRDIKPGNVLLSEDDEPILMDLGSMNpaRI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQKDGVnVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPF------GES-QVAICDGNF 278
Cdd:cd13986 162 EIEGRREAL-ALQDWAAEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFerifqkGDSlALAVLSGNY 240
                       250       260       270
                ....*....|....*....|....*....|...
gi 38787904 279 TIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd13986 241 SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDL 273
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
52-311 1.36e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 184.27  E-value: 1.36e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904     52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMP-DLNVCKREITIMKELsGHKNIVGYLDCAVNSisDNVWevlIL 129
Cdd:smart00220   2 EILEKLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKkDRERILREIKILKKL-KHPNIVRLYDVFEDE--DKLY---LV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    130 MEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNP 209
Cdd:smart00220  76 MEYCEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLADFGLA--RQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    210 qkdgvnvvEEEIKKYT-TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVA-----ICDGNFTIP- 281
Cdd:smart00220 150 --------GEKLTTFVgTPEYMAPEVLL---GKGYGKAVDIWSLGVILYELLTGKPPFpGDDQLLelfkkIGKPKPPFPp 218
                          250       260       270
                   ....*....|....*....|....*....|
gi 38787904    282 DNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:smart00220 219 PEWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
57-311 4.09e-51

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 176.31  E-value: 4.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPD-LNVCKREITIMKELSgHKNIVGYLDCavnSISDNvwEVLILMEYCR 134
Cdd:cd00180   1 LGKGSFGKVYKARdKETGKKVAVKVIPKEKLKKlLEELLREIEILKKLN-HPNIVKLYDV---FETEN--FLYLVMEYCE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQVVNQMNKKLQtGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQkdgv 214
Cdd:cd00180  75 GGSLKDLLKENKG-PLSEEEALSILRQLLSALEYLHSNG--IIHRDLKPENILLDSDGTVKLADFGLA--KDLDSD---- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 215 nvvEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLcfftlpfgesqvaicdgnftipdnsrysRNIHCLI 294
Cdd:cd00180 146 ---DSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------EELKDLI 194
                       250
                ....*....|....*..
gi 38787904 295 RFMLEPDPEHRPDIFQV 311
Cdd:cd00180 195 RRMLQYDPKKRPSAKEL 211
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
44-311 6.43e-42

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: 152.24  E-value: 6.43e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRHqvtleesLAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIV---GYL-Dca 115
Cdd:cd14007   2 FEIGKP-------LGKGKFGNVYLAREkKSGFIVALKVISKSQLQKSGLehqLRREIEIQSHLR-HPNILrlyGYFeD-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 116 vnsiSDNVWevLILmEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV 195
Cdd:cd14007  72 ----KKRIY--LIL-EYAPNGELYKELKK--QKRFDEKEAAKYIYQLALALDYLHSKN--IIHRDIKPENILLGSNGELK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 LCDFGSAtnkflnpqkdgvnVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFG----- 267
Cdd:cd14007 141 LADFGWS-------------VHAPSNRRKTfcgTLDYLPPEMVE---GKEYDYKVDIWSLGVLCYELLVGKPPFEskshq 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 38787904 268 ESQVAICDGNFTIPDN-SRYSRNihcLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14007 205 ETYKRIQNVDIKFPSSvSPEAKD---LISKLLQKDPSKRLSLEQV 246
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
51-310 6.89e-42

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: 152.36  E-value: 6.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlIL 129
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARhKKTGQIVAIKKINLESKEKKESILNEIAILKKCK-HPNIVKYYGSYL--KKDELW---IV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNP 209
Cdd:cd05122  76 MEFCSGGSLKDLLKNTNKT-LTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLTSDGEVKLIDFGLSAQ--LSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 QKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQ-------VAIcDGNFTIPD 282
Cdd:cd05122 151 GKTRNTFV-------GTPYWMAPEVIQ---GKPYGFKADIWSLGITAIEMAEGKPPYSELPpmkalflIAT-NGPPGLRN 219
                       250       260
                ....*....|....*....|....*...
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd05122 220 PKKWSKEFKDFLKKCLQKDPEKRPTAEQ 247
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
57-311 7.85e-41

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 149.63  E-value: 7.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALK-----RMYVNNMpdLNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWevlILM 130
Cdd:cd14099   9 LGKGGFAKCYEVTdMSTGKVYAGKvvpksSLTKPKQ--REKLKSEIKIHRSLK-HPNIVKFHDCFEDE--ENVY---ILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRaGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpq 210
Cdd:cd14099  81 ELCS-NGSLMELLKR-RKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFLDENMNVKIGDFGLAA------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 kdgvnVVEEEIKKYTTL----SYRAPEMinLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIP 281
Cdd:cd14099 150 -----RLEYDGERKKTLcgtpNYIAPEV--LEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKetykrIKKNEYSFP 222
                       250       260       270
                ....*....|....*....|....*....|
gi 38787904 282 DNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14099 223 SHLSISDEAKDLIRSMLQPDPTKRPSLDEI 252
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
52-306 1.78e-40

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: 148.50  E-value: 1.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKR---EITIMKELSgHKNIVGYLDCAVnsISDNVWevl 127
Cdd:cd14014   3 RLVRLLGRGGMGEVYRARdTLLGRPVAIKVLRPELAEDEEFRERflrEARALARLS-HPNIVRVYDVGE--DDGRPY--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRaGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCktPIIHRDLKVENILLNDGGNYVLCDFGSATnkfl 207
Cdd:cd14014  77 IVMEYVE-GGSLADLLRE-RGPLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFGIAR---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 npqkdgvnVVEEEIKKYT-----TLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICDGNFTIP 281
Cdd:cd14014 149 --------ALGDSGLTQTgsvlgTPAYMAPE---QARGGPVDPRSDIYSLGVVLYELLTGRPPFdGDSPAAVLAKHLQEA 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 282 DNSRYSRNIHC------LIRFMLEPDPEHRP 306
Cdd:cd14014 218 PPPPSPLNPDVppaldaIILRALAKDPEERP 248
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
57-311 8.68e-40

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: 146.93  E-value: 8.68e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMY----------------VNNMpdLNVCKREITIMKELSgHKNIV---GYLDcav 116
Cdd:cd14008   1 LGRGSFGKVKLALdTETGQLYAIKIFNksrlrkrregkndrgkIKNA--LDDVRREIAIMKKLD-HPNIVrlyEVID--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 117 nsiSDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVL 196
Cdd:cd14008  75 ---DPESDKLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENG--IVHRDIKPENLLLTADGTVKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 197 CDFGSAtnKFLNPQKDgvnvveeEIKKYT-TLSYRAPEMIN----LYGGKPittkADIWALGCLLYKLCFFTLPF-GESQ 270
Cdd:cd14008 150 SDFGVS--EMFEDGND-------TLQKTAgTPAFLAPELCDgdskTYSGKA----ADIWALGVTLYCLVFGRLPFnGDNI 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 38787904 271 VAICDGNFTIPDNSRYSRNI--HC--LIRFMLEPDPEHRPDIFQV 311
Cdd:cd14008 217 LELYEAIQNQNDEFPIPPELspELkdLLRRMLEKDPEKRITLKEI 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
95-310 1.15e-39

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: 146.53  E-value: 1.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYCRAG--QVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLH-- 170
Cdd:cd08217  49 EVNILRELK-HPNIVRYYDRIVDRANTTLY---IVMEYCEGGdlAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHnr 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 -QCKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQkdgvnvvEEEIKKYT-TLSYRAPEMINlygGKPITTKAD 248
Cdd:cd08217 125 sVGGGKILHRDLKPANIFLDSDNNVKLGDFGLA--RVLSHD-------SSFAKTYVgTPYYMSPELLN---EQSYDEKSD 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 249 IWALGCLLYKLCFFTLPF-GESQVA----ICDGNFT-IPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd08217 193 IWSLGCLIYELCALHPPFqAANQLElakkIKEGKFPrIP--SRYSSELNEVIKSMLNVDPDKRPSVEE 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
52-311 5.71e-39

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: 144.20  E-value: 5.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR---ThgGIRCALKRMYVNNMPDLNV--CKREITIMKELSgHKNIVGYLDcaVNSISDNVWev 126
Cdd:cd14003   3 ELGKTLGEGSFGKVKLARhklT--GEKVAIKIIDKSKLKEEIEekIKREIEIMKLLN-HPNIIKLYE--VIETENKIY-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 lILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkf 206
Cdd:cd14003  76 -LVMEYASGGELFDYIVNN--GRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILLDKNGNLKIIDFGLS---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgvNVVEEEIKKYT---TLSYRAPEMINlyGGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNF 278
Cdd:cd14003 147 --------NEFRGGSLLKTfcgTPAYAAPEVLL--GRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSklfrkILKGKY 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 38787904 279 TIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14003 217 PIP--SHLSPDARDLIRRMLVVDPSKRITIEEI 247
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
52-311 2.63e-38

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: 142.62  E-value: 2.63e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVRTHG-GIRCALK----RMYVNNmpDLNVCKREITIMKELSgHKNIVGYLDCavnsISDNVwEV 126
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKtGEEYAVKiidkKKLKSE--DEEMLRREIEILKRLD-HPNIVKLYEV----FEDDK-NL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL---NDGGNYVLCDFGSAT 203
Cdd:cd05117  75 YLVMELCTGGELFDRIVKK--GSFSEREAAKIMKQILSAVAYLHSQG--IVHRDLKPENILLaskDPDSPIKIIDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nkflnpqkdgvnVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQV----AICD 275
Cdd:cd05117 151 ------------IFEEGEKLKTvcgTPYYVAPEVLK---GKGYGKKCDIWSLGVILYILLCGYPPFyGETEQelfeKILK 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 276 GNFTIPdnSRYSRNIHC----LIRFMLEPDPEHRPDIFQV 311
Cdd:cd05117 216 GKYSFD--SPEWKNVSEeakdLIKRLLVVDPKKRLTAAEA 253
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
52-415 1.94e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 140.15  E-value: 1.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKR---EITIMKELSgHKNIVGYLDCAVNSisDNVWevl 127
Cdd:COG0515  10 RILRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARERfrrEARALARLN-HPNIVRVYDVGEED--GRPY--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAG---QVVNQmnkklQTGFTEPEVLQIFCDTCEAVARLHQCktPIIHRDLKVENILLNDGGNYVLCDFGSATn 204
Cdd:COG0515  84 LVMEYVEGEslaDLLRR-----RGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPDGRVKLIDFGIAR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpQKDGVNVVEEEIKKYtTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICDGNFTIP-- 281
Cdd:COG0515 156 -----ALGGATLTQTGTVVG-TPGYMAPEQAR---GEPVDPRSDVYSLGVTLYELLTGRPPFdGDSPAELLRAHLREPpp 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 282 ----DNSRYSRNIHCLIRFMLEPDPEHRPDifqvSYFAFKFAKKDCPVSNINNSSIPSALPEPMTASEAAARKSQIKARI 357
Cdd:COG0515 227 ppseLRPDLPPALDAIVLRALAKDPEERYQ----SAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 302
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 358 TDTIGPTETSIAPRQRPKANSATTATPSVLTIQSSATPVKVLAPGEFGNHRPKGALRP 415
Cdd:COG0515 303 AAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAA 360
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
57-311 9.49e-35

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 132.52  E-value: 9.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLV-RTHGGIRCALKRMYVNNMPD------LNvckrEITIMKELSgHKNIVGYLDCavnSISDNvwEVLIL 129
Cdd:cd08530   8 LGKGSYGSVYKVkRLSDNQVYALKEVNLGSLSQkeredsVN----EIRLLASVN-HPNIIRYKEA---FLDGN--RLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVN--QMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG---SATN 204
Cdd:cd08530  78 MEYAPFGDLSKliSKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQK--ILHRDLKSANILLSAGDLVKIGDLGiskVLKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPQkdgvnvveeeikkYTTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPF-----GESQVAICDGNFT 279
Cdd:cd08530 156 NLAKTQ-------------IGTPLYAAPE---VWKGRPYDYKSDIWSLGCLLYEMATFRPPFeartmQELRYKVCRGKFP 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 280 IPDNsRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08530 220 PIPP-VYSQDLQQIIRSLLQVNPKKRPSCDKL 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
57-307 1.68e-34

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 131.51  E-value: 1.68e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIrCALKRMYVNNMPD--LNVCKREITIMKELSgHKNIVGYLDCavnSISDNVWevLILMEYCR 134
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTD-VAIKKLKVEDDNDelLKEFRREVSILSKLR-HPNIVQFIGA---CLSPPPL--CIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQCktPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGV 214
Cdd:cd13999  74 GGSLYDLLHKKKIP-LSWSLRLKIALDIARGMNYLHSP--PIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 215 NVveeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE---SQVAICDGNF----TIPDN--SR 285
Cdd:cd13999 151 VV--------GTPRWMAPEVLR---GEPYTEKADVYSFGIVLWELLTGEVPFKElspIQIAAAVVQKglrpPIPPDcpPE 219
                       250       260
                ....*....|....*....|..
gi 38787904 286 YSRnihcLIRFMLEPDPEHRPD 307
Cdd:cd13999 220 LSK----LIKRCWNEDPEKRPS 237
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
55-312 6.38e-34

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: 130.70  E-value: 6.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH--GGIRCALKRMYVNNMPDLNVCKR----------EITIMKELSGHKNIVGYLDCAVNSisDN 122
Cdd:cd08528   6 ELLGSGAFGCVYKVRKKsnGQTLLALKEINMTNPAFGRTEQErdksvgdiisEVNIIKEQLRHPNIVRYYKTFLEN--DR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 VWEVLILMEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKTpIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd08528  84 LYIVMELIEGAPLGEHFSSLKEK-NEHFTEDRIWNIFVQMVLALRYLHKEKQ-IVHRDLKPNNIMLGEDDKVTITDFGLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TNKflnpqkdgvnvvEEEIKKYT----TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQV-----AI 273
Cdd:cd08528 162 KQK------------GPESSKMTsvvgTILYSCPEIVQ---NEPYGEKADIWALGCILYQMCTLQPPFYSTNMltlatKI 226
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 274 CDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd08528 227 VEAEYEPLPEGMYSDDITFVIRSCLTPDPEARPDIVEVS 265
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
57-314 2.49e-33

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: 128.12  E-value: 2.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMyVNNMPDLNVCKREITIMKELS---GHKNIVGYLDCAVNSISDNVWEVLILMey 132
Cdd:cd05118   7 IGEGAFGTVWLARdKVTGEKVAIKKI-KNDFRHPKAALREIKLLKHLNdveGHPNIVKLLDVFEHRGGNHLCLVFELM-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 craGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFGSAtnKFLNPQK 211
Cdd:cd05118  84 ---GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNG--IIHRDLKPENILINlELGQLKLADFGLA--RSFTSPP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 212 DGVNVVeeeikkytTLSYRAPEMInlYGGKPITTKADIWALGCLLYKLcFFTLPF--GESQV----AICD--GNFTIPDn 283
Cdd:cd05118 157 YTPYVA--------TRWYRAPEVL--LGAKPYGSSIDIWSLGCILAEL-LTGRPLfpGDSEVdqlaKIVRllGTPEALD- 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 284 srysrnihcLIRFMLEPDPEHRPDIFQV---SYF 314
Cdd:cd05118 225 ---------LLSKMLKYDPAKRITASQAlahPYF 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
53-311 3.74e-33

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 127.91  E-value: 3.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDCAVNSISDNvwevlIL 129
Cdd:cd08529   4 ILNKLGKGSFGVVYkVVRKVDGRVYALKQIDISRMSrkMREEAIDEARVLSKLN-SPYVIKYYDSFVDKGKLN-----IV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNP 209
Cdd:cd08529  78 MEYAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKK--ILHRDIKSMNIFLDKGDNVKIGDLGVA--KILSD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 QKDGVNVVeeeikkYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVA----ICDGNFTiPDNS 284
Cdd:cd08529 154 TTNFAQTI------VGTPYYLSPELCE---DKPYNEKSDVWALGCVLYELCTGKHPFeAQNQGAlilkIVRGKYP-PISA 223
                       250       260
                ....*....|....*....|....*..
gi 38787904 285 RYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08529 224 SYSQDLSQLIDSCLTKDYRQRPDTTEL 250
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
49-308 3.10e-30

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: 120.01  E-value: 3.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVFLVRTHGGIRCALKRmyVNNMPD----LNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVw 124
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIYALKR--VDLEGAdeqtLQSYKNEIELLKKLKGSDRIIQLYDYEVTDEDDYL- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 evLILMEYcraGQV-VNQM-NKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGgNYVLCDFGSA 202
Cdd:cd14131  78 --YMVMEC---GEIdLATIlKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEG--IVHSDLKPANFLLVKG-RLKLIDFGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TNKflnpQKDGVNVVEEEikKYTTLSYRAPEMI----NLYGGKP---ITTKADIWALGCLLYKLCFFTLPFGESQ----- 270
Cdd:cd14131 150 KAI----QNDTTSIVRDS--QVGTLNYMSPEAIkdtsASGEGKPkskIGRPSDVWSLGCILYQMVYGKTPFQHITnpiak 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 38787904 271 -VAICDGNFTIPDNSRYSRN-IH----CLIRfmlepDPEHRPDI 308
Cdd:cd14131 224 lQAIIDPNHEIEFPDIPNPDlIDvmkrCLQR-----DPKKRPSI 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
57-310 5.99e-30

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: 118.78  E-value: 5.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH--GGIRcALKRMYVNNMPDLNVC--KREITIMKELSgHKNIVGYLDCAVNSISdnvweVLILMEY 132
Cdd:cd06606   8 LGKGSFGSVYLALNLdtGELM-AVKEVELSGDSEEELEalEREIRILSSLK-HPNIVRYLGTERTENT-----LNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CrAGQVVNQMNKKLQtGFTEPEV----LQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkfln 208
Cdd:cd06606  81 V-PGGSLASLLKKFG-KLPEPVVrkytRQIL----EGLEYLHSNG--IVHRDIKGANILVDSDGVVKLADFGCAK----- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pQKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE--SQVAI--CDGNFT----I 280
Cdd:cd06606 148 -RLAEIATGEGTKSLRGTPYWMAPEVIR---GEGYGRAADIWSLGCTVIEMATGKPPWSElgNPVAAlfKIGSSGepppI 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 38787904 281 PDN-SRYSRNI--HCLIRfmlepDPEHRPDIFQ 310
Cdd:cd06606 224 PEHlSEEAKDFlrKCLQR-----DPKKRPTADE 251
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
57-308 3.40e-29

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 116.83  E-value: 3.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDcavnSISDNvWEVLILMEYC 133
Cdd:cd08218   8 IGEGSFGKALLVKsKEDGKQYVIKEINISKMSpkEREESRKEVAVLSKMK-HPNIVQYQE----SFEEN-GNLYIVMDYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNpqkdg 213
Cdd:cd08218  82 DGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRK--ILHRDIKSQNIFLTKDGIIKLGDFGIA--RVLN----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 vNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQ-----VAICDGNFTiPDNSRYSR 288
Cdd:cd08218 153 -STVELARTCIGTPYYLSPEICE---NKPYNNKSDIWALGCVLYEMCTLKHAFEAGNmknlvLKIIRGSYP-PVPSRYSY 227
                       250       260
                ....*....|....*....|
gi 38787904 289 NIHCLIRFMLEPDPEHRPDI 308
Cdd:cd08218 228 DLRSLVSQLFKRNPRDRPSI 247
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
55-308 4.32e-29

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 116.60  E-value: 4.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLdcavNSISDNvWEVLILME 131
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSdSEHCVIKEIDLTKMPvkEKEASKKEVILLAKMK-HPNIVTFF----ASFQEN-GRLFIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-LCDFGSAtnKFLNpq 210
Cdd:cd08225  80 YCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRK--ILHRDIKSQNIFLSKNGMVAkLGDFGIA--RQLN-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 kdgvNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQ-----VAICDGNFTiPDNSR 285
Cdd:cd08225 154 ----DSMELAYTCVGTPYYLSPEICQ---NRPYNNKTDIWSLGCVLYELCTLKHPFEGNNlhqlvLKICQGYFA-PISPN 225
                       250       260
                ....*....|....*....|...
gi 38787904 286 YSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd08225 226 FSRDLRSLISQLFKVSPRDRPSI 248
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
52-315 4.33e-29

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: 116.60  E-value: 4.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDL---NVCKREITIMKELSgHKNIVGYLDcavNSISDNvwEVL 127
Cdd:cd08224   3 EIEKKIGKGQFSVVYRARcLLDGRLVALKKVQIFEMMDAkarQDCLKEIDLLQQLN-HPNIIKYLA---SFIENN--ELN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVvNQMNKKLQT---GFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaTN 204
Cdd:cd08224  77 IVLELADAGDL-SRLIKHFKKqkrLIPERTIWKYFVQLCSALEHMHSKR--IMHRDIKPANVFITANGVVKLGDLG--LG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPQKDGVNvveeeiKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-------ICDGN 277
Cdd:cd08224 152 RFFSSKTTAAH------SLVGTPYYMSPERIR---EQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlyslckkIEKCE 222
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 278 FT-IPDNsRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFA 315
Cdd:cd08224 223 YPpLPAD-LYSQELRDLVAACIQPDPEKRPDISYVLDVA 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
55-307 4.39e-29

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: 116.16  E-value: 4.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNmPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYC 133
Cdd:cd06614   6 EKIGEGASGEVYKaTDRATGKEVAIKKMRLRK-QNKELIINEILIMKECK-HPNIVDYYDSYL--VGDELW---VVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAG---QVVNQMNKKLqtgfTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQ 210
Cdd:cd06614  79 DGGsltDIITQNPVRM----NESQIAYVCREVLQGLEYLHS--QNVIHRDIKSDNILLSKDGSVKLADFGFAAQ--LTKE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 KDGVN-VVeeeikkyTTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLC-----FFTLPFGESQVAICD-GNFTIPDN 283
Cdd:cd06614 151 KSKRNsVV-------GTPYWMAPEVI---KRKDYGPKVDIWSLGIMCIEMAegeppYLEEPPLRALFLITTkGIPPLKNP 220
                       250       260
                ....*....|....*....|....
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd06614 221 EKWSPEFKDFLNKCLVKDPEKRPS 244
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
55-314 6.70e-28

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 113.73  E-value: 6.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR-THGGIRCALKRMYVNN----MPDlnVCKREITIMKELSgHKNIVGYLDCAVNSISdnvweVLIL 129
Cdd:cd07829   5 EKLGEGTYGVVYKAKdKKTGEIVALKKIRLDNeeegIPS--TALREISLLKELK-HPNIVKLLDVIHTENK-----LYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCragqvvnQMN-----KKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtN 204
Cdd:cd07829  77 FEYC-------DQDlkkylDKRPGPLPPNLIKSIMYQLLRGLAYCHSHR--ILHRDLKPQNLLINRDGVLKLADFGLA-R 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPqkdgvnvveeeIKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLLYKLCFFTLPF-GESQVA----IC- 274
Cdd:cd07829 147 AFGIP-----------LRTYThevvTLWYRAPEI--LLGSKHYSTAVDIWSVGCIFAELITGKPLFpGDSEIDqlfkIFq 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 275 -----------------DGNFTIPDN---------SRYSRNIHCLIRFMLEPDPEHRP---DIFQVSYF 314
Cdd:cd07829 214 ilgtpteeswpgvtklpDYKPTFPKWpkndlekvlPRLDPEGIDLLSKMLQYNPAKRIsakEALKHPYF 282
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
60-311 7.38e-28

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


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 112.90  E-value: 7.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRTHGGIR-CALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDcavNSISDNVweVLILMEYCRAG 136
Cdd:cd08220  11 GAYGTVYLCRRKDDNKlVIIKQIPVEQMTkeERQAALNEVKVLSMLH-HPNIIEYYE---SFLEDKA--LMIVMEYAPGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 QVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYV-LCDFGsaTNKFLNPQKDGVN 215
Cdd:cd08220  85 TLFEYIQQRKGSLLSEEEILHFFVQILLALHHVH--SKQILHRDLKTQNILLNKKRTVVkIGDFG--ISKILSSKSKAYT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 216 VVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQV-----AICDGNFTiPDNSRYSRNI 290
Cdd:cd08220 161 VV-------GTPCYISPELCE---GKPYNQKSDIWALGCVLYELASLKRAFEAANLpalvlKIMRGTFA-PISDRYSEEL 229
                       250       260
                ....*....|....*....|.
gi 38787904 291 HCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08220 230 RHLILSMLHLDPNKRPTLSEI 250
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
57-306 1.86e-27

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: 111.60  E-value: 1.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYV-NNMPDLNVCKREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLILMEYCR 134
Cdd:cd08219   8 VGEGSFGRALLVQhVNSDQKYAMKEIRLpKSSSAVEDSRKEAVLLAKMK-HPNIVAFKESF-----EADGHLYIVMEYCD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQVVNQMnkKLQTG--FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFLNPQKD 212
Cdd:cd08219  82 GGDLMQKI--KLQRGklFPEDTILQWFVQMCLGVQHIHEKR--VLHRDIKSKNIFLTQNGKVKLGDFGSA-RLLTSPGAY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 GVNVVeeeikkyTTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQ-----VAICDGNFTiPDNSRYS 287
Cdd:cd08219 157 ACTYV-------GTPYYVPPE---IWENMPYNNKSDIWSLGCILYELCTLKHPFQANSwknliLKVCQGSYK-PLPSHYS 225
                       250
                ....*....|....*....
gi 38787904 288 RNIHCLIRFMLEPDPEHRP 306
Cdd:cd08219 226 YELRSLIKQMFKRNPRSRP 244
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
57-305 1.96e-27

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: 111.45  E-value: 1.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALK-----RMYVNNMPDLNvcKREITIMKELSgHKNIVGyLDCAVNSiSDNVWEVlilM 130
Cdd:cd05123   1 LGKGSFGKVLLVRkKDTGKLYAMKvlrkkEIIKRKEVEHT--LNERNILERVN-HPFIVK-LHYAFQT-EEKLYLV---L 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpq 210
Cdd:cd05123  73 DYVPGGELFSHLSKEGR--FPEERARFYAAEIVLALEYLHSLG--IIYRDLKPENILLDSDGHIKLTDFGLA-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 KDGVNvveEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPD 282
Cdd:cd05123 141 KELSS---DGDRTYTfcgTPEYLAPEVLL---GKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKeiyekILKSPLKFPE 214
                       250       260
                ....*....|....*....|...
gi 38787904 283 NsrYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05123 215 Y--VSPEAKSLISGLLQKDPTKR 235
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
57-259 5.23e-27

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 111.69  E-value: 5.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLDCAVNSISDNVWEVlilME 131
Cdd:cd07845  15 IGEGTYGIVYRARdTTSGEIVALKKVRMDNerdgIPISSL--REITLLLNLR-HPNIVELKEVVVGKHLDSIFLV---ME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRA--GQVVNQMnkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNkFLNP 209
Cdd:cd07845  89 YCEQdlASLLDNM----PTPFSESQVKCLMLQLLRGLQYLHE--NFIIHRDLKVSNLLLTDKGCLKIADFGLART-YGLP 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 210 QKDGV-NVVeeeikkytTLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07845 162 AKPMTpKVV--------TLWYRAPEL--LLGCTTYTTAIDMWAVGCILAEL 202
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
52-311 6.82e-27

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: 110.35  E-value: 6.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFL---VRTHGGIRCALK--------RMYVNN-MPdlnvckREITIMKELSgHKNIVgyldcAVNSI 119
Cdd:cd14080   3 RLGKTIGEGSYSKVKLaeyTKSGLKEKVACKiidkkkapKDFLEKfLP------RELEILRKLR-HPNII-----QVYSI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWEVLILMEYCRAGQVVN--QMNKKLqtgfTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLC 197
Cdd:cd14080  71 FERGSKVFIFMEYAEHGDLLEyiQKRGAL----SESQARIWFRQLALAVQYLHSLD--IAHRDLKCENILLDSNNNVKLS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 198 DFGSATnkfLNPQKDGvnvvEEEIKKYT-TLSYRAPEMINlygGKP-ITTKADIWALGCLLYKLCFFTLPFGESQVA--- 272
Cdd:cd14080 145 DFGFAR---LCPDDDG----DVLSKTFCgSAAYAAPEILQ---GIPyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKkml 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 273 ---ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14080 215 kdqQNRKVRFPSSVKKLSPECKDLIDQLLEPDPTKRATIEEI 256
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
57-313 1.14e-26

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: 110.07  E-value: 1.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVcK--REITIMKELSgHKNIVGYLDCAVNSIsdnvwEVLILMEYC 133
Cdd:cd13996  14 LGSGGFGSVYKVRNKvDGVTYAIKKIRLTEKSSASE-KvlREVKALAKLN-HPNIVRYYTAWVEEP-----PLYIQMELC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQMNKK-LQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-LCDFGSAT--NKFLNP 209
Cdd:cd13996  87 EGGTLRDWIDRRnSSSKNDRKLALELFKQILKGVSYIHSKG--IVHRDLKPSNIFLDNDDLQVkIGDFGLATsiGNQKRE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 QKDGVNVVEEEIKKYT----TLSYRAPEMINlygGKPITTKADIWALGCLLYK-LCFFTLPFGESQVAICDGNFTIPDNS 284
Cdd:cd13996 165 LNNLNNNNNGNTSNNSvgigTPLYASPEQLD---GENYNEKADIYSLGIILFEmLHPFKTAMERSTILTDLRNGILPESF 241
                       250       260       270
                ....*....|....*....|....*....|
gi 38787904 285 RYSRNI-HCLIRFMLEPDPEHRPDIFQVSY 313
Cdd:cd13996 242 KAKHPKeADLIQSLLSKNPEERPSAEQLLR 271
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
52-259 2.79e-25

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: 105.38  E-value: 2.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFL---VRThgGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDCAVNSISdnvweV 126
Cdd:cd06627   3 QLGDLIGRGAFGSVYKglnLNT--GEFVAIKQISLEKIPksDLKSVMGEIDLLKKLN-HPNIVKYIGSVKTKDS-----L 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAG---QVVNQMNKklqtgFTEPEVL----QIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd06627  75 YIILEYVENGslaSIIKKFGK-----FPESLVAvyiyQVL----EGLAYLHEQG--VIHRDIKGANILTTKDGLVKLADF 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATNkfLNPQKDGVNVVEeeikkyTTLSYRAPEMINLyggKPITTKADIWALGCLLYKL 259
Cdd:cd06627 144 GVATK--LNEVEKDENSVV------GTPYWMAPEVIEM---SGVTTASDIWSVGCTVIEL 192
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
57-311 5.34e-25

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: 104.70  E-value: 5.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLV---RTHGGIRCALKRMyvnNMPDLN--------VCKREITIMKELSgHKNIVGYLDCAVNSiSDNVWE 125
Cdd:cd13994   1 IGKGATSVVRIVtkkNPRSGVLYAVKEY---RRRDDEskrkdyvkRLTSEYIISSKLH-HPNIVKVLDLCQDL-HGKWCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VlilMEYCRAGQVVNQMNKKLQTGFTEpeVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtNK 205
Cdd:cd13994  76 V---MEYCPGGDLFTLIEKADSLSLEE--KDCFFKQILRGVAYLHS--HGIAHRDLKPENILLDEDGVLKLTDFGTA-EV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQkdgvnvvEEEI----KKYTTLSYRAPE-MINL-YGGKPittkADIWALGCLLYKLCFFTLPFGES-------QVA 272
Cdd:cd13994 148 FGMPA-------EKESpmsaGLCGSEPYMAPEvFTSGsYDGRA----VDVWSCGIVLFALFTGRFPWRSAkksdsayKAY 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 38787904 273 ICDGNFTIPDNSRYSRNI----HCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd13994 217 EKSGDFTNGPYEPIENLLpsecRRLIYRMLHPDPEKRITIDEA 259
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
50-256 9.06e-25

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: 104.89  E-value: 9.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTH-GGIRCALKRMYvnnmPDLNVCKREITIMKELSgHKNIVGYLDC--AVNSISDNVWEV 126
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLLeTGEVVAIKKVL----QDKRYKNRELQIMRRLK-HPNIVKLKYFfySSGEKKDEVYLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LIlMEYcragqvVNQ-----MNKKLQTGFTEPEVL------QIFCdtceAVARLHqcKTPIIHRDLKVENILLN-DGGNY 194
Cdd:cd14137  80 LV-MEY------MPEtlyrvIRHYSKNKQTIPIIYvklysyQLFR----GLAYLH--SLGICHRDIKPQNLLVDpETGVL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 195 VLCDFGSAtnKFLNPqkDGVNVveeeikKY-TTLSYRAPEMInlYGGKPITTKADIWALGCLL 256
Cdd:cd14137 147 KLCDFGSA--KRLVP--GEPNV------SYiCSRYYRAPELI--FGATDYTTAIDIWSAGCVL 197
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
94-310 1.11e-24

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: 103.49  E-value: 1.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKeLSGHKNIVGYLDcavnsisdnVWE----VLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARL 169
Cdd:cd14081  50 REIAIMK-LIEHPNVLKLYD---------VYEnkkyLYLVLEYVSGGELFDYLVKK--GRLTEKEARKFFRQIISALDYC 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 170 HqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdgvnvVEEEIKKYTT----LSYRAPEMIN--LYGGKpi 243
Cdd:cd14081 118 H--SHSICHRDLKPENLLLDEKNNIKIADFGMAS-------------LQPEGSLLETscgsPHYACPEVIKgeKYDGR-- 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 244 ttKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDN-SRYSRNihcLIRFMLEPDPEHR---PDIFQ 310
Cdd:cd14081 181 --KADIWSCGVILYALLVGALPFDDDNLRqllekVKRGVFHIPHFiSPDAQD---LLRRMLEVNPEKRitiEEIKK 251
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
49-311 1.18e-24

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: 103.62  E-value: 1.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVFLVRTHG-GIRCALK---RMYVNNMPDLNVCKREITIMKELSgHKNIVgyldcAVNSISDNVW 124
Cdd:cd14073   1 HRYELLETLGKGTYGKVKLAIERAtGREVAIKsikKDKIEDEQDMVRIRREIEIMSSLN-HPHII-----RIYEVFENKD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsATN 204
Cdd:cd14073  75 KIVIVMEYASGGELYDYISERRR--LPEREARRIFRQIVSAVHYCHKNG--VVHRDLKLENILLDQNGNAKIADFG-LSN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFlnpqkdgvnvveeeiKKYTTLS-------YRAPEMINlygGKPIT-TKADIWALGCLLYKLCFFTLPFGESQVA---- 272
Cdd:cd14073 150 LY---------------SKDKLLQtfcgsplYASPEIVN---GTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSDFKrlvk 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 273 -ICDGNFTIPdnSRYSRNiHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14073 212 qISSGDYREP--TQPSDA-SGLIRWMLTVNPKRRATIEDI 248
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
94-311 1.96e-24

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: 102.80  E-value: 1.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVgYLDCAVNSISdnvwEVLILMEYCRAGQVVNqmnkKLQTG--FTEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd14075  50 REISSMEKLH-HPNII-RLYEVVETLS----KLHLVMEYASGGELYT----KISTEgkLSESEAKPLFAQIVSAVKHMHE 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdgvnvveeEIKKYTTLS-------YRAPEMI--NLYGGKP 242
Cdd:cd14075 120 NN--IIHRDLKAENVFYASNNCVKVGDFGFST----------------HAKRGETLNtfcgsppYAAPELFkdEHYIGIY 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 243 IttkaDIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDNsrYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14075 182 V----DIWALGVLLYFMVTGVMPFRAETVAklkkcILEGTYTIPSY--VSEPCQELIRGILQPVPSDRYSIDEI 249
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
53-305 2.04e-24

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: 102.85  E-value: 2.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVrTH--GGIRCALKRMYVNNM-PDLNVCKREITIMKELSgHKNIvgyldCAVNSISDNVWEVLIL 129
Cdd:cd14078   7 LHETIGSGGFAKVKLA-THilTGEKVAIKIMDKKALgDDLPRVKTEIEALKNLS-HQHI-----CRLYHVIETDNKIFMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnp 209
Cdd:cd14078  80 LEYCPGGELFDYIVAKDR--LSEDEARVFFRQIVSAVAYVHS--QGYAHRDLKPENLLLDEDQNLKLIDFGLCAKP---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 qKDGVNVveeeiKKYT---TLSYRAPEMINlyGGKPITTKADIWALGCLLYKL-CFFtLPFGESQVA-----ICDGNFTI 280
Cdd:cd14078 152 -KGGMDH-----HLETccgSPAYAAPELIQ--GKPYIGSEADVWSMGVLLYALlCGF-LPFDDDNVMalyrkIQSGKYEE 222
                       250       260
                ....*....|....*....|....*
gi 38787904 281 PdnSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14078 223 P--EWLSPSSKLLLDQMLQVDPKKR 245
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
93-306 3.61e-24

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: 102.38  E-value: 3.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAVNSIsdnvwEVLILMEYCRAGQvvnqMNKKLQTGFTEPEV------LQIFcdtcEAV 166
Cdd:cd06626  47 ADEMKVLEGLD-HPNLVRYYGVEVHRE-----EVYIFMEYCQEGT----LEELLRHGRILDEAvirvytLQLL----EGL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 167 ARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKDgvNVVEEEIKKYT-TLSYRAPEMINLYGGKPITT 245
Cdd:cd06626 113 AYLHENG--IVHRDIKPANIFLDSNGLIKLGDFGSA--VKLKNNTT--TMAPGEVNSLVgTPAYMAPEVITGNKGEGHGR 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 246 KADIWALGCLLYKLCFFTLPFGEsqvaiCDGNF------------TIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06626 187 AADIWSLGCVVLEMATGKRPWSE-----LDNEWaimyhvgmghkpPIPDSLQLSPEGKDFLSRCLESDPKKRP 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
55-310 5.76e-24

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: 101.56  E-value: 5.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR-THGGIRCALKrmYVN----NMPDLNVCKREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLIL 129
Cdd:cd14002   7 ELIGEGSFGKVYKGRrKYTGQVVALK--FIPkrgkSEKELRNLRQEIEILRKLN-HPNIIEMLDSF-----ETKKEFVVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAG--QVVNQmNKKLqtgfTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFL 207
Cdd:cd14002  79 TEYAQGElfQILED-DGTL----PEEEVRSIAKQLVSALHYLHSNR--IIHRDMKPQNILIGKGGVVKLCDFGFARAMSC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NpqkdgvNVVEEEIKKyTTLsYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPD 282
Cdd:cd14002 152 N------TLVLTSIKG-TPL-YMAPELVQ---EQPYDHTADLWSLGCILYELFVGQPPFYTNSIYqlvqmIVKDPVKWPS 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 283 NsrYSRNIHCLIRFMLEPDPEHR---PDIFQ 310
Cdd:cd14002 221 N--MSPEFKSFLQGLLNKDPSKRlswPDLLE 249
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
51-311 7.03e-24

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: 101.31  E-value: 7.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEEsLAEGGFSTVFLVRTHG-GIRCALK-----RMYVNNM---PDLNVCKREITIMKEL--SGHKNIVGYLDCAVNSi 119
Cdd:cd14004   3 TILKE-MGEGAYGQVNLAIYKSkGKEVVIKfifkeRILVDTWvrdRKLGTVPLEIHILDTLnkRSHPNIVKLLDFFEDD- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 sDNVWevlILMEYCRAGqvvnqMNK----KLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV 195
Cdd:cd14004  81 -EFYY---LVMEKHGSG-----MDLfdfiERKPNMDEKEAKYIFRQVADAVKHLHDQG--IVHRDIKDENVILDGNGTIK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 LCDFGSATnkFLNPQKDGVNvveeeikkYTTLSYRAPEMI--NLYGGKPIttkaDIWALGCLLYKLCFFTLPFGESQvAI 273
Cdd:cd14004 150 LIDFGSAA--YIKSGPFDTF--------VGTIDYAAPEVLrgNPYGGKEQ----DIWALGVLLYTLVFKENPFYNIE-EI 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 38787904 274 CDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14004 215 LEADLRIP--YAVSEDLIDLISRMLNRDVGDRPTIEEL 250
Pkinase pfam00069
Protein kinase domain;
52-311 1.27e-23

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 99.63  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    52 TLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPD--LNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWevlI 128
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKaKHRDTGKIVAIKKIKKEKIKKkkDKNILREIKILKKLN-HPNIVRLYDAFEDK--DNLY---L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   129 LMEYCRAGQVvnqmNKKLQ--TGFTEPEVLQIFCDTCEAVARLHQCKTPIIhrdlkvenillndggnyvlcdfgsatnkf 206
Cdd:pfam00069  76 VLEYVEGGSL----FDLLSekGAFSEREAKFIMKQILEGLESGSSLTTFVG----------------------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   207 lnpqkdgvnvveeeikkytTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPFGES------QVAICDGNFTI 280
Cdd:pfam00069 123 -------------------TPWYMAPEVL---GGNPYGPKVDVWSLGCILYELLTGKPPFPGIngneiyELIIDQPYAFP 180
                         250       260       270
                  ....*....|....*....|....*....|.
gi 38787904   281 PDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:pfam00069 181 ELPSNLSEEAKDLLKKLLKKDPSKRLTATQA 211
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
53-253 1.53e-23

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: 100.42  E-value: 1.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNmpDLNVCKREITIMKElSGHKNIVGYLDCAvnSISDNVWevlILME 131
Cdd:cd06612   7 ILEKLGEGSYGSVYKAIhKETGQVVAIKVVPVEE--DLQEIIKEISILKQ-CDSPYIVKYYGSY--FKNTDLW---IVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMnKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqk 211
Cdd:cd06612  79 YCGAGSVSDIM-KITNKTLTEEEIAAILYQTLKGLEYLHSNK--KIHRDIKAGNILLNEEGQAKLADFGVSG-------- 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 38787904 212 dgvNVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALG 253
Cdd:cd06612 148 ---QLTDTMAKRNTvigTPFWMAPEVIQ---EIGYNNKADIWSLG 186
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
52-314 1.67e-23

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: 100.42  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVrTHG--GIRCALKRMYVNNMPDLNV---CKREITIMKeLSGHKNIVGYLDcavnsISDNVWEV 126
Cdd:cd14079   5 ILGKTLGVGSFGKVKLA-EHEltGHKVAVKILNRQKIKSLDMeekIRREIQILK-LFRHPHIIRLYE-----VIETPTDI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkf 206
Cdd:cd14079  78 FMVMEYVSGGELFDYIVQK--GRLSEDEARRFFQQIISGVEYCHRHM--VVHRDLKPENLLLDSNMNVKIADFGLS---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lNPQKDGvnvveeEIKKYTTLS--YRAPEMIN--LYGGkpitTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGN 277
Cdd:cd14079 150 -NIMRDG------EFLKTSCGSpnYAAPEVISgkLYAG----PEVDVWSCGVILYALLCGSLPFDDEHIPnlfkkIKSGI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 278 FTIPDN-SRYSRNihcLIRFMLEPDPEHR---PDIFQVSYF 314
Cdd:cd14079 219 YTIPSHlSPGARD---LIKRMLVVDPLKRitiPEIRQHPWF 256
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
95-306 1.89e-23

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: 100.20  E-value: 1.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLdcavNSISDNVwEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKT 174
Cdd:cd08221  49 EIDILSLLN-HDNIITYY----NHFLDGE-SLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIH--KA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PIIHRDLKVENILLNDGGNYVLCDFGsatnkfLNPQKDGVNVVEEEIkkYTTLSYRAPEMINlygGKPITTKADIWALGC 254
Cdd:cd08221 121 GILHRDIKTLNIFLTKADLVKLGDFG------ISKVLDSESSMAESI--VGTPYYMSPELVQ---GVKYNFKSDIWAVGC 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 255 LLYKLCFFTLPFGESQ-----VAICDGNFTIpDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd08221 190 VLYELLTLKRTFDATNplrlaVKIVQGEYED-IDEQYSEEIIQLVHDCLHQDPEDRP 245
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
90-311 3.81e-23

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: 99.25  E-value: 3.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  90 NVcKREITIMKELSgHKNIVGYLDCAVNsisDNVWEVLILMEYCRAGQVVNQMN---KKLQTGftepEVLQIFCDTCEAV 166
Cdd:cd14119  40 NV-KREIQILRRLN-HRNVIKLVDVLYN---EEKQKLYMVMEYCVGGLQEMLDSapdKRLPIW----QAHGYFVQLIDGL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 167 ARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKDGvnvvEEEIKKYTTLSYRAPEMIN---LYGGKpi 243
Cdd:cd14119 111 EYLHSQG--IIHKDIKPGNLLLTTDGTLKISDFGVA--EALDLFAED----DTCTTSQGSPAFQPPEIANgqdSFSGF-- 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 244 ttKADIWALGCLLYKLCFFTLPF-GESQV----AICDGNFTIPDNsrYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14119 181 --KVDIWSAGVTLYNMTTGKYPFeGDNIYklfeNIGKGEYTIPDD--VDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
57-306 3.89e-23

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: 98.88  E-value: 3.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVcKREITIMKELSgHKNIVGYLDcavnsISDNVWEVLILMEYCRA 135
Cdd:cd14006   1 LGRGRFGVVKRCIEKAtGREFAAKFIPKRDKKKEAV-LREISILNQLQ-HPRIIQLHE-----AYESPTELVLILELCSG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV--LCDFGSATNkfLNPQkdg 213
Cdd:cd14006  74 GELLDRLAERGS--LSEEEVRTYMRQLLEGLQYLHNHH--ILHLDLKPENILLADRPSPQikIIDFGLARK--LNPG--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 vnvveEEIKK-YTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQ------VAICDGNFTIPDNSR 285
Cdd:cd14006 145 -----EELKEiFGTPEFVAPEIVN---GEPVSLATDMWSIGVLTYVLLSGLSPFlGEDDqetlanISACRVDFSEEYFSS 216
                       250       260
                ....*....|....*....|.
gi 38787904 286 YSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14006 217 VSQEAKDFIRKLLVKEPRKRP 237
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
53-305 4.15e-23

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 99.35  E-value: 4.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-----THGGIRCALKRMYVNNMPDLNVCK---REITIMKELSGHKNIVGYLDcavnSISDNVW 124
Cdd:cd13993   4 LISPIGEGAYGVVYLAVdlrtgRKYAIKCLYKSGPNSKDGNDFQKLpqlREIDLHRRVSRHPNIITLHD----VFETEVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 eVLILMEYCRAGQVV-NQMNKKLQTGFTEpEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLN-DGGNYVLCDFGSA 202
Cdd:cd13993  80 -IYIVLEYCPNGDLFeAITENRIYVGKTE-LIKNVFLQLIDAVKHCHS--LGIYHRDIKPENILLSqDEGTVKLCDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TNKFLNPQkdgVNVveeeikkyTTLSYRAPEMINLYG--GKPITTKA-DIWALGCLLYKLCFFTLPF---GESQVAICDg 276
Cdd:cd13993 156 TTEKISMD---FGV--------GSEFYMAPECFDEVGrsLKGYPCAAgDIWSLGIILLNLTFGRNPWkiaSESDPIFYD- 223
                       250       260       270
                ....*....|....*....|....*....|....*
gi 38787904 277 nFTIPDNSRY------SRNIHCLIRFMLEPDPEHR 305
Cdd:cd13993 224 -YYLNSPNLFdvilpmSDDFYNLLRQIFTVNPNNR 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-315 4.84e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 99.33  E-value: 4.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIVGYLDcavNSISDNvwEVLI 128
Cdd:cd08228   6 IEKKIGRGQFSEVYRATCLlDRKPVALKKVQIFEMMDAKArqdCVKEIDLLKQLN-HPNVIKYLD---SFIEDN--ELNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMN--KKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaTNKF 206
Cdd:cd08228  80 VLELADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRR--VMHRDIKPANVFITATGVVKLGDLG--LGRF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LNPQKDGVNVVeeeikkYTTLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPFGESQVAI---------CDgn 277
Cdd:cd08228 156 FSSKTTAAHSL------VGTPYYMSPERIHENG---YNFKSDIWSLGCLLYEMAALQSPFYGDKMNLfslcqkieqCD-- 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 38787904 278 FTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFA 315
Cdd:cd08228 225 YPPLPTEHYSEKLRELVSMCIYPDPDQRPDIGYVHQIA 262
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
48-312 6.11e-23

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: 98.49  E-value: 6.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMY---VNNMPDLNVCKREITIMKELSgHKNIVgyldcAVNSISDNVW 124
Cdd:cd14161   2 KHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRkdrIKDEQDLLHIRREIEIMSSLN-HPHII-----SVYEVFENSS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSA-- 202
Cdd:cd14161  76 KIVIVMEYASRGDLYDYISERQR--LSELEARHFFRQIVSAVHYCHA--NGIVHRDLKLENILLDANGNIKIADFGLSnl 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 --TNKFLnpqkdgvnvveeeiKKYT-TLSYRAPEMINlygGKPIT-TKADIWALGCLLYKLCFFTLPF-GESQ----VAI 273
Cdd:cd14161 152 ynQDKFL--------------QTYCgSPLYASPEIVN---GRPYIgPEVDSWSLGVLLYILVHGTMPFdGHDYkilvKQI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 274 CDGNFTIPDNSRYSrnihC-LIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14161 215 SSGAYREPTKPSDA----CgLIRWLLMVNPERRATLEDVA 250
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
55-306 6.99e-23

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: 98.83  E-value: 6.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR-THGGIRCALKRM---YVNNMPDLNVCKREITIMKELSgHKNIVGyLDCAVNSiSDNVWEVlilM 130
Cdd:cd05581   7 KPLGEGSYSTVVLAKeKETGKEYAIKVLdkrHIIKEKKVKYVTIEKEVLSRLA-HPGIVK-LYYTFQD-ESKLYFV---L 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLN-- 208
Cdd:cd05581  81 EYAPNGDLLEYIRKY--GSLDEKCTRFYTAEIVLALEYLHSKG--IIHRDLKPENILLDEDMHIKITDFGTA--KVLGpd 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 --PQKDGVNVVEEEIKKYT-------TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---GESQV--AIC 274
Cdd:cd05581 155 ssPESTKGDADSQIAYNQAraasfvgTAEYVSPELLN---EKPAGKSSDLWALGCIIYQMLTGKPPFrgsNEYLTfqKIV 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 275 DGNFTIPDNsrYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05581 232 KLEYEFPEN--FPPDAKDLIQKLLVLDPSKRL 261
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
51-306 9.33e-23

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: 98.53  E-value: 9.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEESLAEGGFSTVFLVR-THGGIRCALKRMyvNNMPDLNV-CKREITIMKELSGHKNIVGYLDCAVNSIS----DNVW 124
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARhKKTGQLAAIKIM--DIIEDEEEeIKLEINILRKFSNHPNIATFYGAFIKKDPpggdDQLW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVlilMEYCRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsa 202
Cdd:cd06608  86 LV---MEYCGGGSVTDLVKGLRKKGkrLKEEWIAYILRETLRGLAYLHENK--VIHRDIKGQNILLTEEAEVKLVDFG-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 tnkflnpqkdgvnvVEEEIKKytTLSYR----------APEMI--NLYGGKPITTKADIWALGcllyklcFFTLPFGESQ 270
Cdd:cd06608 159 --------------VSAQLDS--TLGRRntfigtpywmAPEVIacDQQPDASYDARCDVWSLG-------ITAIELADGK 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 38787904 271 VAICDGN-----FTIPDNS--------RYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06608 216 PPLCDMHpmralFKIPRNPpptlkspeKWSKEFNDFISECLIKNYEQRP 264
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
57-316 1.22e-22

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: 98.28  E-value: 1.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcaVNSISDNVWevlILMEYCRA 135
Cdd:cd06611  13 LGDGAFGKVYKAQHkETGLFAAAKIIQIESEEELEDFMVEIDILSECK-HPNIVGLYE--AYFYENKLW---ILIEFCDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKkLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG-SATNKflnpqkdgv 214
Cdd:cd06611  87 GALDSIMLE-LERGLTEPQIRYVCRQMLEALNFLHSHK--VIHRDLKAGNILLTLDGDVKLADFGvSAKNK--------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 215 nvveEEIKKYTTL----SYRAPEMINL--YGGKPITTKADIWALGCLLYKLC--------------FFTLPFGESQvaic 274
Cdd:cd06611 155 ----STLQKRDTFigtpYWMAPEVVACetFKDNPYDYKADIWSLGITLIELAqmepphhelnpmrvLLKILKSEPP---- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 275 dgnfTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAF 316
Cdd:cd06611 227 ----TLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPF 264
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
53-313 2.05e-22

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: 97.11  E-value: 2.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR----THGGIRCALKRMYVNNM-PDLNV-CKREITIMKELSgHKNIVGYLDCAVNSISdnvweV 126
Cdd:cd08222   4 VVRKLGSGNFGTVYLVSdlkaTADEELKVLKEISVGELqPDETVdANREAKLLSKLD-HPAIVKFHDSFVEKES-----F 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMN--KKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDggNYV-LCDFGSAt 203
Cdd:cd08222  78 CIVTEYCEGGDLDDKISeyKKSGTTIDENQILDWFIQLLLAVQYMHERR--ILHRDLKAKNIFLKN--NVIkVGDFGIS- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nKFLNPQKDgvnvveeEIKKYT-TLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPF-GESQVA----ICDGN 277
Cdd:cd08222 153 -RILMGTSD-------LATTFTgTPYYMSPEVLKHEG---YNSKSDIWSLGCILYEMCCLKHAFdGQNLLSvmykIVEGE 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 278 F-TIPDnsRYSRNIHCLIRFMLEPDPEHRP---DIFQVSY 313
Cdd:cd08222 222 TpSLPD--KYSKELNAIYSRMLNKDPALRPsaaEILKIPF 259
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
73-311 2.26e-22

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: 96.97  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  73 GIRCALKRMYvnnmpDLNVCKREITIMKELSGHKNIVGYLDCAVNsISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTE 152
Cdd:cd14089  26 GEKFALKVLR-----DNPKARREVELHWRASGCPHIVRIIDVYEN-TYQGRKCLLVVMECMEGGELFSRIQERADSAFTE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 153 PEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGN---YVLCDFGSA----TNKFLN-PQkdgvnvveeeikkY 224
Cdd:cd14089 100 REAAEIMRQIGSAVAHLHSMN--IAHRDLKPENLLYSSKGPnaiLKLTDFGFAkettTKKSLQtPC-------------Y 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 225 TTLsYRAPEMInlyGGKPITTKADIWALGCLLY-KLCFFTlPFGESQVA---------ICDGNFTIPDN--SRYSRNIHC 292
Cdd:cd14089 165 TPY-YVAPEVL---GPEKYDKSCDMWSLGVIMYiLLCGYP-PFYSNHGLaispgmkkrIRNGQYEFPNPewSNVSEEAKD 239
                       250
                ....*....|....*....
gi 38787904 293 LIRFMLEPDPEHRPDIFQV 311
Cdd:cd14089 240 LIRGLLKTDPSERLTIEEV 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
93-311 2.30e-22

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: 97.46  E-value: 2.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLqtGFTEPEVLQIFCDTCEAVARLHQc 172
Cdd:cd14084  59 ETEIEILKKLS-HPCII-----KIEDFFDAEDDYYIVLELMEGGELFDRVVSNK--RLKEAICKLYFYQMLLAVKYLHS- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 kTPIIHRDLKVENILLNDGGNYVL---CDFGSATNkflnpqkdgvnVVEEEIKKYT--TLSYRAPEMINLYGGKPITTKA 247
Cdd:cd14084 130 -NGIIHRDLKPENVLLSSQEEECLikiTDFGLSKI-----------LGETSLMKTLcgTPTYLAPEVLRSFGTEGYTRAV 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 248 DIWALGCLLYkLCFF-TLPFGES--------QVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14084 198 DCWSLGVILF-ICLSgYPPFSEEytqmslkeQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEA 269
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
54-311 4.09e-22

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 95.91  E-value: 4.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFSTVFLVRTH-GGIRCALKRMYVN--NMPDLNVCKREITIMKELSGHKNIVGYLDCavnsisdnvWE----V 126
Cdd:cd13997   5 LEQIGSGSFSEVFKVRSKvDGCLYAVKKSKKPfrGPKERARALREVEAHAALGQHPNIVRYYSS---------WEegghL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMNKK-LQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd13997  76 YIQMELCENGSLQDALEELsPISKLSEAEVWDLLLQVALGLAFIHSKG--IVHLDIKPDNIFISNKGTCKIGDFGLATRL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQkdgvnvVEEEIKKYTtlsyrAPEMINLYggKPITTKADIWALGCLLYKL-CFFTLPF-GESQVAICDGNFTIPDN 283
Cdd:cd13997 154 ETSGD------VEEGDSRYL-----APELLNEN--YTHLPKADIFSLGVTVYEAaTGEPLPRnGQQWQQLRQGKLPLPPG 220
                       250       260
                ....*....|....*....|....*...
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd13997 221 LVLSQELTRLLKVMLDPDPTRRPTADQL 248
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
57-305 4.49e-22

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: 96.14  E-value: 4.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIVgyldCAVNSISDNVWeVLILMEY 132
Cdd:cd05572   1 LGVGGFGRVELVQLKSkGRTFALKCVKKRHIVQTRQqehIFSEKEILEECN-SPFIV----KLYRTFKDKKY-LYMLMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQV--VNQMNKKLqtgftePEVLQIFCDTC--EAVARLHQckTPIIHRDLKVENILLNDGGnYV-LCDFGSAtnKFL 207
Cdd:cd05572  75 CLGGELwtILRDRGLF------DEYTARFYTACvvLAFEYLHS--RGIIYRDLKPENLLLDSNG-YVkLVDFGFA--KKL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKdgvnvveeeiKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQV-------AICDGN 277
Cdd:cd05572 144 GSGR----------KTWTfcgTPEYVAPEIIL---NKGYDFSVDYWSLGILLYELLTGRPPFGGDDEdpmkiynIILKGI 210
                       250       260
                ....*....|....*....|....*...
gi 38787904 278 FTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05572 211 DKIEFPKYIDKNAKNLIKQLLRRNPEER 238
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
57-306 6.57e-22

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 96.28  E-value: 6.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH-GGIRCALKRMYVN-NMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSIsdnvwEVLILMEYCR 134
Cdd:cd14046  14 LGKGAFGQVVKVRNKlDGRYYAIKKIKLRsESKNNSRILREVMLLSRLN-HQHVVRYYQAWIERA-----NLYIQMEYCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNP----- 209
Cdd:cd14046  88 KSTLRDLIDSGLF--QDTDRLWRLFRQILEGLAYIHS--QGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVelatq 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 ---QKDGVNVVEEE--IKKYTTLSYRAPEMINLYGGKpITTKADIWALGCLLYKLCFftlPFGES----QV--AICDGNF 278
Cdd:cd14046 164 dinKSTSAALGSSGdlTGNVGTALYVAPEVQSGTKST-YNEKVDMYSLGIIFFEMCY---PFSTGmervQIltALRSVSI 239
                       250       260       270
                ....*....|....*....|....*....|
gi 38787904 279 TIPDNSRYSRNIHC--LIRFMLEPDPEHRP 306
Cdd:cd14046 240 EFPPDFDDNKHSKQakLIRWLLNHDPAKRP 269
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
94-254 7.70e-22

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: 96.14  E-value: 7.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYcragqvvnqMNKKLQT-------GFTEPEVLQIFCDTCEAV 166
Cdd:cd07843  53 REINILLKLQ-HPNIVTVKEVVVGSNLDKIY---MVMEY---------VEHDLKSlmetmkqPFLQSEVKCLMLQLLSGV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 167 ARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFLNPqkdgvnvveeeIKKYT----TLSYRAPEMinLYGGKP 242
Cdd:cd07843 120 AHLHDNW--ILHRDLKTSNLLLNNRGILKICDFGLA-REYGSP-----------LKPYTqlvvTLWYRAPEL--LLGAKE 183
                       170
                ....*....|..
gi 38787904 243 ITTKADIWALGC 254
Cdd:cd07843 184 YSTAIDMWSVGC 195
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
60-306 1.98e-21

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: 94.59  E-value: 1.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKReitIMKElsghKNIVgyldCAVNSIS-----------DNVWevl 127
Cdd:cd05579   4 GAYGRVYLAKKKStGDLYAIKVIKKRDMIRKNQVDS---VLAE----RNIL----SQAQNPFvvklyysfqgkKNLY--- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAG---QVVNQMNKklqtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG---- 200
Cdd:cd05579  70 LVMEYLPGGdlySLLENVGA-----LDEDVARIYIAEIVLALEYLHSHG--IIHRDLKPDNILIDANGHLKLTDFGlskv 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 ---SATNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA----- 272
Cdd:cd05579 143 glvRRQIKLSIQKKSNGAPEKEDRRIVGTPDYLAPEILL---GQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEeifqn 219
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 273 ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05579 220 ILNGKIEWPEDPEVSDEAKDLISKLLTPDPEKRL 253
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
57-271 2.64e-21

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 94.95  E-value: 2.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNV-----CKREITIMKELSgHKNIVGYLDcaVNSISDNVWEVLILM 130
Cdd:cd07841   8 LGEGTYAVVYKARdKETGRIVAIKKIKLGERKEAKDginftALREIKLLQELK-HPNIIGLLD--VFGHKSNINLVFEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYcRAGQVVNqmNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnKFLNPQ 210
Cdd:cd07841  85 ET-DLEKVIK--DKSIV--LTPADIKSYMLMTLRGLEYLHSNW--ILHRDLKPNNLLIASDGVLKLADFGLAR-SFGSPN 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 211 kdgvnvveeeiKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLLYKLCFFTlPF--GESQV 271
Cdd:cd07841 157 -----------RKMThqvvTRWYRAPEL--LFGARHYGVGVDMWSVGCIFAELLLRV-PFlpGDSDI 209
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
50-305 4.19e-21

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: 93.55  E-value: 4.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDCAvnsiSDNVWEV 126
Cdd:cd14069   2 DWDLVQTLGEGAFGEVFLaVNRNTEEAVAVKFVDMKRAPgdCPENIKKEVCIQKMLS-HKNVVRFYGHR----REGEFQY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILmEYCRAGQVVNQMNKKLqtGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnKF 206
Cdd:cd14069  77 LFL-EYASGGELFDKIEPDV--GMPEDVAQFYFQQLMAGLKYLHSCG--ITHRDIKPENLLLDENDNLKISDFGLAT-VF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LNPQKdgvnvvEEEIKKYT-TLSYRAPEMI--NLYGGKPittkADIWALGCLLYKLCFFTLPFGESQVA-------ICDG 276
Cdd:cd14069 151 RYKGK------ERLLNKMCgTLPYVAPELLakKKYRAEP----VDVWSCGIVLFAMLAGELPWDQPSDScqeysdwKENK 220
                       250       260
                ....*....|....*....|....*....
gi 38787904 277 NFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14069 221 KTYLTPWKKIDTAALSLLRKILTENPNKR 249
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
52-311 5.58e-21

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: 93.13  E-value: 5.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLV--RTHGgIRCALKRMYVNNMPDLNVCK---REITIMKELSgHKNIVGYLDCavnsISDNVwEV 126
Cdd:cd14162   3 IVGKTLGHGSYAVVKKAysTKHK-CKVAIKIVSKKKAPEDYLQKflpREIEVIKGLK-HPNLICFYEA----IETTS-RV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMNKKlqtGF-TEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd14162  76 YIIMELAENGDLLDYIRKN---GAlPEPQARRWFRQLVAGVEYCH--SKGVVHRDLKCENLLLDKNNNLKITDFGFARGV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNpqKDGVNVVEEeikkyT---TLSYRAPEMINlygGKPIT-TKADIWALGCLLYKLCFFTLPFGESQVAI------CD 275
Cdd:cd14162 151 MKT--KDGKPKLSE-----TycgSYAYASPEILR---GIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVllkqvqRR 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 276 GNFtiPDNSRYSRNIHCLIRFMLEPDPEhRPDIFQV 311
Cdd:cd14162 221 VVF--PKNPTVSEECKDLILRMLSPVKK-RITIEEI 253
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
53-307 7.88e-21

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: 92.37  E-value: 7.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWevlILME 131
Cdd:cd06613   4 LIQRIGSGTYGDVYKARnIATGELAAVKVIKLEPGDDFEIIQQEISMLKECR-HPNIVAYFGSYLRR--DKLW---IVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNkklQTG-FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpq 210
Cdd:cd06613  78 YCGGGSLQDIYQ---VTGpLSELQIAYVCRETLKGLAYLHS--TGKIHRDIKGANILLTEDGDVKLADFGVSA------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 kdgvnVVEEEIKKYT----TLSYRAPEMINLYGGKPITTKADIWALGCLLYKLcfftlpfGESQVAICDGN-----FTIP 281
Cdd:cd06613 146 -----QLTATIAKRKsfigTPYWMAPEVAAVERKGGYDGKCDIWALGITAIEL-------AELQPPMFDLHpmralFLIP 213
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 282 ----------DNSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd06613 214 ksnfdppklkDKEKWSPDFHDFIKKCLTKNPKKRPT 249
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
57-266 1.16e-20

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: 92.90  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKR---EITIMKELSgHKNIVGYLDCAVNSISDNVWEVLIL-ME 131
Cdd:cd13989   1 LGSGGFGYVTLWKHQDtGEYVAIKKCRQELSPSDKNRERwclEVQIMKKLN-HPNVVSARDVPPELEKLSPNDLPLLaME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNK-KLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGN---YVLCDFGSAtnKFL 207
Cdd:cd13989  80 YCSGGDLRKVLNQpENCCGLKESEVRTLLSDISSAISYLHENR--IIHRDLKPENIVLQQGGGrviYKLIDLGYA--KEL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 208 NPQKDGVNVVeeeikkyTTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd13989 156 DQGSLCTSFV-------GTLQYLAPE---LFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
88-305 1.18e-20

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: 92.42  E-value: 1.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  88 DLNVCKREITIMKELSGHKNIVGYLDcavnsisdnVWE----VLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTC 163
Cdd:cd14093  51 LREATRREIEILRQVSGHPNIIELHD---------VFEsptfIFLVFELCRKGELFDYLTEVVT--LSEKKTRRIMRQLF 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 EAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPqkdgvnvvEEEIKKYT-TLSYRAPEMI--NLYGG 240
Cdd:cd14093 120 EAVEFLHSLN--IVHRDLKPENILLDDNLNVKISDFGFATR--LDE--------GEKLRELCgTPGYLAPEVLkcSMYDN 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 241 KPITTK-ADIWALGCLLYKLCFFTLPF-GESQV----AICDGN--FTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14093 188 APGYGKeVDMWACGVIMYTLLAGCPPFwHRKQMvmlrNIMEGKyeFGSPEWDDISDTAKDLISKLLVVDPKKR 260
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
94-305 2.01e-20

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: 91.65  E-value: 2.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVWEVLILMEycrAGQVvnqMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14118  63 REIAILKKLD-HPNVVKLVEVLDDPNEDNLYMVFELVD---KGAV---MEVPTDNPLSEETARSYFRDIVLGIEYLHYQK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 tpIIHRDLKVENILLNDGGNYVLCDFGsATNKFLnpqkdGVNVVEEeiKKYTTLSYRAPEMI----NLYGGKPittkADI 249
Cdd:cd14118 136 --IIHRDIKPSNLLLGDDGHVKIADFG-VSNEFE-----GDDALLS--STAGTPAFMAPEALsesrKKFSGKA----LDI 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 250 WALGCLLYKLCFFTLPFGESQV-----AICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14118 202 WAMGVTLYCFVFGRCPFEDDHIlglheKIKTDPVVFPDDPVVSEQLKDLILRMLDKNPSER 262
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
59-256 2.60e-20

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: 91.86  E-value: 2.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  59 EGGFSTVFLVR-THGGIRCALKRMYVNNMPD------LnvckREITIMKELSgHKNIVGYLDCAVNSISD----NVWEVL 127
Cdd:cd07840   9 EGTYGQVYKARnKKTGELVALKKIRMENEKEgfpitaI----REIKLLQKLD-HPNVVRLKEIVTSKGSAkykgSIYMVF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKklqtgFTEPEV----LQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd07840  84 EYMDHDLTGLLDNPEVK-----FTESQIkcymKQLL----EGLQYLHSNG--ILHRDIKGSNILINNDGVLKLADFGLA- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 204 nKFLNPQKDGvnvveeeikKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLL 256
Cdd:cd07840 152 -RPYTKENNA---------DYTnrviTLWYRPPEL--LLGATRYGPEVDMWSVGCIL 196
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
94-311 5.38e-20

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: 90.24  E-value: 5.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELsGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVN--QMNKKLQtgftEPEVLQIFCDTCEAVARLHq 171
Cdd:cd14076  55 REINILKGL-THPNIVRLLD-----VLKTKKYIGIVLEFVSGGELFDyiLARRRLK----DSVACRLFAQLISGVAYLH- 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 cKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNpqkdgvnvvEEEIKKYTTLS--YRAPEMIN---LYGGkpitTK 246
Cdd:cd14076 124 -KKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHF---------NGDLMSTSCGSpcYAAPELVVsdsMYAG----RK 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 247 ADIWALGCLLYKLCFFTLPF--------GESQVA----ICDGNFTIPDN-SRYSRNihcLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14076 190 ADIWSCGVILYAMLAGYLPFdddphnpnGDNVPRlyryICNTPLIFPEYvTPKARD---LLRRILVPNPRKRIRLSAI 264
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
94-312 6.41e-20

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: 89.91  E-value: 6.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELsGHKNIVGYLDCAVNSISdnvweVLILMEYCRAG-------QVVNQMNKKLQTGFTEPEVLQIFCDTCEAV 166
Cdd:cd00192  45 KEARVMKKL-GHPNVVRLLGVCTEEEP-----LYLVMEYMEGGdlldflrKSRPVFPSPEPSTLSLKDLLSFAIQIAKGM 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 167 ARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqKDGVNVVEEEIKKYTTLSYR--APEMI--NLYggkp 242
Cdd:cd00192 119 EYLASKK--FVHRDLAARNCLVGEDLVVKISDFGLS--------RDIYDDDYYRKKTGGKLPIRwmAPESLkdGIF---- 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 243 iTTKADIWALGCLLYKLcfFTL---PFGE---SQV--AICDGNftipdnsRYSRNIHC---LIRFMLE---PDPEHRPDI 308
Cdd:cd00192 185 -TSKSDVWSFGVLLWEI--FTLgatPYPGlsnEEVleYLRKGY-------RLPKPENCpdeLYELMLScwqLDPEDRPTF 254

                ....
gi 38787904 309 FQVS 312
Cdd:cd00192 255 SELV 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
57-305 6.51e-20

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: 89.59  E-value: 6.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-----THGGIRC-ALKRMYVNNMPDLNvckREITIMKELSgHKNIVGYLDCaVNSiSDNVWEVlilM 130
Cdd:cd14009   1 IGRGSFATVWKGRhkqtgEVVAIKEiSRKKLNKKLQENLE---SEIAILKSIK-HPNIVRLYDV-QKT-EDFIYLV---L 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVvnqmNKKLQTGFTEPEvlqifcdtceAVAR------------LHQckTPIIHRDLKVENILLN-DGGNYVL- 196
Cdd:cd14009  72 EYCAGGDL----SQYIRKRGRLPE----------AVARhfmqqlasglkfLRS--KNIIHRDLKPQNLLLStSGDDPVLk 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 197 -CDFGSAtnKFLNPQkdgvNVVEeeikkytTLS----YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQ 270
Cdd:cd14009 136 iADFGFA--RSLQPA----SMAE-------TLCgsplYMAPEILQ---FQKYDAKADLWSVGAILFEMLVGKPPFrGSNH 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 271 VAI------CDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14009 200 VQLlrnierSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
57-312 6.82e-20

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: 90.07  E-value: 6.82e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTV---FLVRTHGGIRCALKRmyVN-NMPD---LNVCK---REITIMKELSgHKNIVGYLDCAvnSISDNVWev 126
Cdd:cd13990   8 LGKGGFSEVykaFDLVEQRYVACKIHQ--LNkDWSEekkQNYIKhalREYEIHKSLD-HPRIVKLYDVF--EIDTDSF-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAgqvvNQMNKKLQTGFTEPEVLQ--IFCDTCEAVARLHQCKTPIIHRDLKVENILLNDG---GNYVLCDFGs 201
Cdd:cd13990  81 CTVLEYCDG----NDLDFYLKQHKSIPEREArsIIMQVVSALKYLNEIKPPIIHYDLKPGNILLHSGnvsGEIKITDFG- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 aTNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKP-ITTKADIWALGCLLYKLCFFTLPFGE--SQVAICDGN- 277
Cdd:cd13990 156 -LSKIMDDESYNSDGMELTSQGAGTYWYLPPECFVVGKTPPkISSKVDVWSVGVIFYQMLYGRKPFGHnqSQEAILEENt 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 278 ------FTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd13990 235 ilkateVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLA 275
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
52-305 8.03e-20

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: 89.20  E-value: 8.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVR--------THGGIRCALKRMYVNNMPdlnvcKR---EITIMKELSGHKNIVGYLDCAVNSis 120
Cdd:cd14019   4 RIIEKIGEGTFSSVYKAEdklhdlydRNKGRLVALKHIYPTSSP-----SRilnELECLERLGGSNNVSGLITAFRNE-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 121 DNVWEVLILMEYCRAGQVVNQMNKklqtgftePEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDF 199
Cdd:cd14019  77 DQVVAVLPYIEHDDFRDFYRKMSL--------TDIRIYLRNLFKALKHVHSFG--IIHRDVKPGNFLYNrETGKGVLVDF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATNKFLNPQKDGvnvveeeiKKYTTLSYRAPEMINLYGGKpiTTKADIWALGC-LLYKLC-----FFTLPFGESQVAI 273
Cdd:cd14019 147 GLAQREEDRPEQRA--------PRAGTRGFRAPEVLFKCPHQ--TTAIDIWSAGViLLSILSgrfpfFFSSDDIDALAEI 216
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 274 CdgnfTIpdnsRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14019 217 A----TI----FGSDEAYDLLDKLLELDPSKR 240
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
57-311 8.14e-20

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: 89.84  E-value: 8.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGG----IRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcavnsISDNVWEVLILME 131
Cdd:cd14098   8 LGSGTFAEVKKaVEVETGkmraIKQIVKRKVAGNDKNLQLFQREINILKSLE-HPGIVRLID-----WYEDDQHIYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQM--NKKLQTGFTEPEVLQIfcdtCEAVARLHqcKTPIIHRDLKVENILL-NDGGNYV-LCDFGSA----T 203
Cdd:cd14098  82 YVEGGDLMDFImaWGAIPEQHARELTKQI----LEAMAYTH--SMGITHRDLKPENILItQDDPVIVkISDFGLAkvihT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 NKFLNpqkdgvnvveeeiKKYTTLSYRAPEMI-----NLYGGkpITTKADIWALGCLLYKLCFFTLPF-GESQVA----I 273
Cdd:cd14098 156 GTFLV-------------TFCGTMAYLAPEILmskeqNLQGG--YSNLVDMWSVGCLVYVMLTGALPFdGSSQLPvekrI 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 274 CDGNFTI-PDNS-RYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14098 221 RKGRYTQpPLVDfNISEEAIDFILRLLDVDPEKRMTAAQA 260
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
53-256 2.20e-19

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: 89.30  E-value: 2.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLN--VCKREITIMKELSgHKNIVGYLDCAVNSISDN------V 123
Cdd:cd07866  12 ILGKLGEGTFGEVYkARQIKTGRVVALKKILMHNEKDGFpiTALREIKILKKLK-HPNVVPLIDMAVERPDKSkrkrgsV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 124 WEVLILMEYCRAGQVVNQMNKklqtgFTEPEV----LQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd07866  91 YMVTPYMDHDLSGLLENPSVK-----LTESQIkcymLQLL----EGINYLHENH--ILHRDIKAANILIDNQGILKIADF 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 200 GSATNKFLNPQKDGvNVVEEEIKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLL 256
Cdd:cd07866 160 GLARPYDGPPPNPK-GGGGGGTRKYTnlvvTRWYRPPEL--LLGERRYTTAVDIWGIGCVF 217
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
50-306 2.32e-19

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 88.21  E-value: 2.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFlVRTHGGIRCALKRmyVNNMPDlNVCKREiTIMKELSG----HKNIVGYLD----CAVNSISd 121
Cdd:cd13979   4 PLRLQEPLGSGGFGSVY-KATYKGETVAVKI--VRRRRK-NRASRQ-SFWAELNAarlrHENIVRVLAaetgTDFASLG- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 nvwevLILMEYCRAG---QVVNQMNKKLQTGftepEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCD 198
Cdd:cd13979  78 -----LIIMEYCGNGtlqQLIYEGSEPLPLA----HRILISLDIARALRFCH--SHGIVHLDVKPANILISEQGVCKLCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 199 FGSATnkflnpQKDGVNVVEEEIKK-YTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAI--- 273
Cdd:cd13979 147 FGCSV------KLGEGNEVGTPRSHiGGTYTYRAPELLK---GERVTPKADIYSFGITLWQMLTRELPYaGLRQHVLyav 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 274 -------CDGNFTipdNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd13979 218 vakdlrpDLSGLE---DSEFGQRLRSLISRCWSAQPAERP 254
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
51-307 3.27e-19

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: 87.55  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    51 VTLEESLAEGGFSTVFL-----VRTHGGIRCALKRMYVNNMPDLNVC-KREITIMKELSgHKNIVGYLDCAVNSIsdnvw 124
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKgtlkgEGENTKIKVAVKTLKEGADEEEREDfLEEASIMKKLD-HPNIVKLLGVCTQGE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   125 EVLILMEYCRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATN 204
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKHKRK-LTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVSENLVVKISDFGLSRD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   205 KFlnpqKDGVNVVEEE----IKkyttlsYRAPEMINlYGGkpITTKADIWALGCLLYKLcfFTL---PFGE---SQVA-- 272
Cdd:pfam07714 152 IY----DDDYYRKRGGgklpIK------WMAPESLK-DGK--FTSKSDVWSFGVLLWEI--FTLgeqPYPGmsnEEVLef 216
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 38787904   273 ICDGN-FTIPDNSrySRNIHCLIRFMLEPDPEHRPD 307
Cdd:pfam07714 217 LEDGYrLPQPENC--PDELYDLMKQCWAYDPEDRPT 250
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
57-311 3.87e-19

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: 87.29  E-value: 3.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGGIRCALKRMYVNN------MPDLNVCKREITIMKELS--GHKNIVGYLDCAvnSISDNVwevL 127
Cdd:cd14005   8 LGKGGFGTVYSgVRIRDGLPVAVKFVPKSRvtewamINGPVPVPLEIALLLKASkpGVPGVIRLLDWY--ERPDGF---L 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFGSATnkf 206
Cdd:cd14005  83 LIMERPEPCQDLFDFITERGA-LSENLARIIFRQVVEAVRHCHQRG--VLHRDIKDENLLINlRTGEVKLIDFGCGA--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnPQKDGVnvveeeikkYT----TLSYRAPEMI--NLYGGKPITtkadIWALGCLLYKLCFFTLPFgESQVAICDGNFTI 280
Cdd:cd14005 157 --LLKDSV---------YTdfdgTRVYSPPEWIrhGRYHGRPAT----VWSLGILLYDMLCGDIPF-ENDEQILRGNVLF 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 281 PdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14005 221 R--PRLSKECCDLISRCLQFDPSKRPSLEQI 249
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
95-305 1.01e-18

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: 86.23  E-value: 1.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQCKt 174
Cdd:cd14095  48 EVAILRRVK-HPNIVQLIE-----EYDTDTELYLVMELVKGGDLFDAI--TSSTKFTERDASRMVTDLAQALKYLHSLS- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 pIIHRDLKVENILLNDGGNYVLC----DFGSATnkflnpqkdgvnVVEEEIkkYT---TLSYRAPEMINL--YGgkpitT 245
Cdd:cd14095 119 -IVHRDIKPENLLVVEHEDGSKSlklaDFGLAT------------EVKEPL--FTvcgTPTYVAPEILAEtgYG-----L 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 246 KADIWALGCLLYK-LCFFTlPFGES---------QVAICDGNFTIP--DN-SRYSRNihcLIRFMLEPDPEHR 305
Cdd:cd14095 179 KVDIWAAGVITYIlLCGFP-PFRSPdrdqeelfdLILAGEFEFLSPywDNiSDSAKD---LISRMLVVDPEKR 247
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
92-305 1.18e-18

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: 87.36  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  92 CKREITIMKELSGHKNIVGYldcaVNSISDNVwEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd14092  45 TSREVQLLRLCQGHPNIVKL----HEVFQDEL-HTYLVMELLRGGELLERIRKKKR--FTESEASRIMRQLVSAVSFMHS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKtpIIHRDLKVENILL---NDGGNYVLCDFGSATNKflnpqkdgvnvVEEEIKKyT---TLSYRAPEMINLYGGKPITT 245
Cdd:cd14092 118 KG--VVHRDLKPENLLFtdeDDDAEIKIVDFGFARLK-----------PENQPLK-TpcfTLPYAAPEVLKQALSTQGYD 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 246 KA-DIWALGCLLYKLCFFTLPF----GESQVA-----ICDGNFTI--PDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14092 184 EScDLWSLGVILYTMLSGQVPFqspsRNESAAeimkrIKSGDFSFdgEEWKNVSSEAKSLIQGLLTVDPSKR 255
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
48-306 1.23e-18

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: 86.39  E-value: 1.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLV--RTHGGIRcALKRMYVNNmpdlNVCKREITIMKELSgHKNIVGYLDC----------- 114
Cdd:cd14047   5 RQDFKEIELIGSGGFGQVFKAkhRIDGKTY-AIKRVKLNN----EKAEREVKALAKLD-HPNIVRYNGCwdgfdydpets 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 115 AVNSISDNVWEVLILMEYCRAG---QVVNQMNKKLQTGFtepEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDG 191
Cdd:cd14047  79 SSNSSRSKTKCLFIQMEFCEKGtleSWIEKRNGEKLDKV---LALEIFEQITKGVEYIHSKK--LIHRDLKPSNIFLVDT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 192 GNYVLCDFGSATNkflnpQKDGVnvveEEIKKYTTLSYRAPEMINL--YGgkpitTKADIWALGCLLYKLCF-FTLPFGE 268
Cdd:cd14047 154 GKVKIGDFGLVTS-----LKNDG----KRTKSKGTLSYMSPEQISSqdYG-----KEVDIYALGLILFELLHvCDSAFEK 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 38787904 269 SQVAICDGNFTIPDN--SRYSRNIHcLIRFMLEPDPEHRP 306
Cdd:cd14047 220 SKFWTDLRNGILPDIfdKRYKIEKT-IIKKMLSKKPEDRP 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
53-311 1.27e-18

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: 85.92  E-value: 1.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALK-----RMYVNNMpDLNVcKREITIMKELSgHKNIVGYLdcAVNSISDNVWev 126
Cdd:cd14663   4 LGRTLGEGTFAKVKFARnTKTGESVAIKiidkeQVAREGM-VEQI-KREIAIMKLLR-HPNIVELH--EVMATKTKIF-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 lILMEYCRAGQVVNQM--NKKLqtgfTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFG-SA- 202
Cdd:cd14663  77 -FVMELVTGGELFSKIakNGRL----KEDKARKYFQQLIDAVDYCH--SRGVFHRDLKPENLLLDEDGNLKISDFGlSAl 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TNKFlnpQKDGVnvveeeikKYT---TLSYRAPEMI--NLYGGkpitTKADIWALGCLLYKLCFFTLPFGESQVA----- 272
Cdd:cd14663 150 SEQF---RQDGL--------LHTtcgTPNYVAPEVLarRGYDG----AKADIWSCGVILFVLLAGYLPFDDENLMalyrk 214
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 273 ICDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14663 215 IMKGEFEYP--RWFSPGAKSLIKRILDPNPSTRITVEQI 251
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
57-305 2.13e-18

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: 85.85  E-value: 2.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYCrA 135
Cdd:cd06643  13 LGDGAFGKVYKAQNkETGILAAAKVIDTKSEEELEDYMVEIDILASCD-HPNIVKLLDAFY--YENNLW---ILIEFC-A 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQTGFTEPEVlQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG-SATNKFLNPQKDG 213
Cdd:cd06643  86 GGAVDAVMLELERPLTEPQI-RVVCkQTLEALVYLHENK--IIHRDLKAGNILFTLDGDIKLADFGvSAKNTRTLQRRDS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 VnvveeeikkYTTLSYRAPE--MINLYGGKPITTKADIWALGCLLYKLCFFTLPFGES-------QVAICDGNfTIPDNS 284
Cdd:cd06643 163 F---------IGTPYWMAPEvvMCETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELnpmrvllKIAKSEPP-TLAQPS 232
                       250       260
                ....*....|....*....|.
gi 38787904 285 RYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd06643 233 RWSPEFKDFLRKCLEKNVDAR 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
51-306 3.18e-18

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 84.89  E-value: 3.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904     51 VTLEESLAEGGFSTVFL-----VRTHGGIRCALKRMyvNNMPDLNVCK---REITIMKELSgHKNIVGYLdcAVNSISDN 122
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKgklkgKGGKKKVEVAVKTL--KEDASEQQIEeflREARIMRKLD-HPNVVKLL--GVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    123 VWevlILMEYCRAGQVVNQMnKKLQTGFTEPEVLQIFCDTCEAVARLHQCktPIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:smart00219  76 LY---IVMEYMEGGDLLSYL-RKNRPKLSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGENLVVKISDFGLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    203 tnkflnpqkdgVNVVEEEIKKYTT--LSYR--APEMINL--YggkpiTTKADIWALGCLLYKLcfFTL---PFGE---SQ 270
Cdd:smart00219 150 -----------RDLYDDDYYRKRGgkLPIRwmAPESLKEgkF-----TSKSDVWSFGVLLWEI--FTLgeqPYPGmsnEE 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 38787904    271 VA--ICDGNF-TIPDNsrysrnihC---LIRFMLE---PDPEHRP 306
Cdd:smart00219 212 VLeyLKNGYRlPQPPN--------CppeLYDLMLQcwaEDPEDRP 248
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
55-306 3.90e-18

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: 85.17  E-value: 3.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIRC-ALKRMYVNNMPDLNvcK---REITIMKELSgHKNIVGY----LDCAVNSISdnvwev 126
Cdd:cd06621   7 SSLGEGAGGSVTKCRLRNTKTIfALKTITTDPNPDVQ--KqilRELEINKSCA-SPYIVKYygafLDEQDSSIG------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 lILMEYCRAGQVvNQMNKKL--QTGFTEPEVL-QIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd06621  78 -IAMEYCEGGSL-DSIYKKVkkKGGRIGEKVLgKIAESVLKGLSYLHSRK--IIHRDIKPSNILLTRKGQVKLCDFGVSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nkflnpqkdgvNVVEEEIKKYTTLS-YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---GESQVAICD---- 275
Cdd:cd06621 154 -----------ELVNSLAGTFTGTSyYMAPERIQ---GGPYSITSDVWSLGLTLLEVAQNRFPFppeGEPPLGPIEllsy 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 276 ----GNFTIPD----NSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06621 220 ivnmPNPELKDepenGIKWSESFKDFIEKCLEKDGTRRP 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
53-311 4.07e-18

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: 84.37  E-value: 4.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRtH--GGIRCALKRMYVNNMPDLNVCK--REITIMKELSgHKNIVgyldcavnsisdNVWEVL- 127
Cdd:cd14071   4 IERTIGKGNFAVVKLAR-HriTKTEVAIKIIDKSQLDEENLKKiyREVQIMKMLN-HPHII------------KLYQVMe 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ------ILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGs 201
Cdd:cd14071  70 tkdmlyLVTEYASNGEIFDYLAQ--HGRMSEKEARKKFWQILSAVEYCH--KRHIVHRDLKAENLLLDANMNIKIADFG- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 atnkFLNPQKDGvnvveEEIKKYT-TLSYRAPEminLYGGKPIT-TKADIWALGCLLYKLCFFTLPFGESQVA-----IC 274
Cdd:cd14071 145 ----FSNFFKPG-----ELLKTWCgSPPYAAPE---VFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQtlrdrVL 212
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 275 DGNFTIPdnsrY--SRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14071 213 SGRFRIP----FfmSTDCEHLIRRMLVLDPSKRLTIEQI 247
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
52-311 5.01e-18

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: 84.78  E-value: 5.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLV--RTHGGIRCALKRMYVN--NMPDLNVCKREITIMKELS--GHKNIVGYLDcavnsisdnVWE 125
Cdd:cd14052   3 ANVELIGSGEFSQVYKVseRVPTGKVYAVKKLKPNyaGAKDRLRRLEEVSILRELTldGHDNIVQLID---------SWE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 ----VLILMEYCRAGQVVNQMNKK-LQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd14052  74 yhghLYIQTELCENGSLDVFLSELgLLGRLDEFRVWKILVELSLGLRFIHDHH--FVHLDLKPANVLITFEGTLKIGDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SATnkflnpqkdgVNVVEEEIKKYTTLSYRAPEMI--NLYgGKPittkADIWALGCLLYKLCF-FTLP-FGESQVAICDG 276
Cdd:cd14052 152 MAT----------VWPLIRGIEREGDREYIAPEILseHMY-DKP----ADIFSLGLILLEAAAnVVLPdNGDAWQKLRSG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 277 NFT------IPDNSRYSRN-----------------IHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14052 217 DLSdaprlsSTDLHSASSPssnpppdppnmpilsgsLDRVVRWMLSPEPDRRPTADDV 274
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
51-306 6.61e-18

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: 83.75  E-value: 6.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904     51 VTLEESLAEGGFSTVFL-----VRTHGGIRCALKRMyvNNMPDLNVCK---REITIMKELSgHKNIVGYLdcAVNSISDN 122
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKgtlkgKGDGKEVEVAVKTL--KEDASEQQIEeflREARIMRKLD-HPNIVKLL--GVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    123 VWevlILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:smart00221  76 LM---IVMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKN--FIHRDLAARNCLVGENLVVKISDFGLS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    203 tnkflnpqKDGvnvveEEIKKYTTLS----YR--APEMIN--LYggkpiTTKADIWALGCLLYKLcfFTL---PFGE--- 268
Cdd:smart00221 151 --------RDL-----YDDDYYKVKGgklpIRwmAPESLKegKF-----TSKSDVWSFGVLLWEI--FTLgeePYPGmsn 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 38787904    269 SQVAicdgnFTIPDNSRYSRNIHC---LIRFMLE---PDPEHRP 306
Cdd:smart00221 211 AEVL-----EYLKKGYRLPKPPNCppeLYKLMLQcwaEDPEDRP 249
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
57-306 6.90e-18

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: 84.00  E-value: 6.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLdcavNSISDNVWeVLILMEYCRA 135
Cdd:cd06624  16 LGKGTFGVVYAARdLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLS-HKNIVQYL----GSVSEDGF-FKIFMEQVPG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVN--------QMNKKLQTGFTEPEVLqifcdtcEAVARLHQCKtpIIHRDLKVENILLND-GGNYVLCDFGsaTNKF 206
Cdd:cd06624  90 GSLSAllrskwgpLKDNENTIGYYTKQIL-------EGLKYLHDNK--IVHRDIKGDNVLVNTySGVVKISDFG--TSKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LNpqkdGVNVVEEEIKKytTLSYRAPEMIN--LYG-GKPittkADIWALGCLLYKLCFFTLPF---GESQVAICD-GNFT 279
Cdd:cd06624 159 LA----GINPCTETFTG--TLQYMAPEVIDkgQRGyGPP----ADIWSLGCTIIEMATGKPPFielGEPQAAMFKvGMFK 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 280 ----IPDNsrYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06624 229 ihpeIPES--LSEEAKSFILRCFEPDPDKRA 257
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
57-311 7.17e-18

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: 84.70  E-value: 7.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsisdnvWE--VLILMEYC 133
Cdd:cd06644  20 LGDGAFGKVYKAKNkETGALAAAKVIETKSEEELEDYMVEIEILATCN-HPYIVKLLGAFY-------WDgkLWIMIEFC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQMnKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG-SATNkflnpqkd 212
Cdd:cd06644  92 PGGAVDAIM-LELDRGLTEPQIQVICRQMLEALQYLHSMK--IIHRDLKAGNVLLTLDGDIKLADFGvSAKN-------- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 gVNVVEEEIKKYTTLSYRAPE--MINLYGGKPITTKADIWALGCLLYKLCFFTLPFGE-------SQVAICDGNfTIPDN 283
Cdd:cd06644 161 -VKTLQRRDSFIGTPYWMAPEvvMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHElnpmrvlLKIAKSEPP-TLSQP 238
                       250       260
                ....*....|....*....|....*...
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd06644 239 SKWSMEFRDFLKTALDKHPETRPSAAQL 266
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
93-329 1.37e-17

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: 83.29  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKEL--SGHKNIVGYLDCAVNSisDNVWevlILMEYCRAGQVVNQMNKKlqtGFTEPEVLQIFCDTCEAVARLH 170
Cdd:cd06917  47 QKEVALLSQLklGQPKNIIKYYGSYLKG--PSLW---IIMDYCEGGSIRTLMRAG---PIAERYIAVIMREVLVALKFIH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 qcKTPIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdgvNVVEEEIKKYT---TLSYRAPEMINlyGGKPITTKA 247
Cdd:cd06917 119 --KDGIIHRDIKAANILVTNTGNVKLCDFGVAA-----------SLNQNSSKRSTfvgTPYWMAPEVIT--EGKYYDTKA 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 248 DIWALGCLLYKLCFFTLPFgeSQVAICDGNFTIPDN-------SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd06917 184 DIWSLGITTYEMATGNPPY--SDVDALRAVMLIPKSkpprlegNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQH 261

                ....*....
gi 38787904 321 KDCPVSNIN 329
Cdd:cd06917 262 SKTPTSVLK 270
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
95-308 1.47e-17

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


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 83.06  E-value: 1.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLdcavNSISDNVWeVLILMEYCRAGQVVnQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKt 174
Cdd:cd14187  57 EIAIHRSLA-HQHVVGFH----GFFEDNDF-VYVVLELCRRRSLL-ELHKR-RKALTEPEARYYLRQIILGCQYLHRNR- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 pIIHRDLKVENILLNDGGNYVLCDFGSATNKflnpQKDGvnvveeEIKKYT--TLSYRAPEMInlyGGKPITTKADIWAL 252
Cdd:cd14187 128 -VIHRDLKLGNLFLNDDMEVKIGDFGLATKV----EYDG------ERKKTLcgTPNYIAPEVL---SKKGHSFEVDIWSI 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 253 GCLLYKLCFFTLPF-----GESQVAICDGNFTIPdnsrysRNIH----CLIRFMLEPDPEHRPDI 308
Cdd:cd14187 194 GCIMYTLLVGKPPFetsclKETYLRIKKNEYSIP------KHINpvaaSLIQKMLQTDPTARPTI 252
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
57-266 1.48e-17

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 83.43  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALK--RMYVNNMPDLNVCkREITIMKELSgHKNIVGY------LDCAVNSISdnvwevL 127
Cdd:cd14039   1 LGTGGFGNVCLYQNQEtGEKIAIKscRLELSVKNKDRWC-HEIQIMKKLN-HPNVVKAcdvpeeMNFLVNDVP------L 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQT-GFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLND-GGNYV--LCDFGSAt 203
Cdd:cd14039  73 LAMEYCSGGDLRKLLNKPENCcGLKESQVLSLLSDIGSGIQYLHENK--IIHRDLKPENIVLQEiNGKIVhkIIDLGYA- 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 204 nKFLNPQKDGVNVVeeeikkyTTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14039 150 -KDLDQGSLCTSFV-------GTLQYLAPE---LFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
49-310 1.52e-17

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: 83.64  E-value: 1.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVF--LVRTHGGIRCALKRMYVNNMPDLNVCK-------REITIMKELSgHKNIVGYLDCAVnsi 119
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYkaVPLRNTGKPVAIKVVRKADLSSDNLKGssranilKEVQIMKRLS-HPNIVKLLDFQE--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWevLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN---------- 189
Cdd:cd14096  77 SDEYY--YIVLELADGGEIFHQIVR--LTYFSEDLSRHVITQVASAVKYLHEIG--VVHRDIKPENLLFEpipfipsivk 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 190 -----------DGGNYV------------LCDFGSAtnKFLNPqkdgvnvvEEEIKKYTTLSYRAPEMINlygGKPITTK 246
Cdd:cd14096 151 lrkadddetkvDEGEFIpgvggggigivkLADFGLS--KQVWD--------SNTKTPCGTVGYTAPEVVK---DERYSKK 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 247 ADIWALGCLLYK-LCFFTlPFGESQV-----AICDGNFTI--PDNSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd14096 218 VDMWALGCVLYTlLCGFP-PFYDESIetlteKISRGDYTFlsPWWDEISKSAKDLISHLLTVDPAKRYDIDE 288
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-311 2.01e-17

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: 82.48  E-value: 2.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  59 EGGFSTVFLVR-THGGIRCALKRMYVNNMPD--LNVCKREITIMKELSgHKNIVGYLDcavnSISDNVWEVLILMEYCRA 135
Cdd:cd08223  10 KGSYGEVWLVRhKRDRKQYVIKKLNLKNASKreRKAAEQEAKLLSKLK-HPNIVSYKE----SFEGEDGFLYIVMGFCEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMnkKLQTG--FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqkdg 213
Cdd:cd08223  85 GDLYTRL--KEQKGvlLEERQVVEWFVQIAMALQYMHE--RNILHRDLKTQNIFLTKSNIIKVGDLGIA----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 vNVVEEEIKKYTTL----SYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQV-----AICDGNftIPD-N 283
Cdd:cd08223 150 -RVLESSSDMATTLigtpYYMSPE---LFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMnslvyKILEGK--LPPmP 223
                       250       260
                ....*....|....*....|....*...
gi 38787904 284 SRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08223 224 KQYSPELGELIKAMLHQDPEKRPSVKRI 251
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
89-306 2.48e-17

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: 82.58  E-value: 2.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  89 LNVCKREITIMKELSgHKNIVGYLDCAVNSISDNvwevlILMEYCRAGQVVNQMNkklQTG-FTEPEVLQIFCDTCEAVA 167
Cdd:cd06628  50 LDALQREIALLRELQ-HENIVQYLGSSSDANHLN-----IFLEYVPGGSVATLLN---NYGaFEESLVRNFVRQILKGLN 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 168 RLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEIKKytTLSYRAPEMI--NLYggkpiTT 245
Cdd:cd06628 121 YLHNRG--IIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGARPSLQG--SVFWMAPEVVkqTSY-----TR 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 246 KADIWALGCLLYKLCFFTLPFGE-SQV-AICD-GNF---TIPDNSRySRNIHCLiRFMLEPDPEHRP 306
Cdd:cd06628 192 KADIWSLGCLVVEMLTGTHPFPDcTQMqAIFKiGENaspTIPSNIS-SEARDFL-EKTFEIDHNKRP 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
93-306 2.51e-17

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: 82.40  E-value: 2.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSGHKNIVGyldcaVNSISDNVWEVLILMEYCRAGQVvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQc 172
Cdd:cd14106  55 LHEIAVLELCKDCPRVVN-----LHEVYETRSELILILELAAGGEL--QTLLDEEECLTEADVRRLMRQILEGVQYLHE- 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 kTPIIHRDLKVENILLN---DGGNYVLCDFGSAtnKFLNPqkdGVNVveEEIkkYTTLSYRAPEMINlYggKPITTKADI 249
Cdd:cd14106 127 -RNIVHLDLKPQNILLTsefPLGDIKLCDFGIS--RVIGE---GEEI--REI--LGTPDYVAPEILS-Y--EPISLATDM 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 250 WALGCLLYKLCFFTLPFG-----ESQVAICDGNFTIPDN--SRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14106 194 WSIGVLTYVLLTGHSPFGgddkqETFLNISQCNLDFPEElfKDVSPLAIDFIKRLLVKDPEKRL 257
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
75-307 3.17e-17

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: 82.02  E-value: 3.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  75 RCALKRMYVNNMP-DLNVCKREITIMkELSGHKNIVGYLDCAVnsISDNVWevlILMEYCRAGQVVNQMNKKLQTG-FTE 152
Cdd:cd06610  28 KVAIKRIDLEKCQtSMDELRKEIQAM-SQCNHPNVVSYYTSFV--VGDELW---LVMPLLSGGSLLDIMKSSYPRGgLDE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 153 PEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKdgvnvveEEIKKYT---TLSY 229
Cdd:cd06610 102 AIIATVLKEVLKGLEYLH--SNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDR-------TRKVRKTfvgTPCW 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 230 RAPEMINLYGGkpITTKADIWALGCLLYKLC-----FFTLPFGESQVAICDGNF----TIPDNSRYSRNIHCLIRFMLEP 300
Cdd:cd06610 173 MAPEVMEQVRG--YDFKADIWSFGITAIELAtgaapYSKYPPMKVLMLTLQNDPpsleTGADYKKYSKSFRKMISLCLQK 250

                ....*..
gi 38787904 301 DPEHRPD 307
Cdd:cd06610 251 DPSKRPT 257
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
59-259 3.36e-17

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: 82.32  E-value: 3.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  59 EGGFSTVFLVR-THGGIRCALKRM---YVNNMPDLNVckREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEycr 134
Cdd:cd07831   9 EGTFSEVLKAQsRKTGKYYAIKCMkkhFKSLEQVNNL--REIQALRRLSPHPNILRLIEVLFDRKTGRLALVFELMD--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 agqvvnqMN-----KKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDgGNYVLCDFGSATNKFLNP 209
Cdd:cd07831  84 -------MNlyeliKGRKRPLPEKRVKNYMYQLLKSLDHMHRNG--IFHRDIKPENILIKD-DILKLADFGSCRGIYSKP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 210 qkdgvnvveeeikKYT----TLSYRAPEMInLYGGKpITTKADIWALGCLLYKL 259
Cdd:cd07831 154 -------------PYTeyisTRWYRAPECL-LTDGY-YGPKMDIWAVGCVFFEI 192
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
48-259 6.38e-17

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: 82.45  E-value: 6.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEesLAEGGFSTVFLVR---THGGIRCALKRmyVNNMPDLNV-CKR---EITIMKELSGHKNIVGYLDcavnsiS 120
Cdd:cd07857   1 RYELIKE--LGQGAYGIVCSARnaeTSEEETVAIKK--ITNVFSKKIlAKRalrELKLLRHFRGHKNITCLYD------M 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 121 DNVW-----EVLI---LMEY-----CRAGQvvnqmnkKLQTGFTEPEVLQIFCdtceAVARLHQCKtpIIHRDLKVENIL 187
Cdd:cd07857  71 DIVFpgnfnELYLyeeLMEAdlhqiIRSGQ-------PLTDAHFQSFIYQILC----GLKYIHSAN--VLHRDLKPGNLL 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 188 LNDGGNYVLCDFGSATNKFLNPQKdgvnvVEEEIKKY-TTLSYRAPEMINLYggKPITTKADIWALGCLLYKL 259
Cdd:cd07857 138 VNADCELKICDFGLARGFSENPGE-----NAGFMTEYvATRWYRAPEIMLSF--QSYTKAIDVWSVGCILAEL 203
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
150-311 6.91e-17

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: 81.68  E-value: 6.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 150 FTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVlcdfgSATNKFLnpqkdGVNVVEEEIKKYTTL-- 227
Cdd:cd13974 129 LSEREALVIFYDVVRVVEALH--KKNIVHRDLKLGNMVLNKRTRKI-----TITNFCL-----GKHLVSEDDLLKDQRgs 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 228 -SYRAPEMIN--LYGGKPittkADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDNSRYSRNIHCLIRFMLE 299
Cdd:cd13974 197 pAYISPDVLSgkPYLGKP----SDMWALGVVLFTMLYGQFPFYDSIPQelfrkIKAAEYTIPEDGRVSENTVCLIRKLLV 272
                       170
                ....*....|..
gi 38787904 300 PDPEHRPDIFQV 311
Cdd:cd13974 273 LNPQKRLTASEV 284
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
77-311 8.73e-17

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: 80.78  E-value: 8.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  77 ALKRMyvnnMPD-LNVCKREITIMKELSGHKNIVGYLdcAVNSISDNVWevlILMEYCRAG--QVVNQMNKKLQTGFTEP 153
Cdd:cd13982  29 AVKRL----LPEfFDFADREVQLLRESDEHPNVIRYF--CTEKDRQFLY---IALELCAASlqDLVESPRESKLFLRPGL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 154 EVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL---NDGGNY--VLCDFGSAtnKFLNpqkDGVNVVEEEIKKYTTLS 228
Cdd:cd13982 100 EPVRLLRQIASGLAHLHSLN--IVHRDLKPQNILIstpNAHGNVraMISDFGLC--KKLD---VGRSSFSRRSGVAGTSG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMINLYGGKPITTKADIWALGCLLYklcfFTL-----PFGES---QVAICDGNFTIP-DNSRYSRNI--HCLIRFM 297
Cdd:cd13982 173 WIAPEMLSGSTKRRQTRAVDIFSLGCVFY----YVLsggshPFGDKlerEANILKGKYSLDkLLSLGEHGPeaQDLIERM 248
                       250
                ....*....|....
gi 38787904 298 LEPDPEHRPDIFQV 311
Cdd:cd13982 249 IDFDPEKRPSAEEV 262
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
53-311 1.10e-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: 81.23  E-value: 1.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIVGYldcAVNSISDNvwEVLI 128
Cdd:cd08229  28 IEKKIGRGQFSEVYRATcLLDGVPVALKKVQIFDLMDAKAradCIKEIDLLKQLN-HPNVIKY---YASFIEDN--ELNI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMN--KKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaTNKF 206
Cdd:cd08229 102 VLELADAGDLSRMIKhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRR--VMHRDIKPANVFITATGVVKLGDLG--LGRF 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LNPQKDGVNVVeeeikkYTTLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPF-GE--------SQVAICDgn 277
Cdd:cd08229 178 FSSKTTAAHSL------VGTPYYMSPERIHENG---YNFKSDIWSLGCLLYEMAALQSPFyGDkmnlyslcKKIEQCD-- 246
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 278 FTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd08229 247 YPPLPSDHYSEELRQLVNMCINPDPEKRPDITYV 280
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
57-260 1.17e-16

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: 80.39  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRCALKRMYVNNMP-DLNVCKREITIMKELSgHKNIV---GYldCAVNSisdnvwEVLILMEY 132
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAaSKKEFLTELEMLGRLR-HPNLVrllGY--CLESD------EKLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNK-KLQTGFTEPEVLQIFCDTCEAVARLHQ-CKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQ 210
Cdd:cd14066  72 MPNGSLEDRLHChKGSPPLPWPQRLKIAKGIARGLEYLHEeCPPPIIHGDIKSSNILLDEDFEPKLTDFGLA--RLIPPS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 KDGVnvveEEIKKYTTLSYRAPEMInlYGGKPiTTKADIWALGCLLYKLC 260
Cdd:cd14066 150 ESVS----KTSAVKGTIGYLAPEYI--RTGRV-STKSDVYSFGVVLLELL 192
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
55-259 1.20e-16

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 80.94  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH--GGIrCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLDCAvnsISDNvwEVLI 128
Cdd:cd07839   6 EKIGEGTYGTVFKAKNRetHEI-VALKRVRLDDddegVPSSAL--REICLLKELK-HKNIVRLYDVL---HSDK--KLTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCragqvvNQMNKKL---QTGFTEPEVLQIFcdTCEAVARLHQCKTP-IIHRDLKVENILLNDGGNYVLCDFGSATN 204
Cdd:cd07839  77 VFEYC------DQDLKKYfdsCNGDIDPEIVKSF--MFQLLKGLAFCHSHnVLHRDLKPQNLLINKNGELKLADFGLARA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 205 kFLNPqkdgVNVVEEEIkkyTTLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07839 149 -FGIP----VRCYSAEV---VTLWYRPPDV--LFGAKLYSTSIDMWSAGCIFAEL 193
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
53-311 1.29e-16

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: 80.21  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCK---REITIMKELSgHKNIVGYLDcaVNSISDNvwEVLI 128
Cdd:cd14165   5 LGINLGEGSYAKVKSAYSERlKCNVAIKIIDKKKAPDDFVEKflpRELEILARLN-HKSIIKTYE--IFETSDG--KVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLN 208
Cdd:cd14165  80 VMELGVQGDLLEFI--KLRGALPEDVARKMFHQLSSAIKYCHELD--IVHRDLKCENLLLDKDFNIKLTDFGFS--KRCL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 PQKDGVNVVEEEIkkYTTLSYRAPEMINlygGKPITTKA-DIWALGCLLYKLCFFTLPFGESQVAIC-----DGNFTIPD 282
Cdd:cd14165 154 RDENGRIVLSKTF--CGSAAYAAPEVLQ---GIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMlkiqkEHRVRFPR 228
                       250       260
                ....*....|....*....|....*....
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14165 229 SKNLTSECKDLIYRLLQPDVSQRLCIDEV 257
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
44-311 1.32e-16

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: 80.00  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRhqvtleeSLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIV---GYLDcav 116
Cdd:cd14116   7 FEIGR-------PLGKGKFGNVYLAReKQSKFILALKVLFKAQLEKAGVehqLRREVEIQSHLR-HPNILrlyGYFH--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 117 nsisdNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVL 196
Cdd:cd14116  76 -----DATRVYLILEYAPLGTVYRELQK--LSKFDEQRTATYITELANALSYCHSKR--VIHRDIKPENLLLGSAGELKI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 197 CDFGSATNKflnPQKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-----GESQV 271
Cdd:cd14116 147 ADFGWSVHA---PSSRRTTLC-------GTLDYLPPEMIE---GRMHDEKVDLWSLGVLCYEFLVGKPPFeantyQETYK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 272 AICDGNFTIPDN-SRYSRNihcLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14116 214 RISRVEFTFPDFvTEGARD---LISRLLKHNPSQRPMLREV 251
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
57-306 1.51e-16

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 80.09  E-value: 1.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGGIRCALKRMYVNNM-----PDLNVCKREITIMKELSgHKNIVGYLDCAV--NSISdnvwevlI 128
Cdd:cd06625   8 LGQGAFGQVYLcYDADTGRELAVKQVEIDPInteasKEVKALECEIQLLKNLQ-HERIVQYYGCLQdeKSLS-------I 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMnkKLQTGFTEPEV----LQIFcdtcEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATN 204
Cdd:cd06625  80 FMEYMPGGSVKDEI--KAYGALTENVTrkytRQIL----EGLAYLH--SNMIVHRDIKGANILRDSNGNVKLGDFGASKR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPQKDGVNVVeeeikkYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQ-------VAICDGN 277
Cdd:cd06625 152 LQTICSSTGMKSV------TGTPYWMSPEVIN---GEGYGRKADIWSVGCTVVEMLTTKPPWAEFEpmaaifkIATQPTN 222
                       250       260
                ....*....|....*....|....*....
gi 38787904 278 FTIPDNSrySRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06625 223 PQLPPHV--SEDARDFLSLIFVRNKKQRP 249
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
95-310 1.69e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 83.63  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904    95 EITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYCRAGQVVNQMNK--KLQTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:PTZ00266   62 EVNVMRELK-HKNIVRYIDRFLNKANQKLY---ILMEFCDAGDLSRNIQKcyKMFGKIEEHAIVDITRQLLHALAYCHNL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   173 K-----TPIIHRDLKVENILLNDGGNYV-----------------LCDFGSATNkflnpqkdgVNVVEEEIKKYTTLSYR 230
Cdd:PTZ00266  138 KdgpngERVLHRDLKPQNIFLSTGIRHIgkitaqannlngrpiakIGDFGLSKN---------IGIESMAHSCVGTPYYW 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   231 APEMInLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQvaicdgNFT-----------IPDNSRySRNIHCLIRFMLE 299
Cdd:PTZ00266  209 SPELL-LHETKSYDDKSDMWALGCIIYELCSGKTPFHKAN------NFSqliselkrgpdLPIKGK-SKELNILIKNLLN 280
                         250
                  ....*....|.
gi 38787904   300 PDPEHRPDIFQ 310
Cdd:PTZ00266  281 LSAKERPSALQ 291
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
57-259 2.08e-16

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: 80.11  E-value: 2.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR--THGGIrCALKRmYVNNMPDLNVCK---REITIMKELSgHKNIVgyldcavnsisdNVWEVL---- 127
Cdd:cd07847   9 IGEGSYGVVFKCRnrETGQI-VAIKK-FVESEDDPVIKKialREIRMLKQLK-HPNLV------------NLIEVFrrkr 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ---ILMEYCRAgQVVNQMNKKLQtGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd07847  74 klhLVFEYCDH-TVLNELEKNPR-GVPEHLIKKIIWQTLQAVNFCHKHN--CIHRDVKPENILITKQGQIKLCDFGFA-- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 205 KFLNPQKDgvnvveeeikKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07847 148 RILTGPGD----------DYTdyvaTRWYRAPEL--LVGDTQYGPPVDVWAIGCVFAEL 194
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
49-328 2.22e-16

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 79.60  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVFL---VRThgGIRCALKRMyvnnmpDLNVCKREIT-IMKE---LSGHK--NIVGYLDCAVNSI 119
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKgidKRT--NQVVAIKVI------DLEEAEDEIEdIQQEiqfLSQCDspYITKYYGSFLKGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 sdNVWevlILMEYCRAGQVVNQMnkKLQtGFTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd06609  73 --KLW---IIMEYCGGGSVLDLL--KPG-PLDETYIAFILREVLLGLEYLHSEGK--IHRDIKAANILLSEEGDVKLADF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATNkflnpqkdgvnvVEEEIKKYTTLS----YRAPEMI--NLYGgkpitTKADIWALGCLLYKLCFFTLPFGE--SQV 271
Cdd:cd06609 143 GVSGQ------------LTSTMSKRNTFVgtpfWMAPEVIkqSGYD-----EKADIWSLGITAIELAKGEPPLSDlhPMR 205
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 272 AIcdgnFTIPDN-------SRYSRNIHCLIRFMLEPDPEHRPDIFQVSyfAFKFAKKDCPVSNI 328
Cdd:cd06609 206 VL----FLIPKNnppslegNKFSKPFKDFVELCLNKDPKERPSAKELL--KHKFIKKAKKTSYL 263
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
57-306 2.32e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 79.42  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYV--NNMPDLNVCKREITIMkELSGHKNIVGYLDCAVNSIsdnvwEVLILMEYC 133
Cdd:cd13978   1 LGSGGFGTVSKARhVSWFGMVAIKCLHSspNCIEERKALLKEAEKM-ERARHSYVLPLLGVCVERR-----SLGLVMEYM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVvNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDG 213
Cdd:cd13978  75 ENGSL-KSLLEREIQDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 VNVVEEEikkYTTLSYRAPEMINLYGGKPiTTKADIWALGCLLYKLCFFTLPFGESQ------VAICDGNF-TIPDNSRY 286
Cdd:cd13978 154 RRGTENL---GGTPIYMAPEAFDDFNKKP-TSKSDVYSFAIVIWAVLTRKEPFENAInpllimQIVSKGDRpSLDDIGRL 229
                       250       260
                ....*....|....*....|....*
gi 38787904 287 --SRNIHCLIRFML---EPDPEHRP 306
Cdd:cd13978 230 kqIENVQELISLMIrcwDGNPDARP 254
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
128-305 2.53e-16

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: 79.36  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsATNKFL 207
Cdd:cd05583  76 LILDYVNGGELFTHLYQREH--FTESEVRIYIGEIVLALEHLHKLG--IIYRDIKLENILLDSEGHVVLTDFG-LSKEFL 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKDgvnvveeeiKKYT---TLSYRAPEMINlyGGKPITTKA-DIWALGCLLYKLCFFTLPF---GE----SQVA--IC 274
Cdd:cd05583 151 PGEND---------RAYSfcgTIEYMAPEVVR--GGSDGHDKAvDWWSLGVLTYELLTGASPFtvdGErnsqSEISkrIL 219
                       170       180       190
                ....*....|....*....|....*....|.
gi 38787904 275 DGNFTIPdnSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05583 220 KSHPPIP--KTFSAEAKDFILKLLEKDPKKR 248
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
92-311 2.53e-16

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: 79.98  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  92 CKREITIMKELSGHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd14091  40 PSEEIEILLRYGQHPNII-----TLRDVYDDGNSVYLVTELLRGGELLDRILRQKF--FSEREASAVMKTLTKTVEYLHS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 ckTPIIHRDLKVENILL-NDGGN---YVLCDFG-----SATNKFL-NPQkdgvnvveeeikkYTTlSYRAPEMINLYGgk 241
Cdd:cd14091 113 --QGVVHRDLKPSNILYaDESGDpesLRICDFGfakqlRAENGLLmTPC-------------YTA-NFVAPEVLKKQG-- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 242 piTTKA-DIWALGCLLYKLCFFTLPF---------------GESQVAICDGNF-TIPDNSRYsrnihcLIRFMLEPDPEH 304
Cdd:cd14091 175 --YDAAcDIWSLGVLLYTMLAGYTPFasgpndtpevilariGSGKIDLSGGNWdHVSDSAKD------LVRKMLHVDPSQ 246

                ....*..
gi 38787904 305 RPDIFQV 311
Cdd:cd14091 247 RPTAAQV 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
55-259 3.22e-16

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: 79.63  E-value: 3.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR-THGGIRCALKRMYVNN----MPDLNVckREITIMKEL--SGHKNIVGYLDCAVNSISDNVWEVL 127
Cdd:cd07838   5 AEIGEGAYGTVYKARdLQDGRFVALKKVRVPLseegIPLSTI--REIALLKQLesFEHPNVVRLLDVCHGPRTDRELKLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYcragqvVNQ-----MNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd07838  83 LVFEH------VDQdlatyLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHR--IVHRDLKPQNILVTSDGQVKLADFGLA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 203 T----NKFLNPQkdgvnVVeeeikkytTLSYRAPE-MINLYGGKPIttkaDIWALGCLLYKL 259
Cdd:cd07838 155 RiysfEMALTSV-----VV--------TLWYRAPEvLLQSSYATPV----DMWSVGCIFAEL 199
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
57-322 4.46e-16

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: 78.52  E-value: 4.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMpDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWevliLMEYCRA 135
Cdd:cd13987   1 LGEGTYGKVLLAVHKGsGTKMALKFVPKPST-KLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVF----AQEYAPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNqmNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV--LCDFGsATnkflnpQKDG 213
Cdd:cd13987  76 GDLFS--IIPPQVGLPEERVKRCAAQLASALDFMHSKN--LVHRDIKPENVLLFDKDCRRvkLCDFG-LT------RRVG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 VNVVeeeiKKYTTLSYRAPEMINLYGGKPIT--TKADIWALGCLLYklCFFT--LPFgESQVAICDG-----------NF 278
Cdd:cd13987 145 STVK----RVSGTIPYTAPEVCEAKKNEGFVvdPSIDVWAFGVLLF--CCLTgnFPW-EKADSDDQFyeefvrwqkrkNT 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 38787904 279 TIPDN-SRYSRNIHCLIRFMLEPDPEHRPDIFQVsyfaFKFAKKD 322
Cdd:cd13987 218 AVPSQwRRFTPKALRMFKKLLAPEPERRCSIKEV----FKYLGDR 258
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
94-259 4.69e-16

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


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 78.90  E-value: 4.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDcaVNSISDNVWEVlilMEYCraGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd07833  49 REVKVLRQLR-HENIVNLKE--AFRRKGRLYLV---FEYV--ERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHN 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 tpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLnPQKDGVNVVEEeikkYTTLSYRAPEMinLYG----GKPIttkaDI 249
Cdd:cd07833 121 --IIHRDIKPENILVSESGVLKLCDFGFA--RAL-TARPASPLTDY----VATRWYRAPEL--LVGdtnyGKPV----DV 185
                       170
                ....*....|
gi 38787904 250 WALGCLLYKL 259
Cdd:cd07833 186 WAIGCIMAEL 195
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
57-305 4.89e-16

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: 80.02  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMyvnnmpdlnvcKREITIMKELSGH----KNIVgyldcavnSISDNVWEV----- 126
Cdd:cd05573   9 IGRGAFGEVWLVRdKDTGQVYAMKIL-----------RKSDMLKREQIAHvraeRDIL--------ADADSPWIVrlhya 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 -------LILMEYCRAGQVVNQMNKKLQtgFTEPEVlQIFCdtCEAVARLHQC-KTPIIHRDLKVENILLNDGGNYVLCD 198
Cdd:cd05573  70 fqdedhlYLVMEYMPGGDLMNLLIKYDV--FPEETA-RFYI--AELVLALDSLhKLGFIHRDIKPDNILLDADGHIKLAD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 199 FGSAT---------------NKFLNPQKDGVNVVEEEIKKYT------TLSYRAPEMINlygGKPITTKADIWALGCLLY 257
Cdd:cd05573 145 FGLCTkmnksgdresylndsVNTLFQDNVLARRRPHKQRRVRaysavgTPDYIAPEVLR---GTGYGPECDWWSLGVILY 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 258 KLCFFTLPF-GESQVAIC------DGNFTIPDNSRYSRNIHCLIRFMLEpDPEHR 305
Cdd:cd05573 222 EMLYGFPPFySDSLVETYskimnwKESLVFPDDPDVSPEAIDLIRRLLC-DPEDR 275
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
55-310 5.13e-16

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: 78.39  E-value: 5.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcavnSISDNvWEVLILMEYC 133
Cdd:cd14114   8 EELGTGAFGVVHRCTERAtGNNFAAKFIMTPHESDKETVRKEIQIMNQLH-HPKLINLHD----AFEDD-NEMVLILEFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLN--DGGNYVLCDFGSATNkfLNPqk 211
Cdd:cd14114  82 SGGELFERIAAE-HYKMSEAEVINYMRQVCEGLCHMHE--NNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH--LDP-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 212 dgvnvveEEIKKYTTLS--YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GES------QVAICDGNFTIPD 282
Cdd:cd14114 155 -------KESVKVTTGTaeFAAPEIVE---REPVGFYTDMWAVGVLSYVLLSGLSPFaGENddetlrNVKSCDWNFDDSA 224
                       250       260
                ....*....|....*....|....*...
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd14114 225 FSGISEEAKDFIRKLLLADPNKRMTIHQ 252
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
55-256 6.31e-16

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: 78.68  E-value: 6.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRT-HGGIRCALKRMYVN---NMPDLNVckREITIMKELSgHKNIVGYLDcAVNSISdnvwEVLILM 130
Cdd:cd07836   6 EKLGEGTYATVYKGRNrTTGEIVALKEIHLDaeeGTPSTAI--REISLMKELK-HENIVRLHD-VIHTEN----KLMLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRaGQVVNQMNKKLQTGFTEPEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFLNP 209
Cdd:cd07836  78 EYMD-KDLKKYMDTHGVRGALDPNTVKSFTyQLLKGIAFCHENR--VLHRDLKPQNLLINKRGELKLADFGLA-RAFGIP 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 38787904 210 qkdgVNVVEEEIkkyTTLSYRAPEMinLYGGKPITTKADIWALGCLL 256
Cdd:cd07836 154 ----VNTFSNEV---VTLWYRAPDV--LLGSRTYSTSIDIWSVGCIM 191
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
60-256 7.47e-16

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: 79.11  E-value: 7.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFL-VRTHGGIRCALKRmyVNNM-PDLNVCK---REITIMKELSgHKNIVGYLDCAVNSISDNVWEVLILMEYCR 134
Cdd:cd07834  11 GAYGVVCSaYDKRTGRKVAIKK--ISNVfDDLIDAKrilREIKILRHLK-HENIIGLLDILRPPSPEEFNDVYIVTELME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 A--GQVVnQMNKKLQTGFTEPEVLQIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKD 212
Cdd:cd07834  88 TdlHKVI-KSPQPLTDDHIQYFLYQILR----GLKYLHSAG--VIHRDLKPSNILVNSNCDLKICDFGLA--RGVDPDED 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 38787904 213 GVNVVEeeikkY-TTLSYRAPEMINLYG--GKPIttkaDIWALGCLL 256
Cdd:cd07834 159 KGFLTE-----YvVTRWYRAPELLLSSKkyTKAI----DIWSVGCIF 196
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
53-305 7.61e-16

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: 77.84  E-value: 7.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRtH--GGIRCALKRMYVNNMPDLNVCK--REITIMKeLSGHKNIVGYLDcavnsISDNVWEVLI 128
Cdd:cd14074   7 LEETLGRGHFAVVKLAR-HvfTGEKVAVKVIDKTKLDDVSKAHlfQEVRCMK-LVQHPNVVRLYE-----VIDTQTKLYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-LCDFGsATNKFL 207
Cdd:cd14074  80 ILELGDGGDMYDYIMKH-ENGLNEDLARKYFRQIVSAISYCHKLH--VVHRDLKPENVVFFEKQGLVkLTDFG-FSNKFQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKDGVNVveeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQ-----VAICDGNFTIPD 282
Cdd:cd14074 156 PGEKLETSC--------GSLAYSAPEI--LLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANdsetlTMIMDCKYTVPA 225
                       250       260
                ....*....|....*....|....
gi 38787904 283 N-SRYSRNihcLIRFMLEPDPEHR 305
Cdd:cd14074 226 HvSPECKD---LIRRMLIRDPKKR 246
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
73-310 7.79e-16

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: 78.11  E-value: 7.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  73 GIRCALKRMYvnnmpDLNVCKREITIMKELSGHKNIVGYLDcavnsISDNVWE----VLILMEYCRAGQVVNQMNKKLQT 148
Cdd:cd14172  29 GQKCALKLLY-----DSPKARREVEHHWRASGGPHIVHILD-----VYENMHHgkrcLLIIMECMEGGELFSRIQERGDQ 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 149 GFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL---NDGGNYVLCDFGSATNKFLNpqkdgvNVVEEEIkkYT 225
Cdd:cd14172  99 AFTEREASEIMRDIGTAIQYLHSMN--IAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQ------NALQTPC--YT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 226 TLsYRAPEMInlyGGKPITTKADIWALGCLLY-KLCFFTLPFGESQVAICDG----------NFTIPDNSRYSRNIHCLI 294
Cdd:cd14172 169 PY-YVAPEVL---GPEKYDKSCDMWSLGVIMYiLLCGFPPFYSNTGQAISPGmkrrirmgqyGFPNPEWAEVSEEAKQLI 244
                       250
                ....*....|....*.
gi 38787904 295 RFMLEPDPEHRPDIFQ 310
Cdd:cd14172 245 RHLLKTDPTERMTITQ 260
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
55-305 8.95e-16

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: 78.39  E-value: 8.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRT-HGGIRCALKRMY---VNNMPDLNVCKREITIMKELSgHKNIVGYLdcavNSISDNvWEVLILM 130
Cdd:cd05580   7 KTLGTGSFGRVRLVKHkDSGKYYALKILKkakIIKLKQVEHVLNEKRILSEVR-HPFIVNLL----GSFQDD-RNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQV---VNQMNKklqtgFTEPEVL----QIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd05580  81 EYVPGGELfslLRRSGR-----FPNDVAKfyaaEVVL----ALEYLHSLD--IVYRDLKPENLLLDSDGHIKITDFGFA- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nKFLNPqkdgvnvveeeiKKYT---TLSYRAPEMINLYG-GKPittkADIWALGCLLYK-LCFFTLPFGESQVAICD--- 275
Cdd:cd05580 149 -KRVKD------------RTYTlcgTPEYLAPEIILSKGhGKA----VDWWALGILIYEmLAGYPPFFDENPMKIYEkil 211
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 276 -GNFTIPdnSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05580 212 eGKIRFP--SFFDPDAKDLIKRLLVVDLTKR 240
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
48-307 9.06e-16

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: 77.86  E-value: 9.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLdcAVNSISDNVWevl 127
Cdd:cd05148   5 REEFTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLR-HKHLISLF--AVCSVGEPVY--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkfl 207
Cdd:cd05148  79 IITELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQN--SIHRDLAARNILVGEDLVCKVADFGLA----- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 npqkdgvNVVEEEIkkYTTLSYR------APEMINlYGgkPITTKADIWALGCLLYKLcfFT---LPF-----GESQVAI 273
Cdd:cd05148 152 -------RLIKEDV--YLSSDKKipykwtAPEAAS-HG--TFSTKSDVWSFGILLYEM--FTygqVPYpgmnnHEVYDQI 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 274 cDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd05148 218 -TAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPS 250
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
55-306 1.03e-15

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: 77.48  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMpDLNVCKR-------EITIMKELSgHKNIVGYLDcavNSISDNVweVL 127
Cdd:cd06631   7 NVLGKGAYGTVYCGLTSTGQLIAVKQVELDTS-DKEKAEKeyeklqeEVDLLKTLK-HVNIVGYLG---TCLEDNV--VS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNkklQTGFTEPEVL-----QIFcdtcEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd06631  80 IFMEFVPGGSIASILA---RFGALEEPVFcrytkQIL----EGVAYLHN--NNVIHRDIKGNNIMLMPNGVIKLIDFGCA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TNKFLNpqkdGVNVVEEEIKK--YTTLSYRAPEMINLYG-GKpittKADIWALGCLLYKLCFFTLPFGE-----SQVAIC 274
Cdd:cd06631 151 KRLCIN----LSSGSQSQLLKsmRGTPYWMAPEVINETGhGR----KSDIWSIGCTVFEMATGKPPWADmnpmaAIFAIG 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 38787904 275 DGNFTIPD-NSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06631 223 SGRKPVPRlPDKFSPEARDFVHACLTRDQDERP 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
50-312 1.24e-15

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 77.39  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVNSIsdnvwEVLIL 129
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKN-TRHDNLVLFMGACMDPP-----HLAIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRaGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLnDGGNYVLCDFG-SATNKFLN 208
Cdd:cd14063  75 TSLCK-GRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLH--AKGIIHKDLKSKNIFL-ENGRVVITDFGlFSLSGLLQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 P-QKDGVNVVEeeikkYTTLSYRAPEMI-------NLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQV-----AICD 275
Cdd:cd14063 151 PgRREDTLVIP-----NGWLCYLAPEIIralspdlDFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAesiiwQVGC 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 276 GNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14063 226 GKKQSLSQLDIGREVKDILMQCWAYDPEKRPTFSDLL 262
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
93-306 1.27e-15

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: 77.42  E-value: 1.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDC--AVNSISdnvwevlILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLH 170
Cdd:cd06629  56 KSEIDTLKDLD-HPNIVQYLGFeeTEDYFS-------IFLEYVPGGSIGSCLRK--YGKFEEDLVRFFTRQILDGLAYLH 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 qcKTPIIHRDLKVENILLNDGGNYVLCDFGsatnkfLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYgGKPITTKADIW 250
Cdd:cd06629 126 --SKGILHRDLKADNILVDLEGICKISDFG------ISKKSDDIYGNNGATSMQGSVFWMAPEVIHSQ-GQGYSAKVDIW 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 251 ALGCLLYKLCFFTLPFG-ESQVAICDGNFT------IPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06629 197 SLGCVVLEMLAGRRPWSdDEAIAAMFKLGNkrsappVPEDVNLSPEALDFLNACFAIDPRDRP 259
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
50-256 1.65e-15

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: 77.37  E-value: 1.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVR--THGGIrCALKRMYVNNMPD--LNVCKREITIMKELSGHKNIVGYLDcavnsISDNVWE 125
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKdrETGET-VALKKVALRKLEGgiPNQALREIKALQACQGHPYVVKLRD-----VFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAG--QVVnqmnKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd07832  75 FVLVFEYMLSSlsEVL----RDEERPLTEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLISSTGVLKIADFGLA- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 204 nKFLNPQKDgvnvveeeiKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLL 256
Cdd:cd07832 148 -RLFSEEDP---------RLYShqvaTRWYRAPEL--LYGSRKYDEGVDLWAVGCIF 192
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
52-312 1.92e-15

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: 76.82  E-value: 1.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVrTHGGIRCALKRMYVNNM---PDL--NVCKREITIMKELSgHKNIVGYLDCavnsISDNVWEV 126
Cdd:cd14164   3 TLGTTIGEGSFSKVKLA-TSQKYCCKVAIKIVDRRrasPDFvqKFLPRELSILRRVN-HPNIVQMFEC----IEVANGRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEycragQVVNQMNKKLQTGFTEPEVL--QIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFGSAt 203
Cdd:cd14164  77 YIVME-----AAATDLLQKIQEVHHIPKDLarDMFAQMVGAVNYLHDMN--IVHRDLKCENILLSaDDRKIKIADFGFA- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nkflnpqkdgvnvveEEIKKYTTLS--------YRAPEMINLYGGKPitTKADIWALGCLLYKLCFFTLPFGESQVAIC- 274
Cdd:cd14164 149 ---------------RFVEDYPELSttfcgsraYTPPEVILGTPYDP--KKYDVWSLGVVLYVMVTGTMPFDETNVRRLr 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 275 ---DGnFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14164 212 lqqRG-VLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVA 251
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
86-308 1.99e-15

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: 77.30  E-value: 1.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  86 MPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISDNVWEVLILMeycRAGQVvnqMNKKLQTGFTEPEVLQIFCDTCEA 165
Cdd:cd14200  64 LAPLERVYQEIAILKKLD-HVNIVKLIEVLDDPAEDNLYMVFDLL---RKGPV---MEVPSDKPFSEDQARLYFRDIVLG 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 166 VARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsATNKFlnpqkDGVNVVEEEIKKytTLSYRAPEMINlYGGKPITT 245
Cdd:cd14200 137 IEYLHYQK--IVHRDIKPSNLLLGDDGHVKIADFG-VSNQF-----EGNDALLSSTAG--TPAFMAPETLS-DSGQSFSG 205
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 246 KA-DIWALGCLLYKLCFFTLPFGESQV-----AICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR---PDI 308
Cdd:cd14200 206 KAlDVWAMGVTLYCFVYGKCPFIDEFIlalhnKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRitvPEI 277
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
57-266 2.00e-15

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: 76.64  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG------GIRCALKRmyvNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISdnvweVLILM 130
Cdd:cd14120   1 IGHGAFAVVFKGRHRKkpdlpvAIKCITKK---NLSKSQNLLGKEIKILKELS-HENVVALLDCQETSSS-----VYLVM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQmnkkLQTGFTEPE------VLQIFCdtceAVARLHqcKTPIIHRDLKVENILLNDGGN---------YV 195
Cdd:cd14120  72 EYCNGGDLADY----LQAKGTLSEdtirvfLQQIAA----AMKALH--SKGIVHRDLKPQNILLSHNSGrkpspndirLK 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 196 LCDFGSAtnKFLNpqkDGVNVVeeeikkytTLS----YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14120 142 IADFGFA--RFLQ---DGMMAA--------TLCgspmYMAPEVIM---SLQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
94-305 2.37e-15

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: 76.88  E-value: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGHKNIVGYLDCAVNSISdnvweVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqcK 173
Cdd:cd14182  58 KEIDILRKVSGHPNIIQLKDTYETNTF-----FFLVFDLMKKGELFDYLTEKVT--LSEKETRKIMRALLEVICALH--K 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQkdgvnvveEEIKKYT-TLSYRAPEMINL--------YGgkpit 244
Cdd:cd14182 129 LNIVHRDLKPENILLDDDMNIKLTDFGFSCQ--LDPG--------EKLREVCgTPGYLAPEIIECsmddnhpgYG----- 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 245 TKADIWALGCLLYKLCFFTLPFGESQV-----AICDGN--FTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14182 194 KEVDMWSTGVIMYTLLAGSPPFWHRKQmlmlrMIMSGNyqFGSPEWDDRSDTVKDLISRFLVVQPQKR 261
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
94-260 2.67e-15

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: 76.56  E-value: 2.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAvnsISDN----VWEVLIL-----MEYCRAGQVVNQMNKKLqtgftepeVLQIfcdtCE 164
Cdd:cd07835  47 REISLLKELN-HPNIVRLLDVV---HSENklylVFEFLDLdlkkyMDSSPLTGLDPPLIKSY--------LYQL----LQ 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFlnpqkdGVNVveeeiKKYT----TLSYRAPEMinLYGG 240
Cdd:cd07835 111 GIAFCHSHR--VLHRDLKPQNLLIDTEGALKLADFGLA-RAF------GVPV-----RTYThevvTLWYRAPEI--LLGS 174
                       170       180
                ....*....|....*....|
gi 38787904 241 KPITTKADIWALGCLLYKLC 260
Cdd:cd07835 175 KHYSTPVDIWSVGCIFAEMV 194
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
94-313 2.69e-15

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: 76.18  E-value: 2.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVgyldcavnsisdNVWEVL--------ILMEYCRAGQVVNQMnkkLQTG-FTEPEVLQIFCDTCE 164
Cdd:cd14163  49 RELQIVERLD-HKNII------------HVYEMLesadgkiyLVMELAEDGDVFDCV---LHGGpLPEHRAKALFRQLVE 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHQCKtpIIHRDLKVENILLNdGGNYVLCDFGSAtnKFLNpqkdgVNVVEEEIKKYTTLSYRAPEMinLYGGKPIT 244
Cdd:cd14163 113 AIRYCHGCG--VAHRDLKCENALLQ-GFTLKLTDFGFA--KQLP-----KGGRELSQTFCGSTAYAAPEV--LQGVPHDS 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 245 TKADIWALGCLLYKLCFFTLPFGESQVA--IC--DGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSY 313
Cdd:cd14163 181 RKGDIWSMGVVLYVMLCAQLPFDDTDIPkmLCqqQKGVSLPGHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSW 253
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
52-314 2.76e-15

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 76.80  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVRTH--GGIRcALKRM---YVNNMPDLNVckREITIMKELSGHKNIVGYLDcavnSISDNvWEV 126
Cdd:cd07830   2 KVIKQLGDGTFGSVYLARNKetGELV-AIKKMkkkFYSWEECMNL--REVKSLRKLNEHPNIVKLKE----VFREN-DEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRaGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkf 206
Cdd:cd07830  74 YFVFEYME-GNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIH--KHGFFHRDLKPENLLVSGPEVVKIADFGLA---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgvnvveEEIKK---YT----TLSYRAPEMI---NLYgGKPIttkaDIWALGCLLYKLcfFTL-P-F-GESQV-- 271
Cdd:cd07830 147 ------------REIRSrppYTdyvsTRWYRAPEILlrsTSY-SSPV----DIWALGCIMAEL--YTLrPlFpGSSEIdq 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 272 --AIC------------DG-------NFTIPDNSRYSRN----------IHcLIRFMLEPDPEHRP---DIFQVSYF 314
Cdd:cd07830 208 lyKICsvlgtptkqdwpEGyklasklGFRFPQFAPTSLHqlipnaspeaID-LIKDMLRWDPKKRPtasQALQHPYF 283
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
56-307 3.71e-15

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: 75.84  E-value: 3.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  56 SLAEGGFSTVFLVRTHG-GIRCALKRMYVNnmPDLNVCKReitIMKEL-----SGHKNIVG-----YLDCAVNsisdnvw 124
Cdd:cd06605   8 ELGEGNGGVVSKVRHRPsGQIMAVKVIRLE--IDEALQKQ---ILRELdvlhkCNSPYIVGfygafYSEGDIS------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 evlILMEYCRAGQVvNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQcKTPIIHRDLKVENILLNDGGNYVLCDFGSATn 204
Cdd:cd06605  76 ---ICMEYMDGGSL-DKILKEVGR-IPERILGKIAVAVVKGLIYLHE-KHKIIHRDVKPSNILVNSRGQVKLCDFGVSG- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpqkdgvNVVEEEIKKYT-TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNFTIPD- 282
Cdd:cd06605 149 ----------QLVDSLAKTFVgTRSYMAPERIS---GGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFELLSy 215
                       250       260       270
                ....*....|....*....|....*....|....*
gi 38787904 283 ----------NSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd06605 216 ivdepppllpSGKFSPDFQDFVSQCLQKDPTERPS 250
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
55-305 3.75e-15

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: 75.79  E-value: 3.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGG------IRC----ALKRMYVNNMpdlnvcKREITIMKELSgHKNIVGYLDCAVNSisDNVW 124
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSGarevvaVKCvsksSLNKASTENL------LTEIELLKKLK-HPHIVELKDFQWDE--EHIY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 evlILMEYCRAGQVVN--QMNKKLqtgftePEVL------QIFCdtceAVARLHQckTPIIHRDLKVENILLNDGGNYVL 196
Cdd:cd14121  72 ---LIMEYCSGGDLSRfiRSRRTL------PESTvrrflqQLAS----ALQFLRE--HNISHMDLKPQNLLLSSRYNPVL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 197 --CDFGSATNKFLNPQKDGVnvveeeikKYTTLsYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFG------- 267
Cdd:cd14121 137 klADFGFAQHLKPNDEAHSL--------RGSPL-YMAPEMIL---KKKYDARVDLWSVGVILYECLFGRAPFAsrsfeel 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 268 ----ESQVAIcdgnfTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14121 205 eekiRSSKPI-----EIPTRPELSADCRDLLLRLLQRDPDRR 241
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
53-307 3.88e-15

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: 75.77  E-value: 3.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVflVRTHG---GIRCALKRmyVNNMPD-LNVCKREITIMKELSGH-----KNIVGYLDCAVNS----- 118
Cdd:cd14133   3 VLEVLGKGTFGQV--VKCYDlltGEEVALKI--IKNNKDyLDQSLDEIRLLELLNKKdkadkYHIVRLKDVFYFKnhlci 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 119 ----ISDNVWEVLilmeycragqvvnQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNY 194
Cdd:cd14133  79 vfelLSQNLYEFL-------------KQNKF--QYLSLPRIRKIAQQILEALVFLHSLG--LIHCDLKPENILLASYSRC 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 195 V--LCDFGSAtnkflnpqkdgvnvVEEEIKKYT---TLSYRAPEMInLygGKPITTKADIWALGCLLYKLCFFTLPF-GE 268
Cdd:cd14133 142 QikIIDFGSS--------------CFLTQRLYSyiqSRYYRAPEVI-L--GLPYDEKIDMWSLGCILAELYTGEPLFpGA 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 38787904 269 S---QVAICDGNFTIPDN---SRYSRNIHCLIRF---MLEPDPEHRPD 307
Cdd:cd14133 205 SevdQLARIIGTIGIPPAhmlDQGKADDELFVDFlkkLLEIDPKERPT 252
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
94-305 6.29e-15

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: 75.78  E-value: 6.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGHKNIVGYLDCAVNSISdnvweVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqcK 173
Cdd:cd14181  64 KEIHILRQVSGHPSIITLIDSYESSTF-----IFLVFDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLH--A 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPqkdgvnvvEEEIKKYT-TLSYRAPEMINL--------YGgkpit 244
Cdd:cd14181 135 NNIVHRDLKPENILLDDQLHIKLSDFGFSCH--LEP--------GEKLRELCgTPGYLAPEILKCsmdethpgYG----- 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 245 TKADIWALGCLLYKLCFFTLPFGESQV-----AICDG--NFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14181 200 KEVDLWACGVILFTLLAGSPPFWHRRQmlmlrMIMEGryQFSSPEWDDRSSTVKDLISRLLVVDPEIR 267
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
55-306 6.38e-15

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: 75.13  E-value: 6.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPDLNV-----CKREITIMKELSgHKNIVGYLdcAVNSISDNVWevlI 128
Cdd:cd06632   6 QLLGSGSFGSVYEgFNGDTGDFFAVKEVSLVDDDKKSResvkqLEQEIALLSKLR-HPNIVQYY--GTEREEDNLY---I 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKklQTGFTEPEVL----QIFcdtcEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd06632  80 FLEYVPGGSIHKLLQR--YGAFEEPVIRlytrQIL----SGLAYLHSRNT--VHRDIKGANILVDTNGVVKLADFGMA-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 KFLNPQKDGVNVVeeeikkyTTLSYRAPEMINLYgGKPITTKADIWALGCLLYKLCFFTLPFGE-SQVAIC--DGNF--- 278
Cdd:cd06632 150 KHVEAFSFAKSFK-------GSPYWMAPEVIMQK-NSGYGLAVDIWSLGCTVLEMATGKPPWSQyEGVAAIfkIGNSgel 221
                       250       260       270
                ....*....|....*....|....*....|
gi 38787904 279 -TIPDN-SRYSRNihcLIRFMLEPDPEHRP 306
Cdd:cd06632 222 pPIPDHlSPDAKD---FIRLCLQRDPEDRP 248
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
55-255 7.02e-15

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: 74.96  E-value: 7.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYC 133
Cdd:cd06647  13 EKIGQGASGTVYTaIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYL--VGDELW---VVMEYL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQMNkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdg 213
Cdd:cd06647  87 AGGSLTDVVT---ETCMDEGQIAAVCRECLQALEFLHS--NQVIHRDIKSDNILLGMDGSVKLTDFGFCA---------- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 38787904 214 vNVVEEEIKKYT---TLSYRAPEMINLYGGKPittKADIWALGCL 255
Cdd:cd06647 152 -QITPEQSKRSTmvgTPYWMAPEVVTRKAYGP---KVDIWSLGIM 192
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
92-266 8.32e-15

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: 75.02  E-value: 8.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  92 CKR-----EITIMKELSgHKNIVGYLDCAvnSISDNVWEVLilmEYCRAG---QVVNQmnkklQTGFTEPEVLQIFCDTC 163
Cdd:cd14010  36 SKRpevlnEVRLTHELK-HPNVLKFYEWY--ETSNHLWLVV---EYCTGGdleTLLRQ-----DGNLPESSVRKFGRDLV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 EAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSA------TNKFLNPQKDGVNVVEEEIKKYT--TLSYRAPEMI 235
Cdd:cd14010 105 RGLHYIH--SKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeiLKELFGQFSDEGNVNKVSKKQAKrgTPYYMAPELF 182
                       170       180       190
                ....*....|....*....|....*....|.
gi 38787904 236 NlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14010 183 Q---GGVHSFASDLWALGCVLYEMFTGKPPF 210
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
93-312 8.38e-15

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: 74.85  E-value: 8.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAVnsiSDNVWevLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqc 172
Cdd:cd14070  51 RREGRIQQMIR-HPNITQLLDILE---TENSY--YLVMELCPGGNLMHRIYDKKR--LEEREARRYIRQLVSAVEHLH-- 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KTPIIHRDLKVENILLNDGGNYVLCDFG-SATNKFLnpqkdgvNVVEEEIKKYTTLSYRAPEminLYGGKPITTKADIWA 251
Cdd:cd14070 121 RAGVVHRDLKIENLLLDENDNIKLIDFGlSNCAGIL-------GYSDPFSTQCGSPAYAAPE---LLARKKYGPKVDVWS 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 252 LGCLLYKLCFFTLPFGESQVAI-------CDGNFTiPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14070 191 IGVNMYAMLTGTLPFTVEPFSLralhqkmVDKEMN-PLPTDLSPGAISFLRSLLEPDPLKRPNIKQAL 257
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
57-266 1.30e-14

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: 75.13  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITIMKE--LS--GHKNIVgYLDCAVNSISdnvwEVLILME 131
Cdd:cd05582   3 LGQGSFGKVFLVRkITGPDAGTLYAMKVLKKATLKVRDRVRTKMERdiLAdvNHPFIV-KLHYAFQTEG----KLYLILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkfLNPQK 211
Cdd:cd05582  78 FLRGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLDEDGHIKLTDFG------LSKES 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 212 dgvnvVEEEIKKYT---TLSYRAPEMINLYGGkpiTTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05582 148 -----IDHEKKAYSfcgTVEYMAPEVVNRRGH---TQSADWWSFGVLMFEMLTGSLPF 197
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
54-266 1.71e-14

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: 74.69  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFStvfLVR--THG------GIRCALKRMYVNNmpdlnvcKREITIMKELSGHKNIVgyldcAVNSISDNVWE 125
Cdd:cd14179  12 DKPLGEGSFS---ICRkcLHKktnqeyAVKIVSKRMEANT-------QREIAALKLCEGHPNIV-----KLHEVYHDQLH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILL---NDGGNYVLCDFGSA 202
Cdd:cd14179  77 TFLVMELLKGGELLERIKKKQH--FSETEASHIMRKLVSAVSHMHD--VGVVHRDLKPENLLFtdeSDNSEIKIIDFGFA 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 203 TnkfLNPQKDgvnvveEEIKKYT-TLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14179 153 R---LKPPDN------QPLKTPCfTLHYAAPELLNYNG---YDESCDLWSLGVILYTMLSGQVPF 205
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
94-259 1.76e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 75.18  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   94 REITIMKELSgHKNIVGYLDCAVNSISDNVweVLILMEYCRAgQVVNQmnkklQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:PTZ00024  69 RELKIMNEIK-HENIMGLVDVYVEGDFINL--VMDIMASDLK-KVVDR-----KIRLTESQVKCILLQILNGLNVLHKWY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  174 tpIIHRDLKVENILLNDGGNYVLCDFGSATnKFLNP------QKDGVNVVEEEI-KKYTTLSYRAPEMinLYGGKPITTK 246
Cdd:PTZ00024 140 --FMHRDLSPANIFINSKGICKIADFGLAR-RYGYPpysdtlSKDETMQRREEMtSKVVTLWYRAPEL--LMGAEKYHFA 214
                        170
                 ....*....|...
gi 38787904  247 ADIWALGCLLYKL 259
Cdd:PTZ00024 215 VDMWSVGCIFAEL 227
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
48-306 1.77e-14

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 73.91  E-value: 1.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWev 126
Cdd:cd06646   8 QHDYELIQRVGSGTYGDVYKARNlHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECK-HCNIVAYFGSYLSR--EKLW-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 lILMEYCRAGQVvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATNkf 206
Cdd:cd06646  83 -ICMEYCGGGSL--QDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGK--MHRDIKGANILLTDNGDVKLADFGVAAK-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgVNVVEEEIKKYTTLSY-RAPEMINLYGGKPITTKADIWALGCLLYKLC-----FFTLPFGESQVAICDGNFTI 280
Cdd:cd06646 156 -------ITATIAKRKSFIGTPYwMAPEVAAVEKNGGYNQLCDIWAVGITAIELAelqppMFDLHPMRALFLMSKSNFQP 228
                       250       260
                ....*....|....*....|....*....
gi 38787904 281 P---DNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06646 229 PklkDKTKWSSTFHNFVKISLTKNPKKRP 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
53-266 2.21e-14

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: 73.32  E-value: 2.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRtH--GGIRCALKRMYVNNMPDLNVCK--REITIMKELSgHKNIVGYLDcavnsISDNVWEVLI 128
Cdd:cd14072   4 LLKTIGKGNFAKVKLAR-HvlTGREVAIKIIDKTQLNPSSLQKlfREVRIMKILN-HPNIVKLFE-----VIETEKTLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkFLN 208
Cdd:cd14072  77 VMEYASGGEVFDYL--VAHGRMKEKEARAKFRQIVSAVQYCHQKR--IVHRDLKAENLLLDADMNIKIADFG-----FSN 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 209 PQKDGvnvveeeiKKYTTL----SYRAPEMINlyGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14072 148 EFTPG--------NKLDTFcgspPYAAPELFQ--GKKYDGPEVDVWSLGVILYTLVSGSLPF 199
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
95-314 2.26e-14

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: 74.44  E-value: 2.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDCAVNSisdnvWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARL--HQC 172
Cdd:cd05055  88 ELKIMSHLGNHENIVNLLGACTIG-----GPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLasKNC 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 ktpiIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqKDGVNVVEEEIKKYTTL--SYRAPEMI--NLYggkpiTTKAD 248
Cdd:cd05055 163 ----IHRDLAARNVLLTHGKIVKICDFGLA--------RDIMNDSNYVVKGNARLpvKWMAPESIfnCVY-----TFESD 225
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 249 IWALGCLLYKLcfFTLPFGESQVAICDGNFTIPDNSRY--------SRNIHCLIRFMLEPDPEHRPDIFQVSYF 314
Cdd:cd05055 226 VWSYGILLWEI--FSLGSNPYPGMPVDSKFYKLIKEGYrmaqpehaPAEIYDIMKTCWDADPLKRPTFKQIVQL 297
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
50-311 2.36e-14

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: 73.34  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNN------MPDLNVCKREITIMKEL---SGHKNIVGYLDcavnsi 119
Cdd:cd14101   1 QYTMGNLLGKGGFGTVYAgHRISDGLQVAIKQISRNRvqqwskLPGVNPVPNEVALLQSVgggPGHRGVIRLLD------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 sdnvW-----EVLILMEycRAGQVVNQMNKKLQTGfTEPEVL--QIFCDTCEAVARLHQckTPIIHRDLKVENILLN-DG 191
Cdd:cd14101  75 ----WfeipeGFLLVLE--RPQHCQDLFDYITERG-ALDESLarRFFKQVVEAVQHCHS--KGVVHRDIKDENILVDlRT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 192 GNYVLCDFGSATnkflnpqkdgvnVVEEEIkkYT----TLSYRAPEMI--NLYGGKPITtkadIWALGCLLYKLCFFTLP 265
Cdd:cd14101 146 GDIKLIDFGSGA------------TLKDSM--YTdfdgTRVYSPPEWIlyHQYHALPAT----VWSLGILLYDMVCGDIP 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 266 FgESQVAICDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14101 208 F-ERDTDILKAKPSFN--KRVSNDCRSLIRSCLAYNPSDRPSLEQI 250
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
50-289 2.37e-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: 73.51  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIrcALKRMYVNN--MPDLNVCKREITIMKElSGHKNIVGYLDCAVNSisdnvwEVL 127
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRGKWHGDV--AVKILKVTEptPEQLQAFKNEMQVLRK-TRHVNILLFMGFMTRP------NFA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKkLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKfl 207
Cdd:cd14150  72 IITQWCEGSSLYRHLHV-TETRFDTMQLIDVARQTAQGMDYLH--AKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVK-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 nPQKDGVNVVEEeikKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFG----ESQVAICDG-NFTIPD 282
Cdd:cd14150 147 -TRWSGSQQVEQ---PSGSILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSninnRDQIIFMVGrGYLSPD 222

                ....*..
gi 38787904 283 NSRYSRN 289
Cdd:cd14150 223 LSKLSSN 229
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
94-311 2.45e-14

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: 73.64  E-value: 2.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSisdnvWEVLILMEYCRAGQVVNQMnkkLQTG-FTEPEVLQIFCDTCEAVARLHQc 172
Cdd:cd14077  62 REAALSSLLN-HPHICRLRDFLRTP-----NHYYMLFEYVDGGQLLDYI---ISHGkLKEKQARKFARQIASALDYLHR- 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 kTPIIHRDLKVENILLNDGGNYVLCDFGsaTNKFLNPQKdgvnvveeEIKKYT-TLSYRAPEMINlygGKPIT-TKADIW 250
Cdd:cd14077 132 -NSIVHRDLKIENILISKSGNIKIIDFG--LSNLYDPRR--------LLRTFCgSLYFAAPELLQ---AQPYTgPEVDVW 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 251 ALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14077 198 SFGVVLYVLVCGKVPFDDENMPalhakIKKGKVEYP--SYLSSECKSLISRMLVVDPKKRATLEQV 261
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
60-311 2.45e-14

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: 73.20  E-value: 2.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRTHGGIrcALKRMYVNNmP---DLNVCKREITIMKELSgHKNIVGYLDCavnsISDNvwEVLILMEYCRAg 136
Cdd:cd14062   4 GSFGTVYKGRWHGDV--AVKKLNVTD-PtpsQLQAFKNEVAVLRKTR-HVNILLFMGY----MTKP--QLAIVTQWCEG- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 qvvNQMNKKLQTGFTEPEVLQIFcDTCEAVAR----LHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFL----- 207
Cdd:cd14062  73 ---SSLYKHLHVLETKFEMLQLI-DIARQTAQgmdyLHAKN--IIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRwsgsq 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 -NPQKDGvnvveeeikkytTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPF----GESQVAICDG-NFTIP 281
Cdd:cd14062 147 qFEQPTG------------SILWMAPEVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYshinNRDQILFMVGrGYLRP 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 282 DNSRYSRNI-HCLIRFM---LEPDPEHRPDIFQV 311
Cdd:cd14062 215 DLSKVRSDTpKALRRLMedcIKFQRDERPLFPQI 248
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
48-305 2.71e-14

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: 73.87  E-value: 2.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcavnsISDNVWEV 126
Cdd:cd14166   2 RETFIFMEVLGSGAFSEVYLVKQRsTGKLYALKCIKKSPLSRDSSLENEIAVLKRIK-HENIVTLED-----IYESTTHY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMnkkLQTG-FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILL---NDGGNYVLCDFGSA 202
Cdd:cd14166  76 YLVMQLVSGGELFDRI---LERGvYTEKDASRVINQVLSAVKYLHE--NGIVHRDLKPENLLYltpDENSKIMITDFGLS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 tnkflNPQKDGVNVVeeeikKYTTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDG- 276
Cdd:cd14166 151 -----KMEQNGIMST-----ACGTPGYVAPEVL---AQKPYSKAVDCWSIGVITYILLCGYPPFYEETESrlfekIKEGy 217
                       250       260       270
                ....*....|....*....|....*....|
gi 38787904 277 -NFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14166 218 yEFESPFWDDISESAKDFIRHLLEKNPSKR 247
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
94-314 2.76e-14

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: 73.12  E-value: 2.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSisDNVWevlILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQck 173
Cdd:cd14188  50 KEIELHRILH-HKHVVQFYHYFEDK--ENIY---ILLEYCSRRSMAHIL--KARKVLTEPEVRYYLRQIVSGLKYLHE-- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVVeeeikkYTTLSYRAPEMINLYGGKpitTKADIWALG 253
Cdd:cd14188 120 QEILHRDLKLGNFFINENMELKVGDFGLAAR--LEPLEHRRRTI------CGTPNYLSPEVLNKQGHG---CESDIWALG 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 254 CLLYKLCFFTLPF-----GESQVAICDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHRP---DIFQVSYF 314
Cdd:cd14188 189 CVMYTMLLGRPPFettnlKETYRCIREARYSLP--SSLLAPAKHLIASMLSKNPEDRPsldEIIRHDFF 255
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
57-271 2.76e-14

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: 73.03  E-value: 2.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLILMEYCRA 135
Cdd:cd14103   1 LGRGKFGTVYrCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLR-HPRLLQLYDAF-----ETPREMVLVMEYVAG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQ----VVNQmnkklQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENIL-LNDGGNYV-LCDFGSAtnKFLNP 209
Cdd:cd14103  75 GElferVVDD-----DFELTERDCILFMRQICEGVQYMH--KQGILHLDLKPENILcVSRTGNQIkIIDFGLA--RKYDP 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 210 QKDgVNVVeeeikkYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF-GESQV 271
Cdd:cd14103 146 DKK-LKVL------FGTPEFVAPEVVNY---EPISYATDMWSVGVICYVLLSGLSPFmGDNDA 198
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
116-306 2.82e-14

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: 73.42  E-value: 2.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 116 VNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILL---NDGG 192
Cdd:cd14198  73 LHEVYETTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQ--NNIVHLDLKPQNILLssiYPLG 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 193 NYVLCDFGSAtnkflnpQKDGVNVVEEEIkkYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF-GE--- 268
Cdd:cd14198 151 DIKIVDFGMS-------RKIGHACELREI--MGTPEYLAPEILNY---DPITTATDMWNIGVIAYMLLTHESPFvGEdnq 218
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 38787904 269 ------SQVAIcdgNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14198 219 etflniSQVNV---DYSEETFSSVSQLATDFIQKLLVKNPEKRP 259
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
57-314 2.90e-14

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 74.07  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLDCAVNSI--------SDNV 123
Cdd:cd07864  15 IGEGTYGQVYKAKdKDTGELVALKKVRLDNekegFPITAI--REIKILRQLN-HRSVVNLKEIVTDKQdaldfkkdKGAF 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 124 WEVLILMEYCRAGQVVNQMnkklqTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd07864  92 YLVFEYMDHDLMGLLESGL-----VHFSEDHIKSFMKQLLEGLNYCH--KKNFLHRDIKCSNILLNNKGQIKLADFGLA- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nKFLNpqkdgvnvvEEEIKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLLYKLcfFTlpfgesQVAICDGNft 279
Cdd:cd07864 164 -RLYN---------SEESRPYTnkviTLWYRPPEL--LLGEERYGPAIDVWSCGCILGEL--FT------KKPIFQAN-- 221
                       250       260       270
                ....*....|....*....|....*....|....*
gi 38787904 280 ipdnsRYSRNIHCLIRFMLEPDPEHRPDIFQVSYF 314
Cdd:cd07864 222 -----QELAQLELISRLCGSPCPAVWPDVIKLPYF 251
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
57-305 3.06e-14

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: 73.35  E-value: 3.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVrTH--GGIRCALKRMYVNNMPDLNV--CKREITIMKELSgHKNIVgYLDcavnsisdNVWE----VLI 128
Cdd:cd14097   9 LGQGSFGVVIEA-THkeTQTKWAIKKINREKAGSSAVklLEREVDILKHVN-HAHII-HLE--------EVFEtpkrMYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILL-------NDGGNYVLCDFGs 201
Cdd:cd14097  78 VMELCEDGELKELLLRKGF--FSENETRHIIQSLASAVAYLH--KNDIVHRDLKLENILVkssiidnNDKLNIKVTDFG- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 atnkfLNPQKDGVNvvEEEIKKYT-TLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPF---GESQV--AICD 275
Cdd:cd14097 153 -----LSVQKYGLG--EDMLQETCgTPIYMAPEVISAHG---YSQQCDIWSIGVIMYMLLCGEPPFvakSEEKLfeEIRK 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 276 GNFTIPDN--SRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14097 223 GDLTFTQSvwQSVSDAAKNVLQQLLKVDPAHR 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
57-305 3.22e-14

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: 73.28  E-value: 3.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNV---CKREITIMKeLSGHKNIVGYLDCAVNSiSDNVWEVlilMEY 132
Cdd:cd05611   4 ISKGAFGSVYLAKKRsTGDYFAIKVLKKSDMIAKNQvtnVKAERAIMM-IQGESPYVAKLYYSFQS-KDYLYLV---MEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKd 212
Cdd:cd05611  79 LNGGDCASLI--KTLGGLPEDWAKQYIAEVVLGVEDLHQ--RGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 gvnvveeeiKKYT-TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICDG------NFTIPDNS 284
Cdd:cd05611 154 ---------KKFVgTPDYLAPETIL---GVGDDKMSDWWSLGCVIFEFLFGYPPFhAETPDAVFDNilsrriNWPEEVKE 221
                       250       260
                ....*....|....*....|.
gi 38787904 285 RYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05611 222 FCSPEAVDLINRLLCMDPAKR 242
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
94-308 3.25e-14

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: 73.46  E-value: 3.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVWEVLilmEYCRAGQVvnqMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14199  74 QEIAILKKLD-HPNVVKLVEVLDDPSEDHLYMVF---ELVKQGPV---MEVPTLKPLSEDQARFYFQDLIKGIEYLHYQK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 tpIIHRDLKVENILLNDGGNYVLCDFGsATNKFLNPQKDGVNVVeeeikkyTTLSYRAPEMIN----LYGGKPIttkaDI 249
Cdd:cd14199 147 --IIHRDVKPSNLLVGEDGHIKIADFG-VSNEFEGSDALLTNTV-------GTPAFMAPETLSetrkIFSGKAL----DV 212
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 250 WALGCLLYKLCFFTLPFGESQV-----AICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR---PDI 308
Cdd:cd14199 213 WAMGVTLYCFVFGQCPFMDERIlslhsKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRisvPEI 279
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
57-310 3.34e-14

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: 73.01  E-value: 3.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDlnvcKREiTIMKEL-----SGHKNIVG-----YLDCAVNsisdnvwe 125
Cdd:cd06623   9 LGQGSSGVVYKVRHKPtGKIYALKKIHVDGDEE----FRK-QLLRELktlrsCESPYVVKcygafYKEGEIS-------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 vlILMEYCRAGQVVNQMNKKLqtGFTEPEVLQIFCDTCEAVARLHQCKTpIIHRDLKVENILLNDGGNYVLCDFGSAtnK 205
Cdd:cd06623  76 --IVLEYMDGGSLADLLKKVG--KIPEPVLAYIARQILKGLDYLHTKRH-IIHRDIKPSNLLINSKGEVKIADFGIS--K 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNPQKDgvnvveeeiKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQV--------AIC 274
Cdd:cd06623 149 VLENTLD---------QCNTfvgTVTYMSPERIQ---GESYSYAADIWSLGLTLLECALGKFPFLPPGQpsffelmqAIC 216
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 275 DGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd06623 217 DGPPPSLPAEEFSPEFRDFISACLQKDPKKRPSAAE 252
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-305 4.07e-14

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: 73.75  E-value: 4.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEES-LAEGGFSTVFLVR-THGGIRCALK----RMYVNNmpdlnvcKREITIMKELSGHKNIVgyldcAVNSISD 121
Cdd:cd14180   4 CYELDLEEPaLGEGSFSVCRKCRhRQSGQEYAVKiisrRMEANT-------QREVAALRLCQSHPNIV-----ALHEVLH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 NVWEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLND-GGNYVL--CD 198
Cdd:cd14180  72 DQYHTYLVMELLRGGELLDRIKKKAR--FSESEASQLMRSLVSAVSFMHEAG--VVHRDLKPENILYADeSDGAVLkvID 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 199 FGSATnkfLNPQKDgvnvvEEEIKKYTTLSYRAPEMINLYGgkpITTKADIWALGCLLYKLCFFTLPF-------GESQV 271
Cdd:cd14180 148 FGFAR---LRPQGS-----RPLQTPCFTLQYAAPELFSNQG---YDESCDLWSLGVILYTMLSGQVPFqskrgkmFHNHA 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 38787904 272 A-----ICDGNFTIPDNS--RYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14180 217 AdimhkIKEGDFSLEGEAwkGVSEEAKDLVRGLLTVDPAKR 257
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
57-305 5.12e-14

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: 73.43  E-value: 5.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKR---EITIMkELSGHKNIVgYLDCAVNSiSDNVWevlILMEY 132
Cdd:cd05574   9 LGKGDVGRVYLVRLKGtGKLFAMKVLDKEEMIKRNKVKRvltEREIL-ATLDHPFLP-TLYASFQT-STHLC---FVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKLQTGFTE-------PEVLQifcdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDF------ 199
Cdd:cd05574  83 CPGGELFRLLQKQPGKRLPEevarfyaAEVLL-------ALEYLHLLG--FVYRDLKPENILLHESGHIMLTDFdlskqs 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 ---GSATNKFLNPQKDGVNVVEEEIKKYT------------TLSYRAPEMINLYGGkpiTTKADIWALGCLLYKLCFFTL 264
Cdd:cd05574 154 svtPPPVRKSLRKGSRRSSVKSIEKETFVaepsarsnsfvgTEEYIAPEVIKGDGH---GSAVDWWTLGILLYEMLYGTT 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 265 PF-GESQVA----ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05574 231 PFkGSNRDEtfsnILKKELTFPESPPVSSEAKDLIRKLLVKDPSKR 276
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
57-306 5.91e-14

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: 72.31  E-value: 5.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISdnvweVLILMEYCRAG 136
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQ-HPQLVGLLDTFETPTS-----YILVLEMADQG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 QVVNQMnkkLQTG-FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGN---YVLCDFGSATNkflnpqkd 212
Cdd:cd14113  89 RLLDYV---VRWGnLTEEKIRFYLREILEALQYLHNCR--IAHLDLKPENILVDQSLSkptIKLADFGDAVQ-------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 gVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDN---- 283
Cdd:cd14113 156 -LNTTYYIHQLLGSPEFAAPEIIL---GNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEetclnICRLDFSFPDDyfkg 231
                       250       260
                ....*....|....*....|....
gi 38787904 284 -SRYSRNIHClirFMLEPDPEHRP 306
Cdd:cd14113 232 vSQKAKDFVC---FLLQMDPAKRP 252
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
51-305 6.27e-14

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: 72.62  E-value: 6.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEESLAEGGFSTVFLVRTHG-----GIRCALKRMYVNNMpdlNVCKREITIMKELSgHKNIVgyldcAVNSISDNVWE 125
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGsqrlvALKCIPKKALRGKE---AMVENEIAVLRRIN-HENIV-----SLEDIYESPTH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMnkkLQTG-FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN---DGGNYVLCDFGs 201
Cdd:cd14169  76 LYLAMELVTGGELFDRI---IERGsYTEKDASQLIGQVLQAVKYLHQLG--IVHRDLKPENLLYAtpfEDSKIMISDFG- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 aTNKFlnpQKDGVNVVeeeikKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE-------SQVAIC 274
Cdd:cd14169 150 -LSKI---EAQGMLST-----ACGTPGYVAPELLE---QKPYGKAVDVWAIGVISYILLCGYPPFYDendselfNQILKA 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 275 DGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14169 218 EYEFDSPYWDDISESAKDFIRHLLERDPEKR 248
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
57-306 6.51e-14

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: 72.80  E-value: 6.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-----THGGIRCA---LKRMYVNN-MPDLnvcKREITIMKELSgHKNIVGYLDCAVnsiSDNVWEVL 127
Cdd:cd05038  12 LGEGHFGSVELCRydplgDNTGEQVAvksLQPSGEEQhMSDF---KREIEILRTLD-HEYIVKYKGVCE---SPGRRSLR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVV-------NQMNKKLQTGFTEpevlQIfcdtCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd05038  85 LIMEYLPSGSLRdylqrhrDQIDLKRLLLFAS----QI----CKGMEYLGSQR--YIHRDLAARNILVESEDLVKISDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SAtnKFLNPQKDGVNVVEeeiKKYTTLSYRAPEMINLYggkPITTKADIWALGCLLYKLcfFTL------PFGES----- 269
Cdd:cd05038 155 LA--KVLPEDKEYYYVKE---PGESPIFWYAPECLRES---RFSSASDVWSFGVTLYEL--FTYgdpsqsPPALFlrmig 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 38787904 270 ----QVAICDGNFTIPDNSRYSRNIHC------LIRFMLEPDPEHRP 306
Cdd:cd05038 225 iaqgQMIVTRLLELLKSGERLPRPPSCpdevydLMKECWEYEPQDRP 271
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
90-266 7.00e-14

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: 72.29  E-value: 7.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  90 NVCKREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARL 169
Cdd:cd14185  43 DMIESEILIIKSLS-HPNIV-----KLFEVYETEKEIYLILEYVRGGDLFDAIIESVK--FTEHDAALMIIDLCEALVYI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 170 HQckTPIIHRDLKVENILLN---DGGNYV-LCDFGSAtnkflnpqkdgVNVVEEEIKKYTTLSYRAPEMINlygGKPITT 245
Cdd:cd14185 115 HS--KHIVHRDLKPENLLVQhnpDKSTTLkLADFGLA-----------KYVTGPIFTVCGTPTYVAPEILS---EKGYGL 178
                       170       180
                ....*....|....*....|..
gi 38787904 246 KADIWALGCLLY-KLCFFTlPF 266
Cdd:cd14185 179 EVDMWAAGVILYiLLCGFP-PF 199
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
95-308 1.18e-13

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: 72.11  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDCAVNSI-----SDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARL 169
Cdd:cd14171  48 EVRLHMMCSGHPNIVQIYDVYANSVqfpgeSSPRARLLIVMELMEGGELFDRISQ--HRHFTEKQAAQYTKQIALAVQHC 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 170 HQCKtpIIHRDLKVENILLNDGGNYV---LCDFGSA------------TNKFLNPQkdgvnVVEEEIKKYTTLSYRAPEm 234
Cdd:cd14171 126 HSLN--IAHRDLKPENLLLKDNSEDApikLCDFGFAkvdqgdlmtpqfTPYYVAPQ-----VLEAQRRHRKERSGIPTS- 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 235 inlygGKPIT--TKADIWALGCLLY-KLCFFTlPF----------GESQVAICDGNFTIPDN--SRYSRNIHCLIRFMLE 299
Cdd:cd14171 198 -----PTPYTydKSCDMWSLGVIIYiMLCGYP-PFysehpsrtitKDMKRKIMTGSYEFPEEewSQISEMAKDIVRKLLC 271

                ....*....
gi 38787904 300 PDPEHRPDI 308
Cdd:cd14171 272 VDPEERMTI 280
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
55-255 1.26e-13

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: 71.77  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRT-HGGIRCALKRMYVN----NMPDLNVckREITIMKELSgHKNIVGYLDcavnsISDNVWEVLIL 129
Cdd:cd07860   6 EKIGEGTYGVVYKARNkLTGEVVALKKIRLDteteGVPSTAI--REISLLKELN-HPNIVKLLD-----VIHTENKLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYcragqvVNQMNKKLQ-----TGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd07860  78 FEF------LHQDLKKFMdasalTGIPLPLIKSYLFQLLQGLAFCHSHR--VLHRDLKPQNLLINTEGAIKLADFGLA-- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 205 kflnpQKDGVNVveeeiKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCL 255
Cdd:cd07860 148 -----RAFGVPV-----RTYThevvTLWYRAPEI--LLGCKYYSTAVDIWSLGCI 190
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
50-266 1.36e-13

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 71.63  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVNSisdnvwEVLIL 129
Cdd:cd14151   9 QITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRK-TRHVNILLFMGYSTKP------QLAIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKkLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnP 209
Cdd:cd14151  82 TQWCEGSSLYHHLHI-IETKFEMIKLIDIARQTAQGMDYLH--AKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVK---S 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 210 QKDGVNVVEEeikKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14151 156 RWSGSHQFEQ---LSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPY 209
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
47-260 1.72e-13

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 71.84  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  47 GRHQVtlEESLAEGGFSTVFLVR-THGGIRCALK-----RMYVNNMPDlnvckrEITIMKELS-------GHKNIVGYLD 113
Cdd:cd14136  10 GRYHV--VRKLGWGHFSTVWLCWdLQNKRFVALKvvksaQHYTEAALD------EIKLLKCVReadpkdpGREHVVQLLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 114 ------------CAVnsisdnvWEV-----LILMEYCRAgqvvnqmnkklqTGFTEPEVLQIFCDTCEAVARLH-QCKtp 175
Cdd:cd14136  82 dfkhtgpngthvCMV-------FEVlgpnlLKLIKRYNY------------RGIPLPLVKKIARQVLQGLDYLHtKCG-- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLN-DGGNYVLCDFGSA--TNKFLNpqkdgvnvveEEIKkytTLSYRAPEMInLygGKPITTKADIWAL 252
Cdd:cd14136 141 IIHTDIKPENVLLCiSKIEVKIADLGNAcwTDKHFT----------EDIQ---TRQYRSPEVI-L--GAGYGTPADIWST 204

                ....*...
gi 38787904 253 GCLLYKLC 260
Cdd:cd14136 205 ACMAFELA 212
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
94-253 1.72e-13

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 70.94  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSisDNVWEVlilMEYC--RAGQVVNQMNKKLQtgftEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd06607  50 KEVKFLRQLR-HPNTIEYKGCYLRE--HTAWLV---MEYClgSASDIVEVHKKPLQ----EVEIAAICHGALQGLAYLHS 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKTpiIHRDLKVENILLNDGGNYVLCDFGSAT-----NKFLNpqkdgvnvveeeikkytTLSYRAPEMINLYGGKPITTK 246
Cdd:cd06607 120 HNR--IHRDVKAGNILLTEPGTVKLADFGSASlvcpaNSFVG-----------------TPYWMAPEVILAMDEGQYDGK 180

                ....*..
gi 38787904 247 ADIWALG 253
Cdd:cd06607 181 VDVWSLG 187
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
128-266 2.01e-13

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 71.18  E-value: 2.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGsATNKFL 207
Cdd:cd05613  82 LILDYINGGELFTHLSQRER--FTENEVQIYIGEIVLALEHLH--KLGIIYRDIKLENILLDSSGHVVLTDFG-LSKEFL 156
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQkdgvnvVEEEIKKYTTLSYRAPEMINlyGGKPITTKA-DIWALGCLLYKLCFFTLPF 266
Cdd:cd05613 157 LDE------NERAYSFCGTIEYMAPEIVR--GGDSGHDKAvDWWSLGVLMYELLTGASPF 208
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
93-265 2.37e-13

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: 71.28  E-value: 2.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLdcAVNSISDNvwEVLILMEYCRA--GQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLH 170
Cdd:cd14001  53 KEEAKILKSLN-HPNIVGFR--AFTKSEDG--SLCLAMEYGGKslNDLIEERYEAGLGPFPAATILKVALSIARALEYLH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QCKTpIIHRDLKVENILL-NDGGNYVLCDFGSATnkflnPQKDGVNVVEEEIKKYT-TLSYRAPEMINlyGGKPITTKAD 248
Cdd:cd14001 128 NEKK-ILHGDIKSGNVLIkGDFESVKLCDFGVSL-----PLTENLEVDSDPKAQYVgTEPWKAKEALE--EGGVITDKAD 199
                       170
                ....*....|....*..
gi 38787904 249 IWALGCLLYKLCFFTLP 265
Cdd:cd14001 200 IFAYGLVLWEMMTLSVP 216
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
46-266 2.57e-13

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: 70.81  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGI--RCALKRMYVNNMPDLNVC-KREITIMKELSgHKNIVGYLDcaVNSISDN 122
Cdd:cd14201   3 VGDFEYSRKDLVGHGAFAVVFKGRHRKKTdwEVAIKSINKKNLSKSQILlGKEIKILKELQ-HENIVALYD--VQEMPNS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 VWevlILMEYCRAGQVVNQMNKKlqtGFTEPEVLQIFCDTCEAVARLHQCKTpIIHRDLKVENILLN---------DGGN 193
Cdd:cd14201  80 VF---LVMEYCNGGDLADYLQAK---GTLSEDTIRVFLQQIAAAMRILHSKG-IIHRDLKPQNILLSyasrkkssvSGIR 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 194 YVLCDFGSAtnKFLNPQKDGVNVVEEEIkkyttlsYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14201 153 IKIADFGFA--RYLQSNMMAATLCGSPM-------YMAPEVIM---SQHYDAKADLWSIGTVIYQCLVGKPPF 213
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
57-200 2.93e-13

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: 67.08  E-value: 2.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKREITIMKELSGH-KNIVGYLDcavnSISDNVWEVLiLMEYCR 134
Cdd:cd13968   1 MGEGASAKVFWAEGECtTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLeLNIPKVLV----TEDVDGPNIL-LMELVK 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 135 AGQvvnqMNKKLQTGfTEPEV-LQIFCDTC-EAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd13968  76 GGT----LIAYTQEE-ELDEKdVESIMYQLaECMRLLHSFH--LIHRDLNNDNILLSEDGNVKLIDFG 136
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
60-312 3.15e-13

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: 70.25  E-value: 3.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRTHGGIrCALKRMYVNNM---PDLNVCKREITIMKELSgHKNIVGYLDCAVNSISdnvwEVLILMEYCRAG 136
Cdd:cd14064   4 GSFGKVYKGRCRNKI-VAIKRYRANTYcskSDVDMFCREVSILCRLN-HPCVIQFVGACLDDPS----QFAIVTQYVSGG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 QVVNQMNKklQTGFTEPEV-LQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKDgvn 215
Cdd:cd14064  78 SLFSLLHE--QKRVIDLQSkLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLYEDGHAVVADFGES--RFLQSLDE--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 216 vvEEEIKKYTTLSYRAPEMINLYGgkPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNFTI-----PDNSRYSRNI 290
Cdd:cd14064 151 --DNMTKQPGNLRWMAPEVFTQCT--RYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYhhirpPIGYSIPKPI 226
                       250       260
                ....*....|....*....|..
gi 38787904 291 HCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14064 227 SSLLMRGWNAEPESRPSFVEIV 248
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
52-306 3.17e-13

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: 70.03  E-value: 3.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVRT-HGGIRCALKRMY--VNNMPDLNVCKREITIMKELSGHKNIVGYLdcavnsisdNVWE--- 125
Cdd:cd14050   4 TILSKLGEGSFGEVFKVRSrEDGKLYAVKRSRsrFRGEKDRKRKLEEVERHEKLGEHPNCVRFI---------KAWEekg 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 -VLILMEYCRAGQvvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSatn 204
Cdd:cd14050  75 iLYIQTELCDTSL---QQYCEETHSLPESEVWNILLDLLKGLKHLHDHG--LIHLDIKPANIFLSKDGVCKLGDFGL--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpqkdgvnVVEEEIKKYTTLS-----YRAPEMINlygGKPiTTKADIWALGCLLYKL-CFFTLP-FGESQVAICDGN 277
Cdd:cd14050 147 -----------VVELDKEDIHDAQegdprYMAPELLQ---GSF-TKAADIFSLGITILELaCNLELPsGGDGWHQLRQGY 211
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 278 ftIPDN--SRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14050 212 --LPEEftAGLSPELRSIIKLMMDPDPERRP 240
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
48-305 3.17e-13

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: 70.44  E-value: 3.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLV---RTHG--GIRCALKRMYVNNMpdlNVCKREITIMKELSgHKNIVgyldcAVNSISDN 122
Cdd:cd14167   2 RDIYDFREVLGTGAFSEVVLAeekRTQKlvAIKCIAKKALEGKE---TSIENEIAVLHKIK-HPNIV-----ALDDIYES 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 VWEVLILMEYCRAGQVVNQMNKKlqtGF-TEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENIL---LNDGGNYVLCD 198
Cdd:cd14167  73 GGHLYLIMQLVSGGELFDRIVEK---GFyTERDASKLIFQILDAVKYLHDMG--IVHRDLKPENLLyysLDEDSKIMISD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 199 FGsatnkfLNPQKDGVNVVEEEIKkytTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPFGE-------SQV 271
Cdd:cd14167 148 FG------LSKIEGSGSVMSTACG---TPGYVAPEVL---AQKPYSKAVDCWSIGVIAYILLCGYPPFYDendaklfEQI 215
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 272 AICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14167 216 LKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKR 249
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
55-259 3.71e-13

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: 70.38  E-value: 3.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAE---GGFSTVFLVRT-HGGIRCALKRMYV----NNMPDLNVckREITIMKELSG--HKNIVGYLDCAVNSISDNVW 124
Cdd:cd07863   3 EPVAEigvGAYGTVYKARDpHSGHFVALKSVRVqtneDGLPLSTV--REVALLKRLEAfdHPNIVRLMDVCATSRTDRET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYcragqvVNQ-----MNKKLQTGFTEPEVLQIFCDTCEAVARLH-QCktpIIHRDLKVENILLNDGGNYVLCD 198
Cdd:cd07863  81 KVTLVFEH------VDQdlrtyLDKVPPPGLPAETIKDLMRQFLRGLDFLHaNC---IVHRDLKPENILVTSGGQVKLAD 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 199 FGSAtnKFLNPQKDGVNVVeeeikkyTTLSYRAPEMI--NLYGgkpitTKADIWALGCLLYKL 259
Cdd:cd07863 152 FGLA--RIYSCQMALTPVV-------VTLWYRAPEVLlqSTYA-----TPVDMWSVGCIFAEM 200
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
43-255 3.73e-13

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 70.52  E-value: 3.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  43 VFAVG--RHQVTLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVnsI 119
Cdd:cd06656  11 IVSVGdpKKKYTRFEKIGQGASGTVYTaIDIATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYL--V 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWevlILMEYCRAGQVVNQMNkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd06656  88 GDELW---VVMEYLAGGSLTDVVT---ETCMDEGQIAAVCRECLQALDFLHS--NQVIHRDIKSDNILLGMDGSVKLTDF 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 200 GSATnkflnpqkdgvNVVEEEIKKYT---TLSYRAPEMINLYGGKPittKADIWALGCL 255
Cdd:cd06656 160 GFCA-----------QITPEQSKRSTmvgTPYWMAPEVVTRKAYGP---KVDIWSLGIM 204
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
43-255 3.85e-13

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: 70.52  E-value: 3.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  43 VFAVG--RHQVTLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVnsI 119
Cdd:cd06654  12 IVSVGdpKKKYTRFEKIGQGASGTVYTaMDVATGQEVAIRQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYL--V 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWevlILMEYCRAGQVVNQMNkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd06654  89 GDELW---VVMEYLAGGSLTDVVT---ETCMDEGQIAAVCRECLQALEFLHS--NQVIHRDIKSDNILLGMDGSVKLTDF 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 200 GSATnkflnpqkdgvNVVEEEIKKYT---TLSYRAPEMINLYGGKPittKADIWALGCL 255
Cdd:cd06654 161 GFCA-----------QITPEQSKRSTmvgTPYWMAPEVVTRKAYGP---KVDIWSLGIM 205
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
94-269 5.06e-13

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: 70.16  E-value: 5.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDnvweVLILMEYCRAGQVvNQMNKKLqtGFTEPEVL-QIFCDTCEAVARLHQc 172
Cdd:cd06620  52 RELQILHECH-SPYIVSFYGAFLNENNN----IIICMEYMDCGSL-DKILKKK--GPFPEEVLgKIAVAVLEGLTYLYN- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KTPIIHRDLKVENILLNDGGNYVLCDFG-------SATNKFLNpqkdgvnvveeeikkytTLSYRAPEMINlyGGKpITT 245
Cdd:cd06620 123 VHRIIHRDIKPSNILVNSKGQIKLCDFGvsgelinSIADTFVG-----------------TSTYMSPERIQ--GGK-YSV 182
                       170       180
                ....*....|....*....|....
gi 38787904 246 KADIWALGCLLYKLCFFTLPFGES 269
Cdd:cd06620 183 KSDVWSLGLSIIELALGEFPFAGS 206
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
57-311 5.95e-13

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: 69.19  E-value: 5.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFStvflvRTHGGIRCALKRMY-VNNMPDLNVCK--------REITIMKELSgHKNIVGYLDCAVNSisDNVWevl 127
Cdd:cd14189   9 LGKGGFA-----RCYEMTDLATNKTYaVKVIPHSRVAKphqrekivNEIELHRDLH-HKHVVKFSHHFEDA--ENIY--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATnkFL 207
Cdd:cd14189  78 IFLELCSRKSLAHIW--KARHTLLEPEVRYYLKQIISGLKYLHL--KGILHRDLKLGNFFINENMELKVGDFGLAA--RL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPqkdgvnvveEEIKKYT---TLSYRAPEMINLYGGKPittKADIWALGCLLYK-LC----FFTLPFGESQVAICDGNFT 279
Cdd:cd14189 152 EP---------PEQRKKTicgTPNYLAPEVLLRQGHGP---ESDVWSLGCVMYTlLCgnppFETLDLKETYRCIKQVKYT 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 280 IPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14189 220 LP--ASLSLPARHLLAGILKRNPGDRLTLDQI 249
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
147-305 6.31e-13

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: 69.67  E-value: 6.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 147 QTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqkdgVNVVEEE-IK-KY 224
Cdd:cd05630  96 QAGFPEARAVFYAAEICCGLEDLHRER--IVYRDLKPENILLDDHGHIRISDLGLA-----------VHVPEGQtIKgRV 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 225 TTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNF-----TIPD--NSRYSRNIHCLIRFM 297
Cdd:cd05630 163 GTVGYMAPEVVK---NERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVerlvkEVPEeySEKFSPQARSLCSML 239

                ....*...
gi 38787904 298 LEPDPEHR 305
Cdd:cd05630 240 LCKDPAER 247
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
44-269 8.28e-13

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: 68.84  E-value: 8.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRHQVtleesLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcAVNSISDn 122
Cdd:cd14192   4 YAVCPHEV-----LGGGRFGQVHkCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLN-HVNLIQLYD-AFESKTN- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 vweVLILMEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENIL-LNDGGNYV-LCDFG 200
Cdd:cd14192  76 ---LTLIMEYVDGGELFDRITDE-SYQLTELDAILFTRQICEGVHYLHQ--HYILHLDLKPENILcVNSTGNQIkIIDFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SAtNKFLNPQKDGVNvveeeikkYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF-GES 269
Cdd:cd14192 150 LA-RRYKPREKLKVN--------FGTPEFLAPEVVNY---DFVSFPTDMWSVGVITYMLLSGLSPFlGET 207
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
93-269 8.71e-13

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: 68.78  E-value: 8.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLILMEYCRAGQVVNQMNKklqTGFTEPEVLQIFCDTCEAVARLHQc 172
Cdd:cd14108  46 RRELALLAELD-HKSIVRFHDAF-----EKRRVVIIVTELCHEELLERITKR---PTVCESEVRSYMRQLLEGIEYLHQ- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 kTPIIHRDLKVENILLNDGGN--YVLCDFGSATNkfLNPQkdgvnvvEEEIKKYTTLSYRAPEMINlygGKPITTKADIW 250
Cdd:cd14108 116 -NDVLHLDLKPENLLMADQKTdqVRICDFGNAQE--LTPN-------EPQYCKYGTPEFVAPEIVN---QSPVSKVTDIW 182
                       170       180
                ....*....|....*....|.
gi 38787904 251 ALGCLLYkLCFFTL-PF-GES 269
Cdd:cd14108 183 PVGVIAY-LCLTGIsPFvGEN 202
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
55-314 8.79e-13

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: 69.27  E-value: 8.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH-GGIRCALKRMYVNN---MPDLNVckREITIMKELSgHKNIVGYLDcavnsisdnvwevLILM 130
Cdd:cd07871  11 DKLGEGTYATVFKGRSKlTENLVALKEIRLEHeegAPCTAI--REVSLLKNLK-HANIVTLHD-------------IIHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAgqvvnqmnkkLQTGFTEPEVLQiFCDTCEAVARLHQCKT---------------PIIHRDLKVENILLNDGGNYV 195
Cdd:cd07871  75 ERCLT----------LVFEYLDSDLKQ-YLDNCGNLMSMHNVKIfmfqllrglsychkrKILHRDLKPQNLLINEKGELK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 LCDFGSATNKFLnPQKDGVNVVeeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCLLYKLcfftlpfgesqvaiCD 275
Cdd:cd07871 144 LADFGLARAKSV-PTKTYSNEV-------VTLWYRPPDV--LLGSTEYSTPIDMWGVGCILYEM--------------AT 199
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 276 GNFTIPdNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYF 314
Cdd:cd07871 200 GRPMFP-GSTVKEELHLIFRLLGTPTEETWPGVTSNEEF 237
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
57-311 1.19e-12

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: 68.62  E-value: 1.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMyvnnmpDLNVCKR------EITIMKELSgHKNIVGYLDCAVnsISDNVWevlIL 129
Cdd:cd06648  15 IGEGSTGIVCIATdKSTGRQVAVKKM------DLRKQQRrellfnEVVIMRDYQ-HPNIVEMYSSYL--VGDELW---VV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNkklQTGFTEPEVLQIfCDTC-EAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkfln 208
Cdd:cd06648  83 MEFLEGGALTDIVT---HTRMNEEQIATV-CRAVlKALSFLHSQG--VIHRDIKSDSILLTSDGRVKLSDFGFCAQ---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pqkdgvnvVEEEIKKYTTLS----YRAPEMINLyggKPITTKADIWALGCLLYKLC-----FFTLPFGESQVAICDgnfT 279
Cdd:cd06648 153 --------VSKEVPRRKSLVgtpyWMAPEVISR---LPYGTEVDIWSLGIMVIEMVdgeppYFNEPPLQAMKRIRD---N 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 280 IPDNSRYSRNI----HCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd06648 219 EPPKLKNLHKVsprlRSFLDRMLVRDPAQRATAAEL 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
54-257 1.21e-12

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: 68.98  E-value: 1.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFSTVF-LVRTHGGIRCALKrmYVNNMPDLNVCK--REITIMKELSGHKNIvgyLDCaVNSISDNVWEVLILm 130
Cdd:cd14090   7 GELLGEGAYASVQtCINLYTGKEYAVK--IIEKHPGHSRSRvfREVETLHQCQGHPNI---LQL-IEYFEDDERFYLVF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYV---LCDFGSATNKFL 207
Cdd:cd14090  80 EKMRGGPLLSHIEKRVH--FTEQEASLVVRDIASALDFLH--DKGIAHRDLKPENILCESMDKVSpvkICDFDLGSGIKL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 38787904 208 NPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPIT--TKADIWALGCLLY 257
Cdd:cd14090 156 SSTSMTPVTTPELLTPVGSAEYMAPEVVDAFVGEALSydKRCDLWSLGVILY 207
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
95-333 1.24e-12

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: 68.90  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckT 174
Cdd:cd14175  44 EIEILLRYGQHPNII-----TLKDVYDDGKHVYLVTELMRGGELLDKILR--QKFFSEREASSVLHTICKTVEYLHS--Q 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PIIHRDLKVENIL-LNDGGN---YVLCDFG-----SATNKFLnpqkdgvnvveeeIKKYTTLSYRAPEMINLYGgkpITT 245
Cdd:cd14175 115 GVVHRDLKPSNILyVDESGNpesLRICDFGfakqlRAENGLL-------------MTPCYTANFVAPEVLKRQG---YDE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 246 KADIWALGCLLYKLCFFTLPFG--------ESQVAICDGNFTIPDNS--RYSRNIHCLIRFMLEPDPEHRPDIFQVSYFA 315
Cdd:cd14175 179 GCDIWSLGILLYTMLAGYTPFAngpsdtpeEILTRIGSGKFTLSGGNwnTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHP 258
                       250
                ....*....|....*...
gi 38787904 316 FKFAKKDCPVSNINNSSI 333
Cdd:cd14175 259 WITQKDKLPQSQLNHQDV 276
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
48-255 1.31e-12

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 68.98  E-value: 1.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDnvwEV 126
Cdd:cd06655  18 KKKYTRYEKIGQGASGTVFTAIDVAtGQEVAIKQINLQKQPKKELIINEILVMKELK-NPNIVNFLDSFL--VGD---EL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LILMEYCRAGQVVNQMNkklQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATnkf 206
Cdd:cd06655  92 FVVMEYLAGGSLTDVVT---ETCMDEAQIAAVCRECLQALEFLH--ANQVIHRDIKSDNVLLGMDGSVKLTDFGFCA--- 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 38787904 207 lnpqkdgvNVVEEEIKKYT---TLSYRAPEMINLYGGKPittKADIWALGCL 255
Cdd:cd06655 164 --------QITPEQSKRSTmvgTPYWMAPEVVTRKAYGP---KVDIWSLGIM 204
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
53-316 1.58e-12

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: 68.59  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVcKREITIMKELSGHKNIVGYLDCAVNS----ISDNVWevl 127
Cdd:cd06637  10 LVELVGNGTYGQVYKGRhVKTGQLAAIKVMDVTGDEEEEI-KQEINMLKKYSHHRNIATYYGAFIKKnppgMDDQLW--- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkfL 207
Cdd:cd06637  86 LVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHK--VIHRDIKGQNVLLTENAEVKLVDFG------V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKDgvNVVEEEIKKYTTLSYRAPEMINLYGGKPITT--KADIWALGcllyklcFFTLPFGESQVAICDGN-----FTI 280
Cdd:cd06637 158 SAQLD--RTVGRRNTFIGTPYWMAPEVIACDENPDATYdfKSDLWSLG-------ITAIEMAEGAPPLCDMHpmralFLI 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 38787904 281 PDN-------SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAF 316
Cdd:cd06637 229 PRNpaprlksKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPF 271
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
44-256 1.58e-12

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: 69.26  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGrHQVTLEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMPDLnvCKR---EITIMKELSgHKNIVGYLDCAVNSI 119
Cdd:cd07849   1 FDVG-PRYQNLSYIGEGAYGMVCSaVHKPTGQKVAIKKISPFEHQTY--CLRtlrEIKILLRFK-HENIIGILDIQRPPT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWEVLI---LMEycragqvvNQMNKKLQTGFTEPEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV 195
Cdd:cd07849  77 FESFKDVYIvqeLME--------TDLYKLIKTQHLSNDHIQYFLyQILRGLKYIHSAN--VLHRDLKPSNLLLNTNCDLK 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 196 LCDFGSATNKflNPQKDGVNVVEEEIkkyTTLSYRAPE-MINlygGKPITTKADIWALGCLL 256
Cdd:cd07849 147 ICDFGLARIA--DPEHDHTGFLTEYV---ATRWYRAPEiMLN---SKGYTKAIDIWSVGCIL 200
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
94-268 2.05e-12

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: 67.46  E-value: 2.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQM-NKKLQTGFTEPEVLQiFCDTC-EAVARLHQ 171
Cdd:cd14058  35 VEVRQLSRVD-HPNII-----KLYGACSNQKPVCLVMEYAEGGSLYNVLhGKEPKPIYTAAHAMS-WALQCaKGVAYLHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CK-TPIIHRDLKVENILLNDGGNYV-LCDFGSATnkflnpqkdgvnvveeEIKKYTT-----LSYRAPEMINlygGKPIT 244
Cdd:cd14058 108 MKpKALIHRDLKPPNLLLTNGGTVLkICDFGTAC----------------DISTHMTnnkgsAAWMAPEVFE---GSKYS 168
                       170       180
                ....*....|....*....|....
gi 38787904 245 TKADIWALGCLLYKLCFFTLPFGE 268
Cdd:cd14058 169 EKCDVFSWGIILWEVITRRKPFDH 192
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
105-316 2.09e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 69.66  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  105 HKNIVGYLDcavNSISDNvwEVLILMEYCRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLK 182
Cdd:PTZ00267 124 HFGIVKHFD---DFKSDD--KLLLIMEYGSGGDLNKQIKQRLKEHlpFQEYEVGLLFYQIVLALDEVHSRK--MMHRDLK 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  183 VENILLNDGGNYVLCDFGsatnkFLNPQKDGVNVvEEEIKKYTTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFF 262
Cdd:PTZ00267 197 SANIFLMPTGIIKLGDFG-----FSKQYSDSVSL-DVASSFCGTPYYLAPE---LWERKRYSKKADMWSLGVILYELLTL 267
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904  263 TLPF-GESQVAICD----GNFTiPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAF 316
Cdd:PTZ00267 268 HRPFkGPSQREIMQqvlyGKYD-PFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEF 325
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
55-255 2.28e-12

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: 68.22  E-value: 2.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR--THGGIrCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLDCAvnsISDN----VW 124
Cdd:cd07861   6 EKIGEGTYGVVYKGRnkKTGQI-VAMKKIRLESeeegVPSTAI--REISLLKELQ-HPNIVCLEDVL---MQENrlylVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLIL-----MEYCRAGQvvnQMNKKLQTGFTEpEVLQ--IFCdtceavarlHQCKtpIIHRDLKVENILLNDGGNYVLC 197
Cdd:cd07861  79 EFLSMdlkkyLDSLPKGK---YMDAELVKSYLY-QILQgiLFC---------HSRR--VLHRDLKPQNLLIDNKGVIKLA 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 198 DFGSAtNKFLNPqkdgVNVVEEEIkkyTTLSYRAPEMinLYGGKPITTKADIWALGCL 255
Cdd:cd07861 144 DFGLA-RAFGIP----VRVYTHEV---VTLWYRAPEV--LLGSPRYSTPVDIWSIGTI 191
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
125-266 2.29e-12

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: 67.65  E-value: 2.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDG---GNYVLCDFGs 201
Cdd:cd14197  83 EMILVLEYAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHN--NNVVHLDLKPQNILLTSEsplGDIKIVDFG- 159
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 202 aTNKFLNPQkdgvnvveEEIKKYT-TLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14197 160 -LSRILKNS--------EELREIMgTPEYVAPEILSY---EPISTATDMWSIGVLAYVMLTGISPF 213
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
53-306 2.50e-12

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: 67.61  E-value: 2.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLNVcKREITIMKELSgHKNIVGYLDcavnSISDNVWEVLILmE 131
Cdd:cd14107   6 VKEEIGRGTFGFVKRVTHKGnGECCAAKFIPLRSSTRARA-FQERDILARLS-HRRLTCLLD----QFETRKTLILIL-E 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILL--NDGGNYVLCDFGSATNkflnp 209
Cdd:cd14107  79 LCSSEELLDRLFLK--GVVTEAEVKLYIQQVLEGIGYLHG--MNILHLDIKPDNILMvsPTREDIKICDFGFAQE----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 qkdgVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVA----ICDG--NFTIPD 282
Cdd:cd14107 150 ----ITPSEHQFSKYGSPEFVAPEIVH---QEPVSAATDIWALGVIAYLSLTCHSPFaGENDRAtllnVAEGvvSWDTPE 222
                       250       260
                ....*....|....*....|....
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14107 223 ITHLSEDAKDFIKRVLQPDPEKRP 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
53-306 2.53e-12

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: 67.76  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSisDNVWevlILME 131
Cdd:cd06645  15 LIQRIGSGTYGDVYKARNvNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCK-HSNIVAYFGSYLRR--DKLW---ICME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqk 211
Cdd:cd06645  89 FCGGGSL--QDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGK--MHRDIKGANILLTDNGHVKLADFGVSAQ------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 212 dgVNVVEEEIKKYTTLSY-RAPEMINLYGGKPITTKADIWALGCLLYKLC-----FFTLPFGESQVAICDGNFTIP---D 282
Cdd:cd06645 158 --ITATIAKRKSFIGTPYwMAPEVAAVERKGGYNQLCDIWAVGITAIELAelqppMFDLHPMRALFLMTKSNFQPPklkD 235
                       250       260
                ....*....|....*....|....
gi 38787904 283 NSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06645 236 KMKWSNSFHHFVKMALTKNPKKRP 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
48-269 2.85e-12

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: 67.34  E-value: 2.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHG------GIRCALKRmyvNNMPDLNVCKREITIMKELSgHKNIVGYLDcaVNSISD 121
Cdd:cd14202   1 KFEFSRKDLIGHGAFAVVFKGRHKEkhdlevAVKCINKK---NLAKSQTLLGKEIKILKELK-HENIVALYD--FQEIAN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 NVWevlILMEYCRAGQVVNQMNKKlqtGFTEPEVLQIFCDTCEAVARLHQCKTpIIHRDLKVENILLNDGG------NYV 195
Cdd:cd14202  75 SVY---LVMEYCNGGDLADYLHTM---RTLSEDTIRLFLQQIAGAMKMLHSKG-IIHRDLKPQNILLSYSGgrksnpNNI 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 196 ---LCDFGSAtnKFLNPQKDGVNVVEEEIkkyttlsYRAPEMI--NLYGGkpittKADIWALGCLLYKLCFFTLPFGES 269
Cdd:cd14202 148 rikIADFGFA--RYLQNNMMAATLCGSPM-------YMAPEVImsQHYDA-----KADLWSIGTIIYQCLTGKAPFQAS 212
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
50-289 3.26e-12

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 67.75  E-value: 3.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMyVNNMPD-LNVCKREITIMKElSGHKNIV---GYLdcavnsISDNVwe 125
Cdd:cd14149  13 EVMLSTRIGSGSFGTVYKGKWHGDVAVKILKV-VDPTPEqFQAFRNEVAVLRK-TRHVNILlfmGYM------TKDNL-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 vLILMEYCRAGQVVNQMNKkLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd14149  83 -AIVTQWCEGSSLYKHLHV-QETKFQMFQLIDIARQTAQGMDYLH--AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 flnPQKDGVNVVEEEIKkytTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGE----SQVAICDG-NFTI 280
Cdd:cd14149 159 ---SRWSGSQQVEQPTG---SILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHinnrDQIIFMVGrGYAS 232

                ....*....
gi 38787904 281 PDNSRYSRN 289
Cdd:cd14149 233 PDLSKLYKN 241
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-306 3.31e-12

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: 67.83  E-value: 3.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDcavnSISDNVWEVLIL 129
Cdd:cd14086   5 LKEELGKGAFSVVRrCVQKSTGQEFAAKIINTKKLSarDHQKLEREARICRLLK-HPNIVRLHD----SISEEGFHYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 mEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILL---NDGGNYVLCDFGSATNkf 206
Cdd:cd14086  80 -DLVTGGELFEDIVAR--EFYSEADASHCIQQILESVNHCHQ--NGIVHRDLKPENLLLaskSKGAAVKLADFGLAIE-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgvnvVEEEIKKY----TTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE-------SQVAICD 275
Cdd:cd14086 153 ----------VQGDQQAWfgfaGTPGYLSPEVLR---KDPYGKPVDIWACGVILYILLVGYPPFWDedqhrlyAQIKAGA 219
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 276 GNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14086 220 YDYPSPEWDTVTPEAKDLINQMLTVNPAKRI 250
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
94-259 3.37e-12

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: 68.08  E-value: 3.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYC--------------RAGQVVNQMNKKLqtgftepeVLQIF 159
Cdd:cd07842  51 REIALLRELK-HENVVSLVEVFLEHADKSVY---LLFDYAehdlwqiikfhrqaKRVSIPPSMVKSL--------LWQIL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 160 CdtceAVARLHQckTPIIHRDLKVENILL----NDGGNYVLCDFGSAtNKFLNPQK-----DGVnVVeeeikkytTLSYR 230
Cdd:cd07842 119 N----GIHYLHS--NWVLHRDLKPANILVmgegPERGVVKIGDLGLA-RLFNAPLKpladlDPV-VV--------TIWYR 182
                       170       180
                ....*....|....*....|....*....
gi 38787904 231 APEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07842 183 APEL--LLGARHYTKAIDIWAIGCIFAEL 209
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
49-266 3.71e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 67.92  E-value: 3.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   49 HQVTLEESLAEGGFSTVFLVRTHG-----GIRCaLKRMYVNNMPDLNVCKREITIMKELSgHKNIV----GYLDcavnsi 119
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKHKGtgeyyAIKC-LKKREILKMKQVQHVAQEKSILMELS-HPFIVnmmcSFQD------ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  120 sDNvwEVLILMEYCRAGQVVNQMNKklqTGFTEPEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCD 198
Cdd:PTZ00263  90 -EN--RVYFLLEFVVGGELFTHLRK---AGRFPNDVAKFYHaELVLAFEYLHSKD--IIYRDLKPENLLLDNKGHVKVTD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904  199 FGSATnkflnpqkdgvNVVEEEIKKYTTLSYRAPEMINLYG-GKPIttkaDIWALGCLLYKLCFFTLPF 266
Cdd:PTZ00263 162 FGFAK-----------KVPDRTFTLCGTPEYLAPEVIQSKGhGKAV----DWWTMGVLLYEFIAGYPPF 215
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
49-266 3.80e-12

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: 66.86  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcAVNSISDnvweVL 127
Cdd:cd14193   4 YNVNKEEILGGGRFGQVHkCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLN-HANLIQLYD-AFESRND----IV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQM---NKKLqtgfTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENIL-LNDGGNYV-LCDFGSA 202
Cdd:cd14193  78 LVMEYVDGGELFDRIideNYNL----TELDTILFIKQICEGIQYMHQMY--ILHLDLKPENILcVSREANQVkIIDFGLA 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 203 tNKFLNPQKDGVNvveeeikkYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14193 152 -RRYKPREKLRVN--------FGTPEFLAPEVVNY---EFVSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
95-347 3.98e-12

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: 67.35  E-value: 3.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHqCKT 174
Cdd:cd14177  47 EIEILMRYGQHPNIITLKD-----VYDDGRYVYLVTELMKGGELLDRILR--QKFFSEREASAVLYTITKTVDYLH-CQG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 pIIHRDLKVENIL-LNDGGN---YVLCDFGSATnkflnpQKDGVNVVEeeIKKYTTLSYRAPEMINLYGgkpITTKADIW 250
Cdd:cd14177 119 -VVHRDLKPSNILyMDDSANadsIRICDFGFAK------QLRGENGLL--LTPCYTANFVAPEVLMRQG---YDAACDIW 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 251 ALGCLLYKLCFFTLPFG--------ESQVAICDGNFTIPDNS--RYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd14177 187 SLGVLLYTMLAGYTPFAngpndtpeEILLRIGSGKFSLSGGNwdTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACR 266
                       250       260
                ....*....|....*....|....*..
gi 38787904 321 KDCPVSNINNSSIPSALPEPMTASEAA 347
Cdd:cd14177 267 DQLPHYQLNRQDAPHLVKGAMAATYSA 293
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
57-266 4.28e-12

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: 68.13  E-value: 4.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH--GGIrCALKRMYVNNMPDLNvckrEIT-IMKElsghKNIVgyldcavnSISDNVWEVLIL---- 129
Cdd:cd05600  19 VGQGGYGSVFLARKKdtGEI-CALKIMKKKVLFKLN----EVNhVLTE----RDIL--------TTTNSPWLVKLLyafq 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 --------MEYCRAGQVVNQMNkklQTG-FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd05600  82 dpenvylaMEYVPGGDFRTLLN---NSGiLSEEHARFYIAEMFAAISSLHQLG--YIHRDLKPENFLIDSSGHIKLTDFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SATNKfLNPQKDGVNVVE-EEIKKYTTL-----------------------------SYRAPEMINlygGKPITTKADIW 250
Cdd:cd05600 157 LASGT-LSPKKIESMKIRlEEVKNTAFLeltakerrniyramrkedqnyansvvgspDYMAPEVLR---GEGYDLTVDYW 232
                       250
                ....*....|....*..
gi 38787904 251 ALGCLLYK-LCFFTlPF 266
Cdd:cd05600 233 SLGCILFEcLVGFP-PF 248
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
55-311 4.73e-12

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: 67.21  E-value: 4.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIrC--ALKRMYV-NNMPDLNVCKREITIMKELSgHKNIVGYLDcAVNSISDNVWE------ 125
Cdd:cd14048  12 QCLGRGGFGVVFEAKNKVDD-CnyAVKRIRLpNNELAREKVLREVRALAKLD-HPGIVRYFN-AWLERPPEGWQekmdev 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 -VLILMEYCRAGQVVNQMNKKLQTGFTEPEV-LQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd14048  89 yLYIQMQLCRKENLKDWMNRRCTMESRELFVcLNIFKQIASAVEYLHS--KGLIHRDLKPSNVFFSLDDVVKVGDFGLVT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 NKFLNPQKDGVNVVEEEIKKYT----TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFftlPFG---ESQVAICD- 275
Cdd:cd14048 167 AMDQGEPEQTVLTPMPAYAKHTgqvgTRLYMSPEQIH---GNQYSEKVDIFALGLILFELIY---SFStqmERIRTLTDv 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 38787904 276 --GNFTIPDNSRYSRNiHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14048 241 rkLKFPALFTNKYPEE-RDMVQQMLSPSPSERPEAHEV 277
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
94-256 4.79e-12

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: 67.58  E-value: 4.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGHKNIVGYLDC--AVNSIsdNVWEVLILME-----YCRAGqVVNQMNKKLqtgftepevlqIFCDTCEAV 166
Cdd:cd07852  55 REIMFLQELNDHPNIIKLLNVirAENDK--DIYLVFEYMEtdlhaVIRAN-ILEDIHKQY-----------IMYQLLKAL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 167 ARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEIkkyTTLSYRAPEMinLYGGKPITTK 246
Cdd:cd07852 121 KYLHSGG--VIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENPVLTDYV---ATRWYRAPEI--LLGSTRYTKG 193
                       170
                ....*....|
gi 38787904 247 ADIWALGCLL 256
Cdd:cd07852 194 VDMWSVGCIL 203
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
57-259 4.96e-12

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 66.98  E-value: 4.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR--THGGIRCALKRMYVNN----MPDLNVckREITIMKELSG--HKNIVGYLDCAVNSISDNVWEVLI 128
Cdd:cd07862   9 IGEGAYGKVFKARdlKNGGRFVALKRVRVQTgeegMPLSTI--REVAVLRHLETfeHPNVVRLFDVCTVSRTDRETKLTL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAgQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLN 208
Cdd:cd07862  87 VFEHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHR--VVHRDLKPQNILVTSSGQIKLADFGLA--RIYS 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 209 PQKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKL 259
Cdd:cd07862 162 FQMALTSVV-------VTLWYRAPEVLL---QSSYATPVDLWSVGCIFAEM 202
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
56-305 4.97e-12

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: 67.04  E-value: 4.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  56 SLAEGGFSTVFLVRTHGGIRC-ALKRMyvnnmpdlnvCKREITIMKELS---GHKNIVG-----YLDCAVNSISDNVWEV 126
Cdd:cd14209   8 TLGTGSFGRVMLVRHKETGNYyAMKIL----------DKQKVVKLKQVEhtlNEKRILQainfpFLVKLEYSFKDNSNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LIlMEYCRAGQVVNQMNKKLQtgFTEPE----VLQIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd14209  78 MV-MEYVPGGEMFSHLRRIGR--FSEPHarfyAAQIVL----AFEYLHSLD--LIYRDLKPENLLIDQQGYIKVTDFGFA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 tnkflnpqkdgvnvveEEIKKYT-----TLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPFGESQV-----A 272
Cdd:cd14209 149 ----------------KRVKGRTwtlcgTPEYLAPEIILS---KGYNKAVDWWALGVLIYEMAAGYPPFFADQPiqiyeK 209
                       250       260       270
                ....*....|....*....|....*....|...
gi 38787904 273 ICDGNFTIPdnSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14209 210 IVSGKVRFP--SHFSSDLKDLLRNLLQVDLTKR 240
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
83-266 5.01e-12

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: 67.52  E-value: 5.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  83 VNNMPDLNVCKREITIMKELSgHKNIVGYLdcAVNSISDNVWEVLIlMEYCRAGQVVNQMNKKLQT-GFTEPEVLQIFCD 161
Cdd:cd13988  29 LSFMRPLDVQMREFEVLKKLN-HKNIVKLF--AIEEELTTRHKVLV-MELCPCGSLYTVLEEPSNAyGLPESEFLIVLRD 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 162 TCEAVARLHQCKtpIIHRDLKVENIL--LNDGGN--YVLCDFGSATNKFLNpqkdgvnvvEEEIKKYTTLSYRAPEM--- 234
Cdd:cd13988 105 VVAGMNHLRENG--IVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARELEDD---------EQFVSLYGTEEYLHPDMyer 173
                       170       180       190
                ....*....|....*....|....*....|....
gi 38787904 235 --INLYGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd13988 174 avLRKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
128-305 5.15e-12

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: 67.64  E-value: 5.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGsATNKFL 207
Cdd:cd05614  82 LILDYVSGGELFTHLYQR--DHFSEDEVRFYSGEIILALEHLH--KLGIVYRDIKLENILLDSEGHVVLTDFG-LSKEFL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NpqkdgvnvvEEEIKKYT---TLSYRAPEMINLYGGKpiTTKADIWALGCLLYKLCFFTLPF---GE--SQVAI------ 273
Cdd:cd05614 157 T---------EEKERTYSfcgTIEYMAPEIIRGKSGH--GKAVDWWSLGILMFELLTGASPFtleGEknTQSEVsrrilk 225
                       170       180       190
                ....*....|....*....|....*....|..
gi 38787904 274 CDGNFTipdnSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05614 226 CDPPFP----SFIGPVARDLLQKLLCKDPKKR 253
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
92-316 5.27e-12

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: 66.61  E-value: 5.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  92 CKREI-TIMKELSG-----HKNIVGYLDCAVN-SISDNVWEVLILMEYCragqvvnqmnkklqTGFTEPEVLQIFCDTC- 163
Cdd:cd14012  38 GKKQIqLLEKELESlkklrHPNLVSYLAFSIErRGRSDGWKVYLLTEYA--------------PGGSLSELLDSVGSVPl 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 -----------EAVARLHqcKTPIIHRDLKVENILL-NDGGNYV--LCDFgSATNKFLNPQKDGVNVVEEEIKkyttlsY 229
Cdd:cd14012 104 dtarrwtlqllEALEYLH--RNGVVHKSLHAGNVLLdRDAGTGIvkLTDY-SLGKTLLDMCSRGSLDEFKQTY------W 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 230 RAPEMINlyGGKPITTKADIWALGcllykLCFFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIF 309
Cdd:cd14012 175 LPPELAQ--GSKSPTRKTDVWDLG-----LLFLQMLFGLDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTAL 247

                ....*..
gi 38787904 310 QVSYFAF 316
Cdd:cd14012 248 ELLPHEF 254
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
94-259 5.41e-12

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: 67.25  E-value: 5.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGH-----KNIVGYLD--------CAV-NSISDNVWEVLilMEYCRagqvvNQmnkklqtGFTEPEV---- 155
Cdd:cd14135  46 KELEILKKLNDAdpddkKHCIRLLRhfehknhlCLVfESLSMNLREVL--KKYGK-----NV-------GLNIKAVrsya 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 156 LQIFcdtceaVARLHQCKTPIIHRDLKVENILLNDGGNYV-LCDFGSAtnkflnpqkdgVNVVEEEIKKYtTLS--YRAP 232
Cdd:cd14135 112 QQLF------LALKHLKKCNILHADIKPDNILVNEKKNTLkLCDFGSA-----------SDIGENEITPY-LVSrfYRAP 173
                       170       180
                ....*....|....*....|....*..
gi 38787904 233 EMINlygGKPITTKADIWALGCLLYKL 259
Cdd:cd14135 174 EIIL---GLPYDYPIDMWSVGCTLYEL 197
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
57-256 5.43e-12

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 66.36  E-value: 5.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCkREITIMKELSgHKNIVGYLDCAVNsisDNvwEVLILMEYCRAG 136
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFL-KEVKLMRRLS-HPNILRFIGVCVK---DN--KLNFITEYVNGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 qVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL---NDGGNYVLCDFGSATNKFLNPQKDG 213
Cdd:cd14065  74 -TLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKN--IIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKP 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 214 vnvveEEIKKYTTLS---YRAPEMINlygGKPITTKADIWALGCLL 256
Cdd:cd14065 151 -----DRKKRLTVVGspyWMAPEMLR---GESYDEKVDVFSFGIVL 188
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
94-259 5.50e-12

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: 66.95  E-value: 5.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDN-VWEVLI--LMEYCR-AGQVVNQMNKKLQtgftepeVLQIFcdtcEAVARL 169
Cdd:cd07873  49 REVSLLKDLK-HANIVTLHDIIHTEKSLTlVFEYLDkdLKQYLDdCGNSINMHNVKLF-------LFQLL----RGLAYC 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 170 HQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLnPQKDGVNVVeeeikkyTTLSYRAPEMinLYGGKPITTKADI 249
Cdd:cd07873 117 HRRK--VLHRDLKPQNLLINERGELKLADFGLARAKSI-PTKTYSNEV-------VTLWYRPPDI--LLGSTDYSTQIDM 184
                       170
                ....*....|
gi 38787904 250 WALGCLLYKL 259
Cdd:cd07873 185 WGVGCIFYEM 194
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
95-311 6.01e-12

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: 66.96  E-value: 6.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckT 174
Cdd:cd14178  46 EIEILLRYGQHPNIITLKD-----VYDDGKFVYLVMELMRGGELLDRILR--QKCFSEREASAVLCTITKTVEYLHS--Q 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PIIHRDLKVENIL-LNDGGN---YVLCDFGSAtnKFLNPQKDGVnvveeeIKKYTTLSYRAPEMINLYGgkpITTKADIW 250
Cdd:cd14178 117 GVVHRDLKPSNILyMDESGNpesIRICDFGFA--KQLRAENGLL------MTPCYTANFVAPEVLKRQG---YDAACDIW 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 251 ALGCLLYKLCFFTLPF---------------GESQVAICDGNF-TIPDNSRYsrnihcLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14178 186 SLGILLYTMLAGFTPFangpddtpeeilariGSGKYALSGGNWdSISDAAKD------IVSKMLHVDPHQRLTAPQV 256
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
54-266 6.25e-12

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: 66.48  E-value: 6.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcAVNSISdnvwEVLILMEY 132
Cdd:cd14190   9 KEVLGGGKFGKVHtCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLN-HRNLIQLYE-AIETPN----EIVLFMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL-NDGGNYV-LCDFGSAtnKFLNPq 210
Cdd:cd14190  83 VEGGELFERIVDE-DYHLTEVDAMVFVRQICEGIQFMHQMR--VLHLDLKPENILCvNRTGHQVkIIDFGLA--RRYNP- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 211 kdgvnvvEEEIK-KYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14190 157 -------REKLKvNFGTPEFLSPEVVNY---DQVSFPTDMWSMGVITYMLLSGLSPF 203
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
121-306 6.38e-12

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 68.36  E-value: 6.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  121 DNVWEVLILMEYCRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCD 198
Cdd:PTZ00283 109 ENVLMIALVLDYANAGDLRQEIKSRAKTNrtFREHEAGLLFIQVLLAVHHVHS--KHMIHRDIKSANILLCSNGLVKLGD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  199 FGSAtnkflnpqKDGVNVVEEEIKKY--TTLSYRAPEminLYGGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICD 275
Cdd:PTZ00283 187 FGFS--------KMYAATVSDDVGRTfcGTPYYVAPE---IWRRKPYSKKADMFSLGVLLYELLTLKRPFdGENMEEVMH 255
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 38787904  276 ----GNFT-IPDNSrySRNIHCLIRFMLEPDPEHRP 306
Cdd:PTZ00283 256 ktlaGRYDpLPPSI--SPEMQEIVTALLSSDPKRRP 289
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
47-256 7.67e-12

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: 66.38  E-value: 7.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  47 GRHQVTLEESLAEGGFSTVFLVR-THGGIRCALK--RMYVNNMPDLNVCKrEITIMK--ELSGhknivgyldcavnSISD 121
Cdd:cd13991   4 EVHWATHQLRIGRGSFGEVHRMEdKQTGFQCAVKkvRLEVFRAEELMACA-GLTSPRvvPLYG-------------AVRE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 NVWeVLILMEYcRAGQVVNQMnKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFG 200
Cdd:cd13991  70 GPW-VNIFMDL-KEGGSLGQL-IKEQGCLPEDRALHYLGQALEGLEYLHSRK--ILHGDVKADNVLLSsDGSDAFLCDFG 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 201 SATNkfLNPQKDGVNVVEEEIKKYTTlSYRAPEMINlygGKPITTKADIWALGCLL 256
Cdd:cd13991 145 HAEC--LDPDGLGKSLFTGDYIPGTE-THMAPEVVL---GKPCDAKVDVWSSCCMM 194
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
88-311 9.36e-12

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: 65.78  E-value: 9.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  88 DLNVcKREITIMKELSgHKNIVGYLDCAVNSIsdnvwEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVA 167
Cdd:cd14665  40 DENV-QREIINHRSLR-HPNIVRFKEVILTPT-----HLAIVMEYAAGGELFERICNAGR--FSEDEARFFFQQLISGVS 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 168 RLHQCKtpIIHRDLKVENILLnDGG---NYVLCDFGSATNKFLNPQ-KDGVNvveeeikkytTLSYRAPEMI--NLYGGK 241
Cdd:cd14665 111 YCHSMQ--ICHRDLKLENTLL-DGSpapRLKICDFGYSKSSVLHSQpKSTVG----------TPAYIAPEVLlkKEYDGK 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 242 pittKADIWALGCLLYKLCFFTLPFGESQVA---------ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14665 178 ----IADVWSCGVTLYVMLVGAYPFEDPEEPrnfrktiqrILSVQYSIPDYVHISPECRHLISRIFVADPATRITIPEI 252
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
91-266 9.86e-12

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 65.63  E-value: 9.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  91 VCKREITIMKELSgHKNIVGYLDcaVNSISDNVWevlILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLH 170
Cdd:cd14087  43 VCESELNVLRRVR-HTNIIQLIE--VFETKERVY---MVMELATGGELFDRIIAK--GSFTERDATRVLQMVLDGVKYLH 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QCKtpIIHRDLKVENILLNDGGN---YVLCDFGSATNkflnpQKDGvnvvEEEIKKYT--TLSYRAPEMInlyGGKPITT 245
Cdd:cd14087 115 GLG--ITHRDLKPENLLYYHPGPdskIMITDFGLAST-----RKKG----PNCLMKTTcgTPEYIAPEIL---LRKPYTQ 180
                       170       180
                ....*....|....*....|.
gi 38787904 246 KADIWALGCLLYKLCFFTLPF 266
Cdd:cd14087 181 SVDMWAVGVIAYILLSGTMPF 201
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
53-316 1.00e-11

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 66.18  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVcKREITIMKELSGHKNIVGYLDCAVNSI----SDNVWevl 127
Cdd:cd06636  20 LVEVVGNGTYGQVYKGRhVKTGQLAAIKVMDVTEDEEEEI-KLEINMLKKYSHHRNIATYYGAFIKKSppghDDQLW--- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkfL 207
Cdd:cd06636  96 LVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFG------V 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKDgvNVVEEEIKKYTTLSYRAPEMINLyGGKPITT---KADIWALGcllyklcFFTLPFGESQVAICDGN-----FT 279
Cdd:cd06636 168 SAQLD--RTVGRRNTFIGTPYWMAPEVIAC-DENPDATydyRSDIWSLG-------ITAIEMAEGAPPLCDMHpmralFL 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 38787904 280 IPDN-------SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAF 316
Cdd:cd06636 238 IPRNpppklksKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPF 281
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
147-305 1.07e-11

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: 66.01  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 147 QTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKdgvnvveeEIKKYT- 225
Cdd:cd05577  89 TRGFSEARAIFYAAEIICGLEHLHNRF--IVYRDLKPENILLDDHGHVRISDLGLAVE--FKGGK--------KIKGRVg 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 226 TLSYRAPEMinLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNF---------TIPDnsRYSRNIHCLIRF 296
Cdd:cd05577 157 THGYMAPEV--LQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELkrrtlemavEYPD--SFSPEARSLCEG 232

                ....*....
gi 38787904 297 MLEPDPEHR 305
Cdd:cd05577 233 LLQKDPERR 241
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
59-256 1.11e-11

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 66.24  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  59 EGGFSTVFLVRT-HGGIRCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLD-CAVNSISDNVWE--VLILM 130
Cdd:cd07865  22 QGTFGEVFKARHrKTGQIVALKKVLMENekegFPITAL--REIKILQLLK-HENVVNLIEiCRTKATPYNRYKgsIYLVF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCR---AGqVVNQMNKKlqtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFL 207
Cdd:cd07865  99 EFCEhdlAG-LLSNKNVK----FTLSEIKKVMKMLLNGLYYIHRNK--ILHRDMKAANILITKDGVLKLADFGLA-RAFS 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 208 NPQKDGVNvveeeikKYT----TLSYRAPEMinLYG----GKPIttkaDIWALGCLL 256
Cdd:cd07865 171 LAKNSQPN-------RYTnrvvTLWYRPPEL--LLGerdyGPPI----DMWGAGCIM 214
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
60-259 1.34e-11

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: 66.69  E-value: 1.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRT-HGGIRCALKRMyVNNMPDLNVCKREITIMKELS--GHKNIVGYLDCAVNSISDNVWEVLILMEYcrag 136
Cdd:cd07853  11 GAFGVVWSVTDpRDGKRVALKKM-PNVFQNLVSCKRVFRELKMLCffKHDNVLSALDILQPPHIDPFEEIYVVTEL---- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 qvvnqMNKKLQTGFTEPEVL----------QIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkf 206
Cdd:cd07853  86 -----MQSDLHKIIVSPQPLssdhvkvflyQIL----RGLKYLHSAG--ILHRDIKPGNLLVNSNCVLKICDFGLAR--- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 38787904 207 LNPQKDGVNVVEEEIKKYttlsYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07853 152 VEEPDESKHMTQEVVTQY----YRAPEI--LMGSRHYTSAVDIWSVGCIFAEL 198
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
57-266 1.42e-11

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 65.75  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGGIRCALKRMyvnnMPDLNVCKR-----EITIMKELSgHKNIVGYLDC--AVNSISDNVWEvLI 128
Cdd:cd14038   2 LGTGGFGNVLRwINQETGEQVAIKQC----RQELSPKNRerwclEIQIMKRLN-HPNVVAARDVpeGLQKLAPNDLP-LL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNK-KLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGN---YVLCDFGSAtn 204
Cdd:cd14038  76 AMEYCQGGDLRKYLNQfENCCGLREGAILTLLSDISSALRYLHENR--IIHRDLKPENIVLQQGEQrliHKIIDLGYA-- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 205 KFLNPQKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14038 152 KELDQGSLCTSFV-------GTLQYLAPELLE---QQKYTVTVDYWSFGTLAFECITGFRPF 203
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
149-260 1.64e-11

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: 66.05  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 149 GFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDgGNYV--------------------LCDFGSATnkfLN 208
Cdd:cd14134 111 PFPLEHVQHIAKQLLEAVAFLHDLK--LTHTDLKPENILLVD-SDYVkvynpkkkrqirvpkstdikLIDFGSAT---FD 184
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 38787904 209 PQKDGvNVVeeeikkyTTLSYRAPEMINLYG-GKPittkADIWALGCLLYKLC 260
Cdd:cd14134 185 DEYHS-SIV-------STRHYRAPEVILGLGwSYP----CDVWSIGCILVELY 225
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
93-308 1.67e-11

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: 65.04  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14194  56 EREVSILKEIQ-HPNVI-----TLHEVYENKTDVILILELVAGGELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILLNDGG----NYVLCDFGSA-----TNKFLNpqkdgvnvveeeikKYTTLSYRAPEMINLyggKPI 243
Cdd:cd14194 128 Q--IAHFDLKPENIMLLDRNvpkpRIKIIDFGLAhkidfGNEFKN--------------IFGTPEFVAPEIVNY---EPL 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 244 TTKADIWALGCLLYKLCFFTLPF-GESQ------VAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd14194 189 GLEADMWSIGVITYILLSGASPFlGDTKqetlanVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTI 260
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
125-308 1.77e-11

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: 65.75  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd05604  71 KLYFVLDFVNGGELFFHLQR--ERSFPEPRARFYAAEIASALGYLHSIN--IVYRDLKPENILLDSQGHIVLTDFGLC-- 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpqKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFgesqvaicdgnftipdns 284
Cdd:cd05604 145 ------KEGISNSDTTTTFCGTPEYLAPEVIR---KQPYDNTVDWWCLGSVLYEMLYGLPPF------------------ 197
                       170       180
                ....*....|....*....|....
gi 38787904 285 rYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd05604 198 -YCRDTAEMYENILHKPLVLRPGI 220
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
93-270 1.90e-11

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 64.98  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14196  56 EREVSILRQVL-HPNIITLHD-----VYENRTDVVLILELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILLNDGG----NYVLCDFGSAtnkflNPQKDGVnvveeEIKK-YTTLSYRAPEMINLyggKPITTKA 247
Cdd:cd14196 128 K--IAHFDLKPENIMLLDKNipipHIKLIDFGLA-----HEIEDGV-----EFKNiFGTPEFVAPEIVNY---EPLGLEA 192
                       170       180
                ....*....|....*....|....
gi 38787904 248 DIWALGCLLYKLCFFTLPF-GESQ 270
Cdd:cd14196 193 DMWSIGVITYILLSGASPFlGDTK 216
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-310 2.06e-11

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: 65.23  E-value: 2.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVFLVRTHGGIR-CALKRMyvNNMPDLNVCKREITIMKELSgHKNIVgyldcAVNSISDNVWEVL 127
Cdd:cd14085   3 DFFEIESELGRGATSVVYRCRQKGTQKpYAVKKL--KKTVDKKIVRTEIGVLLRLS-HPNII-----KLKEIFETPTEIS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYV---LCDFGSAtn 204
Cdd:cd14085  75 LVLELVTGGELFDRIVEK--GYYSERDAADAVKQILEAVAYLH--ENGIVHRDLKPENLLYATPAPDAplkIADFGLS-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpqkdgvNVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLY-KLCFFTlPF----GESQ----VA 272
Cdd:cd14085 149 ----------KIVDQQVTMKTvcgTPGYCAPEILR---GCAYGPEVDMWSVGVITYiLLCGFE-PFyderGDQYmfkrIL 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 38787904 273 ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd14085 215 NCDYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQ 252
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
57-268 2.08e-11

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: 64.68  E-value: 2.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLV-RTHGGIRCALKRMYVN-----NMPDLNVCKREITIMKELSgHKNIVGYLDCavnsISDNVWEVL-IL 129
Cdd:cd06652  10 LGQGAFGRVYLCyDADTGRELAVKQVQFDpespeTSKEVNALECEIQLLKNLL-HERIVQYYGC----LRDPQERTLsIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsATNKFLNP 209
Cdd:cd06652  85 MEYMPGGSIKDQL--KSYGALTENVTRKYTRQILEGVHYLHS--NMIVHRDIKGANILRDSVGNVKLGDFG-ASKRLQTI 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 QKDGVNvveeeIKKYTTLSY-RAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE 268
Cdd:cd06652 160 CLSGTG-----MKSVTGTPYwMSPEVIS---GEGYGRKADIWSVGCTVVEMLTEKPPWAE 211
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
126-308 2.10e-11

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: 64.84  E-value: 2.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLIlMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNk 205
Cdd:cd14111  75 VLI-AEFCSGKELLHSLIDRFR--YSEDDVVGYLVQILQGLEYLHGRR--VLHLDIKPDNIMVTNLNAIKIVDFGSAQS- 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 fLNPQkdgvnVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-----GESQVAICDGNFti 280
Cdd:cd14111 149 -FNPL-----SLRQLGRRTGTLEYMAPEMVK---GEPVGPPADIWSIGVLTYIMLSGRSPFedqdpQETEAKILVAKF-- 217
                       170       180       190
                ....*....|....*....|....*....|..
gi 38787904 281 pDNSRY----SRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd14111 218 -DAFKLypnvSQSASLFLKKVLSSYPWSRPTT 248
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
47-273 2.46e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 66.74  E-value: 2.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   47 GRHQvtLEESLAEGGFSTVFLVR-THGGIRCALKRMYvnnmPDLnvC---------KREITIMKELSgHKNIVgyldcav 116
Cdd:NF033483   7 GRYE--IGERIGRGGMAEVYLAKdTRLDRDVAVKVLR----PDL--ArdpefvarfRREAQSAASLS-HPNIV------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  117 nSISDnVWE----VLILMEYcragqvVNQMNKK--LQTG--FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL 188
Cdd:NF033483  71 -SVYD-VGEdggiPYIVMEY------VDGRTLKdyIREHgpLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  189 NDGGNYVLCDFGSA----------TNKFLnpqkdGvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYK 258
Cdd:NF033483 141 TKDGRVKVTDFGIAralssttmtqTNSVL-----G------------TVHYLSPEQAR---GGTVDARSDIYSLGIVLYE 200
                        250
                 ....*....|....*.
gi 38787904  259 LCFFTLPF-GESQVAI 273
Cdd:NF033483 201 MLTGRPPFdGDSPVSV 216
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
93-305 2.58e-11

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: 64.82  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14105  56 EREVSILRQVL-HPNII-----TLHDVFENKTDVVLILELVAGGELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHTK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILLNDGG----NYVLCDFGSAtnkflNPQKDGVnvveeEIKK-YTTLSYRAPEMINLyggKPITTKA 247
Cdd:cd14105 128 N--IAHFDLKPENIMLLDKNvpipRIKLIDFGLA-----HKIEDGN-----EFKNiFGTPEFVAPEIVNY---EPLGLEA 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 248 DIWALGCLLYKLCFFTLPF-----GESQVAICDGNFTIPDnsRYSRNIHCL----IRFMLEPDPEHR 305
Cdd:cd14105 193 DMWSIGVITYILLSGASPFlgdtkQETLANITAVNYDFDD--EYFSNTSELakdfIRQLLVKDPRKR 257
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
128-311 3.09e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 63.67  E-value: 3.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTgftEPEVLqifCDTCEAVAR----LHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaT 203
Cdd:cd14059  58 ILMEYCPYGQLYEVLRAGREI---TPSLL---VDWSKQIASgmnyLHLHK--IIHRDLKSPNVLVTYNDVLKISDFG--T 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 NKFLNpqkdgvnvveEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE-SQVAICDG--- 276
Cdd:cd14059 128 SKELS----------EKSTKMSfagTVAWMAPEVIR---NEPCSEKVDIWSFGVVLWELLTGEIPYKDvDSSAIIWGvgs 194
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 38787904 277 -NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14059 195 nSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQI 230
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
55-308 3.38e-11

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: 64.65  E-value: 3.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH-GGIRCALKrmYVNNMPDLNV-CKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEY 132
Cdd:cd06638  24 ETIGKGTYGKVFKVLNKkNGSKAAVK--ILDPIHDIDEeIEAEYNILKALSDHPNVVKFYGMYYKKDVKNGDQLWLVLEL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATnkflnpq 210
Cdd:cd06638 102 CNGGSVTDLVKGFLKRGerMEEPIIAYILHEALMGLQHLHVNKT--IHRDVKGNNILLTTEGGVKLVDFGVSA------- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 kdgvNVVEEEIKKYTTLS---YRAPEMINLYGGKPIT--TKADIWALGCLLYKLcfftlpfGESQVAICDGN-----FTI 280
Cdd:cd06638 173 ----QLTSTRLRRNTSVGtpfWMAPEVIACEQQLDSTydARCDVWSLGITAIEL-------GDGDPPLADLHpmralFKI 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 281 PDN--------SRYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd06638 242 PRNppptlhqpELWSNEFNDFIRKCLTKDYEKRPTV 277
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
93-310 3.44e-11

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: 64.25  E-value: 3.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14195  56 EREVNILREIQ-HPNII-----TLHDIFENKTDVVLILELVSGGELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILLNDGG----NYVLCDFG-----SATNKFLNpqkdgvnvveeeikKYTTLSYRAPEMINLyggKPI 243
Cdd:cd14195 128 R--IAHFDLKPENIMLLDKNvpnpRIKLIDFGiahkiEAGNEFKN--------------IFGTPEFVAPEIVNY---EPL 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 244 TTKADIWALGCLLYKLCFFTLPF-GESQ------VAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQ 310
Cdd:cd14195 189 GLEADMWSIGVITYILLSGASPFlGETKqetltnISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQ 262
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
60-307 3.74e-11

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: 63.85  E-value: 3.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVF--LVRthgGIRCALKRMYVNNMPDLNVCKREITIMKELSG---HKNIVgyldcAVNSISDNVWEVLILMEYCR 134
Cdd:cd14148   5 GGFGKVYkgLWR---GEEVAVKAARQDPDEDIAVTAENVRQEARLFWmlqHPNII-----ALRGVCLNPPHLCLVMEYAR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQvvnqMNKKLQTGFTEPEVLqifCDTCEAVAR----LH-QCKTPIIHRDLKVENILL------NDGGNYVL--CDFGS 201
Cdd:cd14148  77 GGA----LNRALAGKKVPPHVL---VNWAVQIARgmnyLHnEAIVPIIHRDLKSSNILIlepienDDLSGKTLkiTDFGL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 AtnkflnpqkdgvnvveEEIKKYTTLS------YRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPFGE-SQVAIC 274
Cdd:cd14148 150 A----------------REWHKTTKMSaagtyaWMAPEVIRL---SLFSKSSDVWSFGVLLWELLTGEVPYREiDALAVA 210
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 275 DG----NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd14148 211 YGvamnKLTLPIPSTCPEPFARLLEECWDPDPHGRPD 247
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
94-271 4.08e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 65.44  E-value: 4.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   94 REITIMKELSgHKNIV-----GYLDCaVNSISDNVWeVLILMEYCRagQVVNQ-MNKKLQTGFTEPEVL-QIFC-DTCEA 165
Cdd:PTZ00036 108 RELLIMKNLN-HINIIflkdyYYTEC-FKKNEKNIF-LNVVMEFIP--QTVHKyMKHYARNNHALPLFLvKLYSyQLCRA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  166 VARLHQckTPIIHRDLKVENILLNDGGNYV-LCDFGSATNkFLNPQKdgvnvveeEIKKYTTLSYRAPEMinLYGGKPIT 244
Cdd:PTZ00036 183 LAYIHS--KFICHRDLKPQNLLIDPNTHTLkLCDFGSAKN-LLAGQR--------SVSYICSRFYRAPEL--MLGATNYT 249
                        170       180
                 ....*....|....*....|....*...
gi 38787904  245 TKADIWALGCLLYKLCF-FTLPFGESQV 271
Cdd:PTZ00036 250 THIDLWSLGCIIAEMILgYPIFSGQSSV 277
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
71-318 4.18e-11

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 63.95  E-value: 4.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  71 HGGIRCALKRMYVNNMPDLNVcKREITIMKELSgHKNIVGYLdcavnSISDNVWEVLILMEYCRAG---QVVNQMNKKLQ 147
Cdd:cd13992  23 YGGRTVAIKHITFSRTEKRTI-LQELNQLKELV-HDNLNKFI-----GICINPPNIAVVTEYCTRGslqDVLLNREIKMD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 148 TGFTepevLQIFCDTCEAVARLHqcKTPII-HRDLKVENILLNDggNYV--LCDFGSAtnkflNPQKDGVNVVEEEIKKY 224
Cdd:cd13992  96 WMFK----SSFIKDIVKGMNYLH--SSSIGyHGRLKSSNCLVDS--RWVvkLTDFGLR-----NLLEEQTNHQLDEDAQH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 225 TTLSYRAPEMINLYGGKP-ITTKADIWALGCLLYKLCFFTLPFG------ESQVAICDGNFTI-PD----NSRYSRNIHC 292
Cdd:cd13992 163 KKLLWTAPELLRGSLLEVrGTQKGDVYSFAIILYEILFRSDPFAlerevaIVEKVISGGNKPFrPElavlLDEFPPRLVL 242
                       250       260
                ....*....|....*....|....*.
gi 38787904 293 LIRFMLEPDPEHRPDIFQVSYFAFKF 318
Cdd:cd13992 243 LVKQCWAENPEKRPSFKQIKKTLTEN 268
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
94-312 4.32e-11

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: 64.31  E-value: 4.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDcavnSISDNVWEVLILMEYCRAGQVvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14040  59 REYRIHKELD-HPRIVKLYD----YFSLDTDTFCTVLEYCEGNDL--DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDG---GNYVLCDFGsaTNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMInLYGGKP--ITTKAD 248
Cdd:cd14040 132 PPIIHYDLKPGNILLVDGtacGEIKITDFG--LSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECF-VVGKEPpkISNKVD 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 249 IWALGCLLYKLCFFTLPFG--ESQVAICDGNFTI-------PDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd14040 209 VWSVGVIFFQCLYGRKPFGhnQSQQDILQENTILkatevqfPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLA 281
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
57-259 4.79e-11

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: 64.24  E-value: 4.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYCRA 135
Cdd:cd06659  29 IGEGSTGVVCIAReKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQ-HPNVVEMYKSYL--VGEELW---VLMEYLQG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvn 215
Cdd:cd06659 103 GALTDIVS---QTRLNEEQIATVCEAVLQALAYLHS--QGVIHRDIKSDSILLTLDGRVKLSDFGFCAQ----------- 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 38787904 216 vVEEEIKKYTTLS----YRAPEMINlygGKPITTKADIWALGCLLYKL 259
Cdd:cd06659 167 -ISKDVPKRKSLVgtpyWMAPEVIS---RCPYGTEVDIWSLGIMVIEM 210
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
130-305 5.00e-11

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 64.54  E-value: 5.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG--------- 200
Cdd:cd05570  75 MEYVNGGDLMFHIQRARR--FTEERARFYAAEICLALQFLHERG--IIYRDLKLDNVLLDAEGHIKIADFGmckegiwgg 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SATNKFLNpqkdgvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---GESQV--AICD 275
Cdd:cd05570 151 NTTSTFCG-----------------TPDYIAPEILR---EQDYGFSVDWWALGVLLYEMLAGQSPFegdDEDELfeAILN 210
                       170       180       190
                ....*....|....*....|....*....|.
gi 38787904 276 GNFTIPDN-SRYSRNIhclIRFMLEPDPEHR 305
Cdd:cd05570 211 DEVLYPRWlSREAVSI---LKGLLTKDPARR 238
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
53-256 5.22e-11

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: 63.40  E-value: 5.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFL-VRTHGGIRCALKRMYVNNMP--DLNVCKREITIMKELSgHKNIVGYLDCAVNSISDNVweVLI- 128
Cdd:cd13983   5 FNEVLGRGSFKTVYRaFDTEEGIEVAWNEIKLRKLPkaERQRFKQEIEILKSLK-HPNIIKFYDSWESKSKKEV--IFIt 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 -------LMEYCRAGQVVNqmnkklqtgftePEVLQIFC-DTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYV-LCDF 199
Cdd:cd13983  82 elmtsgtLKQYLKRFKRLK------------LKVIKSWCrQILEGLNYLHTRDPPIIHRDLKCDNIFINGNTGEVkIGDL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 200 GSATNKFLNpqkdgvnvveeeiKKYT---TLSYRAPEMinlYGGKpITTKADIWALG-CLL 256
Cdd:cd13983 150 GLATLLRQS-------------FAKSvigTPEFMAPEM---YEEH-YDEKVDIYAFGmCLL 193
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
95-380 5.69e-11

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: 64.27  E-value: 5.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckT 174
Cdd:cd14176  62 EIEILLRYGQHPNIITLKD-----VYDDGKYVYVVTELMKGGELLDKILR--QKFFSEREASAVLFTITKTVEYLHA--Q 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PIIHRDLKVENIL-LNDGGN---YVLCDFGSAtnKFLNPQKDGVnvveeeIKKYTTLSYRAPEMINLYGgkpITTKADIW 250
Cdd:cd14176 133 GVVHRDLKPSNILyVDESGNpesIRICDFGFA--KQLRAENGLL------MTPCYTANFVAPEVLERQG---YDAACDIW 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 251 ALGCLLYKLCFFTLPFG--------ESQVAICDGNFTIPDN--SRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAK 320
Cdd:cd14176 202 SLGVLLYTMLTGYTPFAngpddtpeEILARIGSGKFSLSGGywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHW 281
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 321 KDCPVSNINNSSIPSALPEPMTASEAAARKSQikARITDTIGptETSIAPRQRPKANSAT 380
Cdd:cd14176 282 DQLPQYQLNRQDAPHLVKGAMAATYSALNRNQ--SPVLEPVG--RSTLAQRRGIKKITST 337
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
150-314 6.25e-11

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: 63.43  E-value: 6.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 150 FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKflnpqKDGVNVVEeeikKYTTLSY 229
Cdd:cd05578  97 FSEETVKFYICEIVLALDYLHSKN--IIHRDIKPDNILLDEQGHVHITDFNIATKL-----TDGTLATS----TSGTKPY 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 230 RAPEMINLYG-GKPIttkaDIWALGCLLYKLCFFTLPF------GESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDP 302
Cdd:cd05578 166 MAPEVFMRAGySFAV----DWWSLGVTAYEMLRGKRPYeihsrtSIEEIRAKFETASVLYPAGWSEEAIDLINKLLERDP 241
                       170
                ....*....|....*.
gi 38787904 303 EHR----PDIFQVSYF 314
Cdd:cd05578 242 QKRlgdlSDLKNHPYF 257
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
55-306 7.10e-11

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 62.85  E-value: 7.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDLnvcKR----EITIMKELSgHKNIVGYLDCAVNSisdnvWEVLIL 129
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPdNTEVAVKTCRETLPPDL---KRkflqEARILKQYD-HPNIVKLIGVCVQK-----QPIMIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQ--CktpiIHRDLKVENILLNDGGNYVLCDFGSATNkfl 207
Cdd:cd05041  72 MELVPGGSLLTFLRKK-GARLTVKQLLQMCLDAAAGMEYLESknC----IHRDLAARNCLVGENNVLKISDFGMSRE--- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 npQKDGVNVVEEEIK----KYTtlsyrAPEMINlYGgkPITTKADIWALGCLLYKlcffTLPFGESQVAICDGNFT---I 280
Cdd:cd05041 144 --EEDGEYTVSDGLKqipiKWT-----APEALN-YG--RYTSESDVWSFGILLWE----IFSLGATPYPGMSNQQTreqI 209
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 281 PDNSRYSRNIHC---LIRFML---EPDPEHRP 306
Cdd:cd05041 210 ESGYRMPAPELCpeaVYRLMLqcwAYDPENRP 241
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
152-306 7.53e-11

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: 62.83  E-value: 7.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 152 EPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGgnyvlcdfgSATNKFLNPQKDGVNVVEEEIK---KYTTLS 228
Cdd:cd13976  83 EPEAARLFRQIASAVAHCHR--NGIVLRDLKLRKFVFADE---------ERTKLRLESLEDAVILEGEDDSlsdKHGCPA 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMIN---LYGGKPittkADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDNsrYSRNIHCLIRFMLEP 300
Cdd:cd13976 152 YVSPEILNsgaTYSGKA----ADVWSLGVILYTMLVGRYPFHDSEPAslfakIRRGQFAIPET--LSPRARCLIRSLLRR 225

                ....*.
gi 38787904 301 DPEHRP 306
Cdd:cd13976 226 EPSERL 231
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
55-327 8.93e-11

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: 63.47  E-value: 8.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCK-REITIMKELSgHKNIVGYLDCAVNSISDN-VWEVL---- 127
Cdd:cd07872  12 EKLGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAiREVSLLKDLK-HANIVTLHDIVHTDKSLTlVFEYLdkdl 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 -ILMEYCraGQVVNQMNKKLQtgftepeVLQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKF 206
Cdd:cd07872  91 kQYMDDC--GNIMSMHNVKIF-------LYQIL----RGLAYCHRRK--VLHRDLKPQNLLINERGELKLADFGLARAKS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LnPQKDGVNVVeeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCLLYKLcfftlpfgesqvaiCDGNFTIPdNSRY 286
Cdd:cd07872 156 V-PTKTYSNEV-------VTLWYRPPDV--LLGSSEYSTQIDMWGVGCIFFEM--------------ASGRPLFP-GSTV 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 38787904 287 SRNIHCLIRFMLEPDPEHRPDIFQVSYF-AFKFAK-KDCPVSN 327
Cdd:cd07872 211 EDELHLIFRLLGTPTEETWPGISSNDEFkNYNFPKyKPQPLIN 253
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-305 1.02e-10

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: 62.77  E-value: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLV--RTHG---GIRCALKRMYVNNMPDLNvckREITIMKELSgHKNIVGYLDcavnsISDNVWEVL 127
Cdd:cd14083   7 FKEVLGTGAFSEVVLAedKATGklvAIKCIDKKALKGKEDSLE---NEIAVLRKIK-HPNIVQLLD-----IYESKSHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILlndggnyvlcdfgsatnkFL 207
Cdd:cd14083  78 LVMELVTGGELFDRIVEK--GSYTEKDASHLIRQVLEAVDYLHSLG--IVHRDLKPENLL------------------YY 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 NPQKD--------GVNVVEEEIKKYT---TLSYRAPEMInlyGGKPITTKADIWALGCLLY-KLCFFTlPFGE------- 268
Cdd:cd14083 136 SPDEDskimisdfGLSKMEDSGVMSTacgTPGYVAPEVL---AQKPYGKAVDCWSIGVISYiLLCGYP-PFYDendsklf 211
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 269 SQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14083 212 AQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPNKR 248
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
45-262 1.15e-10

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: 62.37  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  45 AVGRHQVTLEESLAEGGFSTVFLvRTHGGIRCALKRMYvNNMPDLNVCKREITIMKELSgHKNIVGYLdcAVNSISDNVw 124
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVML-GDYRGQKVAVKCLK-DDSTAAQAFLAEASVMTTLR-HPNLVQLL--GVVLEGNGL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 evLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATN 204
Cdd:cd05039  76 --YIVTEYMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKK--FVHRDLAARNVLVSEDNVAKVSDFGLAKE 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 205 KFLNPQKDGVNVveeeikKYTtlsyrAPEMINLyggKPITTKADIWALGCLLYKLCFF 262
Cdd:cd05039 152 ASSNQDGGKLPI------KWT-----APEALRE---KKFSTKSDVWSFGILLWEIYSF 195
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
98-305 1.27e-10

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 62.57  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   98 IMKElsgHKNIVGYLDCaVNSISDNVWevliLMEYCRAGQVVN--QMNKKLqtgfTEPEVLQIFCDTCEAVARLHqcKTP 175
Cdd:PHA03390  64 LMKD---NPNFIKLYYS-VTTLKGHVL----IMDYIKDGDLFDllKKEGKL----SEAEVKKIIRQLVEALNDLH--KHN 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  176 IIHRDLKVENILLNDGGNYV-LCDFGSATNKFLNPQKDGvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGC 254
Cdd:PHA03390 130 IIHNDIKLENVLYDRAKDRIyLCDYGLCKIIGTPSCYDG------------TLDYFSPEKIK---GHNYDVSFDWWAVGV 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904  255 LLYKLCFFTLPFGESQvaicDGNFTIPD-NSRYSRNIHCL----------IRFMLEPDPEHR 305
Cdd:PHA03390 195 LTYELLTGKHPFKEDE----DEELDLESlLKRQQKKLPFIknvsknandfVQSMLKYNINYR 252
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
88-305 1.31e-10

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: 62.48  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  88 DLNVcKREITIMKELSgHKNIVGYLDCAVNSIsdnvwEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVA 167
Cdd:cd14662  40 DENV-QREIINHRSLR-HPNIIRFKEVVLTPT-----HLAIVMEYAAGGELFERICNAGR--FSEDEARYFFQQLISGVS 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 168 RLHQCKtpIIHRDLKVENILLnDGG---NYVLCDFGSATNKFLNPQ-KDGVNvveeeikkytTLSYRAPEMINL--YGGK 241
Cdd:cd14662 111 YCHSMQ--ICHRDLKLENTLL-DGSpapRLKICDFGYSKSSVLHSQpKSTVG----------TPAYIAPEVLSRkeYDGK 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 242 pittKADIWALGCLLYKLCFFTLPFGESQ---------VAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14662 178 ----VADVWSCGVTLYVMLVGAYPFEDPDdpknfrktiQRIMSVQYKIPDYVRVSQDCRHLLSRIFVANPAKR 246
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
57-316 1.39e-10

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: 62.19  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRT-HGGIRCALKRMYVNNMPDLNVCKR---EITIMKELSgHKNIVGYLdcavNSISDNVWEVLILmEY 132
Cdd:cd14186   9 LGKGSFACVYRARSlHTGLEVAIKMIDKKAMQKAGMVQRvrnEVEIHCQLK-HPSILELY----NYFEDSNYVYLVL-EM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATnKFLNPQKd 212
Cdd:cd14186  83 CHNGEMSRYLKNRKKP-FTEDEARHFMHQIVTGMLYLHS--HGILHRDLTLSNLLLTRNMNIKIADFGLAT-QLKMPHE- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 gvnvveeeiKKYT---TLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPFGESQV-----AICDGNFTIPDNs 284
Cdd:cd14186 158 ---------KHFTmcgTPNYISPEIATR---SAHGLESDVWSLGCMFYTLLVGRPPFDTDTVkntlnKVVLADYEMPAF- 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 38787904 285 rYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAF 316
Cdd:cd14186 225 -LSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
126-307 1.46e-10

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: 62.56  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFcdtceAVARLHQCKT-----PIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd06622  74 VYMCMEYMDAGSLDKLYAGGVATEGIPEDVLRRI-----TYAVVKGLKFlkeehNIIHRDVKPTNVLVNGNGQVKLCDFG 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 SATNkflnpqkdgvnvVEEEIKKyTTL---SYRAPEMI---NLYGGKPITTKADIWALGCLLYKLCFFTLPFGE------ 268
Cdd:cd06622 149 VSGN------------LVASLAK-TNIgcqSYMAPERIksgGPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPetyani 215
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 38787904 269 -SQV-AICDGN-FTIPDNsrYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd06622 216 fAQLsAIVDGDpPTLPSG--YSDDAQDFVAKCLNKIPNRRPT 255
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
149-305 1.46e-10

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: 62.70  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 149 GFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnPQKDGVNvveeeiKKYTTLS 228
Cdd:cd05631  98 GFDEQRAIFYAAELCCGLEDLQ--RERIVYRDLKPENILLDDRGHIRISDLGLAVQI---PEGETVR------GRVGTVG 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---------GESQVAICDGNFTIPDnsRYSRNIHCLIRFMLE 299
Cdd:cd05631 167 YMAPEVIN---NEKYTFSPDWWGLGCLIYEMIQGQSPFrkrkervkrEEVDRRVKEDQEEYSE--KFSEDAKSICRMLLT 241

                ....*.
gi 38787904 300 PDPEHR 305
Cdd:cd05631 242 KNPKER 247
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
57-266 1.49e-10

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: 62.81  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGG-------IRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIV---------GYLdcavnsi 119
Cdd:cd05584   4 LGKGGYGKVFQVRkTTGSdkgkifaMKVLKKASIVRNQKDTAHTKAERNILEAVK-HPFIVdlhyafqtgGKL------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 sdnvweVLILmEYCRAGQVVNQMNKKlqtG-FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCD 198
Cdd:cd05584  76 ------YLIL-EYLSGGELFMHLERE---GiFMEDTACFYLAEITLALGHLHS--LGIIYRDLKPENILLDAQGHVKLTD 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 199 FGSATNKflnpqkdgvnvVEEEIKKYT---TLSYRAPEMINLYG-GKPIttkaDIWALGCLLYKLCFFTLPF 266
Cdd:cd05584 144 FGLCKES-----------IHDGTVTHTfcgTIEYMAPEILTRSGhGKAV----DWWSLGALMYDMLTGAPPF 200
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
120-334 1.89e-10

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: 62.71  E-value: 1.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWEVlilMEYCRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd05601  73 SENLYLV---MEYHPGGDLLSLLSRYDDI-FEESMARFYLAELVLAIHSLHS--MGYVHRDIKPENILIDRTGHIKLADF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATNkfLNPQKDgvnvVEEEIkKYTTLSYRAPEM---INLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDG 276
Cdd:cd05601 147 GSAAK--LSSDKT----VTSKM-PVGTPDYIAPEVltsMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYS 219
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 277 N-------FTIPDNSRYSRNIHCLIRFMLEpDPEHR---PDIFQVSYFAfkfakkDCPVSNINNSSIP 334
Cdd:cd05601 220 NimnfkkfLKFPEDPKVSESAVDLIKGLLT-DAKERlgyEGLCCHPFFS------GIDWNNLRQTVPP 280
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
165-305 2.05e-10

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: 62.59  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFG---------SATNKFLNpqkdgvnvveeeikkytTLSYRAPEMi 235
Cdd:cd05586 108 ALEHLH--KNDIVYRDLKPENILLDANGHIALCDFGlskadltdnKTTNTFCG-----------------TTEYLAPEV- 167
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 236 nLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDN--SRYSRNihcLIRFMLEPDPEHR 305
Cdd:cd05586 168 -LLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQqmyrnIAFGKVRFPKDvlSDEGRS---FVKGLLNRNPKHR 240
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
57-311 2.06e-10

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: 61.51  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGGIRCALKRMY---VNNMPDLN--VCKREITIMKEL-SGHKNIVGYLDcavnsisdnvW----- 124
Cdd:cd14102   8 LGSGGFGTVYAgSRIADGLPVAVKHVVkerVTEWGTLNgvMVPLEIVLLKKVgSGFRGVIKLLD----------Wyerpd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEycRAGQVVNQMNKKLQTG-FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFGSA 202
Cdd:cd14102  78 GFLIVME--RPEPVKDLFDFITEKGaLDEDTARGFFRQVLEAVRHCYSCG--VVHRDIKDENLLVDlRTGELKLIDFGSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 TnkflnPQKDGVnvveeeikkYT----TLSYRAPEMINL--YGGKpittKADIWALGCLLYKLCFFTLPFgESQVAICDG 276
Cdd:cd14102 154 A-----LLKDTV---------YTdfdgTRVYSPPEWIRYhrYHGR----SATVWSLGVLLYDMVCGDIPF-EQDEEILRG 214
                       250       260       270
                ....*....|....*....|....*....|....*
gi 38787904 277 NFTIpdNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14102 215 RLYF--RRRVSPECQQLIKWCLSLRPSDRPTLEQI 247
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
60-311 2.17e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.92  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   60 GGFSTVFLVRTHGGIRC-ALKRMYVNNMPDL--NVCkREITIMKELSgHKNIVgylDCavNSISDNVWEVLILMEYCRAG 136
Cdd:PLN00034  85 GAGGTVYKVIHRPTGRLyALKVIYGNHEDTVrrQIC-REIEILRDVN-HPNVV---KC--HDMFDHNGEIQVLLEFMDGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  137 QVVN-QMNKKLQTGFTEPEVLQifcdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaTNKFLNPQKDGVN 215
Cdd:PLN00034 158 SLEGtHIADEQFLADVARQILS-------GIAYLHRRH--IVHRDIKPSNLLINSAKNVKIADFG--VSRILAQTMDPCN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  216 vveeeiKKYTTLSYRAPEMIN--LYGGKPITTKADIWALGCLLYKLCFFTLPFGESQ--------VAIC--DGNFTIPDN 283
Cdd:PLN00034 227 ------SSVGTIAYMSPERINtdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRqgdwaslmCAICmsQPPEAPATA 300
                        250       260
                 ....*....|....*....|....*...
gi 38787904  284 SRYSRNihcLIRFMLEPDPEHRPDIFQV 311
Cdd:PLN00034 301 SREFRH---FISCCLQREPAKRWSAMQL 325
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
42-306 2.26e-10

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: 62.36  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  42 RVFaVGRHQVtleeslAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNVCK---REITIMKELSgHKNIVGYLDCAVN 117
Cdd:cd06633  21 EIF-VDLHEI------GHGSFGAVYFATnSHTNEVVAIKKMSYSGKQTNEKWQdiiKEVKFLQQLK-HPNTIEYKGCYLK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 118 SisDNVWevlILMEYC--RAGQVVNQMNKKLQtgftEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYV 195
Cdd:cd06633  93 D--HTAW---LVMEYClgSASDLLEVHKKPLQ----EVEIAAITHGALQGLAYLHS--HNMIHRDIKAGNILLTEPGQVK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 LCDFGSATnkFLNPQKDGVNvveeeikkytTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLC-----FFTLPFGESQ 270
Cdd:cd06633 162 LADFGSAS--IASPANSFVG----------TPYWMAPEVILAMDEGQYDGKVDIWSLGITCIELAerkppLFNMNAMSAL 229
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 271 VAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06633 230 YHIAQNDSPTLQSNEWTDSFRGFVDYCLQKIPQERP 265
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-259 2.31e-10

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 62.01  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH-GGIRCALKRMYVNN---MPdlnvCK--REITIMKELSgHKNIVGYLDCAVNSISDN-VWEVL 127
Cdd:cd07844   6 DKLGEGSYATVYKGRSKlTGQLVALKEIRLEHeegAP----FTaiREASLLKDLK-HANIVTLHDIIHTKKTLTlVFEYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 I-----LMEYCraGQVVNQMNKKLqtgFTepevLQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd07844  81 DtdlkqYMDDC--GGGLSMHNVRL---FL----FQLL----RGLAYCHQRR--VLHRDLKPQNLLISERGELKLADFGLA 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 203 TNKFLnPQKDGVNVVeeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07844 146 RAKSV-PSKTYSNEV-------VTLWYRPPDV--LLGSTEYSTSLDMWGVGCIFYEM 192
pknD PRK13184
serine/threonine-protein kinase PknD;
144-266 2.42e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.02  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  144 KKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKD---GVNVVEEE 220
Cdd:PRK13184 104 KELAEKTSVGAFLSIFHKICATIEYVHS--KGVLHRDLKPDNILLGLFGEVVILDWGAA--IFKKLEEEdllDIDVDERN 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904  221 I---------KKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:PRK13184 180 IcyssmtipgKIVGTPDYMAPERLL---GVPASESTDIYALGVILYQMLTLSFPY 231
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
55-259 2.73e-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: 61.14  E-value: 2.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMpDLNVCKREITIMKELSgHKNIVGYLdcAVNSISDNVWevlILMEYCR 134
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTTKVAVKTLKPGTM-SPEAFLQEAQIMKKLR-HDKLVQLY--AVCSDEEPIY---IVTELMS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLnpqKDGV 214
Cdd:cd05034  74 KGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRN--YIHRDLAARNILVGENNVCKVADFGLA--RLI---EDDE 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 38787904 215 NVVEEEIK---KYTtlsyrAPEMINlYGgkPITTKADIWALGCLLYKL 259
Cdd:cd05034 147 YTAREGAKfpiKWT-----APEAAL-YG--RFTIKSDVWSFGILLYEI 186
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
46-306 2.98e-10

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: 61.60  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMpDLNVCKREITIMKELSGHKNIVGYldcAVNSISDNVWe 125
Cdd:cd05072   4 IPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTM-SVQAFLEEANLMKTLQHDKLVRLY---AVVTKEEPIY- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 vlILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnk 205
Cdd:cd05072  79 --IITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIE--RKNYIHRDLRAANVLVSESLMCKIADFGLA--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 flnpqkdgvNVVEEEikKYTT-------LSYRAPEMINlYGGkpITTKADIWALGCLLYKLCFF-TLPF-----GESQVA 272
Cdd:cd05072 152 ---------RVIEDN--EYTAregakfpIKWTAPEAIN-FGS--FTIKSDVWSFGILLYEIVTYgKIPYpgmsnSDVMSA 217
                       250       260       270
                ....*....|....*....|....*....|....
gi 38787904 273 ICDGnFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05072 218 LQRG-YRMPRMENCPDELYDIMKTCWKEKAEERP 250
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
105-259 3.14e-10

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 61.61  E-value: 3.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQvvnqmnkkLQTGFTEPEV-LQIFCDTCEAVAR----LH-------QC 172
Cdd:cd14054  48 HSNILRFIGADERPTADGRMEYLLVLEYAPKGS--------LCSYLRENTLdWMSSCRMALSLTRglayLHtdlrrgdQY 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGvNVVEEEIKKYT---TLSYRAPEM----INLYGGKPITT 245
Cdd:cd14054 120 KPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVRG-RPGAAENASISevgTLRYMAPEVlegaVNLRDCESALK 198
                       170
                ....*....|....
gi 38787904 246 KADIWALGCLLYKL 259
Cdd:cd14054 199 QVDVYALGLVLWEI 212
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
176-256 3.57e-10

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: 61.28  E-value: 3.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSAtnKFLN-PQKDGVNVVeeeikkyTTLSYRAPEMinLYG----GKPIttkaDIW 250
Cdd:cd07846 121 IIHRDIKPENILVSQSGVVKLCDFGFA--RTLAaPGEVYTDYV-------ATRWYRAPEL--LVGdtkyGKAV----DVW 185

                ....*.
gi 38787904 251 ALGCLL 256
Cdd:cd07846 186 AVGCLV 191
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
44-266 3.68e-10

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: 61.03  E-value: 3.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRhqvtleeSLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIVGYLdcavNSI 119
Cdd:cd14117   8 FDIGR-------PLGKGKFGNVYLAReKQSKFIVALKVLFKSQIEKEGVehqLRREIEIQSHLR-HPNILRLY----NYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVwEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd14117  76 HDRK-RIYLILEYAPRGELYKELQKHGR--FDEQRTATFMEELADALHYCHEKK--VIHRDIKPENLLMGYKGELKIADF 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSAtnkflnpqkdgvnVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14117 151 GWS-------------VHAPSLRRRTmcgTLDYLPPEMIE---GRTHDEKVDLWCIGVLCYELLVGMPPF 204
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
50-306 4.21e-10

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: 60.66  E-value: 4.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVfLVRTHGGIRCALKR----MYVNNMPDlnvckrEITIMKELSgHKNIVGYLDCAVNSisdnvwE 125
Cdd:cd05083   7 KLTLGEIIGEGEFGAV-LQGEYMGQKVAVKNikcdVTAQAFLE------ETAVMTKLQ-HKNLVRLLGVILHN------G 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnk 205
Cdd:cd05083  73 LYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKK--LVHRDLAARNILVSEDGVAKISDFGLA--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 flNPQKDGVNVVEEEIKkyttlsYRAPEMINlygGKPITTKADIWALGCLLYKLCFF------TLPFGESQVAICDG-NF 278
Cdd:cd05083 148 --KVGSMGVDNSRLPVK------WTAPEALK---NKKFSSKSDVWSYGVLLWEVFSYgrapypKMSVKEVKEAVEKGyRM 216
                       250       260
                ....*....|....*....|....*...
gi 38787904 279 TIPDNSrySRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05083 217 EPPEGC--PPDVYSIMTSCWEAEPGKRP 242
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
94-256 4.91e-10

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: 61.66  E-value: 4.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKeLSGHKNIVGYLDCAVNSIS-DNVWEVLILMEYCRAG--QVVnQMNkkLQTGFTEPEVLQIFCdtceAVARLH 170
Cdd:cd07850  48 RELVLMK-LVNHKNIIGLLNVFTPQKSlEEFQDVYLVMELMDANlcQVI-QMD--LDHERMSYLLYQMLC----GIKHLH 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QckTPIIHRDLKVENILLNDGGNYVLCDFGSA----TNKFLNPQkdgvnVVeeeikkytTLSYRAPEMINlygGKPITTK 246
Cdd:cd07850 120 S--AGIIHRDLKPSNIVVKSDCTLKILDFGLArtagTSFMMTPY-----VV--------TRYYRAPEVIL---GMGYKEN 181
                       170
                ....*....|
gi 38787904 247 ADIWALGCLL 256
Cdd:cd07850 182 VDIWSVGCIM 191
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
149-266 6.51e-10

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: 61.14  E-value: 6.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 149 GFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnPQKDGVNvveeeiKKYTTLS 228
Cdd:cd05632 100 GFEEERALFYAAEILCGLEDLHR--ENTVYRDLKPENILLDDYGHIRISDLGLAVKI---PEGESIR------GRVGTVG 168
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMIN--LYGGKPittkaDIWALGCLLYKLCFFTLPF 266
Cdd:cd05632 169 YMAPEVLNnqRYTLSP-----DYWGLGCLIYEMIEGQSPF 203
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
57-306 7.53e-10

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: 59.98  E-value: 7.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFL-VRTHGGIRCALKRMYVN------NMPDLNVCKREITIMKEL-SGHKNIVGYLDCAVNSISdnvweVLI 128
Cdd:cd14100   8 LGSGGFGSVYSgIRVADGAPVAIKHVEKDrvsewgELPNGTRVPMEIVLLKKVgSGFRGVIRLLDWFERPDS-----FVL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEycRAGQVVNQMNKKLQTGFTEPEVLQ-IFCDTCEAVARLHQCKtpIIHRDLKVENILLN-DGGNYVLCDFGSATnkf 206
Cdd:cd14100  83 VLE--RPEPVQDLFDFITERGALPEELARsFFRQVLEAVRHCHNCG--VLHRDIKDENILIDlNTGELKLIDFGSGA--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnPQKDGVnvveeeikkYT----TLSYRAPEMINL--YGGKpittKADIWALGCLLYKLCFFTLPFgESQVAICDGNFTI 280
Cdd:cd14100 156 --LLKDTV---------YTdfdgTRVYSPPEWIRFhrYHGR----SAAVWSLGILLYDMVCGDIPF-EHDEEIIRGQVFF 219
                       250       260
                ....*....|....*....|....*.
gi 38787904 281 pdNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14100 220 --RQRVSSECQHLIKWCLALRPSDRP 243
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
122-306 7.67e-10

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: 60.47  E-value: 7.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 NVWEVLILMEYCragqvVNQMNKKLQTGFTEPEVLQIfcdTCEAVARLHQCKTP--IIHRDLKVENILLNDGGNYVLCDF 199
Cdd:cd06618  88 DVFICMELMSTC-----LDKLLKRIQGPIPEDILGKM---TVSIVKALHYLKEKhgVIHRDVKPSNILLDESGNVKLCDF 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATnkflnpqkdgvNVVEEEIKKYTT--LSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGEsqvaiCDGN 277
Cdd:cd06618 160 GISG-----------RLVDSKAKTRSAgcAAYMAPERIDPPDNPKYDIRADVWSLGISLVELATGQFPYRN-----CKTE 223
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 38787904 278 FTI------------PDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06618 224 FEVltkilneeppslPPNEGFSPDFCSFVDLCLTKDHRYRP 264
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
44-262 7.72e-10

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: 60.00  E-value: 7.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRHQVTLEESLAEGGFSTVfLVRTHGGIRCALKrmYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISDnv 123
Cdd:cd05082   1 WALNMKELKLLQTIGKGEFGDV-MLGDYRGNKVAVK--CIKNDATAQAFLAEASVMTQLR-HSNLVQLLGVIVEEKGG-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 124 weVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGsat 203
Cdd:cd05082  75 --LYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLE--GNNFVHRDLAARNVLVSEDNVAKVSDFG--- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 204 nkfLNPQKDGVNVVEEEIKKYTtlsyrAPEMINlygGKPITTKADIWALGCLLYKLCFF 262
Cdd:cd05082 148 ---LTKEASSTQDTGKLPVKWT-----APEALR---EKKFSTKSDVWSFGILLWEIYSF 195
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
57-268 7.89e-10

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: 60.04  E-value: 7.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLV-RTHGGIRCALKRMYVNnmPD-------LNVCKREITIMKELSgHKNIVGYLDCavnsISDNVWEVL- 127
Cdd:cd06653  10 LGRGAFGEVYLCyDADTGRELAVKQVPFD--PDsqetskeVNALECEIQLLKNLR-HDRIVQYYGC----LRDPEEKKLs 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsATNKFL 207
Cdd:cd06653  83 IFVEYMPGGSVKDQL--KAYGALTENVTRRYTRQILQGVSYLHS--NMIVHRDIKGANILRDSAGNVKLGDFG-ASKRIQ 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 208 NPQKDGVNvveeeIKKYTTLSY-RAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGE 268
Cdd:cd06653 158 TICMSGTG-----IKSVTGTPYwMSPEVIS---GEGYGRKADVWSVACTVVEMLTEKPPWAE 211
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
129-272 7.98e-10

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: 60.75  E-value: 7.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkfln 208
Cdd:cd05603  74 VLDYVNGGELFFHLQR--ERCFLEPRARFYAAEVASAIGYLHSLN--IIYRDLKPENILLDCQGHVVLTDFGLC------ 143
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 209 pqKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVA 272
Cdd:cd05603 144 --KEGMEPEETTSTFCGTPEYLAPEVLR---KEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVS 202
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
50-306 1.11e-09

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: 59.67  E-value: 1.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVrTHGGIRCALKRmyVNNMPDLNVCKREITIMKE-----LSGHKNIVGYLDCAVNSISdnvw 124
Cdd:cd14145   7 ELVLEEIIGIGGFGKVYRA-IWIGDEVAVKA--ARHDPDEDISQTIENVRQEaklfaMLKHPNIIALRGVCLKEPN---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 eVLILMEYCRAGQvvnqMNKKLQTGFTEPEVLqifCDTCEAVAR----LH-QCKTPIIHRDLKVENILLNDggnyvLCDF 199
Cdd:cd14145  80 -LCLVMEFARGGP----LNRVLSGKRIPPDIL---VNWAVQIARgmnyLHcEAIVPVIHRDLKSSNILILE-----KVEN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATNKFLNPQKDGVNVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAICD 275
Cdd:cd14145 147 GDLSNKILKITDFGLAREWHRTTKMSaagTYAWMAPEVIR---SSMFSKGSDVWSYGVLLWELLTGEVPFrGIDGLAVAY 223
                       250       260       270
                ....*....|....*....|....*....|....*
gi 38787904 276 G----NFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14145 224 GvamnKLSLPIPSTCPEPFARLMEDCWNPDPHSRP 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
48-264 1.21e-09

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 59.74  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLV-------RTHGGIRCALKRMYVNNMP-DLNVCKREITIMKELSGHKNIVGYLDCAVNSi 119
Cdd:cd05053  11 RDRLTLGKPLGEGAFGQVVKAeavgldnKPNEVVTVAVKMLKDDATEkDLSDLVSEMEMMKMIGKHKNIINLLGACTQD- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 sdnvWEVLILMEYCRAGQV---------VNQMNKKLQTGFTEPEVLQIFCDTCE-AVAR----LHQCKtpIIHRDLKVEN 185
Cdd:cd05053  90 ----GPLYVVVEYASKGNLreflrarrpPGEEASPDDPRVPEEQLTQKDLVSFAyQVARgmeyLASKK--CIHRDLAARN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 186 ILLNDGGNYVLCDFGSATnkflnpqkdgvNVVEEEIKKYTT-----LSYRAPEMI--NLYggkpiTTKADIWALGCLLYK 258
Cdd:cd05053 164 VLVTEDNVMKIADFGLAR-----------DIHHIDYYRKTTngrlpVKWMAPEALfdRVY-----THQSDVWSFGVLLWE 227

                ....*.
gi 38787904 259 LcfFTL 264
Cdd:cd05053 228 I--FTL 231
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
45-271 1.35e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 60.63  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   45 AVGRHQVTLEESLAEGGFSTVFLVRTHGGI---RCALKRMYVNNMPDlnvckREITIMKELSgHKNIVgyldcavNSISD 121
Cdd:PHA03207  88 SVVRMQYNILSSLTPGSEGEVFVCTKHGDEqrkKVIVKAVTGGKTPG-----REIDILKTIS-HRAII-------NLIHA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  122 NVWEVLILM---EY-CRAGQVVNQMNK-KLQTGFTEPEVLqifcdtCEAVARLHQckTPIIHRDLKVENILLNDGGNYVL 196
Cdd:PHA03207 155 YRWKSTVCMvmpKYkCDLFTYVDRSGPlPLEQAITIQRRL------LEALAYLHG--RGIIHRDVKTENIFLDEPENAVL 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904  197 CDFGSATNKFLNPQKDgvnvveeeiKKY---TTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPFGESQV 271
Cdd:PHA03207 227 GDFGAACKLDAHPDTP---------QCYgwsGTLETNSPELLAL---DPYCAKTDIWSAGLVLFEMSVKNVTLFGKQV 292
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
71-305 1.48e-09

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: 59.67  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  71 HGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYCRAGQVVNQMNkklQTGF 150
Cdd:cd06658  45 HTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYH-HENVVDMYNSYL--VGDELW---VVMEFLEGGALTDIVT---HTRM 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 151 TEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvnvVEEEIKKYTTLS-- 228
Cdd:cd06658 116 NEEQIATVCLSVLRALSYLHN--QGVIHRDIKSDSILLTSDGRIKLSDFGFCAQ------------VSKEVPKRKSLVgt 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 --YRAPEMINLYggkPITTKADIWALGCLLYKLC-----FFTLPFGESQVAICDgnfTIPDNSRYSRNIHCLIR----FM 297
Cdd:cd06658 182 pyWMAPEVISRL---PYGTEVDIWSLGIMVIEMIdgeppYFNEPPLQAMRRIRD---NLPPRVKDSHKVSSVLRgfldLM 255

                ....*...
gi 38787904 298 LEPDPEHR 305
Cdd:cd06658 256 LVREPSQR 263
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
94-270 1.56e-09

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 59.69  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDcavnSISDNVWEVLILMEYCRAGQVvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14041  59 REYRIHKELD-HPRIVKLYD----YFSLDTDSFCTVLEYCEGNDL--DFYLKQHKLMSEKEARSIIMQIVNALKYLNEIK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDG---GNYVLCDFGsaTNKFLNPQKDG-VNVVEEEIKKYTTLSYRAPEMInLYGGKP--ITTKA 247
Cdd:cd14041 132 PPIIHYDLKPGNILLVNGtacGEIKITDFG--LSKIMDDDSYNsVDGMELTSQGAGTYWYLPPECF-VVGKEPpkISNKV 208
                       170       180
                ....*....|....*....|...
gi 38787904 248 DIWALGCLLYKLCFFTLPFGESQ 270
Cdd:cd14041 209 DVWSVGVIFYQCLYGRKPFGHNQ 231
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
60-266 1.96e-09

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: 59.48  E-value: 1.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFL-VRTHGGIRCALKRMyvNNMPDLNVcKREITIMKELSGHKNIVGYLDCAVNSISDNVweVLIlMEYcragqv 138
Cdd:cd14132  29 GKYSEVFEgINIGNNEKVVIKVL--KPVKKKKI-KREIKILQNLRGGPNIVKLLDVVKDPQSKTP--SLI-FEY------ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 139 VNQMN-KKLQTGFTEPEV-LQIFcdtcEAVARLHQC-KTPIIHRDLKVENILLNDGGNYV-LCDFGSAtnKFLNPQKD-G 213
Cdd:cd14132  97 VNNTDfKTLYPTLTDYDIrYYMY----ELLKALDYChSKGIMHRDVKPHNIMIDHEKRKLrLIDWGLA--EFYHPGQEyN 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 214 VNVveeeikkyTTLSYRAPEM---INLYggkpiTTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14132 171 VRV--------ASRYYKGPELlvdYQYY-----DYSLDMWSLGCMLASMIFRKEPF 213
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
95-270 2.24e-09

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: 58.94  E-value: 2.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLDCavnsISDNVWEVL-ILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCEAVARLHqcK 173
Cdd:cd06651  59 EIQLLKNLQ-HERIVQYYGC----LRDRAEKTLtIFMEYMPGGSVKDQL--KAYGALTESVTRKYTRQILEGMSYLH--S 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDGGNYVLCDFGsATNKFLNPQKDGVNvveeeIKKYTTLSY-RAPEMINlygGKPITTKADIWAL 252
Cdd:cd06651 130 NMIVHRDIKGANILRDSAGNVKLGDFG-ASKRLQTICMSGTG-----IRSVTGTPYwMSPEVIS---GEGYGRKADVWSL 200
                       170
                ....*....|....*...
gi 38787904 253 GCLLYKLCFFTLPFGESQ 270
Cdd:cd06651 201 GCTVVEMLTEKPPWAEYE 218
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
50-259 2.39e-09

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 58.83  E-value: 2.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVNSIsdnvwEVLIL 129
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQ-TRHENVVLFMGACMHPP-----HLAII 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRaGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLnDGGNYVLCDFGSAtnkflnp 209
Cdd:cd14152  75 TSFCK-GRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLH--AKGIVHKDLKSKNVFY-DNGKVVITDFGLF------- 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 210 qkdGVNVV------EEEIK-KYTTLSYRAPEMINLYG-GK-----PITTKADIWALGCLLYKL 259
Cdd:cd14152 144 ---GISGVvqegrrENELKlPHDWLCYLAPEIVREMTpGKdedclPFSKAADVYAFGTIWYEL 203
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
152-314 2.60e-09

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: 58.14  E-value: 2.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 152 EPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGgnyvlcdfgSATNKFLNPQKDgVNVVEEE----IKKYTTL 227
Cdd:cd14023  83 EEEAARLFKQIVSAVAHCHQ--SAIVLGDLKLRKFVFSDE---------ERTQLRLESLED-THIMKGEddalSDKHGCP 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 228 SYRAPEMINL---YGGKpittKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDNsrYSRNIHCLIRFMLE 299
Cdd:cd14023 151 AYVSPEILNTtgtYSGK----SADVWSLGVMLYTLLVGRYPFHDSDPSalfskIRRGQFCIPDH--VSPKARCLIRSLLR 224
                       170
                ....*....|....*...
gi 38787904 300 PDPEHR---PDIFQVSYF 314
Cdd:cd14023 225 REPSERltaPEILLHPWF 242
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-305 2.60e-09

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: 58.91  E-value: 2.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLV--RTHG---GIRCALKRMYVNNMPDLnvcKREITIMKELSgHKNIVgyldcAVNSISDNVWEVL 127
Cdd:cd14168  14 FKEVLGTGAFSEVVLAeeRATGklfAVKCIPKKALKGKESSI---ENEIAVLRKIK-HENIV-----ALEDIYESPNHLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqtGF-TEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILL---NDGGNYVLCDFGsat 203
Cdd:cd14168  85 LVMQLVSGGELFDRIVEK---GFyTEKDASTLIRQVLDAVYYLH--RMGIVHRDLKPENLLYfsqDEESKIMISDFG--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 nkfLNPQKDGVNVVEEEIKkytTLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPFGE-------SQVAICDG 276
Cdd:cd14168 157 ---LSKMEGKGDVMSTACG---TPGYVAPEVL---AQKPYSKAVDCWSIGVIAYILLCGYPPFYDendsklfEQILKADY 227
                       250       260
                ....*....|....*....|....*....
gi 38787904 277 NFTIPDNSRYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd14168 228 EFDSPYWDDISDSAKDFIRNLMEKDPNKR 256
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
57-306 2.79e-09

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: 58.59  E-value: 2.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHG-GIRCALKRM-YVNNMP--DLNVC---KREITIMKELSgHKNIVGYLDCAVNSISDNvwevlIL 129
Cdd:cd06630   8 LGTGAFSSCYQARDVKtGTLMAVKQVsFCRNSSseQEEVVeaiREEIRMMARLN-HPNIVRMLGATQHKSHFN-----IF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-LCDFGSATNkfLN 208
Cdd:cd06630  82 VEWMAGGSVASLLSK--YGAFSENVIINYTLQILRGLAYLHDNQ--IIHRDLKGANLLVDSTGQRLrIADFGAAAR--LA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 PQKDGVNVVEEEIkkYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGES----------QVAICDGNF 278
Cdd:cd06630 156 SKGTGAGEFQGQL--LGTIAFMAPEVLR---GEQYGRSCDVWSVGCVIIEMATAKPPWNAEkisnhlalifKIASATTPP 230
                       250       260
                ....*....|....*....|....*....
gi 38787904 279 TIPDN-SRYSRNIhcLIRfMLEPDPEHRP 306
Cdd:cd06630 231 PIPEHlSPGLRDV--TLR-CLELQPEDRP 256
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
57-277 2.82e-09

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: 58.66  E-value: 2.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNV-CKREITIMKELSgHKNIVGYLDCAVNSISDnvwevLILMEYCRA 135
Cdd:cd14664   1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDHgFQAEIQTLGMIR-HRNIVRLRGYCSNPTTN-----LLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARLHQ-CKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKD 212
Cdd:cd14664  75 GSLGELLHSRPESQppLDWETRQRIALGSARGLAYLHHdCSPLIIHRDVKSNNILLDEEFEAHVADFGLA--KLMDDKDS 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 213 GVNVVEEeikkyTTLSYRAPEMinLYGGKpITTKADIWALGCLLYKLCFFTLPFGESQVAicDGN 277
Cdd:cd14664 153 HVMSSVA-----GSYGYIAPEY--AYTGK-VSEKSDVYSYGVVLLELITGKRPFDEAFLD--DGV 207
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
53-305 2.95e-09

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: 58.72  E-value: 2.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVflvrtHGGIRCALKRMYVNNM-----PDLNVCKREITIMKELSgHKNIVgYLDCAVNSISdnvwEVL 127
Cdd:cd14104   4 IAEELGRGQFGIV-----HRCVETSSKKTYMAKFvkvkgADQVLVKKEISILNIAR-HRNIL-RLHESFESHE----ELV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCrAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENIL-LNDGGNYV-LCDFGSATNk 205
Cdd:cd14104  73 MIFEFI-SGVDIFERITTARFELNEREIVSYVRQVCEALEFLH--SKNIGHFDIRPENIIyCTRRGSYIkIIEFGQSRQ- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 fLNPqKDGVNVveeeikKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQV----AICDGNFTI 280
Cdd:cd14104 149 -LKP-GDKFRL------QYTSAEFYAPEVHQ---HESVSTATDMWSLGCLVYVLLSGINPFeAETNQqtieNIRNAEYAF 217
                       250       260
                ....*....|....*....|....*..
gi 38787904 281 PDNSRYSRNIHCL--IRFMLEPDPEHR 305
Cdd:cd14104 218 DDEAFKNISIEALdfVDRLLVKERKSR 244
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
45-266 3.41e-09

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: 59.28  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  45 AVGRHQVTLEESLAEGGFSTVFLVRTHGGIRC----ALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSIs 120
Cdd:cd05618  16 SLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIyamkVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTES- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 121 dnvwEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd05618  95 ----RLFFVIEYVNGGDLMFHMQR--QRKLPEEHARFYSAEISLALNYLHE--RGIIYRDLKLDNVLLDSEGHIKLTDYG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 201 SAtnkflnpqKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05618 167 MC--------KEGLRPGDTTSTFCGTPNYIAPEILR---GEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
157-305 3.43e-09

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: 58.38  E-value: 3.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 157 QIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpQKDGVNVVEeeikKYTTLSYRAPEMIN 236
Cdd:cd05607 112 QITC----GILHLHSLK--IVYRDMKPENVLLDDNGNCRLSDLGLAVE-----VKEGKPITQ----RAGTNGYMAPEILK 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 237 lygGKPITTKADIWALGCLLYKLCFFTLPFG----------------ESQVAICDGNFTIPdnsrySRNIhclIRFMLEP 300
Cdd:cd05607 177 ---EESYSYPVDWFAMGCSIYEMVAGRTPFRdhkekvskeelkrrtlEDEVKFEHQNFTEE-----AKDI---CRLFLAK 245

                ....*
gi 38787904 301 DPEHR 305
Cdd:cd05607 246 KPENR 250
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
105-259 3.93e-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: 58.22  E-value: 3.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLdCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTgftepevLQIFCDTCEAVAR----LH-------QCK 173
Cdd:cd13998  48 HENILQFI-AADERDTALRTELWLVTAFHPNGSL*DYLSLHTID-------WVSLCRLALSVARglahLHseipgctQGK 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVveEEIKKYTTLSYRAPEM----INLYGGKPItTKADI 249
Cdd:cd13998 120 PAIAHRDLKSKNILVKNDGTCCIADFGLAVR--LSPSTGEEDN--ANNGQVGTKRYMAPEVlegaINLRDFESF-KRVDI 194
                       170
                ....*....|
gi 38787904 250 WALGCLLYKL 259
Cdd:cd13998 195 YAMGLVLWEM 204
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
55-259 3.99e-09

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: 58.43  E-value: 3.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVF--LVRTHGGIrCALKRMYVNNMPDLNVCK-REITIMKELSgHKNIVgyldcAVNSISDNVWEVLILME 131
Cdd:cd07870   6 EKLGEGSYATVYkgISRINGQL-VALKVISMKTEEGVPFTAiREASLLKGLK-HANIV-----LLHDIIHTKETLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRA--GQVVNQmnkklQTGFTEPEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLN 208
Cdd:cd07870  79 YMHTdlAQYMIQ-----HPGGLHPYNVRLFMfQLLRGLAYIHGQH--ILHRDLKPQNLLISYLGELKLADFGLARAKSIP 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 209 PQKDGVNVVeeeikkytTLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07870 152 SQTYSSEVV--------TLWYRPPDV--LLGATDYSSALDIWGAGCIFIEM 192
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
147-305 4.36e-09

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: 58.14  E-value: 4.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 147 QTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqkdgVNVVEEEIKK--Y 224
Cdd:cd05605  96 NPGFEEERAVFYAAEITCGLEHLHSER--IVYRDLKPENILLDDHGHVRISDLGLA-----------VEIPEGETIRgrV 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 225 TTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---------GESQVAICDGnfTIPDNSRYSRNIHCLIR 295
Cdd:cd05605 163 GTVGYMAPEVVK---NERYTFSPDWWGLGCLIYEMIEGQAPFrarkekvkrEEVDRRVKED--QEEYSEKFSEEAKSICS 237
                       170
                ....*....|
gi 38787904 296 FMLEPDPEHR 305
Cdd:cd05605 238 QLLQKDPKTR 247
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
94-256 5.62e-09

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: 58.38  E-value: 5.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSIS-DNVWEVLILMEYCRAgqvvnQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqc 172
Cdd:cd07879  63 RELTLLKHMQ-HENVIGLLDVFTSAVSgDEFQDFYLVMPYMQT-----DLQKIMGHPLSEDKVQYLVYQMLCGLKYIH-- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KTPIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvnvVEEEIKKY-TTLSYRAPEMInlYGGKPITTKADIWA 251
Cdd:cd07879 135 SAGIIHRDLKPGNLAVNEDCELKILDFGLARH------------ADAEMTGYvVTRWYRAPEVI--LNWMHYNQTVDIWS 200

                ....*
gi 38787904 252 LGCLL 256
Cdd:cd07879 201 VGCIM 205
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
89-311 6.38e-09

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: 56.89  E-value: 6.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  89 LNVCKREITIMKELSgHKNIVGYLDCAVNSISDNvwevlILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVAR 168
Cdd:cd14060  26 LLKIEKEAEILSVLS-HRNIIQFYGAILEAPNYG-----IVTEYASYGSLFDYLNSNESEEMDMDQIMTWATDIAKGMHY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LH-QCKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNpQKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKA 247
Cdd:cd14060 100 LHmEAPVKVIHRDLKSRNVVIAADGVLKICDFGAS--RFHS-HTTHMSLV-------GTFPWMAPEVIQ---SLPVSETC 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 248 DIWALGCLLYKLCFFTLPFG---ESQVA--ICDGN--FTIPdnSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14060 167 DTYSYGVVLWEMLTREVPFKgleGLQVAwlVVEKNerPTIP--SSCPRSFAELMRRCWEADVKERPSFKQI 235
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
156-312 6.97e-09

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: 57.33  E-value: 6.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 156 LQIfcdtCEAVARLHQ-CKtpIIHRDLKVENILLNDGGNYVLCDFG------SATNKFLNPQKDGVNVVEEEIKkytTLS 228
Cdd:cd14011 121 LQI----SEALSFLHNdVK--LVHGNICPESVVINSNGEWKLAGFDfcisseQATDQFPYFREYDPNLPPLAQP---NLN 191
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMINlygGKPITTKADIWALGCLLYKLcFFTLpfgeSQVAICDGNFTIPD---NSRYSRNIHCL----------IR 295
Cdd:cd14011 192 YLAPEYIL---SKTCDPASDMFSLGVLIYAI-YNKG----KPLFDCVNNLLSYKknsNQLRQLSLSLLekvpeelrdhVK 263
                       170
                ....*....|....*..
gi 38787904 296 FMLEPDPEHRPDIFQVS 312
Cdd:cd14011 264 TLLNVTPEVRPDAEQLS 280
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
48-259 7.48e-09

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: 57.33  E-value: 7.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEEsLAEGGFSTVFLVR-----THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISDN 122
Cdd:cd14205   4 RHLKFLQQ-LGKGNFGSVEMCRydplqDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQ-HDNIVKYKGVCYSAGRRN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 VwevLILMEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsa 202
Cdd:cd14205  82 L---RLIMEYLPYGSLRDYLQKH-KERIDHIKLLQYTSQICKGMEYLGTKR--YIHRDLATRNILVENENRVKIGDFG-- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 203 TNKFLNPQKDGVNVVEeeiKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKL 259
Cdd:cd14205 154 LTKVLPQDKEYYKVKE---PGESPIFWYAPESLT---ESKFSVASDVWSFGVVLYEL 204
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
176-306 8.01e-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: 57.37  E-value: 8.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSA---TNKFLNPQKDGVNvveeeikkyttlSYRAPEMINLYGG-KPITTKADIWA 251
Cdd:cd06616 131 IIHRDVKPSNILLDRNGNIKLCDFGISgqlVDSIAKTRDAGCR------------PYMAPERIDPSASrDGYDVRSDVWS 198
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 252 LGCLLYKLCFFTLPFGE--------SQVAicDGNFTIPDNSRYSRNIHCLIRFM---LEPDPEHRP 306
Cdd:cd06616 199 LGITLYEVATGKFPYPKwnsvfdqlTQVV--KGDPPILSNSEEREFSPSFVNFVnlcLIKDESKRP 262
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
53-260 8.22e-09

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 57.12  E-value: 8.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRTHGGI-RCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYldcaVNSISDNVW------E 125
Cdd:cd13975   4 LGRELGRGQYGVVYACDSWGGHfPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSL----HGSVIDYSYgggssiA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEycragQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsatnk 205
Cdd:cd13975  80 VLLIME-----RLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHS--QGLVHRDIKLKNVLLDKKNRAKITDLG----- 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 206 FLNPQK--DGvNVVEEEIkkyttlsYRAPEminLYGGKpITTKADIWALGCLLYKLC 260
Cdd:cd13975 148 FCKPEAmmSG-SIVGTPI-------HMAPE---LFSGK-YDNSVDVYAFGILFWYLC 192
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
50-311 8.24e-09

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 57.55  E-value: 8.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNM---PDLNV--CKREITIMKELSgHKNIVGYLDcAVNSisdnV 123
Cdd:cd14094   4 VYELCEVIGKGPFSVVRrCIHRETGQQFAVKIVDVAKFtssPGLSTedLKREASICHMLK-HPHIVELLE-TYSS----D 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 124 WEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVL------QIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-- 195
Cdd:cd14094  78 GMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVashymrQIL----EALRYCHDNN--IIHRDVKPHCVLLASKENSApv 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 -LCDFGSATnkflnpQKDGVNVVEEeiKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGESQVAIC 274
Cdd:cd14094 152 kLGGFGVAI------QLGESGLVAG--GRVGTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 38787904 275 DG------NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14094 221 EGiikgkyKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEA 263
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
77-306 8.66e-09

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 57.30  E-value: 8.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  77 ALKR--MYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISdnVWEVLILMEYCRAGQVvnqmnkkLQTGFTE-- 152
Cdd:cd08216  29 AVKKinLESDSKEDLKFLQQEILTSRQLQ-HPNILPYVTSFVVDND--LYVVTPLMAYGSCRDL-------LKTHFPEgl 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 153 PEVL--QIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNkFLNPQKDGVNVVEEEIKKYTTLSYR 230
Cdd:cd08216  99 PELAiaFILRDVLNALEYIH--SKGYIHRSVKASHILISGDGKVVLSGLRYAYS-MVKHGKRQRVVHDFPKSSEKNLPWL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 231 APEMI--NLYGgkpITTKADIWALG---C-----------------LLYKL-----CFF---TLPFGE-SQVAICDGNFT 279
Cdd:cd08216 176 SPEVLqqNLLG---YNEKSDIYSVGitaCelangvvpfsdmpatqmLLEKVrgttpQLLdcsTYPLEEdSMSQSEDSSTE 252
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 280 IPDNSR---------YSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd08216 253 HPNNRDtrdipyqrtFSEAFHQFVELCLQRDPELRP 288
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
94-259 8.78e-09

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: 57.58  E-value: 8.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDnVWEVLILMEycragqvvNQMNKKLQTGFTEPEVLQIFC-DTCEAVARLHQC 172
Cdd:cd07856  58 RELKLLKHLR-HENIISLSDIFISPLED-IYFVTELLG--------TDLHRLLTSRPLEKQFIQYFLyQILRGLKYVHSA 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKDGVnvveeeikkYTTLSYRAPEMINLYggKPITTKADIWAL 252
Cdd:cd07856 128 G--VIHRDLKPSNILVNENCDLKICDFGLA--RIQDPQMTGY---------VSTRYYRAPEIMLTW--QKYDVEVDIWSA 192

                ....*..
gi 38787904 253 GCLLYKL 259
Cdd:cd07856 193 GCIFAEM 199
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
50-306 9.31e-09

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: 56.69  E-value: 9.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKrEITIMKELSgHKNIVG-YLDCAVNSisdnvwEVLI 128
Cdd:cd05059   5 ELTFLKELGSGQFGVVHLGKWRGKIDVAIKMIKEGSMSEDDFIE-EAKVMMKLS-HPKLVQlYGVCTKQR------PIFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVN---QMNKKLQTGFtepeVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnK 205
Cdd:cd05059  77 VTEYMANGCLLNylrERRGKFQTEQ----LLEMCKDVCEAMEYLE--SNGFIHRDLAARNCLVGEQNVVKVSDFGLA--R 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FlnpqkdgvnVVEEEikkYTT-------LSYRAPEMINlYGgkPITTKADIWALGCLLYKLcfFT---LPFG---ESQVA 272
Cdd:cd05059 149 Y---------VLDDE---YTSsvgtkfpVKWSPPEVFM-YS--KFSSKSDVWSFGVLMWEV--FSegkMPYErfsNSEVV 211
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 273 --ICDGnFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05059 212 ehISQG-YRLYRPHLAPTEVYTIMYSCWHEKPEERP 246
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
164-280 9.67e-09

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 56.93  E-value: 9.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 EAVARLHQC-KTPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGvNVVEEEIKKYttlsYRAPEMINlygGKP 242
Cdd:cd07848 108 QLIKAIHWChKNDIVHRDIKPENLLISHNDVLKLCDFGFARN--LSEGSNA-NYTEYVATRW----YRSPELLL---GAP 177
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 38787904 243 ITTKADIWALGCLLYKLCFFTLPF-GESQVaicDGNFTI 280
Cdd:cd07848 178 YGKAVDMWSVGCILGELSDGQPLFpGESEI---DQLFTI 213
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
129-270 1.03e-08

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: 57.32  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNkklQTG-FTEPEVlqIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFL 207
Cdd:cd05616  79 VMEYVNGGDLMYHIQ---QVGrFKEPHA--VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIW 153
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 208 npqkDGVNVveeeiKKYT-TLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF-GESQ 270
Cdd:cd05616 154 ----DGVTT-----KTFCgTPDYIAPEIIAY---QPYGKSVDWWAFGVLLYEMLAGQAPFeGEDE 206
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
165-266 1.06e-08

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: 57.33  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkflnpqkdgvnVVEEEIKKYTTLS-------YRAPEMINl 237
Cdd:cd05575 108 ALGYLHSLN--IIYRDLKPENILLDSQGHVVLTDFG---------------LCKEGIEPSDTTStfcgtpeYLAPEVLR- 169
                        90       100
                ....*....|....*....|....*....
gi 38787904 238 ygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05575 170 --KQPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
53-266 1.11e-08

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: 56.55  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDcAVNSISDnvweVLILME 131
Cdd:cd14191   6 IEERLGSGKFGQVFrLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLH-HPKLVQCVD-AFEEKAN----IVMVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENIL-LNDGGNYV-LCDFGSATNKflnP 209
Cdd:cd14191  80 MVSGGELFERIIDE-DFELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMcVNKTGTKIkLIDFGLARRL---E 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 210 QKDGVNVVeeeikkYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14191 154 NAGSLKVL------FGTPEFVAPEVINY---EPIGYATDMWSIGVICYILVSGLSPF 201
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
55-259 1.19e-08

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: 57.01  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCK-REITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEY 132
Cdd:cd07869  11 EKLGEGSYATVYKGKSKvNGKLVALKVIRLQEEEGTPFTAiREASLLKGLK-HANIV-----LLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAgQVVNQMNKklQTGFTEPEVLQIFC-DTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQK 211
Cdd:cd07869  85 VHT-DLCQYMDK--HPGGLHPENVKLFLfQLLRGLSYIHQ--RYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 38787904 212 DGVNVVeeeikkytTLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07869 160 YSNEVV--------TLWYRPPDV--LLGSTEYSTCLDMWGVGCIFVEM 197
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
57-311 1.37e-08

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: 56.75  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH-GGIRCALKRMYVNNMPDLNVCK--REITIMKELSgHKNIVGYLDCAVNSISDNVWevlILMEYC 133
Cdd:cd14049  14 LGKGGYGKVYKVRNKlDGQYYAIKKILIKKVTKRDCMKvlREVKVLAGLQ-HPNIVGYHTAWMEHVQLMLY---IQMQLC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 ----------RAGQVVNQMNKKLQTGFTEPEV-LQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYV-LCDFGS 201
Cdd:cd14049  90 elslwdwiveRNKRPCEEEFKSAPYTPVDVDVtTKILQQLLEGVTYIHS--MGIVHRDLKPRNIFLHGSDIHVrIGDFGL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 202 ATNKFLNPQKDGVNVVEEEIKKYT----TLSYRAPEMINlygGKPITTKADIWALGCLLYKLcffTLPFG----ESQVAI 273
Cdd:cd14049 168 ACPDILQDGNDSTTMSRLNGLTHTsgvgTCLYAAPEQLE---GSHYDFKSDMYSIGVILLEL---FQPFGtemeRAEVLT 241
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 274 CDGNFTIPDNSRYSRNIHC-LIRFMLEPDPEHRPDIFQV 311
Cdd:cd14049 242 QLRNGQIPKSLCKRWPVQAkYIKLLTSTEPSERPSASQL 280
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
55-259 1.39e-08

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: 56.77  E-value: 1.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHG-GIRCALKRMYVNnMPDLNV---CKREITIMKELSGHKNIVGYLDcaVNSISDNVWEVLILM 130
Cdd:cd07837   7 EKIGEGTYGKVYKARDKNtGKLVALKKTRLE-MEEEGVpstALREVSLLQMLSQSIYIVRLLD--VEHVEENGKPLLYLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 -EYCRAG--QVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYV-LCDFGSAtNKF 206
Cdd:cd07837  84 fEYLDTDlkKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCH--SHGVMHRDLKPQNLLVDKQKGLLkIADLGLG-RAF 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 207 LNPqkdgvnvveeeIKKYT----TLSYRAPEMinLYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07837 161 TIP-----------IKSYTheivTLWYRAPEV--LLGSTHYSTPVDMWSVGCIFAEM 204
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
94-266 1.52e-08

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: 56.57  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQck 173
Cdd:cd14173  48 REVEMLYQCQGHRNVLELIE-----FFEEEDKFYLVFEKMRGGSILSHIHRRRH--FNELEASVVVQDIASALDFLHN-- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILL---NDGGNYVLCDFGSATNKFLNPQKDGVNvVEEEIKKYTTLSYRAPEMINLYGGKP--ITTKAD 248
Cdd:cd14173 119 KGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLNSDCSPIS-TPELLTPCGSAEYMAPEVVEAFNEEAsiYDKRCD 197
                       170
                ....*....|....*...
gi 38787904 249 IWALGCLLYKLCFFTLPF 266
Cdd:cd14173 198 LWSLGVILYIMLSGYPPF 215
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
128-305 1.64e-08

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 56.26  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKklqTGFTEPEVLQI-FCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFG------ 200
Cdd:cd05609  77 MVMEYVEGGDCATLLKN---IGPLPVDMARMyFAETVLALEYLHS--YGIVHRDLKPDNLLITSMGHIKLTDFGlskigl 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 --SATNKFL-NPQKDGVNVVEEEIkkYTTLSYRAPEMINLYG-GKPIttkaDIWALGCLLYKLCFFTLPF-GES------ 269
Cdd:cd05609 152 msLTTNLYEgHIEKDTREFLDKQV--CGTPEYIAPEVILRQGyGKPV----DWWAMGIILYEFLVGCVPFfGDTpeelfg 225
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 38787904 270 -----QVAICDGNFTIPDNSRYsrnihcLIRFMLEPDPEHR 305
Cdd:cd05609 226 qvisdEIEWPEGDDALPDDAQD------LITRLLQQNPLER 260
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
56-259 1.73e-08

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: 56.97  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  56 SLAEGGFSTVFLVRThgGIRCALKRMY--VNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSIS----DNVWEVLIL 129
Cdd:cd07877  27 SGAYGSVCAAFDTKT--GLRVAVKKLSrpFQSIIHAKRTYRELRLLKHMK-HENVIGLLDVFTPARSleefNDVYLVTHL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MeycraGQVVNQMNK--KLQTGFTEPEVLQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkfl 207
Cdd:cd07877 104 M-----GADLNNIVKcqKLTDDHVQFLIYQIL----RGLKYIHSAD--IIHRDLKPSNLAVNEDCELKILDFGLARH--- 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 208 npqkdgvnvVEEEIKKY-TTLSYRAPE-MINLYGgkpITTKADIWALGCLLYKL 259
Cdd:cd07877 170 ---------TDDEMTGYvATRWYRAPEiMLNWMH---YNQTVDIWSVGCIMAEL 211
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
149-305 1.82e-08

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: 56.43  E-value: 1.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 149 GFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpQKDGvnvvEEEIKKYT-TL 227
Cdd:cd05608 101 GFQEPRACFYTAQIISGLEHLHQRR--IIYRDLKPENVLLDDDGNVRISDLGLAVE-----LKDG----QTKTKGYAgTP 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 228 SYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF---------GESQVAICDGNFTIPDnsRYSRNIHCLIRFML 298
Cdd:cd05608 170 GFMAPELLL---GEEYDYSVDYFTLGVTLYEMIAARGPFrargekvenKELKQRILNDSVTYSE--KFSPASKSICEALL 244

                ....*..
gi 38787904 299 EPDPEHR 305
Cdd:cd05608 245 AKDPEKR 251
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
144-306 2.14e-08

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: 55.89  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 144 KKLQTGFTEPE-VL-QIFCDTCEAVARLHQcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnpqkdgVNVVEEEI 221
Cdd:cd06617  92 KVYDKGLTIPEdILgKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLINRNGQVKLCDFGISGYL--------VDSVAKTI 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 222 KKYTTlSYRAPEMINLYG-GKPITTKADIWALGCLLYKLCFFTLPFGE--------SQVaICDGNFTIPdNSRYSRNIHC 292
Cdd:cd06617 163 DAGCK-PYMAPERINPELnQKGYDVKSDVWSLGITMIELATGRFPYDSwktpfqqlKQV-VEEPSPQLP-AEKFSPEFQD 239
                       170
                ....*....|....
gi 38787904 293 LIRFMLEPDPEHRP 306
Cdd:cd06617 240 FVNKCLKKNYKERP 253
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
57-270 2.26e-08

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 55.97  E-value: 2.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRThGGIRCALKR---MYVNNMPDLN-VCKREITIMKELSgHKNIVGYLDCavnsiSDNVWEVLILMEY 132
Cdd:cd14158  23 LGEGGFGVVFKGYI-NDKNVAVKKlaaMVDISTEDLTkQFEQEIQVMAKCQ-HENLVELLGY-----SCDGPQLCLVYTY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKLQTgftEPEVLQIFCDTCEAVAR----LHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKfln 208
Cdd:cd14158  96 MPNGSLLDRLACLNDT---PPLSWHMRCKIAQGTANginyLHE--NNHIHRDIKSANILLDETFVPKISDFGLARAS--- 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 209 pQKDGVNVVEEEIkkYTTLSYRAPEMinlYGGKpITTKADIWALGCLLYKLCFFTLPFGESQ 270
Cdd:cd14158 168 -EKFSQTIMTERI--VGTTAYMAPEA---LRGE-ITPKSDIFSFGVVLLEIITGLPPVDENR 222
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
144-305 2.26e-08

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: 55.43  E-value: 2.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 144 KKLQtgftEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGgNYVLCDFGSATNKF-LNPQKDGVNvveeeiK 222
Cdd:cd14022  79 KKLR----EEEAARLFYQIASAVAHCHD--GGLVLRDLKLRKFVFKDE-ERTRVKLESLEDAYiLRGHDDSLS------D 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 223 KYTTLSYRAPEMINL---YGGKpittKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPDNsrYSRNIHCLI 294
Cdd:cd14022 146 KHGCPAYVSPEILNTsgsYSGK----AADVWSLGVMLYTMLVGRYPFHDIEPSslfskIRRGQFNIPET--LSPKAKCLI 219
                       170
                ....*....|.
gi 38787904 295 RFMLEPDPEHR 305
Cdd:cd14022 220 RSILRREPSER 230
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
93-266 2.32e-08

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: 55.81  E-value: 2.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14184  47 ENEVSILRRVK-HPNIIMLIEEM-----DTPAELYLVMELVKGGDLFDAITS--STKYTERDASAMVYNLASALKYLHGL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILL----NDGGNYVLCDFGSATnkflnpqkdgvnVVEEEIkkYT---TLSYRAPEMINLYGgkpITT 245
Cdd:cd14184 119 C--IVHRDIKPENLLVceypDGTKSLKLGDFGLAT------------VVEGPL--YTvcgTPTYVAPEIIAETG---YGL 179
                       170       180
                ....*....|....*....|..
gi 38787904 246 KADIWALGCLLY-KLCFFTlPF 266
Cdd:cd14184 180 KVDIWAAGVITYiLLCGFP-PF 200
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
50-260 2.67e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 55.91  E-value: 2.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGiRCALKrmyVNNMPDLNVCKREITIMKE-LSGHKNIVGYL--DCAVNSISDNVWev 126
Cdd:cd14142   6 QITLVECIGKGRYGEVWRGQWQGE-SVAVK---IFSSRDEKSWFRETEIYNTvLLRHENILGFIasDMTSRNSCTQLW-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 lILMEYCRAGQVVNQMNKklqTGFTEPEVLQIFCDTCEAVARLH------QCKTPIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd14142  80 -LITHYHENGSLYDYLQR---TTLDHQEMLRLALSAASGLVHLHteifgtQGKPAIAHRDLKSKNILVKSNGQCCIADLG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 201 SATNKflNPQKDGVNVVEEeiKKYTTLSYRAPEMINlyggKPITT-------KADIWALGCLLYKLC 260
Cdd:cd14142 156 LAVTH--SQETNQLDVGNN--PRVGTKRYMAPEVLD----ETINTdcfesykRVDIYAFGLVLWEVA 214
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
54-311 3.15e-08

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: 55.42  E-value: 3.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFSTV-FLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDcavnSISDNVWEVLILmEY 132
Cdd:cd14174   7 DELLGEGAYAKVqGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQGNKNILELIE----FFEDDTRFYLVF-EK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLN--DGGNYV-LCDFGSATNKFLNP 209
Cdd:cd14174  82 LRGGSILAHIQK--RKHFNEREASRVVRDIASALDFLHT--KGIAHRDLKPENILCEspDKVSPVkICDFDLGSGVKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 210 QKDGVNvVEEEIKKYTTLSYRAPEMINLYGGKPI--TTKADIWALGCLLYKLCFFTLPF--------GESQVAIC----- 274
Cdd:cd14174 158 ACTPIT-TPELTTPCGSAEYMAPEVVEVFTDEATfyDKRCDLWSLGVILYIMLSGYPPFvghcgtdcGWDRGEVCrvcqn 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 275 -------DGNFTIPDN--SRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14174 237 klfesiqEGKYEFPDKdwSHISSEAKDLISKLLVRDAKERLSAAQV 282
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
93-311 3.26e-08

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: 55.39  E-value: 3.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAvnsisDNVWEVLILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQC 172
Cdd:cd14183  52 QNEVSILRRVK-HPNIVLLIEEM-----DMPTELYLVMELVKGGDLFDAITST--NKYTERDASGMLYNLASAIKYLHSL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 173 KtpIIHRDLKVENILL---NDGGNYV-LCDFGSATnkflnpqkdgvnVVEEEIkkYT---TLSYRAPEMINLYGgkpITT 245
Cdd:cd14183 124 N--IVHRDIKPENLLVyehQDGSKSLkLGDFGLAT------------VVDGPL--YTvcgTPTYVAPEIIAETG---YGL 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 246 KADIWALGCLLY-KLCFFTlPF---GESQVAICDG------NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14183 185 KVDIWAAGVITYiLLCGFP-PFrgsGDDQEVLFDQilmgqvDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQV 259
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
55-260 3.60e-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: 55.36  E-value: 3.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIrCALKRMYVNNMPDLnvcKREITIMK-ELSGHKNIVGYLDCAVNSiSDNVWEVLILMEYC 133
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEK-VAVKIFSSRDEDSW---FRETEIYQtVMLRHENILGFIAADIKS-TGSWTQLWLITEYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVVNQmnkkLQTG-FTEPEVLQIFCDTCEAVARLH------QCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKf 206
Cdd:cd14056  76 EHGSLYDY----LQRNtLDTEEALRLAYSAASGLAHLHteivgtQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRY- 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 207 lnpqKDGVNVVEEEI-KKYTTLSYRAPEMINlyggKPITTK-------ADIWALGCLLYKLC 260
Cdd:cd14056 151 ----DSDTNTIDIPPnPRVGTKRYMAPEVLD----DSINPKsfesfkmADIYSFGLVLWEIA 204
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
128-323 3.84e-08

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: 55.06  E-value: 3.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQmnkkLQTG-FTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATnkf 206
Cdd:cd06640  79 IIMEYLGGGSALDL----LRAGpFDEFQIATMLKEILKGLDYLHSEKK--IHRDIKAANVLLSEQGDVKLADFGVAG--- 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgvNVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPfgESQVAICDGNFTIPDN 283
Cdd:cd06640 150 --------QLTDTQIKRNTfvgTPFWMAPEVIQ---QSAYDSKADIWSLGITAIELAKGEPP--NSDMHPMRVLFLIPKN 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 284 S------RYSRNIHCLIRFMLEPDPEHRPDIFQVsyFAFKFAKKDC 323
Cdd:cd06640 217 NpptlvgDFSKPFKEFIDACLNKDPSFRPTAKEL--LKHKFIVKNA 260
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
46-259 3.89e-08

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: 54.89  E-value: 3.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKrEITIMKELSgHKNIVGYLdcavnSISDNVWE 125
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIE-EAKVMMNLS-HEKLVQLY-----GVCTKQRP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMnKKLQTGFTEPEVLQIFCDTCEAVARL--HQcktpIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd05113  74 IFIITEYMANGCLLNYL-REMRKRFQTQQLLEMCKDVCEAMEYLesKQ----FLHRDLAARNCLVNDQGVVKVSDFGLSR 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 204 nkflnpqkdgvNVVEEEikkYTT-------LSYRAPEMInLYggKPITTKADIWALGCLLYKL 259
Cdd:cd05113 149 -----------YVLDDE---YTSsvgskfpVRWSPPEVL-MY--SKFSSKSDVWAFGVLMWEV 194
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
129-311 4.07e-08

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 55.64  E-value: 4.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQvvnqMNKKLQTGFTEPEVLQIFC-DTCEAVARLHqcKTPIIHRDLKVENILLNDG-GNYVL--CDFGSA-- 202
Cdd:cd13977 113 VMEFCDGGD----MNEYLLSRRPDRQTNTSFMlQLSSALAFLH--RNQIVHRDLKPDNILISHKrGEPILkvADFGLSkv 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 -TNKFLNPQKDgVNVVEEEIKKYT-TLSYRAPEminLYGGKpITTKADIWALGCLLY----KLCFF-------------- 262
Cdd:cd13977 187 cSGSGLNPEEP-ANVNKHFLSSACgSDFYMAPE---VWEGH-YTAKADIFALGIIIWamveRITFRdgetkkellgtyiq 261
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 263 ----TLPFGESQVAICDGNFTIPDNSRYSRN--IHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd13977 262 qgkeIVPLGEALLENPKLELQIPLKKKKSMNddMKQLLRDMLAANPQERPDAFQL 316
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
46-266 4.21e-08

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: 55.80  E-value: 4.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRC----ALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSIsd 121
Cdd:cd05617  12 LGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIyamkVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTS-- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 nvwEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGS 201
Cdd:cd05617  90 ---RLFLVIEYVNGGDLMFHMQR--QRKLPEEHARFYAAEICIALNFLHE--RGIIYRDLKLDNVLLDADGHIKLTDYGM 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 202 AtnkflnpqKDGVNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05617 163 C--------KEGLGPGDTTSTFCGTPNYIAPEILR---GEEYGFSVDWWALGVLMFEMMAGRSPF 216
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
48-259 4.58e-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: 54.72  E-value: 4.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMpDLNVCKREITIMKELSGHKNIVGYldcAVNSISDNVWEVL 127
Cdd:cd05068   7 RKSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTM-DPEDFLREAQIMKKLRHPKLIQLY---AVCTLEEPIYIIT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKLQTgftePEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATnkfl 207
Cdd:cd05068  83 ELMKHGSLLEYLQGKGRSLQL----PQLIDMAAQVASGMAYLES--QNYIHRDLAARNVLVGENNICKVADFGLAR---- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 208 npqkdgVNVVEEEikkYTT-------LSYRAPEMINLyggKPITTKADIWALGCLLYKL 259
Cdd:cd05068 153 ------VIKVEDE---YEAregakfpIKWTAPEAANY---NRFSIKSDVWSFGILLTEI 199
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
68-256 4.66e-08

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: 55.45  E-value: 4.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  68 VRTHGGIRCALKRMyVNNMPDLNVCKR---EITIMKELSgHKNIVGYLDC----AVNSISDNVWEVLILMEyCRAGQVVN 140
Cdd:cd07855  25 IDTKSGQKVAIKKI-PNAFDVVTTAKRtlrELKILRHFK-HDNIIAIRDIlrpkVPYADFKDVYVVLDLME-SDLHHIIH 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 141 QmNKKLQTGFTEPEVLQIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtNKFLNPQKDGVNVVEEE 220
Cdd:cd07855 102 S-DQPLTLEHIRYFLYQLLR----GLKYIHSAN--VIHRDLKPSNLLVNENCELKIGDFGMA-RGLCTSPEEHKYFMTEY 173
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 38787904 221 IkkyTTLSYRAPEMINLYGGKpiTTKADIWALGCLL 256
Cdd:cd07855 174 V---ATRWYRAPELMLSLPEY--TQAIDMWSVGCIF 204
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
57-256 5.70e-08

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: 54.86  E-value: 5.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRC-ALKrMYVNNMPDLNVCKREITIMKEL-----SGHKNIVGYLD--------CAVNSI-SD 121
Cdd:cd14210  21 LGKGSFGQVVKCLDHKTGQLvAIK-IIRNKKRFHQQALVEVKILKHLndndpDDKHNIVRYKDsfifrghlCIVFELlSI 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 122 NVWEVLilmeycragqvvnqMNKKLQtGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL--NDGGNYVLCDF 199
Cdd:cd14210 100 NLYELL--------------KSNNFQ-GLSLSLIRKFAKQILQALQFLHKLN--IIHCDLKPENILLkqPSKSSIKVIDF 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSATnkFLNPqkdgvnvveeeiKKYTTLS---YRAPEMInLygGKPITTKADIWALGCLL 256
Cdd:cd14210 163 GSSC--FEGE------------KVYTYIQsrfYRAPEVI-L--GLPYDTAIDMWSLGCIL 205
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
129-266 6.19e-08

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: 55.02  E-value: 6.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkfln 208
Cdd:cd05602  86 VLDYINGGELFYHLQR--ERCFLEPRARFYAAEIASALGYLHSLN--IVYRDLKPENILLDSQGHIVLTDFG-------- 153
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 209 pqkdgvnVVEEEIKKYTTLS-------YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05602 154 -------LCKENIEPNGTTStfcgtpeYLAPEVLH---KQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
57-305 6.64e-08

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: 55.01  E-value: 6.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHggircALKRMYVnnmpdLNVCKREITIMKELSGH--------KNIVGYLDCAVNSISDNVWEVLI 128
Cdd:cd05595   3 LGKGTFGKVILVREK-----ATGRYYA-----MKILRKEVIIAKDEVAHtvtesrvlQNTRHPFLTALKYAFQTHDRLCF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkfln 208
Cdd:cd05595  73 VMEYANGGELFFHLSR--ERVFTEDRARFYGAEIVSALEYLHS--RDVVYRDIKLENLMLDKDGHIKITDFGLC------ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pqKDGVNvVEEEIKKYT-TLSYRAPEMI--NLYGgkpitTKADIWALGCLLYKLCFFTLPFgESQVAICDGNFTIPDNSR 285
Cdd:cd05595 143 --KEGIT-DGATMKTFCgTPEYLAPEVLedNDYG-----RAVDWWGLGVVMYEMMCGRLPF-YNQDHERLFELILMEEIR 213
                       250       260
                ....*....|....*....|....
gi 38787904 286 YSRNI----HCLIRFMLEPDPEHR 305
Cdd:cd05595 214 FPRTLspeaKSLLAGLLKKDPKQR 237
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
57-253 7.71e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 54.36  E-value: 7.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDL-NVCKREITIMKELSGhKNIVGYLDCAVnsiSDNvwEVLILMEYCR 134
Cdd:cd06615   9 LGAGNGGVVTKVLhRPSGLIMARKLIHLEIKPAIrNQIIRELKVLHECNS-PYIVGFYGAFY---SDG--EISICMEHMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 135 AG---QVVNQMNKKlqtgftePEvlQIFCDTCEAVAR----LHQcKTPIIHRDLKVENILLNDGGNYVLCDFG------- 200
Cdd:cd06615  83 GGsldQVLKKAGRI-------PE--NILGKISIAVLRgltyLRE-KHKIMHRDVKPSNILVNSRGEIKLCDFGvsgqlid 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 38787904 201 SATNKFLNpqkdgvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALG 253
Cdd:cd06615 153 SMANSFVG-----------------TRSYMSPERLQ---GTHYTVQSDIWSLG 185
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
95-264 7.97e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 54.42  E-value: 7.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDCAVNSISDnvweVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKT 174
Cdd:cd05054  60 ELKILIHIGHHLNVVNLLGACTKPGGP----LMVIVEFCKFGNLSNYLRSKREEFVPYRDKGARDVEEEEDDDELY--KE 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PI------------------------IHRDLKVENILLNDGGNYVLCDFGSATNKFLNPqkDGVNVVEEEIKkyttLSYR 230
Cdd:cd05054 134 PLtledlicysfqvargmeflasrkcIHRDLAARNILLSENNVVKICDFGLARDIYKDP--DYVRKGDARLP----LKWM 207
                       170       180       190
                ....*....|....*....|....*....|....
gi 38787904 231 APEMINlygGKPITTKADIWALGCLLYKLcfFTL 264
Cdd:cd05054 208 APESIF---DKVYTTQSDVWSFGVLLWEI--FSL 236
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
128-321 8.05e-08

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: 54.31  E-value: 8.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQmnkkLQTG-FTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATnkf 206
Cdd:cd06641  79 IIMEYLGGGSALDL----LEPGpLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLSEHGEVKLADFGVAG--- 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpqkdgvNVVEEEIKK---YTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPfgESQVAICDGNFTIPDN 283
Cdd:cd06641 150 --------QLTDTQIKRn*fVGTPFWMAPEVIK---QSAYDSKADIWSLGITAIELARGEPP--HSELHPMKVLFLIPKN 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 38787904 284 S------RYSRNIHCLIRFMLEPDPEHRPDIFQV--SYFAFKFAKK 321
Cdd:cd06641 217 NpptlegNYSKPLKEFVEACLNKEPSFRPTAKELlkHKFILRNAKK 262
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
128-294 8.27e-08

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: 55.01  E-value: 8.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMnkklqTGFTEPEVLQIFCdTCEAVARLHQCKT-PIIHRDLKVENILLNDGGNYVLCDFGSAtnkf 206
Cdd:cd05622 150 MVMEYMPGGDLVNLM-----SNYDVPEKWARFY-TAEVVLALDAIHSmGFIHRDVKPDNMLLDKSGHLKLADFGTC---- 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 LNPQKDGVNVVEEEIKkytTLSYRAPEMINLYGGKPITTK-ADIWALGCLLYKLCFFTLPF-------GESQVAICDGNF 278
Cdd:cd05622 220 MKMNKEGMVRCDTAVG---TPDYISPEVLKSQGGDGYYGReCDWWSVGVFLYEMLVGDTPFyadslvgTYSKIMNHKNSL 296
                       170
                ....*....|....*.
gi 38787904 279 TIPDNSRYSRNIHCLI 294
Cdd:cd05622 297 TFPDDNDISKEAKNLI 312
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
165-305 8.97e-08

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: 54.50  E-value: 8.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATnkfLNPQKDGvnvveeeiKKYT---TLSYRAPEMINLYGgk 241
Cdd:cd05585 106 ALECLH--KFNVIYRDLKPENILLDYTGHIALCDFGLCK---LNMKDDD--------KTNTfcgTPEYLAPELLLGHG-- 170
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 242 pITTKADIWALGCLLYKLCFFTLPFGESQV-----AICDGNFTIPDNSRysRNIHCLIRFMLEPDPEHR 305
Cdd:cd05585 171 -YTKAVDWWTLGVLLYEMLTGLPPFYDENTnemyrKILQEPLRFPDGFD--RDAKDLLIGLLNRDPTKR 236
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
46-283 1.43e-07

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 53.50  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVF------LVRTHGGIRCALKRMYVN-NMPDLNVCKREITIMKELSGHkNIVGYLdcavnS 118
Cdd:cd05032   3 LPREKITLIRELGQGSFGMVYeglakgVVKGEPETRVAIKTVNENaSMRERIEFLNEASVMKEFNCH-HVVRLL-----G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 119 ISDNVWEVLILMEYCRAGQVVN----QMNKKLQTGFTEP----EVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLND 190
Cdd:cd05032  77 VVSTGQPTLVVMELMAKGDLKSylrsRRPEAENNPGLGPptlqKFIQMAAEIADGMAYLAAKK--FVHRDLAARNCMVAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 191 GGNYVLCDFGSATNKFLNP--QKDGvnvveeeiKKYTTLSYRAPEmiNLYGGKpITTKADIWALGCLLYKLCFF-TLPF- 266
Cdd:cd05032 155 DLTVKIGDFGMTRDIYETDyyRKGG--------KGLLPVRWMAPE--SLKDGV-FTTKSDVWSFGVVLWEMATLaEQPYq 223
                       250       260
                ....*....|....*....|..
gi 38787904 267 GES--QVA--ICDGNF-TIPDN 283
Cdd:cd05032 224 GLSneEVLkfVIDGGHlDLPEN 245
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
94-259 1.67e-07

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: 53.52  E-value: 1.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVW--------EVLILMEYCRAGQVvNQMNKKLQTGFTEPEVLQIFcdtcEA 165
Cdd:cd07868  63 REIALLRELK-HPNVISLQKVFLSHADRKVWllfdyaehDLWHIIKFHRASKA-NKKPVQLPRGMVKSLLYQIL----DG 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 166 VARLHqcKTPIIHRDLKVENIL-LNDG---GNYVLCDFGSAT--NKFLNPQKDGVNVVeeeikkyTTLSYRAPEMinLYG 239
Cdd:cd07868 137 IHYLH--ANWVLHRDLKPANILvMGEGperGRVKIADMGFARlfNSPLKPLADLDPVV-------VTFWYRAPEL--LLG 205
                       170       180
                ....*....|....*....|
gi 38787904 240 GKPITTKADIWALGCLLYKL 259
Cdd:cd07868 206 ARHYTKAIDIWAIGCIFAEL 225
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
94-306 1.75e-07

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: 53.49  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSisDNVWevlILMEYC--RAGQVVNQMNKKLQtgftEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd06634  64 KEVKFLQKLR-HPNTIEYRGCYLRE--HTAW---LVMEYClgSASDLLEVHKKPLQ----EVEIAAITHGALQGLAYLHS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkFLNPQKDGVNvveeeikkytTLSYRAPEMINLYGGKPITTKADIWA 251
Cdd:cd06634 134 HN--MIHRDVKAGNILLTEPGLVKLGDFGSAS--IMAPANSFVG----------TPYWMAPEVILAMDEGQYDGKVDVWS 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 252 LGCLLYKLC-----FFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd06634 200 LGITCIELAerkppLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRP 259
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
94-253 1.77e-07

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: 53.52  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSisDNVWevlILMEYC--RAGQVVNQMNKKLQtgftEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd06635  74 KEVKFLQRIK-HPNSIEYKGCYLRE--HTAW---LVMEYClgSASDLLEVHKKPLQ----EIEIAAITHGALQGLAYLHS 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkFLNPQKDGVNvveeeikkytTLSYRAPEMINLYGGKPITTKADIWA 251
Cdd:cd06635 144 HN--MIHRDIKAGNILLTEPGQVKLADFGSAS--IASPANSFVG----------TPYWMAPEVILAMDEGQYDGKVDVWS 209

                ..
gi 38787904 252 LG 253
Cdd:cd06635 210 LG 211
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
49-308 1.81e-07

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: 52.80  E-value: 1.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  49 HQVTLEESLAEGGFSTVFlvrthGGI-RCALKRMYVNNMPDLNV-------CKREITIMKELSgHKNIVgyldcavnsIS 120
Cdd:cd14082   3 YQIFPDEVLGSGQFGIVY-----GGKhRKTGRDVAIKVIDKLRFptkqesqLRNEVAILQQLS-HPGVV---------NL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 121 DNVWE----VLILMEYCRAGQ---VVNQMNKKLQTGFTEPEVLQIFCdtceAVARLHqcKTPIIHRDLKVENILLNDGGN 193
Cdd:cd14082  68 ECMFEtperVFVVMEKLHGDMlemILSSEKGRLPERITKFLVTQILV----ALRYLH--SKNIVHCDLKPENVLLASAEP 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 194 Y---VLCDFGSAtnKFLNPQKDGVNVVeeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFGES- 269
Cdd:cd14082 142 FpqvKLCDFGFA--RIIGEKSFRRSVV-------GTPAYLAPEVLR---NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDe 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 38787904 270 --QVAICDGNFTIPDN--SRYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd14082 210 diNDQIQNAAFMYPPNpwKEISPDAIDLINNLLQVKMRKRYSV 252
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
157-300 1.86e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 54.31  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  157 QIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnKFLNPQkdgvnvVEEEIKKYTTLSYRAPEMIN 236
Cdd:PHA03210 275 QLLC----AVEYIHDKK--LIHRDIKLENIFLNCDGKIVLGDFGTAM-PFEKER------EAFDYGWVGTVATNSPEILA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  237 LYGGKPITtkaDIWALG-CLLYKLCFFTLPFGES-------------QVAICDGNFTIP--------DNSRYSRNIHC-- 292
Cdd:PHA03210 342 GDGYCEIT---DIWSCGlILLDMLSHDFCPIGDGggkpgkqllkiidSLSVCDEEFPDPpcklfdyiDSAEIDHAGHSvp 418

                 ....*....
gi 38787904  293 -LIRFMLEP 300
Cdd:PHA03210 419 pLIRNLGLP 427
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
60-266 1.89e-07

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: 53.21  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVR-THGGIRCALKRMYVNNMPDLNV---CKREITIMKELSgHKNIVGyLDCAvnsiSDNVWEVLILMEYCRA 135
Cdd:cd05612  12 GTFGRVHLVRdRISEHYYALKVMAIPEVIRLKQeqhVHNEKRVLKEVS-HPFIIR-LFWT----EHDQRFLYMLMEYVPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKL----QTG-FTEPEvlqIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpq 210
Cdd:cd05612  86 GELFSYLRNSGrfsnSTGlFYASE---IVC----ALEYLHSKE--IVYRDLKPENILLDKEGHIKLTDFGFAK------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 211 kdgvnvvEEEIKKYT---TLSYRAPEMInlyGGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05612 150 -------KLRDRTWTlcgTPEYLAPEVI---QSKGHNKAVDWWALGILIYEMLVGYPPF 198
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
94-259 1.94e-07

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: 53.45  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDC-----AVNSISDnVWEVLILMeycraGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVAR 168
Cdd:cd07851  63 RELRLLKHMK-HENVIGLLDVftpasSLEDFQD-VYLVTHLM-----GADLNNIVK--CQKLSDDHIQFLVYQILRGLKY 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKflnpqkdgvnvvEEEIKKY-TTLSYRAPEMINLYGGkpITTKA 247
Cdd:cd07851 134 IHSAG--IIHRDLKPSNLAVNEDCELKILDFGLARHT------------DDEMTGYvATRWYRAPEIMLNWMH--YNQTV 197
                       170
                ....*....|..
gi 38787904 248 DIWALGCLLYKL 259
Cdd:cd07851 198 DIWSVGCIMAEL 209
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
57-266 2.04e-07

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: 53.55  E-value: 2.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHggircALKRMYVnnmpdLNVCKREITIMKELSGH--------KNIVGYLDCAVNSISDNVWEVLI 128
Cdd:cd05593  23 LGKGTFGKVILVREK-----ASGKYYA-----MKILKKEVIIAKDEVAHtltesrvlKNTRHPFLTSLKYSFQTKDRLCF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkfln 208
Cdd:cd05593  93 VMEYVNGGELFFHLSR--ERVFSEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLMLDKDGHIKITDFGLC------ 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pqKDGVNVVEEEIKKYTTLSYRAPEMI--NLYGgkpitTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05593 163 --KEGITDAATMKTFCGTPEYLAPEVLedNDYG-----RAVDWWGLGVVMYEMMCGRLPF 215
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
57-306 2.21e-07

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 52.89  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLV--RTHGGIrcALKRMYVNnmPDLNVCKR----EITIMKELSgHKNIVGYLDCAvnsISDNVWEvlILM 130
Cdd:cd14027   1 LDSGGFGKVSLCfhRTQGLV--VLKTVYTG--PNCIEHNEalleEGKMMNRLR-HSRVVKLLGVI---LEEGKYS--LVM 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVnQMNKKLQTGFTEPEvlQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQ 210
Cdd:cd14027  71 EYMEKGNLM-HVLKKVSVPLSVKG--RIILEIIEGMAYLH--GKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 211 KDGVNVVEEEIKKYT-----TLSYRAPEMINLYGGKPiTTKADIWALGCLLYKLCFFTLPF----GESQV--AICDGNF- 278
Cdd:cd14027 146 TKEEHNEQREVDGTAkknagTLYYMAPEHLNDVNAKP-TEKSDVYSFAIVLWAIFANKEPYenaiNEDQIimCIKSGNRp 224
                       250       260       270
                ....*....|....*....|....*....|.
gi 38787904 279 ---TIPDNSrySRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14027 225 dvdDITEYC--PREIIDLMKLCWEANPEARP 253
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
94-259 2.29e-07

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: 53.13  E-value: 2.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSIS----DNVWEVLILMeycraGQVVNQMNK--KLQTGFTEPEVLQIFcdtcEAVA 167
Cdd:cd07878  63 RELRLLKHMK-HENVIGLLDVFTPATSienfNEVYLVTNLM-----GADLNNIVKcqKLSDEHVQFLIYQLL----RGLK 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 168 RLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpQKDgvnvveEEIKKY-TTLSYRAPE-MINLYGgkpITT 245
Cdd:cd07878 133 YIHSAG--IIHRDLKPSNVAVNEDCELRILDFGLAR------QAD------DEMTGYvATRWYRAPEiMLNWMH---YNQ 195
                       170
                ....*....|....
gi 38787904 246 KADIWALGCLLYKL 259
Cdd:cd07878 196 TVDIWSVGCIMAEL 209
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
177-264 2.69e-07

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 53.08  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKFLNPqkdgvnvveEEIKKYTT---LSYRAPEMINlygGKPITTKADIWALG 253
Cdd:cd14207 202 IHRDLAARNILLSENNVVKICDFGLARDIYKNP---------DYVRKGDArlpLKWMAPESIF---DKIYSTKSDVWSYG 269
                        90
                ....*....|.
gi 38787904 254 CLLYKLcfFTL 264
Cdd:cd14207 270 VLLWEI--FSL 278
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
95-308 3.10e-07

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: 52.69  E-value: 3.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIV---GYLDCAVNSISDNVWEVLilmEYCRAGQVVNQMNKKLQTG--FTEPEVLQIFCDTCEAVARL 169
Cdd:cd06639  68 EYNILRSLPNHPNVVkfyGMFYKADQYVGGQLWLVL---ELCNGGSVTELVKGLLKCGqrLDEAMISYILYGALLGLQHL 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 170 HQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdgvNVVEEEIKKYTTLS---YRAPEMINLYGGKPIT-- 244
Cdd:cd06639 145 HNNR--IIHRDVKGNNILLTTEGGVKLVDFGVSA-----------QLTSARLRRNTSVGtpfWMAPEVIACEQQYDYSyd 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 245 TKADIWALGCLLYKLCFFTLPFGESQVAicDGNFTIPDN--------SRYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd06639 212 ARCDVWSLGITAIELADGDPPLFDMHPV--KALFKIPRNppptllnpEKWCRGFSHFISQCLIKDFEKRPSV 281
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
50-266 3.28e-07

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 52.32  E-value: 3.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKElSGHKNIVGYLDCAVNSIsdnvwEVLIL 129
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQ-TRHENVVLFMGACMSPP-----HLAII 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRaGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLnDGGNYVLCDFGSATNKFL-- 207
Cdd:cd14153  75 TSLCK-GRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLH--AKGILHKDLKSKNVFY-DNGKVVITDFGLFTISGVlq 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 208 -NPQKDGVNVveeeikKYTTLSYRAPEMINLYGGK------PITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd14153 151 aGRREDKLRI------QSGWLCHLAPEIIRQLSPEteedklPFSKHSDVFAFGTIWYELHAREWPF 210
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
120-321 3.47e-07

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 52.37  E-value: 3.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWevlILMEYCRAGQVVNQmnkkLQTG-FTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCD 198
Cdd:cd06642  74 GTKLW---IIMEYLGGGSALDL----LKPGpLEETYIATILREILKGLDYLHSERK--IHRDIKAANVLLSEQGDVKLAD 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 199 FGSATnkflnpqkdgvNVVEEEIKKYT---TLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPFgeSQVAICD 275
Cdd:cd06642 145 FGVAG-----------QLTDTQIKRNTfvgTPFWMAPEVIK---QSAYDFKADIWSLGITAIELAKGEPPN--SDLHPMR 208
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 276 GNFTIPDNS------RYSRNIHCLIRFMLEPDPEHRPDIFQV--SYFAFKFAKK 321
Cdd:cd06642 209 VLFLIPKNSpptlegQHSKPFKEFVEACLNKDPRFRPTAKELlkHKFITRYTKK 262
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
169-305 3.51e-07

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: 52.39  E-value: 3.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvNVVEEeiKKYTTL----SYRAPEMINlygGKPIT 244
Cdd:cd05592 112 LH--SRGIIYRDLKLDNVLLDREGHIKIADFGMCKE----------NIYGE--NKASTFcgtpDYIAPEILK---GQKYN 174
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 245 TKADIWALGCLLYKLCFFTLPF---GESQV--AICDGNFTIPdnsRY-SRNIHCLIRFMLEPDPEHR 305
Cdd:cd05592 175 QSVDWWSFGVLLYEMLIGQSPFhgeDEDELfwSICNDTPHYP---RWlTKEAASCLSLLLERNPEKR 238
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
93-266 4.49e-07

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: 51.95  E-value: 4.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKeLSGHKNIVGYLDcavnsISDNVWEVLILMEYCRAGQVVNQMnkkLQTGF-TEPEVLQIFCDTCEAVARLHQ 171
Cdd:cd14088  47 KNEINILK-MVKHPNILQLVD-----VFETRKEYFIFLELATGREVFDWI---LDQGYySERDTSNVIRQVLEAVAYLHS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKtpIIHRDLKVENILLND---GGNYVLCDFGSAtnkflnpqKDGVNVVEEEIKkytTLSYRAPEMI--NLYgGKPIttk 246
Cdd:cd14088 118 LK--IVHRNLKLENLVYYNrlkNSKIVISDFHLA--------KLENGLIKEPCG---TPEYLAPEVVgrQRY-GRPV--- 180
                       170       180
                ....*....|....*....|
gi 38787904 247 aDIWALGCLLYKLCFFTLPF 266
Cdd:cd14088 181 -DCWAIGVIMYILLSGNPPF 199
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
94-266 4.60e-07

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 51.84  E-value: 4.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVgYLDCAVNSISdnvwEVLILMEYCRAGQVVNqmNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14110  48 REYQVLRRLS-HPRIA-QLHSAYLSPR----HLVLIEELCSGPELLY--NLAERNSYSEAEVTDYLWQILSAVDYLHSRR 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 tpIIHRDLKVENILLNDGGNYVLCDFGSAtnKFLNPQKdgvnVVEEEIKKYTTLSyRAPEMINLYGGKPITtkaDIWALG 253
Cdd:cd14110 120 --ILHLDLRSENMIITEKNLLKIVDLGNA--QPFNQGK----VLMTDKKGDYVET-MAPELLEGQGAGPQT---DIWAIG 187
                       170
                ....*....|...
gi 38787904 254 CLLYKLCFFTLPF 266
Cdd:cd14110 188 VTAFIMLSADYPV 200
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
129-270 4.66e-07

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: 52.31  E-value: 4.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNkklQTG-FTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFL 207
Cdd:cd05615  89 VMEYVNGGDLMYHIQ---QVGkFKEPQAVFYAAEISVGLFFLH--KKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMV 163
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 208 npqkDGVNVVEeeikKYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKLCFFTLPF-GESQ 270
Cdd:cd05615 164 ----EGVTTRT----FCGTPDYIAPEIIAY---QPYGRSVDWWAYGVLLYEMLAGQPPFdGEDE 216
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
48-315 5.23e-07

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: 52.34  E-value: 5.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEES-----LAEGGFSTVFLVRTHggircALKRMYVnnmpdLNVCKREITIMKELSGH---KNIV------GYLD 113
Cdd:cd05594  19 KHKVTMNDFeylklLGKGTFGKVILVKEK-----ATGRYYA-----MKILKKEVIVAKDEVAHtltENRVlqnsrhPFLT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 114 CAVNSISDNVwEVLILMEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKTpIIHRDLKVENILLNDGGN 193
Cdd:cd05594  89 ALKYSFQTHD-RLCFVMEYANGGELFFHLSR--ERVFSEDRARFYGAEIVSALDYLHSEKN-VVYRDLKLENLMLDKDGH 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 194 YVLCDFGSATNKFlnpqKDGVNvveeeIKKYT-TLSYRAPEMI--NLYGgkpitTKADIWALGCLLYKLCFFTLPF-GES 269
Cdd:cd05594 165 IKITDFGLCKEGI----KDGAT-----MKTFCgTPEYLAPEVLedNDYG-----RAVDWWGLGVVMYEMMCGRLPFyNQD 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 270 QVAICDgnFTIPDNSRYSRNI----HCLIRFMLEPDPEHR--------PDIFQVSYFA 315
Cdd:cd05594 231 HEKLFE--LILMEEIRFPRTLspeaKSLLSGLLKKDPKQRlgggpddaKEIMQHKFFA 286
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
163-259 5.24e-07

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: 52.32  E-value: 5.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 163 CEAVARLHQCKTPIIHRDLKVENILL-NDGGNYV-LCDFGSATNkflnpqkdgvnvVEEEIKKY-TTLSYRAPEMINlyg 239
Cdd:cd14226 126 CTALLFLSTPELSIIHCDLKPENILLcNPKRSAIkIIDFGSSCQ------------LGQRIYQYiQSRFYRSPEVLL--- 190
                        90       100
                ....*....|....*....|
gi 38787904 240 GKPITTKADIWALGCLLYKL 259
Cdd:cd14226 191 GLPYDLAIDMWSLGCILVEM 210
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
46-259 5.33e-07

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 51.57  E-value: 5.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMpDLNVCKREITIMKELSgHKNIVgYLDCAVNSisdnvWE 125
Cdd:cd05073   8 IPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSM-SVEAFLAEANVMKTLQ-HDKLV-KLHAVVTK-----EP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnk 205
Cdd:cd05073  80 IYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQ--RNYIHRDLRAANILVSASLVCKIADFGLA--- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 206 flNPQKDGVNVVEEEIKkyTTLSYRAPEMINlYGGkpITTKADIWALGCLLYKL 259
Cdd:cd05073 155 --RVIEDNEYTAREGAK--FPIKWTAPEAIN-FGS--FTIKSDVWSFGILLMEI 201
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
161-306 5.33e-07

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 51.50  E-value: 5.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 161 DTCEAVARLHQCKtpIIHRDLKVENILLN-----------DGGNYVLCDFGSATNKFL-NPQkdgvnvveeeikkyttls 228
Cdd:cd14115  97 DIMEALQYLHNCR--VAHLDIKPENLLIDlripvprvkliDLEDAVQISGHRHVHHLLgNPE------------------ 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 229 YRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-----GESQVAICDGNFTIPDN--SRYSRNIHCLIRFMLEPD 301
Cdd:cd14115 157 FAAPEVIQ---GTPVSLATDIWSIGVLTYVMLSGVSPFldeskEETCINVCRVDFSFPDEyfGDVSQAARDFINVILQED 233

                ....*
gi 38787904 302 PEHRP 306
Cdd:cd14115 234 PRRRP 238
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
57-256 5.69e-07

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: 52.09  E-value: 5.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVF-LVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSISDNVWEVLILMEYCRA 135
Cdd:cd07854  13 LGCGSNGLVFsAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLD-HDNIVKVYEVLGPSGSDLTEDVGSLTELNSV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKL-----QTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDgGNYVL--CDFGSAtnKFLN 208
Cdd:cd07854  92 YIVQEYMETDLanvleQGPLSEEHARLFMYQLLRGLKYIHSAN--VLHRDLKPANVFINT-EDLVLkiGDFGLA--RIVD 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 209 PQKDGVNVVEEEIkkyTTLSYRAPEMI---NLYggkpiTTKADIWALGCLL 256
Cdd:cd07854 167 PHYSHKGYLSEGL---VTKWYRSPRLLlspNNY-----TKAIDMWAAGCIF 209
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
130-266 6.17e-07

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: 51.97  E-value: 6.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKklQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsatnkflnp 209
Cdd:cd05571  74 MEYVNGGELFFHLSR--ERVFSEDRTRFYGAEIVLALGYLHSQG--IVYRDLKLENLLLDKDGHIKITDFG--------- 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 210 qkdgvnVVEEEIKKYTTLS-------YRAPEMI--NLYGgkpitTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05571 141 ------LCKEEISYGATTKtfcgtpeYLAPEVLedNDYG-----RAVDWWGLGVVMYEMMCGRLPF 195
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
43-306 6.35e-07

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 51.61  E-value: 6.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  43 VFAVGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKrEITIMKELSGHKNIVGYldcAVNSISdn 122
Cdd:cd05070   3 VWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLE-EAQIMKKLKHDKLVQLY---AVVSEE-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 vwEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSA 202
Cdd:cd05070  77 --PIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIE--RMNYIHRDLRSANILVGNGLICKIADFGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 tnkflnpqkdgvNVVEEeiKKYTT-------LSYRAPEMInLYGgkPITTKADIWALGCLLYKLCFF-TLPF----GESQ 270
Cdd:cd05070 153 ------------RLIED--NEYTArqgakfpIKWTAPEAA-LYG--RFTIKSDVWSFGILLTELVTKgRVPYpgmnNREV 215
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 271 VAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd05070 216 LEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERP 251
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
176-304 6.37e-07

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: 51.87  E-value: 6.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILL--NDGGNYVLCDFGSATnkflnpqkdgvnvveeeIKKYTTLS------YRAPEMINlygGKPITTKA 247
Cdd:cd14212 124 IIHCDLKPENILLvnLDSPEIKLIDFGSAC-----------------FENYTLYTyiqsrfYRSPEVLL---GLPYSTAI 183
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 248 DIWALGCLLYKLcFFTLPFgesqvaicdgnftIPDNSRYsrNIHCLIRFMLEPDPEH 304
Cdd:cd14212 184 DMWSLGCIAAEL-FLGLPL-------------FPGNSEY--NQLSRIIEMLGMPPDW 224
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
128-306 6.61e-07

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: 51.19  E-value: 6.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQvvnqMNKKLQTGFTEPEVL-------QIFCDTCEAVAR----LH-QCKTPIIHRDLKVENILL------N 189
Cdd:cd14146  70 LVMEFARGGT----LNRALAAANAAPGPRrarrippHILVNWAVQIARgmlyLHeEAVVPILHRDLKSSNILLlekiehD 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 190 DGGNYVL--CDFGSATNKFLNPQKDGVNvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF- 266
Cdd:cd14146 146 DICNKTLkiTDFGLAREWHRTTKMSAAG----------TYAWMAPEVIK---SSLFSKGSDIWSYGVLLWELLTGEVPYr 212
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 38787904 267 GESQVAICDG----NFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14146 213 GIDGLAVAYGvavnKLTLPIPSTCPEPFAKLMKECWEQDPHIRP 256
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
128-202 6.86e-07

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 49.57  E-value: 6.86e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 128 ILMEYCRaGQVVNQMnkkLQTGFTEPEVLQifcDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLcDFGSA 202
Cdd:COG3642  33 LVMEYIE-GETLADL---LEEGELPPELLR---ELGRLLARLHRAG--IVHGDLTTSNILVDDGGVYLI-DFGLA 97
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
61-259 7.19e-07

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: 51.56  E-value: 7.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  61 GFSTVFLVRTHGGIrCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVnsISDNVWevlILMEYCRAGQVVN 140
Cdd:cd06657  34 GIVCIATVKSSGKL-VAVKKMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYL--VGDELW---VVMEFLEGGALTD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 141 QMNkklQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvnvVEEE 220
Cdd:cd06657 107 IVT---HTRMNEEQIAAVCLAVLKALSVLHA--QGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ------------VSKE 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 38787904 221 IKKYTTLS----YRAPEMINLYggkPITTKADIWALGCLLYKL 259
Cdd:cd06657 170 VPRRKSLVgtpyWMAPELISRL---PYGPEVDIWSLGIMVIEM 209
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
60-307 7.23e-07

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: 51.24  E-value: 7.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFlvrtHG---GIRCALKRMYVNNMPDLNVC----KREITIMKELSgHKNIVgyldcAVNSISDNVWEVLILMEY 132
Cdd:cd14061   5 GGFGKVY----RGiwrGEEVAVKAARQDPDEDISVTlenvRQEARLFWMLR-HPNII-----ALRGVCLQPPNLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQvvnqMNKKLQTGFTEPEVLqifCDTCEAVAR----LH-QCKTPIIHRDLKVENILL------NDGGNYVL--CDF 199
Cdd:cd14061  75 ARGGA----LNRVLAGRKIPPHVL---VDWAIQIARgmnyLHnEAPVPIIHRDLKSSNILIleaienEDLENKTLkiTDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 200 GSAtnkflnpqkdgvnvveEEIKKYT------TLSYRAPEMI--NLYggkpitTKA-DIWALGCLLYKLCFFTLPF-GES 269
Cdd:cd14061 148 GLA----------------REWHKTTrmsaagTYAWMAPEVIksSTF------SKAsDVWSYGVLLWELLTGEVPYkGID 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 270 QVAICDG----NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd14061 206 GLAVAYGvavnKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPS 247
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
176-259 7.34e-07

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: 51.60  E-value: 7.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATNKflnpqkdgvNVVEEEIKKY-TTLSYRAPEMinLYGGKPITTKADIWALGC 254
Cdd:cd07858 129 VLHRDLKPSNLLLNANCDLKICDFGLARTT---------SEKGDFMTEYvVTRWYRAPEL--LLNCSEYTTAIDVWSVGC 197

                ....*
gi 38787904 255 LLYKL 259
Cdd:cd07858 198 IFAEL 202
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
126-266 7.35e-07

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: 51.45  E-value: 7.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsatnk 205
Cdd:cd05590  71 LFFVMEFVNGGDLMFHIQKSRR--FDEARARFYAAEITSALMFLHD--KGIIYRDLKLDNVLLDHEGHCKLADFG----- 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 flnpqkdgvnVVEEEIKKYTTLS-------YRAPEMIN--LYGgkpitTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05590 142 ----------MCKEGIFNGKTTStfcgtpdYIAPEILQemLYG-----PSVDWWAMGVLLYEMLCGHAPF 196
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
164-306 7.47e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 51.80  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  164 EAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNvveeeikkyTTLSYRAPEMInlyGGKPI 243
Cdd:PHA03209 168 EGLRYLHAQR--IIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLA---------GTVETNAPEVL---ARDKY 233
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38787904  244 TTKADIWALGCLLyklcFFTLPFGESqvaICDGNFTIPDNSRYSRNIHcLIRFM--LEPDPEHRP 306
Cdd:PHA03209 234 NSKADIWSAGIVL----FEMLAYPST---IFEDPPSTPEEYVKSCHSH-LLKIIstLKVHPEEFP 290
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
94-259 8.09e-07

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: 51.61  E-value: 8.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAVNSISDNVW--------EVLILMEYCRAGQVvNQMNKKLQTGFTEPEVLQIFcdtcEA 165
Cdd:cd07867  48 REIALLRELK-HPNVIALQKVFLSHSDRKVWllfdyaehDLWHIIKFHRASKA-NKKPMQLPRSMVKSLLYQIL----DG 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 166 VARLHqcKTPIIHRDLKVENIL-LNDG---GNYVLCDFGSAT--NKFLNPQKDGVNVVeeeikkyTTLSYRAPEMinLYG 239
Cdd:cd07867 122 IHYLH--ANWVLHRDLKPANILvMGEGperGRVKIADMGFARlfNSPLKPLADLDPVV-------VTFWYRAPEL--LLG 190
                       170       180
                ....*....|....*....|
gi 38787904 240 GKPITTKADIWALGCLLYKL 259
Cdd:cd07867 191 ARHYTKAIDIWAIGCIFAEL 210
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
44-266 9.18e-07

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: 50.88  E-value: 9.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  44 FAVGRHQVTLEESLAEGGFSTVflvrtHGGIrcalkrmYVNNMPD-LNV----CKREIT------------IMKELSgHK 106
Cdd:cd05056   1 YEIQREDITLGRCIGEGQFGDV-----YQGV-------YMSPENEkIAVavktCKNCTSpsvrekflqeayIMRQFD-HP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 107 NIVGYldcaVNSISDN-VWevlILMEYCRAGQvvnqMNKKLQTGFTEPEV--LQIFC-DTCEAVARLHQCKtpIIHRDLK 182
Cdd:cd05056  68 HIVKL----IGVITENpVW---IVMELAPLGE----LRSYLQVNKYSLDLasLILYAyQLSTALAYLESKR--FVHRDIA 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 183 VENILLNDGGNYVLCDFGsaTNKFLNpqkdgvnvvEEEIKKYTT----LSYRAPEMINLyggKPITTKADIWALG-CLLY 257
Cdd:cd05056 135 ARNVLVSSPDCVKLGDFG--LSRYME---------DESYYKASKgklpIKWMAPESINF---RRFTSASDVWMFGvCMWE 200

                ....*....
gi 38787904 258 KLCFFTLPF 266
Cdd:cd05056 201 ILMLGVKPF 209
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
130-305 9.73e-07

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 51.24  E-value: 9.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNkklQTG-FTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkfln 208
Cdd:cd05587  76 MEYVNGGDLMYHIQ---QVGkFKEPVAVFYAAEIAVGLFFLH--SKGIIYRDLKLDNVMLDAEGHIKIADFGMC------ 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pqKDGVNvveEEIKKYT---TLSYRAPEMInLYggKPITTKADIWALGCLLYKLCFFTLPF-GESQ----VAICDGNFTI 280
Cdd:cd05587 145 --KEGIF---GGKTTRTfcgTPDYIAPEII-AY--QPYGKSVDWWAYGVLLYEMLAGQPPFdGEDEdelfQSIMEHNVSY 216
                       170       180
                ....*....|....*....|....*
gi 38787904 281 PDNsrYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05587 217 PKS--LSKEAVSICKGLLTKHPAKR 239
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
50-266 1.19e-06

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: 50.25  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKrEITIMKELSGHKNIVGYLDCAVNSisdnvwEVLIL 129
Cdd:cd05114   5 ELTFMKELGSGLFGVVRLGKWRAQYKVAIKAIREGAMSEEDFIE-EAKVMMKLTHPKLVQLYGVCTQQK------PIYIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKKlqTGFTEPEVLQIFC-DTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsATNKFLN 208
Cdd:cd05114  78 TEFMENGCLLNYLRQR--RGKLSRDMLLSMCqDVCEGMEYLER--NNFIHRDLAARNCLVNDTGVVKVSDFG-MTRYVLD 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 209 PQKDGVNVVEEEIKkyttlsYRAPEMINLyggKPITTKADIWALGCLLYKLcfFT---LPF 266
Cdd:cd05114 153 DQYTSSSGAKFPVK------WSPPEVFNY---SKFSSKSDVWSFGVLMWEV--FTegkMPF 202
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
60-259 1.26e-06

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: 51.11  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTV-FLVRTHGGIRCALKRMYVNNMPDLNVCK--REITIMKELSgHKNIVGYLDCAVNSIS-DNVWEVLILMEYcrA 135
Cdd:cd07880  26 GAYGTVcSALDRRTGAKVAIKKLYRPFQSELFAKRayRELRLLKHMK-HENVIGLLDVFTPDLSlDRFHDFYLVMPF--M 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNK--KLQTGFTEPEVLQIFcdtcEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdg 213
Cdd:cd07880 103 GTDLGKLMKheKLSEDRIQFLVYQML----KGLKYIHAAG--IIHRDLKPGNLAVNEDCELKILDFGLARQ--------- 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 38787904 214 vnvVEEEIKKY-TTLSYRAPEMInlYGGKPITTKADIWALGCLLYKL 259
Cdd:cd07880 168 ---TDSEMTGYvVTRWYRAPEVI--LNWMHYTQTVDIWSVGCIMAEM 209
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
54-255 1.33e-06

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 50.59  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   54 EESLAEGGFSTVFLVR-THGGIRCALKRMYVNN----MPDLNVckREITIMKELSgHKNIVGYLDcavnsISDNVWEVLI 128
Cdd:PLN00009   7 VEKIGEGTYGVVYKARdRVTNETIALKKIRLEQedegVPSTAI--REISLLKEMQ-HGNIVRLQD-----VVHSEKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  129 LMEYCRAgQVVNQMNKKLQTGfTEPEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYV-LCDFGSAtNKF 206
Cdd:PLN00009  79 VFEYLDL-DLKKHMDSSPDFA-KNPRLIKTYLyQILRGIAYCHSHR--VLHRDLKPQNLLIDRRTNALkLADFGLA-RAF 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 38787904  207 LNPqkdgVNVVEEEIkkyTTLSYRAPEMinLYGGKPITTKADIWALGCL 255
Cdd:PLN00009 154 GIP----VRTFTHEV---VTLWYRAPEI--LLGSRHYSTPVDIWSVGCI 193
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
55-312 1.34e-06

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: 50.04  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTV----FLVRTHGGIRCALKRMYVNNMPDLnvcKREI----TIMKELSgHKNIVGYLDCAVNsisdnvwEV 126
Cdd:cd05060   1 KELGHGNFGSVrkgvYLMKSGKEVEVAVKTLKQEHEKAG---KKEFlreaSVMAQLD-HPCIVRLIGVCKG-------EP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 127 LIL-MEYCRAGQvvnqMNKKLQ--TGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGsaT 203
Cdd:cd05060  70 LMLvMELAPLGP----LLKYLKkrREIPVSDLKELAHQVAMGMAYLESKH--FVHRDLAARNVLLVNRHQAKISDFG--M 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 NKFLNPqkdgvnvvEEEIKKYTT-----LSYRAPEMINLYggkPITTKADIWALGCLLYK-LCFFTLPFGESQ----VAI 273
Cdd:cd05060 142 SRALGA--------GSDYYRATTagrwpLKWYAPECINYG---KFSSKSDVWSYGVTLWEaFSYGAKPYGEMKgpevIAM 210
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 38787904 274 CDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVS 312
Cdd:cd05060 211 LESGERLPRPEECPQEIYSIMLSCWKYRPEDRPTFSELE 249
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
152-305 1.36e-06

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: 49.88  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 152 EPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNvveeeiKKYTTLSYRA 231
Cdd:cd14024  83 EDEARGLFTQMARAVAHCHQ--HGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLT------DKHGCPAYVG 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 232 PEMINL---YGGKpittKADIWALGCLLYKLCFFTLPFGESQVA-----ICDGNFTIPdnSRYSRNIHCLIRFMLEPDPE 303
Cdd:cd14024 155 PEILSSrrsYSGK----AADVWSLGVCLYTMLLGRYPFQDTEPAalfakIRRGAFSLP--AWLSPGARCLVSCMLRRSPA 228

                ..
gi 38787904 304 HR 305
Cdd:cd14024 229 ER 230
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
128-292 1.37e-06

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: 51.15  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNqmnkkLQTGFTEPEVLQIFCdTCEAVARLHQCKT-PIIHRDLKVENILLNDGGNYVLCDFGSATnkf 206
Cdd:cd05621 129 MVMEYMPGGDLVN-----LMSNYDVPEKWAKFY-TAEVVLALDAIHSmGLIHRDVKPDNMLLDKYGHLKLADFGTCM--- 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 207 lnpQKDGVNVVEEEiKKYTTLSYRAPEMINLYGGKPITTK-ADIWALGCLLYKLCFFTLPF-GESQVA----ICD--GNF 278
Cdd:cd05621 200 ---KMDETGMVHCD-TAVGTPDYISPEVLKSQGGDGYYGReCDWWSVGVFLFEMLVGDTPFyADSLVGtyskIMDhkNSL 275
                       170
                ....*....|....*..
gi 38787904 279 TIPDN---SRYSRNIHC 292
Cdd:cd05621 276 NFPDDveiSKHAKNLIC 292
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
46-314 1.44e-06

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 50.46  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNM-PDLNVckREITIMKELSGHKNIVGYldcAVNSISdnvw 124
Cdd:cd05069   9 IPRESLRLDVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMmPEAFL--QEAQIMKKLRHDKLVPLY---AVVSEE---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd05069  80 PIYIVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIE--RMNYIHRDLRAANILVGDNLVCKIADFGLA-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 205 kflnpqkdgvNVVEEeiKKYTT-------LSYRAPEMInLYGgkPITTKADIWALGCLLYKLCFF-TLPF----GESQVA 272
Cdd:cd05069 156 ----------RLIED--NEYTArqgakfpIKWTAPEAA-LYG--RFTIKSDVWSFGILLTELVTKgRVPYpgmvNREVLE 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 273 ICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYF 314
Cdd:cd05069 221 QVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSF 262
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
176-271 1.47e-06

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: 50.86  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGG--NYVLCDFGSAtnkflnpqkdgvnvVEEEIKKYTTLS---YRAPEMINlygGKPITTKADIW 250
Cdd:cd14225 167 IIHCDLKPENILLRQRGqsSIKVIDFGSS--------------CYEHQRVYTYIQsrfYRSPEVIL---GLPYSMAIDMW 229
                        90       100
                ....*....|....*....|...
gi 38787904 251 ALGCLLYKLcFFTLPF--GESQV 271
Cdd:cd14225 230 SLGCILAEL-YTGYPLfpGENEV 251
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
94-308 1.52e-06

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 50.20  E-value: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDcavnSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCK 173
Cdd:cd14109  45 REVDIHNSLD-HPNIVQMHD----AYDDEKLAVTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 tpIIHRDLKVENILLNDGgNYVLCDFGSAtnKFLNpqkDGvnvveeeikKYTTLSYRAPEMIN--LYGGKPITTKADIWA 251
Cdd:cd14109 120 --IAHLDLRPEDILLQDD-KLKLADFGQS--RRLL---RG---------KLTTLIYGSPEFVSpeIVNSYPVTLATDMWS 182
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904 252 LGCLLYKLCFFTLPF-----GESQVAICDGNFTIPDN--SRYSRNIHCLIRFMLEPDPEHRPDI 308
Cdd:cd14109 183 VGVLTYVLLGGISPFlgdndRETLTNVRSGKWSFDSSplGNISDDARDFIKKLLVYIPESRLTV 246
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
53-256 1.54e-06

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: 50.81  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVRTHGgircalKRMYvnnmpdlnvckREITIMKELSgHKNIVGYLDCAVNSIS-DNVWEVLILME 131
Cdd:cd07875  48 LERNVAIKKLSRPFQNQTHA------KRAY-----------RELVLMKCVN-HKNIIGLLNVFTPQKSlEEFQDVYIVME 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAG--QVVnQMnkKLQTGFTEPEVLQIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA----TNK 205
Cdd:cd07875 110 LMDANlcQVI-QM--ELDHERMSYLLYQMLC----GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLArtagTSF 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 206 FLNPqkdgvnvveEEIKKYttlsYRAPEMINLYGGKpitTKADIWALGCLL 256
Cdd:cd07875 181 MMTP---------YVVTRY----YRAPEVILGMGYK---ENVDIWSVGCIM 215
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
53-210 1.62e-06

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: 50.15  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  53 LEESLAEGGFSTVFLVR-THGGIRCALKRMYVNNMPDLNvcKREITIMKELSGHKNI--VGYldcavnSISDNVWEVLIl 129
Cdd:cd14016   4 LVKKIGSGSFGEVYLGIdLKTGEEVAIKIEKKDSKHPQL--EYEAKVYKLLQGGPGIprLYW------FGQEGDYNVMV- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCraG----QVVNQMNKKlqtgFTEPEVLQIfcdTCEAVARL---HQCKtpIIHRDLKVENILLNDGGN----YvLCD 198
Cdd:cd14016  75 MDLL--GpsleDLFNKCGRK----FSLKTVLML---ADQMISRLeylHSKG--YIHRDIKPENFLMGLGKNsnkvY-LID 142
                       170
                ....*....|..
gi 38787904 199 FGSATnKFLNPQ 210
Cdd:cd14016 143 FGLAK-KYRDPR 153
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
177-264 1.92e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 50.36  E-value: 1.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKFLNPqkDGVNVVEEEIKkyttLSYRAPEMINlygGKPITTKADIWALGCLL 256
Cdd:cd05103 201 IHRDLAARNILLSENNVVKICDFGLARDIYKDP--DYVRKGDARLP----LKWMAPETIF---DRVYTIQSDVWSFGVLL 271

                ....*...
gi 38787904 257 YKLcfFTL 264
Cdd:cd05103 272 WEI--FSL 277
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
46-256 1.95e-06

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 49.89  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNM-PDLNVckREITIMKELSgHKNIVgYLDCAVNSisdnvW 124
Cdd:cd05067   4 VPRETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMsPDAFL--AEANLMKQLQ-HQRLV-RLYAVVTQ-----E 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd05067  75 PIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEE--RNYIHRDLRAANILVSDTLSCKIADFGLA-- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 205 kflnpqkdgvNVVEEeiKKYTT-------LSYRAPEMINlYGgkPITTKADIWALGCLL 256
Cdd:cd05067 151 ----------RLIED--NEYTAregakfpIKWTAPEAIN-YG--TFTIKSDVWSFGILL 194
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
130-305 2.19e-06

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: 50.07  E-value: 2.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNKklqtgFTEPEVLQIF--CDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKfl 207
Cdd:cd05596 105 MDYMPGGDLVNLMSN-----YDVPEKWARFytAEVVLALDAIH--SMGFVHRDVKPDNMLLDASGHLKLADFGTCMKM-- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 208 npQKDGVNVVEEEIKkytTLSYRAPEMI------NLYGGkpittKADIWALGCLLYKLCFFTLPF-GESQVA----ICD- 275
Cdd:cd05596 176 --DKDGLVRSDTAVG---TPDYISPEVLksqggdGVYGR-----ECDWWSVGVFLYEMLVGDTPFyADSLVGtygkIMNh 245
                       170       180       190
                ....*....|....*....|....*....|.
gi 38787904 276 -GNFTIPDNSRYSRNIHCLIRFMLEpDPEHR 305
Cdd:cd05596 246 kNSLQFPDDVEISKDAKSLICAFLT-DREVR 275
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
129-266 2.20e-06

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 50.18  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMNKKLQtgFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkfln 208
Cdd:cd05591  74 VMEYVNGGDLMFQIQRARK--FDEPRARFYAAEVTLALMFLHR--HGVIYRDLKLDNILLDAEGHCKLADFGMC------ 143
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 pqKDGVNVVEEEIKKYTTLSYRAPEMINL--YGgkpitTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05591 144 --KEGILNGKTTTTFCGTPDYIAPEILQEleYG-----PSVDWWALGVLMYEMMAGQPPF 196
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
57-265 2.32e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVrTH--GGIRCALKRMYVNNMPDL-NVCKREITIMKELSGhKNIVGYLDCAVnsiSDNvwEVLILMEYC 133
Cdd:cd06650  13 LGAGNGGVVFKV-SHkpSGLVMARKLIHLEIKPAIrNQIIRELQVLHECNS-PYIVGFYGAFY---SDG--EISICMEHM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 134 RAGQVvNQMNKKlqTGFTEPEVL-QIFCDTCEAVARLHQcKTPIIHRDLKVENILLNDGGNYVLCDFG-------SATNK 205
Cdd:cd06650  86 DGGSL-DQVLKK--AGRIPEQILgKVSIAVIKGLTYLRE-KHKIMHRDVKPSNILVNSRGEIKLCDFGvsgqlidSMANS 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 206 FLNpqkdgvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLP 265
Cdd:cd06650 162 FVG-----------------TRSYMSPERLQ---GTHYSVQSDIWSMGLSLVEMAVGRYP 201
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
176-270 2.40e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 49.49  E-value: 2.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqkdgvNVVEEEIKKYT-TLSYRAPEMINlygGKPITTKADIWALGC 254
Cdd:cd06619 116 ILHRDVKPSNMLVNTRGQVKLCDFGVST-----------QLVNSIAKTYVgTNAYMAPERIS---GEQYGIHSDVWSLGI 181
                        90
                ....*....|....*.
gi 38787904 255 LLYKLCFFTLPFGESQ 270
Cdd:cd06619 182 SFMELALGRFPYPQIQ 197
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
177-306 2.82e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 49.98  E-value: 2.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKFLNPqkdgvnvveEEIKKYTT---LSYRAPEMINlygGKPITTKADIWALG 253
Cdd:cd05102 194 IHRDLAARNILLSENNVVKICDFGLARDIYKDP---------DYVRKGSArlpLKWMAPESIF---DKVYTTQSDVWSFG 261
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 254 CLLYKLcfFTL---PFGESQV--AIC----DGN-FTIPDNSrySRNIHcliRFML---EPDPEHRP 306
Cdd:cd05102 262 VLLWEI--FSLgasPYPGVQIneEFCqrlkDGTrMRAPEYA--TPEIY---RIMLscwHGDPKERP 320
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
57-213 3.00e-06

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: 49.18  E-value: 3.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-THGGIRCALKRMYVNNmpDLNVCKREITIMKELSGHKNIVGYLDCAVNSisDNVWevlILMEYCra 135
Cdd:cd14017   8 IGGGGFGEIYKVRdVVDGEEVAMKVESKSQ--PKQVLKMEVAVLKKLQGKPHFCRLIGCGRTE--RYNY---IVMTLL-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQTG-FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGN-----YVLcDFGSAtNKFLNP 209
Cdd:cd14017  79 GPNLAELRRSQPRGkFSVSTTLRLGIQILKAIEDIHEVG--FLHRDVKPSNFAIGRGPSdertvYIL-DFGLA-RQYTNK 154

                ....
gi 38787904 210 QKDG 213
Cdd:cd14017 155 DGEV 158
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
94-256 3.48e-06

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 49.18  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNI-----VGYLDCAVNSISdnvwevlilmEYCRAGqVVNQMNKKLQTGFTEPEVLQIFCDTCEAVAR 168
Cdd:cd14221  39 KEVKVMRCLE-HPNVlkfigVLYKDKRLNFIT----------EYIKGG-TLRGIIKSMDSHYPWSQRVSFAKDIASGMAY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA---TNKFLNPQKDGVNVVEEEIKKYTTLS---YRAPEMINlygGKP 242
Cdd:cd14221 107 LHSMN--IIHRDLNSHNCLVRENKSVVVADFGLArlmVDEKTQPEGLRSLKKPDRKKRYTVVGnpyWMAPEMIN---GRS 181
                       170
                ....*....|....
gi 38787904 243 ITTKADIWALGCLL 256
Cdd:cd14221 182 YDEKVDVFSFGIVL 195
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
50-259 3.90e-06

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: 48.79  E-value: 3.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVcKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVL-- 127
Cdd:cd05112   5 ELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDF-IEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMeh 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 -ILMEYCRAgqvvnqmnkklQTG-FTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGsATNK 205
Cdd:cd05112  84 gCLSDYLRT-----------QRGlFSAETLLGMCLDVCEGMAYLEE--ASVIHRDLAARNCLVGENQVVKVSDFG-MTRF 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 206 FLNPQKDGVNVVEEEIKkyttlsYRAPEMINlYGGkpITTKADIWALGCLLYKL 259
Cdd:cd05112 150 VLDDQYTSSTGTKFPVK------WSSPEVFS-FSR--YSSKSDVWSFGVLMWEV 194
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
52-340 3.94e-06

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: 49.49  E-value: 3.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTVFLVRTHGGIRC-ALKRMYVNNMPDLNVCKREITIMKELSGHKN-IVGYLDCAVNSISDnvweVLIL 129
Cdd:cd05610   7 VIVKPISRGAFGKVYLGRKKNNSKLyAVKVVKKADMINKNMVHQVQAERDALALSKSpFIVHLYYSLQSANN----VYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMNkkLQTGFTEPEVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSA------- 202
Cdd:cd05610  83 MEYLIGGDVKSLLH--IYGYFDEEMAVKYISEVALALDYLHR--HGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnre 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 203 --------TNKFLNPQKD-------------------------------GVNVVEEEiKKYTTLSYRAPEminLYGGKPI 243
Cdd:cd05610 159 lnmmdiltTPSMAKPKNDysrtpgqvlslisslgfntptpyrtpksvrrGAARVEGE-RILGTPDYLAPE---LLLGKPH 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 244 TTKADIWALGCLLYKLCFFTLPFGE---SQV--AICDGNFTIPD-NSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFk 317
Cdd:cd05610 235 GPAVDWWALGVCLFEFLTGIPPFNDetpQQVfqNILNRDIPWPEgEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPL- 313
                       330       340
                ....*....|....*....|...
gi 38787904 318 FAKKDCpvSNINNSSIPsALPEP 340
Cdd:cd05610 314 FHGVDW--ENLQNQTMP-FIPQP 333
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
52-259 4.06e-06

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: 49.39  E-value: 4.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  52 TLEESLAEGGFSTV-FLVRTHGGIRCALKRMY--VNNMPDLNVCKREITIMKELSgHKNIVG----YLDCAVNSISDnVW 124
Cdd:cd07859   3 KIQEVIGKGSYGVVcSAIDTHTGEKVAIKKINdvFEHVSDATRILREIKLLRLLR-HPDIVEikhiMLPPSRREFKD-IY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEyCRAGQVVnQMNKKLQtgftePEVLQIFC-DTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd07859  81 VVFELME-SDLHQVI-KANDDLT-----PEHHQFFLyQLLRALKYIHTAN--VFHRDLKPKNILANADCKLKICDFGLAR 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 204 NKFLNPQ-----KDGVnvveeeikkyTTLSYRAPEMINLYGGKpITTKADIWALGCLLYKL 259
Cdd:cd07859 152 VAFNDTPtaifwTDYV----------ATRWYRAPELCGSFFSK-YTPAIDIWSIGCIFAEV 201
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
128-271 4.22e-06

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: 49.62  E-value: 4.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKklqtgFTE--PEVLQIF--CDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd05624 149 LVMDYYVGGDLLTLLSK-----FEDklPEDMARFyiGEMVLAIHSIHQLH--YVHRDIKPDNVLLDMNGHIRLADFGSC- 220
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 204 nkfLNPQKDGvnVVEEEIkKYTTLSYRAPEMINLY--GGKPITTKADIWALGCLLYKLCFFTLPF-GESQV 271
Cdd:cd05624 221 ---LKMNDDG--TVQSSV-AVGTPDYISPEILQAMedGMGKYGPECDWWSLGVCMYEMLYGETPFyAESLV 285
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
177-312 4.28e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 49.64  E-value: 4.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKFLNPqkdgvNVVEEEiKKYTTLSYRAPEMI--NLYggkpiTTKADIWALGC 254
Cdd:cd05105 259 VHRDLAARNVLLAQGKIVKICDFGLARDIMHDS-----NYVSKG-STFLPVKWMAPESIfdNLY-----TTLSDVWSYGI 327
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 255 LLYKLcfFTLPFGESQVAICDGNF--TIPDNSRYSRNIHC---LIRFMLE---PDPEHRPDIFQVS 312
Cdd:cd05105 328 LLWEI--FSLGGTPYPGMIVDSTFynKIKSGYRMAKPDHAtqeVYDIMVKcwnSEPEKRPSFLHLS 391
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
159-210 4.28e-06

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 48.91  E-value: 4.28e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38787904 159 FCDTCEAVAR----LHQ----C---KTPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQ 210
Cdd:cd14055 100 LCKMAGSLARglahLHSdrtpCgrpKIPIAHRDLKSSNILVKNDGTCVLADFGLALR--LDPS 160
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
57-259 4.72e-06

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: 48.74  E-value: 4.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTH-----GGIRCALKRMYVNNMPDLNVC-KREITIMKELSgHKNIVGYLDCAVNSISDNVwevLILM 130
Cdd:cd05080  12 LGEGHFGKVSLYCYDptndgTGEMVAVKALKADCGPQHRSGwKQEIDILKTLY-HENIVKYKGCCSEQGGKSL---QLIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 EYCRAGQVVNQMNKKlQTGFTEpevLQIFCDT-CEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAT-----N 204
Cdd:cd05080  88 EYVPLGSLRDYLPKH-SIGLAQ---LLLFAQQiCEGMAYLHSQH--YIHRDLAARNVLLDNDRLVKIGDFGLAKavpegH 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 38787904 205 KFLNPQKDGVNVVeeeikkyttlSYRAPEMINLYggkPITTKADIWALGCLLYKL 259
Cdd:cd05080 162 EYYRVREDGDSPV----------FWYAPECLKEY---KFYYASDVWSFGVTLYEL 203
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
57-263 5.57e-06

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: 48.74  E-value: 5.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-----THGGIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCavnSISDNVWEVLILME 131
Cdd:cd05081  12 LGKGNFGSVELCRydplgDNTGALVAVKQLQHSGPDQQRDFQREIQILKALH-SDFIVKYRGV---SYGPGRRSLRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARL--HQCktpiIHRDLKVENILLNDGGNYVLCDFGSAtnKFLnP 209
Cdd:cd05081  88 YLPSGCLRDFLQRH-RARLDASRLLLYSSQICKGMEYLgsRRC----VHRDLAARNILVESEAHVKIADFGLA--KLL-P 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 210 QKDGVNVVEEeiKKYTTLSYRAPEMI--NLYggkpiTTKADIWALGCLLYKLcfFT 263
Cdd:cd05081 160 LDKDYYVVRE--PGQSPIFWYAPESLsdNIF-----SRQSDVWSFGVVLYEL--FT 206
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
105-259 6.54e-06

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 48.32  E-value: 6.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLDCAVNSISdnvweVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARL-HQCKTPIIHRDLKV 183
Cdd:cd05086  56 HPNILQCVGQCVEAIP-----YLLVFEFCDLGDLKTYLANQQEKLRGDSQIMLLQRMACEIAAGLaHMHKHNFLHSDLAL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 184 ENILLNDGGNYVLCDFGsatnkfLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPIT---TK-ADIWALGCLLYKL 259
Cdd:cd05086 131 RNCYLTSDLTVKVGDYG------IGFSRYKEDYIETDDKKYAPLRWTAPELVTSFQDGLLAaeqTKySNIWSLGVTLWEL 204
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
118-257 6.61e-06

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: 48.76  E-value: 6.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 118 SISDNVWEVLIlMEYCRAGQVVNQMNKKlqTGFTEpEVLQIF-CDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVL 196
Cdd:cd05599  69 SFQDEENLYLI-MEFLPGGDMMTLLMKK--DTLTE-EETRFYiAETVLAIESIHKLG--YIHRDIKPDNLLLDARGHIKL 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 197 CDFGSATNkflnpqkdgvnvVEEEIKKYTTL---SYRAPE--MINLYGgkpitTKADIWALGCLLY 257
Cdd:cd05599 143 SDFGLCTG------------LKKSHLAYSTVgtpDYIAPEvfLQKGYG-----KECDWWSLGVIMY 191
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
177-264 7.50e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 48.85  E-value: 7.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKFLNpqkdgvnvvEEEIKKYTT---LSYRAPEMI--NLYggkpiTTKADIWA 251
Cdd:cd05107 261 VHRDLAARNVLICEGKLVKICDFGLARDIMRD---------SNYISKGSTflpLKWMAPESIfnNLY-----TTLSDVWS 326
                        90
                ....*....|...
gi 38787904 252 LGCLLYKLcfFTL 264
Cdd:cd05107 327 FGILLWEI--FTL 337
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
105-306 7.92e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 47.92  E-value: 7.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGY----LDcavnsISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPE-VLQIFC-DTCEAVARLHQCKTPIIH 178
Cdd:cd13984  54 HPNIVKFhrywTD-----VQEEKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEkSWKRWCtQILSALSYLHSCDPPIIH 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 179 RDLKVENILLNDGGnyvLCDFGSATNKFLNpqkdgvNVVEEEIKKYTTLSYRAPEminlYGG-KPITTKADIWALG-CLL 256
Cdd:cd13984 129 GNLTCDTIFIQHNG---LIKIGSVAPDAIH------NHVKTCREEHRNLHFFAPE----YGYlEDVTTAVDIYSFGmCAL 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 257 YKLCFFTLPFGE----SQVAICDGNFTIPDNsrysrNIHCLIRFMLEPDPEHRP 306
Cdd:cd13984 196 EMAALEIQSNGEkvsaNEEAIIRAIFSLEDP-----LQKDFIRKCLSVAPQDRP 244
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
150-305 8.79e-06

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: 47.82  E-value: 8.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 150 FTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVveeeikkyTTLSY 229
Cdd:cd05606  95 FSEAEMRFYAAEVILGLEHMH--NRFIVYRDLKPANILLDEHGHVRISDLGLACD--FSKKKPHASV--------GTHGY 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 230 RAPEMinLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVA--------ICDGNFTIPDNsrYSRNIHCLIRFMLEPD 301
Cdd:cd05606 163 MAPEV--LQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKdkheidrmTLTMNVELPDS--FSPELKSLLEGLLQRD 238

                ....
gi 38787904 302 PEHR 305
Cdd:cd05606 239 VSKR 242
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
46-259 8.99e-06

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 47.76  E-value: 8.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNM-PDLNVckREITIMKELSGHKNIVGYldcAVNSISdnvw 124
Cdd:cd05071   6 IPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMsPEAFL--QEAQVMKKLRHEKLVQLY---AVVSEE---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtn 204
Cdd:cd05071  77 PIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVE--RMNYVHRDLRAANILVGENLVCKVADFGLA-- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 205 kflnpqkdgvNVVEEeiKKYTT-------LSYRAPEMInLYGgkPITTKADIWALGCLLYKL 259
Cdd:cd05071 153 ----------RLIED--NEYTArqgakfpIKWTAPEAA-LYG--RFTIKSDVWSFGILLTEL 199
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
54-303 9.27e-06

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 48.12  E-value: 9.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  54 EESLAEGGFSTVFLVRThggircaLKRMYVNNMPDLNV----CKREITIMKELsgHKNIVGylDCAVNSISDNVW----- 124
Cdd:cd13981   5 SKELGEGGYASVYLAKD-------DDEQSDGSLVALKVekppSIWEFYICDQL--HSRLKN--SRLRESISGAHSahlfq 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 -EVLILMEYCRAG---QVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILL------------ 188
Cdd:cd13981  74 dESILVMDYSSQGtllDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVG--IIHGDIKPDNFLLrleicadwpgeg 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 189 -NDGGNYV--LCDFGSATNkfLNPQKDGVNVveeeIKKYTTLSYRAPEMINlygGKPITTKADIWALGCllyklCFFTLP 265
Cdd:cd13981 152 eNGWLSKGlkLIDFGRSID--MSLFPKNQSF----KADWHTDSFDCIEMRE---GRPWTYQIDYFGIAA-----TIHVML 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38787904 266 FGES-QVAICDGNFTIPDN-SRYS-RNI-HCLIRFMLEPDPE 303
Cdd:cd13981 218 FGKYmELTQESGRWKINQNlKRYWqRDIwNKFFDTLLNPEPS 259
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
165-259 1.02e-05

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 48.21  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHQCKtpIIHRDLKVENILLNDGGNY----VLCDFGSATNkflnpqkdgvnvVEEEIKKYTTLS--YRAPEMINly 238
Cdd:cd14211 113 ALLKLKSLG--LIHADLKPENIMLVDPVRQpyrvKVIDFGSASH------------VSKAVCSTYLQSryYRAPEIIL-- 176
                        90       100
                ....*....|....*....|.
gi 38787904 239 gGKPITTKADIWALGCLLYKL 259
Cdd:cd14211 177 -GLPFCEAIDMWSLGCVIAEL 196
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
50-307 1.08e-05

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: 47.72  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGFSTVFLVRTHGGIrCALKRMYVNNMPDLNV----CKREITIMKELSgHKNIVgyldcAVNSISDNVWE 125
Cdd:cd14147   4 ELRLEEVIGIGGFGKVYRGSWRGEL-VAVKAARQDPDEDISVtaesVRQEARLFAMLA-HPNII-----ALKAVCLEEPN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQvvnqMNKKLQTGFTEPEVLQIFC-DTCEAVARLH-QCKTPIIHRDLKVENILLNDGG--------NYV 195
Cdd:cd14147  77 LCLVMEYAAGGP----LSRALAGRRVPPHVLVNWAvQIARGMHYLHcEALVPVIHRDLKSNNILLLQPIenddmehkTLK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 196 LCDFGSATNKFLNPQKDGVNvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAIC 274
Cdd:cd14147 153 ITDFGLAREWHKTTQMSAAG----------TYAWMAPEVIK---ASTFSKGSDVWSFGVLLWELLTGEVPYrGIDCLAVA 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38787904 275 DG----NFTIPDNSRYSRNIHCLIRFMLEPDPEHRPD 307
Cdd:cd14147 220 YGvavnKLTLPIPSTCPEPFAQLMADCWAQDPHRRPD 256
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
57-259 1.16e-05

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 47.51  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRcALKRMYVNNMPDLNVCKRE-ITIMKELSG--HKNIV---GYldCAVNSISdnvweVLILM 130
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTEY-AVKRLKEDSELDWSVVKNSfLTEVEKLSRfrHPNIVdlaGY--SAQQGNY-----CLIYV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 131 eYCRAGQVVNQMNKklQTGF---TEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnKFL 207
Cdd:cd14159  73 -YLPNGSLEDRLHC--QVSCpclSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLDAALNPKLGDFGLA--RFS 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 38787904 208 NPQKDGVN--VVEEEIKKYTTLSYRAPEMINLygGKpITTKADIWALGCLLYKL 259
Cdd:cd14159 148 RRPKQPGMssTLARTQTVRGTLAYLPEEYVKT--GT-LSVEIDVYSFGVVLLEL 198
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
176-258 1.19e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 48.35  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  176 IIHRDLKVENILLNDGGNYVLCDFGSAT---NKFLNPQKDGVNvveeeikkyTTLSYRAPEMInlyGGKPITTKADIWAL 252
Cdd:PHA03211 281 IIHRDIKTENVLVNGPEDICLGDFGAACfarGSWSTPFHYGIA---------GTVDTNAPEVL---AGDPYTPSVDIWSA 348

                 ....*.
gi 38787904  253 GCLLYK 258
Cdd:PHA03211 349 GLVIFE 354
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
55-259 1.20e-05

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 47.29  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIRCAlkRMYVNNMPDLNVCKREITIMKELS-----GHKNIVGYL-DCAvnsisdNVWEVLI 128
Cdd:cd05087   3 KEIGHGWFGKVFLGEVNSGLSST--QVVVKELKASASVQDQMQFLEEAQpyralQHTNLLQCLaQCA------EVTPYLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQVVNQMN--KKLQTGFTEPEVLQ-IFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNK 205
Cdd:cd05087  75 VMEFCPLGDLKGYLRscRAAESMAPDPLTLQrMACEVACGLLHLH--RNNFVHSDLALRNCLLTADLTVKIGDYGLSHCK 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 206 FlnpqKDGVNVVEEEikKYTTLSYRAPEMINLYGGKPI----TTKADIWALGCLLYKL 259
Cdd:cd05087 153 Y----KEDYFVTADQ--LWVPLRWIAPELVDEVHGNLLvvdqTKQSNVWSLGVTIWEL 204
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
164-306 1.30e-05

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: 47.49  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 EAVARLHQCKtpIIHRDLKVENILL---NDGGNY-VLCDFGSAtnkfLNPQKDGVNV--VEEEIKKYTTLSYRAPEMINL 237
Cdd:cd14018 149 EGVDHLVRHG--IAHRDLKSDNILLeldFDGCPWlVIADFGCC----LADDSIGLQLpfSSWYVDRGGNACLMAPEVSTA 222
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 238 YGGKPIT---TKADIWALGCLLYKLC-----FFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRP 306
Cdd:cd14018 223 VPGPGVVinySKADAWAVGAIAYEIFglsnpFYGLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRV 299
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
128-271 1.42e-05

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: 48.09  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKklqtgFTE--PEVLQIF--CDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAt 203
Cdd:cd05623 149 LVMDYYVGGDLLTLLSK-----FEDrlPEDMARFylAEMVLAIDSVHQLH--YVHRDIKPDNILMDMNGHIRLADFGSC- 220
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904 204 nkfLNPQKDGvnVVEEEIkKYTTLSYRAPEMIN-LYGGK-PITTKADIWALGCLLYKLCFFTLPF-GESQV 271
Cdd:cd05623 221 ---LKLMEDG--TVQSSV-AVGTPDYISPEILQaMEDGKgKYGPECDWWSLGVCMYEMLYGETPFyAESLV 285
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
73-259 1.44e-05

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: 47.72  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  73 GIRCALKRMY--VNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSIS-DNVWEVLILMEYCRAG--QVVNQMNKKLQ 147
Cdd:cd07876  46 GINVAVKKLSrpFQNQTHAKRAYRELVLLKCVN-HKNIISLLNVFTPQKSlEEFQDVYLVMELMDANlcQVIHMELDHER 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 148 TGFTepeVLQIFCdtceAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSA----TNKFLNPQkdgvnvveeeikk 223
Cdd:cd07876 125 MSYL---LYQMLC----GIKHLHSAG--IIHRDLKPSNIVVKSDCTLKILDFGLArtacTNFMMTPY------------- 182
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 38787904 224 YTTLSYRAPEMINLYGGKpitTKADIWALGCLLYKL 259
Cdd:cd07876 183 VVTRYYRAPEVILGMGYK---ENVDIWSVGCIMGEL 215
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
154-259 1.60e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 47.68  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  154 EVLQIFCDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSATNKflnpqkdgVNVVEEEIKKYT-TLSYRAP 232
Cdd:PHA03212 183 DILAIERSVLRAIQYLHE--NRIIHRDIKAENIFINHPGDVCLGDFGAACFP--------VDINANKYYGWAgTIATNAP 252
                         90       100
                 ....*....|....*....|....*..
gi 38787904  233 EMInlyGGKPITTKADIWALGCLLYKL 259
Cdd:PHA03212 253 ELL---ARDPYGPAVDIWSAGIVLFEM 276
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
97-259 1.73e-05

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 47.05  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  97 TIMKElsgHKNIVGYLdcAVNSISDNVWEVLILM-EYCRAGQVVNQMNKKLQTGFTepeVLQIFCDTCEAVARLH----- 170
Cdd:cd14143  43 TVMLR---HENILGFI--AADNKDNGTWTQLWLVsDYHEHGSLFDYLNRYTVTVEG---MIKLALSIASGLAHLHmeivg 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 -QCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVVEEEikKYTTLSYRAPEMINlyggKPITTK--- 246
Cdd:cd14143 115 tQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVR--HDSATDTIDIAPNH--RVGTKRYMAPEVLD----DTINMKhfe 186
                       170
                ....*....|....*..
gi 38787904 247 ----ADIWALGCLLYKL 259
Cdd:cd14143 187 sfkrADIYALGLVFWEI 203
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
48-264 1.85e-05

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 47.32  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLV--------RTHGGIRCALKRMYVNNM-PDLNVCKREITIMKELSGHKNIVGYLDCAVNS 118
Cdd:cd05100  11 RTRLTLGKPLGEGCFGQVVMAeaigidkdKPNKPVTVAVKMLKDDATdKDLSDLVSEMEMMKMIGKHKNIINLLGACTQD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 119 isdnvWEVLILMEYCRAGQVVNQMNKKLQTGFTE-------PEVLQIFCD--TCE-AVAR--LHQCKTPIIHRDLKVENI 186
Cdd:cd05100  91 -----GPLYVLVEYASKGNLREYLRARRPPGMDYsfdtcklPEEQLTFKDlvSCAyQVARgmEYLASQKCIHRDLAARNV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 187 LLNDGGNYVLCDFGSAtnkflnpqKDGVNVveEEIKKYTT----LSYRAPEMINlygGKPITTKADIWALGCLLYKLcfF 262
Cdd:cd05100 166 LVTEDNVMKIADFGLA--------RDVHNI--DYYKKTTNgrlpVKWMAPEALF---DRVYTHQSDVWSFGVLLWEI--F 230

                ..
gi 38787904 263 TL 264
Cdd:cd05100 231 TL 232
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
48-264 1.96e-05

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: 46.93  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHG--------GIRCALKRMYVN-NMPDLNVCKREITIMKELSGHKNIVGYLDCAVNS 118
Cdd:cd05101  23 RDKLTLGKPLGEGCFGQVVMAEAVGidkdkpkeAVTVAVKMLKDDaTEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 119 isdnvWEVLILMEYCRAGQVVNQMNKKLQTGFT----------EPEVLQIFCDTCEAVAR--LHQCKTPIIHRDLKVENI 186
Cdd:cd05101 103 -----GPLYVIVEYASKGNLREYLRARRPPGMEysydinrvpeEQMTFKDLVSCTYQLARgmEYLASQKCIHRDLAARNV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 187 LLNDGGNYVLCDFGSAtnkflnpqKDGVNVveEEIKKYTT----LSYRAPEMINlygGKPITTKADIWALGCLLYKLcfF 262
Cdd:cd05101 178 LVTENNVMKIADFGLA--------RDINNI--DYYKKTTNgrlpVKWMAPEALF---DRVYTHQSDVWSFGVLMWEI--F 242

                ..
gi 38787904 263 TL 264
Cdd:cd05101 243 TL 244
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
171-259 1.99e-05

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: 47.43  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QC-----KTPIIHRDLKVENILLNDGGNYVL--CDFGSAtnkflnpqkdgvnvVEEEIKKYTTLS---YRAPEMI--NLY 238
Cdd:cd14224 179 QCldalhRNKIIHCDLKPENILLKQQGRSGIkvIDFGSS--------------CYEHQRIYTYIQsrfYRAPEVIlgARY 244
                        90       100
                ....*....|....*....|.
gi 38787904 239 gGKPIttkaDIWALGCLLYKL 259
Cdd:cd14224 245 -GMPI----DMWSFGCILAEL 260
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
176-266 2.25e-05

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: 46.84  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVveeeikkyTTLSYRAPEMINlygGKPITTKADIWALGCL 255
Cdd:cd05619 127 IVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTSTFC--------GTPDYIAPEILL---GQKYNTSVDWWSFGVL 195
                        90
                ....*....|.
gi 38787904 256 LYKLCFFTLPF 266
Cdd:cd05619 196 LYEMLIGQSPF 206
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
95-258 2.30e-05

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: 46.54  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLdcavnSISDNVWEVLILMEYCRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQckT 174
Cdd:cd05085  43 EARILKQYD-HPNIVKLI-----GVCTQRQPIYIVMELVPGGDFLSFLRKK-KDELKTKQLVKFSLDAAAGMAYLES--K 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 175 PIIHRDLKVENILLNDGGNYVLCDFGsatnkfLNPQKDGvNVVEEEIKKYTTLSYRAPEMINlYGgkPITTKADIWALGC 254
Cdd:cd05085 114 NCIHRDLAARNCLVGENNALKISDFG------MSRQEDD-GVYSSSGLKQIPIKWTAPEALN-YG--RYSSESDVWSFGI 183

                ....
gi 38787904 255 LLYK 258
Cdd:cd05085 184 LLWE 187
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
93-272 4.01e-05

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: 45.84  E-value: 4.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDCAVNSISDNVWEVLIlMEYCRAGQVVNQMnKKLQTgfTEPEVLQIFC-DTCEAVARLHQ 171
Cdd:cd14032  48 KEEAEMLKGLQ-HPNIVRFYDFWESCAKGKRCIVLV-TELMTSGTLKTYL-KRFKV--MKPKVLRSWCrQILKGLLFLHT 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKTPIIHRDLKVENILLND-GGNYVLCDFGSATNKFLNPQKDGVNVVEeeikkyttlsYRAPEMINLYGGKPIttkaDIW 250
Cdd:cd14032 123 RTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLKRASFAKSVIGTPE----------FMAPEMYEEHYDESV----DVY 188
                       170       180
                ....*....|....*....|..
gi 38787904 251 ALGCLLYKLCFFTLPFGESQVA 272
Cdd:cd14032 189 AFGMCMLEMATSEYPYSECQNA 210
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
93-272 4.21e-05

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: 45.87  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  93 KREITIMKELSgHKNIVGYLDcAVNSISDNVWEVLILMEYCRAGQVVNQMnKKLQTgfTEPEVLQIFC-DTCEAVARLHQ 171
Cdd:cd14031  57 KEEAEMLKGLQ-HPNIVRFYD-SWESVLKGKKCIVLVTELMTSGTLKTYL-KRFKV--MKPKVLRSWCrQILKGLQFLHT 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 172 CKTPIIHRDLKVENILLND-GGNYVLCDFGSATNKFLNPQKDGVNVVEeeikkyttlsYRAPEMINLYGGKPIttkaDIW 250
Cdd:cd14031 132 RTPPIIHRDLKCDNIFITGpTGSVKIGDLGLATLMRTSFAKSVIGTPE----------FMAPEMYEEHYDESV----DVY 197
                       170       180
                ....*....|....*....|..
gi 38787904 251 ALGCLLYKLCFFTLPFGESQVA 272
Cdd:cd14031 198 AFGMCMLEMATSEYPYSECQNA 219
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
125-265 4.69e-05

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: 45.81  E-value: 4.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 125 EVLILMEYCRAGQvvnqMNKKLQTGFTEPEVL--QIFCDTCEAVARLHQcKTPIIHRDLKVENILLNDGGNYVLCDFG-- 200
Cdd:cd06649  77 EISICMEHMDGGS----LDQVLKEAKRIPEEIlgKVSIAVLRGLAYLRE-KHQIMHRDVKPSNILVNSRGEIKLCDFGvs 151
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 201 -----SATNKFLNpqkdgvnvveeeikkytTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLP 265
Cdd:cd06649 152 gqlidSMANSFVG-----------------TRSYMSPERLQ---GTHYSVQSDIWSMGLSLVELAIGRYP 201
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
57-259 5.62e-05

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: 45.29  E-value: 5.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRTHGGIRCALKRMYVNNM-PDLNVckREITIMKELSGHKNIVGYldcAVnsISDNvwEVLILMEYCRA 135
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMsPEAFL--EEAQIMKKLRHDKLVQLY---AV--VSEE--PIYIVTEFMSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqkdgvN 215
Cdd:cd14203  74 GSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIE--RMNYIHRDLRAANILVGDNLVCKIADFGLA------------R 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 38787904 216 VVEEEikKYTT-------LSYRAPEMInLYGgkPITTKADIWALGCLLYKL 259
Cdd:cd14203 140 LIEDN--EYTArqgakfpIKWTAPEAA-LYG--RFTIKSDVWSFGILLTEL 185
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
164-311 7.91e-05

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: 44.91  E-value: 7.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 164 EAVARLHqcKTPIIHRDLKVENILL-----NDGGNYVLCDFGSATNKFlnpqKDGVNVVEeeikkyTTLSYRAPEMINly 238
Cdd:cd14000 123 DGLRYLH--SAMIIYRDLKSHNVLVwtlypNSAIIIKIADYGISRQCC----RMGAKGSE------GTPGFRAPEIAR-- 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 239 GGKPITTKADIWALGCLLYKLCFFTLPF-GESQVAIC-DGNFTIPD-----NSRYSRNIHCLIRFMLEPDPEHRPDIFQV 311
Cdd:cd14000 189 GNVIYNEKVDVFSFGMLLYEILSGGAPMvGHLKFPNEfDIHGGLRPplkqyECAPWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
165-305 8.54e-05

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: 45.03  E-value: 8.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 165 AVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAtnkfLNPQKDG-----VNVveeeikkyTTLSYRAPEMIN-LY 238
Cdd:cd05597 114 AIDSIHQLG--YVHRDIKPDNVLLDRNGHIRLADFGSC----LKLREDGtvqssVAV--------GTPDYISPEILQaME 179
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 239 GGK-PITTKADIWALGCLLYKLCFFTLPF-GESQVAIC------DGNFTIPDNS-RYSRNIHCLIRFMLEpDPEHR 305
Cdd:cd05597 180 DGKgRYGPECDWWSLGVCMYEMLYGETPFyAESLVETYgkimnhKEHFSFPDDEdDVSEEAKDLIRRLIC-SRERR 254
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
105-262 8.74e-05

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 44.94  E-value: 8.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLDCAVNSISdnvweVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVAR------LHQCKTPIIH 178
Cdd:cd14206  56 HPNILQCLGLCTETIP-----FLLIMEFCQLGDLKRYLRAQRKADGMTPDLPTRDLRTLQRMAYeitlglLHLHKNNYIH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 179 RDLKVENILLNDGGNYVLCDFGSATNKFlnpqKDGVNVVEEEIkkYTTLSYRAPEMINLYGGKPI----TTKADIWALGC 254
Cdd:cd14206 131 SDLALRNCLLTSDLTVRIGDYGLSHNNY----KEDYYLTPDRL--WIPLRWVAPELLDELHGNLIvvdqSKESNVWSLGV 204

                ....*...
gi 38787904 255 LLYKLCFF 262
Cdd:cd14206 205 TIWELFEF 212
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
94-256 9.36e-05

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: 45.08  E-value: 9.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNIVGYLDCAV-NSISDNVWEVLILMEYCRAG--QVVNQMNKKLQTGFTepeVLQIFCdtceAVARLH 170
Cdd:cd07874  65 RELVLMKCVN-HKNIISLLNVFTpQKSLEEFQDVYLVMELMDANlcQVIQMELDHERMSYL---LYQMLC----GIKHLH 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QCKtpIIHRDLKVENILLNDGGNYVLCDFGSA----TNKFLNPQkdgvnvveeeikkYTTLSYRAPEMINLYGGKpitTK 246
Cdd:cd07874 137 SAG--IIHRDLKPSNIVVKSDCTLKILDFGLArtagTSFMMTPY-------------VVTRYYRAPEVILGMGYK---EN 198
                       170
                ....*....|
gi 38787904 247 ADIWALGCLL 256
Cdd:cd07874 199 VDIWSVGCIM 208
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
176-266 1.01e-04

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: 44.93  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATNkflnpqkdgvNVVEEeiKKYTTL----SYRAPEMINlygGKPITTKADIWA 251
Cdd:cd05620 117 IIYRDLKLDNVMLDRDGHIKIADFGMCKE----------NVFGD--NRASTFcgtpDYIAPEILQ---GLKYTFSVDWWS 181
                        90
                ....*....|....*
gi 38787904 252 LGCLLYKLCFFTLPF 266
Cdd:cd05620 182 FGVLLYEMLIGQSPF 196
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
60-266 1.02e-04

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: 44.72  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLVRTHGGIRC----ALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSIsdnvwEVLILMEYCRA 135
Cdd:cd05588   6 GSYAKVLMVELKKTKRIyamkVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTES-----RLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 136 GQVVNQMNKKLQTgftePEVLQIF--CDTCEAVARLHQckTPIIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqKDG 213
Cdd:cd05588  81 GDLMFHMQRQRRL----PEEHARFysAEISLALNFLHE--KGIIYRDLKLDNVLLDSEGHIKLTDYGMC--------KEG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 38787904 214 VNVVEEEIKKYTTLSYRAPEMINlygGKPITTKADIWALGCLLYKLCFFTLPF 266
Cdd:cd05588 147 LRPGDTTSTFCGTPNYIAPEILR---GEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
95-272 1.06e-04

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 44.61  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSgHKNIVGYLDCAVNSISDNVWEVLIlMEYCRAGQVVNQMNKKLQTgftEPEVLQIFC-DTCEAVARLHQCK 173
Cdd:cd14033  50 EVEMLKGLQ-HPNIVRFYDSWKSTVRGHKCIILV-TELMTSGTLKTYLKRFREM---KLKLLQRWSrQILKGLHFLHSRC 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLND-GGNYVLCDFGSATNKFLNPQKDGVNVVEeeikkyttlsYRAPEMinlYGGKpITTKADIWAL 252
Cdd:cd14033 125 PPILHRDLKCDNIFITGpTGSVKIGDLGLATLKRASFAKSVIGTPE----------FMAPEM---YEEK-YDEAVDVYAF 190
                       170       180
                ....*....|....*....|
gi 38787904 253 GCLLYKLCFFTLPFGESQVA 272
Cdd:cd14033 191 GMCILEMATSEYPYSECQNA 210
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
176-305 1.12e-04

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: 45.05  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVveeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCL 255
Cdd:cd05633 129 VVYRDLKPANILLDEHGHVRISDLGLACD--FSKKKPHASV--------GTHGYMAPEV--LQKGTAYDSSADWFSLGCM 196
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38787904 256 LYKLCFFTLPFGESQVA--------ICDGNFTIPDNsrYSRNIHCLIRFMLEPDPEHR 305
Cdd:cd05633 197 LFKLLRGHSPFRQHKTKdkheidrmTLTVNVELPDS--FSPELKSLLEGLLQRDVSKR 252
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
94-259 1.13e-04

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: 44.54  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAgQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHqcK 173
Cdd:cd14020  52 KERAALEQLQGHRNIVTLYGVFTNHYSANVPSRCLLLELLDV-SVSELLLRSSNQGCSMWMIQHCARDVLEALAFLH--H 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 174 TPIIHRDLKVENILLN-DGGNYVLCDFGSATnkflnpqKDGvnvvEEEIKKYTTLSYRAPE--------MINLYGGKPIT 244
Cdd:cd14020 129 EGYVHADLKPRNILWSaEDECFKLIDFGLSF-------KEG----NQDVKYIQTDGYRAPEaelqnclaQAGLQSETECT 197
                       170
                ....*....|....*
gi 38787904 245 TKADIWALGCLLYKL 259
Cdd:cd14020 198 SAVDLWSLGIVLLEM 212
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
55-271 1.25e-04

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 44.41  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVR-----THGGIRCAlkrmyvnnmPDLNVCKRE-ITIMKELSGHKNIVGYLDCAVNSISDNvwEVLI 128
Cdd:cd14025   2 EKVGSGGFGQVYKVRhkhwkTWLAIKCP---------PSLHVDDSErMELLEEAKKMEMAKFRHILPVYGICSE--PVGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 129 LMEYCRAGQvvnqMNKKLQT-GFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSAT-NKF 206
Cdd:cd14025  71 VMEYMETGS----LEKLLASePLPWELRFRIIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAKwNGL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 207 LNP---QKDGVnvveeeikkYTTLSYRAPEMInLYGGKPITTKADIWALGCLLYKLCFFTLPF-GESQV 271
Cdd:cd14025 147 SHShdlSRDGL---------RGTIAYLPPERF-KEKNRCPDTKHDVYSFAIVIWGILTQKKPFaGENNI 205
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
55-259 1.30e-04

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 44.12  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHGGIRCAlkRMYVNNMPDLNVCKREITIMKELS-----GHKNIVGYLDCAVNSISdnvweVLIL 129
Cdd:cd05042   1 QEIGNGWFGKVLLGEIYSGTSVA--QVVVKELKASANPKEQDTFLKEGQpyrilQHPNILQCLGQCVEAIP-----YLLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 130 MEYCRAGQVVNQMN--KKLQTGFTEPEVLQ-IFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKF 206
Cdd:cd05042  74 MEFCDLGDLKAYLRseREHERGDSDTRTLQrMACEVAAGLAHLH--KLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRY 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 207 lnpqKDGVNVVEEeiKKYTTLSYRAPEMINLYGGKPI----TTKADIWALGCLLYKL 259
Cdd:cd05042 152 ----KEDYIETDD--KLWFPLRWTAPELVTEFHDRLLvvdqTKYSNIWSLGVTLWEL 202
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
126-305 1.46e-04

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: 44.21  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLqtgFTEPEVlqIFCDTCEAVAR--LHQCKtpIIHRDLKVENILLNDGGnYV------LC 197
Cdd:cd05589  77 VCFVMEYAAGGDLMMHIHEDV---FSEPRA--VFYAACVVLGLqfLHEHK--IVYRDLKLDNLLLDTEG-YVkiadfgLC 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 198 D----FGSATNKFLNpqkdgvnvveeeikkytTLSYRAPEMINlyggKPITTKA-DIWALGCLLYKLCFFTLPF-GESQV 271
Cdd:cd05589 149 KegmgFGDRTSTFCG-----------------TPEFLAPEVLT----DTSYTRAvDWWGLGVLIYEMLVGESPFpGDDEE 207
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 38787904 272 AICDGnfTIPDNSRYSRNIH----CLIRFMLEPDPEHR 305
Cdd:cd05589 208 EVFDS--IVNDEVRYPRFLSteaiSIMRRLLRKNPERR 243
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
128-266 1.48e-04

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: 44.66  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAT---- 203
Cdd:cd05627  79 LIMEFLPGGDMMTLLMKK--DTLSEEATQFYIAETVLAIDAIHQLG--FIHRDIKPDNLLLDAKGHVKLSDFGLCTglkk 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 204 --------NKFLNPQKD------GVNVVEEEIKK------YTTL---SYRAPEMINLYGGKPIttkADIWALGCLLYKLC 260
Cdd:cd05627 155 ahrtefyrNLTHNPPSDfsfqnmNSKRKAETWKKnrrqlaYSTVgtpDYIAPEVFMQTGYNKL---CDWWSLGVIMYEML 231

                ....*.
gi 38787904 261 FFTLPF 266
Cdd:cd05627 232 IGYPPF 237
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
55-307 1.55e-04

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: 43.77  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  55 ESLAEGGFSTVFLVRTHG-GIRCALKRMYVNNMPDL-NVCKREITIMKELSgHKNIVGYLdcavnSISDNVWEVLILMEY 132
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRAdNTPVAVKSCRETLPPDLkAKFLQEARILKQYS-HPNIVRLI-----GVCTQKQPIYIVMEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 133 CRAGQVVNQMNKKlQTGFTEPEVLQIFCDTCEAVARLHQCKTpiIHRDLKVENILLNDGGNYVLCDFGSATNkflnpQKD 212
Cdd:cd05084  76 VQGGDFLTFLRTE-GPRLKVKELIRMVENAAAGMEYLESKHC--IHRDLAARNCLVTEKNVLKISDFGMSRE-----EED 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 213 GVNVVEEEIKKyTTLSYRAPEMINlYGgkPITTKADIWALGCLLYKlcffTLPFGESQvaicdgnFTIPDNSRYSRNIHC 292
Cdd:cd05084 148 GVYAATGGMKQ-IPVKWTAPEALN-YG--RYSSESDVWSFGILLWE----TFSLGAVP-------YANLSNQQTREAVEQ 212
                       250
                ....*....|....*
gi 38787904 293 LIRFmlePDPEHRPD 307
Cdd:cd05084 213 GVRL---PCPENCPD 224
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
48-306 1.89e-04

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 44.05  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHGGIR------CALKRMYVNNMPDLNV-CKREITIMKELSgHKNIVGYLD-CAVNSI 119
Cdd:cd05050   4 RNNIEYVRDIGQGAFGRVFQARAPGLLPyepftmVAVKMLKEEASADMQAdFQREAALMAEFD-HPNIVKLLGvCAVGKP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SDNVWEVLI---LMEYCRAGQVVNQMNKKLQTG-----------FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVEN 185
Cdd:cd05050  83 MCLLFEYMAygdLNEFLRHRSPRAQCSLSHSTSsarkcglnplpLSCTEQLCIAKQVAAGMAYLSERK--FVHRDLATRN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 186 ILLNDGGNYVLCDFGSATNKFLnpqKDGVNVVEEEikkYTTLSYRAPEMI--NLYggkpiTTKADIWALGCLLYKLC--- 260
Cdd:cd05050 161 CLVGENMVVKIADFGLSRNIYS---ADYYKASEND---AIPIRWMPPESIfyNRY-----TTESDVWAYGVVLWEIFsyg 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 38787904 261 ---FFTLPFGESQVAICDGN-FTIPDNSRYSrnIHCLIRFMLEPDPEHRP 306
Cdd:cd05050 230 mqpYYGMAHEEVIYYVRDGNvLSCPDNCPLE--LYNLMRLCWSKLPSDRP 277
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
94-259 2.04e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 43.62  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKE-LSGHKNIVGYLdcAVNSISDNVW-EVLILMEYCRAGQVVNQmnkkLQTGFTEPEVLQIFCDTCEA-VARLH 170
Cdd:cd14144  36 RETEIYQTvLMRHENILGFI--AADIKGTGSWtQLYLITDYHENGSLYDF----LRGNTLDTQSMLKLAYSAACgLAHLH 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 ------QCKTPIIHRDLKVENILLNDGGNYVLCDFGSATnKFlNPQKDGVNVVEEeiKKYTTLSYRAPEMINLYGGK--- 241
Cdd:cd14144 110 teifgtQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAV-KF-ISETNEVDLPPN--TRVGTKRYMAPEVLDESLNRnhf 185
                       170
                ....*....|....*...
gi 38787904 242 PITTKADIWALGCLLYKL 259
Cdd:cd14144 186 DAYKMADMYSFGLVLWEI 203
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
105-259 2.10e-04

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 43.86  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLdCAVNSISDNVWEVLILMEYCRAGQVvnqmnkklqTGFTEPEVLQI--FCDTCEAVAR----LH-------- 170
Cdd:cd14053  48 HENILQFI-GAEKHGESLEAEYWLITEFHERGSL---------CDYLKGNVISWneLCKIAESMARglayLHedipatng 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 QCKTPIIHRDLKVENILLNDGGNYVLCDFGSATnKFLNPQKDGvnvveEEIKKYTTLSYRAPEMinLYGGKPITTKA--- 247
Cdd:cd14053 118 GHKPSIAHRDFKSKNVLLKSDLTACIADFGLAL-KFEPGKSCG-----DTHGQVGTRRYMAPEV--LEGAINFTRDAflr 189
                       170
                ....*....|...
gi 38787904 248 -DIWALGCLLYKL 259
Cdd:cd14053 190 iDMYAMGLVLWEL 202
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
46-259 2.30e-04

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: 43.49  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHG------GIRCALKRMYVNNMPDLNVCKREITIMKELSgHKNIVGYLDCAVNSI 119
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVFLAECYNlcpeqdKILVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 120 SdnvweVLILMEYCRAGqvvnQMNKKLQ---------------TGFTEPEVLQIFCDTceAVARLHQCKTPIIHRDLKVE 184
Cdd:cd05093  81 P-----LIMVFEYMKHG----DLNKFLRahgpdavlmaegnrpAELTQSQMLHIAQQI--AAGMVYLASQHFVHRDLATR 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 185 NILLNDGGNYVLCDFGSAtnkflnpqKDGVNVVEEEIKKYTTLSYR--APEMInLYggKPITTKADIWALGCLLYKL 259
Cdd:cd05093 150 NCLVGENLLVKIGDFGMS--------RDVYSTDYYRVGGHTMLPIRwmPPESI-MY--RKFTTESDVWSLGVVLWEI 215
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
176-305 2.66e-04

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 43.25  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904   176 IIHRDLKVENILLNDGGNYVLCDFGSATnkflnpqKDGVNVVEEEIKKyttlSYRAPEMINLYGGKP------ITTKADI 249
Cdd:pfam14531 165 LVHGQFTVDNFFLDQRGGVFLGGFEHLV-------RDGTKVVASEVPR----GFAPPELLGSRGGYTmknttlMTHAFDA 233
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38787904   250 WALGCLLYKLCFFTLPFGE-SQVAICDGNFT----IPDNSRYsrnihcLIRFMLEPDPEHR 305
Cdd:pfam14531 234 WQLGLVIYWIWCLDLPNTLdAEEGGIEWKFRlcknIPEPVRA------LLKGFLNYSQEDR 288
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
46-264 2.88e-04

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 43.46  E-value: 2.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHGG--------IRCALKRMYVN-NMPDLNVCKREITIMKELSGHKNIVGYLDCAV 116
Cdd:cd05098  10 LPRDRLVLGKPLGEGCFGQVVLAEAIGLdkdkpnrvTKVAVKMLKSDaTEKDLSDLISEMEMMKMIGKHKNIINLLGACT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 117 NSisdnvWEVLILMEYCRAGQVVNQMNKKLQTGFT-------EPEVLQIFCD--TCE-AVAR--LHQCKTPIIHRDLKVE 184
Cdd:cd05098  90 QD-----GPLYVIVEYASKGNLREYLQARRPPGMEycynpshNPEEQLSSKDlvSCAyQVARgmEYLASKKCIHRDLAAR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 185 NILLNDGGNYVLCDFGSATNkflnpqKDGVNVVEEEIKKYTTLSYRAPEMI--NLYggkpiTTKADIWALGCLLYKLcfF 262
Cdd:cd05098 165 NVLVTEDNVMKIADFGLARD------IHHIDYYKKTTNGRLPVKWMAPEALfdRIY-----THQSDVWSFGVLLWEI--F 231

                ..
gi 38787904 263 TL 264
Cdd:cd05098 232 TL 233
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
57-268 3.16e-04

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 42.98  E-value: 3.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVRtHGGIR--CALKRMYVNNMP---DLNVCKREITIMkelsgHKNIVGYLdCAVNSISDNVWEVLILME 131
Cdd:cd14026   5 LSRGAFGTVSRAR-HADWRvtVAIKCLKLDSPVgdsERNCLLKEAEIL-----HKARFSYI-LPILGICNEPEFLGIVTE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 132 YCRAGQVvNQM--NKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLN- 208
Cdd:cd14026  78 YMTNGSL-NELlhEKDIYPDVAWPLRLRILYEIALGVNYLHNMSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSi 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 209 PQKDGVNVVEEEikkyTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGE 268
Cdd:cd14026 157 SQSRSSKSAPEG----GTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPFEE 212
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
176-266 3.33e-04

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: 43.11  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYVLCDFGSATNkfLNPQKDGVNVveeeikkyTTLSYRAPEMinLYGGKPITTKADIWALGCL 255
Cdd:cd14223 124 VVYRDLKPANILLDEFGHVRISDLGLACD--FSKKKPHASV--------GTHGYMAPEV--LQKGVAYDSSADWFSLGCM 191
                        90
                ....*....|.
gi 38787904 256 LYKLCFFTLPF 266
Cdd:cd14223 192 LFKLLRGHSPF 202
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
94-256 3.73e-04

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: 42.88  E-value: 3.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNI-----VGYLDCAVNsisdnvwevlILMEYCRAGQVVNQMNKKLQTgFTEPEVLQIFCDTCEAVAR 168
Cdd:cd14154  39 KEVKVMRSLD-HPNVlkfigVLYKDKKLN----------LITEYIPGGTLKDVLKDMARP-LPWAQRVRFAKDIASGMAY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEI---------KKYTTLS---YRAPEMIN 236
Cdd:cd14154 107 LHSMN--IIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPSGNMSPSETLrhlkspdrkKRYTVVGnpyWMAPEMLN 184
                       170       180
                ....*....|....*....|
gi 38787904 237 lygGKPITTKADIWALGCLL 256
Cdd:cd14154 185 ---GRSYDEKVDIFSFGIVL 201
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
176-266 3.75e-04

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: 43.09  E-value: 3.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLND----GGNYVLCDFGSATnkflnpqkdgvNVVEEEIKKY-TTLSYRAPEMINlygGKPITTKADIW 250
Cdd:cd14229 123 LIHADLKPENIMLVDpvrqPYRVKVIDFGSAS-----------HVSKTVCSTYlQSRYYRAPEIIL---GLPFCEAIDMW 188
                        90
                ....*....|....*.
gi 38787904 251 ALGCLLYKLcFFTLPF 266
Cdd:cd14229 189 SLGCVIAEL-FLGWPL 203
PTZ00284 PTZ00284
protein kinase; Provisional
150-260 3.78e-04

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 43.42  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  150 FTEPEVLQIFCDTCEAVARLHQcKTPIIHRDLKVENILLNDGGNYVlcdfGSATNKFLNPQKDGVNVVE-----EEIKKY 224
Cdd:PTZ00284 228 FSHRHLAQIIFQTGVALDYFHT-ELHLMHTDLKPENILMETSDTVV----DPVTNRALPPDPCRVRICDlggccDERHSR 302
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 38787904  225 T----TLSYRAPEMInLYGGKPITTkaDIWALGCLLYKLC 260
Cdd:PTZ00284 303 TaivsTRHYRSPEVV-LGLGWMYST--DMWSMGCIIYELY 339
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
57-259 6.05e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 42.22  E-value: 6.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  57 LAEGGFSTVFLVR-----THGGIRCALKRMYV----NNMPDLnvcKREITIMKELSgHKNIVGYLDCAVNSISDNVwevL 127
Cdd:cd05079  12 LGEGHFGKVELCRydpegDNTGEQVAVKSLKPesggNHIADL---KKEIEILRNLY-HENIVKYKGICTEDGGNGI---K 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 128 ILMEYCRAGQV-------VNQMNKKLQTGFTepevLQIfcdtCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFG 200
Cdd:cd05079  85 LIMEFLPSGSLkeylprnKNKINLKQQLKYA----VQI----CKGMDYLGSRQ--YVHRDLAARNVLVESEHQVKIGDFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 201 SA----TNKFLNPQKDGVNvveeeikkyTTLSYRAPEMInlyggkpITTK----ADIWALGCLLYKL 259
Cdd:cd05079 155 LTkaieTDKEYYTVKDDLD---------SPVFWYAPECL-------IQSKfyiaSDVWSFGVTLYEL 205
PRK14879 PRK14879
Kae1-associated kinase Bud32;
122-200 7.99e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 41.43  E-value: 7.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904  122 NVWEVLILMEYCRaGQVVNQMNKKLqtgftEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLcDFG 200
Cdd:PRK14879  70 DPENFIIVMEYIE-GEPLKDLINSN-----GMEELELSREIGRLVGKLH--SAGIIHGDLTTSNMILSGGKIYLI-DFG 139
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
51-259 8.26e-04

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: 41.91  E-value: 8.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEESLAEGGFSTVF--LVRTHGGIRCALKRMYV-----NNMPDLnvcKREITIMKELSGHKNIVGYLDCAvnsisDNV 123
Cdd:cd05089   4 IKFEDVIGEGNFGQVIkaMIKKDGLKMNAAIKMLKefaseNDHRDF---AGELEVLCKLGHHPNIINLLGAC-----ENR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 124 WEVLILMEYCRAGQVVNQMNKK--LQTG------------FTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLN 189
Cdd:cd05089  76 GYLYIAIEYAPYGNLLDFLRKSrvLETDpafakehgtastLTSQQLLQFASDVAKGMQYLSEKQ--FIHRDLAARNVLVG 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 190 DGGNYVLCDFGSATnkflnpqkdGVNVVEEEIKKYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKL 259
Cdd:cd05089 154 ENLVSKIADFGLSR---------GEEVYVKKTMGRLPVRWMAIESLNY---SVYTTKSDVWSFGVLLWEI 211
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
46-259 8.81e-04

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 41.88  E-value: 8.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  46 VGRHQVTLEESLAEGGFSTVFLVRTHG----------GIRcALKRMYVNNMPDLnvcKREITIMKELSgHKNIVGYLDCA 115
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVFLAECHNllpeqdkmlvAVK-ALKEATESARQDF---QREAELLTVLQ-HQHIVRFYGVC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 116 VNSisdnvwEVLILM-EYCRAG-------------QVVNQMNKKLQTGFTEPEVLQIFCDTCEA---VARLHqcktpIIH 178
Cdd:cd05092  77 TEG------EPLIMVfEYMRHGdlnrflrshgpdaKILDGGEGQAPGQLTLGQMLQIASQIASGmvyLASLH-----FVH 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 179 RDLKVENILLNDGGNYVLCDFGSAtnkflnpqKDGVNVVEEEIKKYTTLSYR--APEMInLYggKPITTKADIWALGCLL 256
Cdd:cd05092 146 RDLATRNCLVGQGLVVKIGDFGMS--------RDIYSTDYYRVGGRTMLPIRwmPPESI-LY--RKFTTESDIWSFGVVL 214

                ...
gi 38787904 257 YKL 259
Cdd:cd05092 215 WEI 217
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
105-306 9.68e-04

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 41.45  E-value: 9.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVG----YLDcavnsISDNVWEVLILMEYCRAG---QVVNQMNKKLQTgfTEPEVLQIFC-DTCEAVARLHQCKTPI 176
Cdd:cd14035  54 HPNIVKfhkyWLD-----VKDNHARVVFITEYVSSGslkQFLKKTKKNHKT--MNARAWKRWCtQILSALSYLHSCEPPI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGnyvLCDFGSATNK-FLNPQKDG-----VNVVEEEIKkytTLSYRAPEminlYGGKPITTKADIW 250
Cdd:cd14035 127 IHGNLTSDTIFIQHNG---LIKIGSVWHRlFVNVLPEGgvrgpLRQEREELR---NLHFFPPE----YGSCEDGTAVDIF 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 251 ALG-CLLYKLCFFTLPFGESQV---AICDGNFTIPDNSRYSRNIHCLIRfmlepDPEHRP 306
Cdd:cd14035 197 SFGmCALEMAVLEIQANGDTRVseeAIARARHSLEDPNMREFILSCLRH-----NPCKRP 251
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
94-259 1.00e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 41.56  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKE-LSGHKNIVGYLDCAVNSISDNVwEVLILMEYCRAGQVVNQMnkKLQTGFTEPEVLQIFCDTCeAVARLH-- 170
Cdd:cd14220  36 RETEIYQTvLMRHENILGFIAADIKGTGSWT-QLYLITDYHENGSLYDFL--KCTTLDTRALLKLAYSAAC-GLCHLHte 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 171 ----QCKTPIIHRDLKVENILLNDGGNYVLCDFGSATnKFlNPQKDGVNVVEEeiKKYTTLSYRAPEMINLYGGK---PI 243
Cdd:cd14220 112 iygtQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAV-KF-NSDTNEVDVPLN--TRVGTKRYMAPEVLDESLNKnhfQA 187
                       170
                ....*....|....*.
gi 38787904 244 TTKADIWALGCLLYKL 259
Cdd:cd14220 188 YIMADIYSFGLIIWEM 203
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
94-256 1.05e-03

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: 41.47  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  94 REITIMKELSgHKNI-----VGYLDCAVNSISDNVwEVLILMEYCRAgqvvnqmnkklQTGFTEPEVLQIFCDTCEAVAR 168
Cdd:cd14222  39 TEVKVMRSLD-HPNVlkfigVLYKDKRLNLLTEFI-EGGTLKDFLRA-----------DDPFPWQQKVSFAKGIASGMAY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 169 LHQckTPIIHRDLKVENILLNDGGNYVLCDFGSA----TNKFLNPQKDGVNVVE-----EEIKKYTTLS---YRAPEMIN 236
Cdd:cd14222 106 LHS--MSIIHRDLNSHNCLIKLDKTVVVADFGLSrlivEEKKKPPPDKPTTKKRtlrknDRKKRYTVVGnpyWMAPEMLN 183
                       170       180
                ....*....|....*....|
gi 38787904 237 lygGKPITTKADIWALGCLL 256
Cdd:cd14222 184 ---GKSYDEKVDIFSFGIVL 200
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
176-266 1.44e-03

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 41.50  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  176 IIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqkdgvNVVeeEIKKYT---TLSYRAPE-MINLYGGKpittKADIWA 251
Cdd:PTZ00426 152 IVYRDLKPENLLLDKDGFIKMTDFGFA------------KVV--DTRTYTlcgTPEYIAPEiLLNVGHGK----AADWWT 213
                         90
                 ....*....|....*
gi 38787904  252 LGCLLYKLCFFTLPF 266
Cdd:PTZ00426 214 LGIFIYEILVGCPPF 228
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
105-253 1.47e-03

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 40.89  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 105 HKNIVGYLDCAVNsISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPE-VLQIFC-DTCEAVARLHQCKTPIIHRDLK 182
Cdd:cd14034  69 HLNIVKFHKYWAD-VKENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEkAWKRWCtQILSALSYLHSCDPPIIHGNLT 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38787904 183 VENILLNDGGnyvLCDFGSATNKFLNpqkDGVNVVEEEIKkytTLSYRAPEminlYGG-KPITTKADIWALG 253
Cdd:cd14034 148 CDTIFIQHNG---LIKIGSVAPDTIN---NHVKTCREEQK---NLHFFAPE----YGEvANVTTAVDIYSFG 206
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
163-270 1.48e-03

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: 41.38  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 163 CEAVARLHQCKtpIIHRDLKVENILLNDGgNYV--------------------LCDFGSATNKFlnpqkdgvnvvEEEIK 222
Cdd:cd14213 126 CKSVNFLHHNK--LTHTDLKPENILFVQS-DYVvkynpkmkrdertlknpdikVVDFGSATYDD-----------EHHST 191
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 38787904 223 KYTTLSYRAPEMINLYGGkpiTTKADIWALGCLL--YKLCFFTLPFGESQ 270
Cdd:cd14213 192 LVSTRHYRAPEVILALGW---SQPCDVWSIGCILieYYLGFTVFQTHDSK 238
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
128-203 1.48e-03

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: 41.37  E-value: 1.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38787904 128 ILMEYCRAGQVVNqMNKKLQTgFTEpEVLQIFCDTCE-AVARLHqcKTPIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd05629  78 LIMEFLPGGDLMT-MLIKYDT-FSE-DVTRFYMAECVlAIEAVH--KLGFIHRDIKPDNILIDRGGHIKLSDFGLST 149
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
128-203 1.56e-03

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: 41.18  E-value: 1.56e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38787904 128 ILMEYCRAGQVVNQMNKKlqTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLNDGGNYVLCDFGSAT 203
Cdd:cd05628  78 LIMEFLPGGDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLG--FIHRDIKPDNLLLDSKGHVKLSDFGLCT 149
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
50-259 1.60e-03

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: 41.10  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  50 QVTLEESLAEGGF-----STVFLVRTHGGIR-CALKRMYVNNMP-DLNVCKREITIMKELSgHKNIVGYLDCAVNSISdn 122
Cdd:cd05045   1 NLVLGKTLGEGEFgkvvkATAFRLKGRAGYTtVAVKMLKENASSsELRDLLSEFNLLKQVN-HPHVIKLYGACSQDGP-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 123 vweVLILMEYCRAGQVVN--QMNKKLQTGF--------------------TEPEVLQIFCDTCEAVARLHQCKtpIIHRD 180
Cdd:cd05045  78 ---LLLIVEYAKYGSLRSflRESRKVGPSYlgsdgnrnssyldnpderalTMGDLISFAWQISRGMQYLAEMK--LVHRD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 181 LKVENILLNDGGNYVLCDFGSA-----TNKFLNPQKDGVNVveeeikkyttlSYRAPEMI--NLYggkpiTTKADIWALG 253
Cdd:cd05045 153 LAARNVLVAEGRKMKISDFGLSrdvyeEDSYVKRSKGRIPV-----------KWMAIESLfdHIY-----TTQSDVWSFG 216

                ....*.
gi 38787904 254 CLLYKL 259
Cdd:cd05045 217 VLLWEI 222
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
95-259 1.60e-03

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: 40.79  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  95 EITIMKELSGHKNIVGYLDCAvnsisDNVWEVLILMEYCRAGQVVNQMNKK--LQTG------------FTEPEVLQIFC 160
Cdd:cd05047  45 ELEVLCKLGHHPNIINLLGAC-----EHRGYLYLAIEYAPHGNLLDFLRKSrvLETDpafaianstastLSSQQLLHFAA 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 161 DTCEAVARLHQCKtpIIHRDLKVENILLNDggNYV--LCDFGSATnkflnpqkdGVNVVEEEIKKYTTLSYRAPEMINLy 238
Cdd:cd05047 120 DVARGMDYLSQKQ--FIHRDLAARNILVGE--NYVakIADFGLSR---------GQEVYVKKTMGRLPVRWMAIESLNY- 185
                       170       180
                ....*....|....*....|.
gi 38787904 239 ggKPITTKADIWALGCLLYKL 259
Cdd:cd05047 186 --SVYTTNSDVWSYGVLLWEI 204
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
48-314 1.70e-03

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 41.37  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  48 RHQVTLEESLAEGGFSTVFLVRTHG------GIRCALKRMYVNNMPD-LNVCKREITIMKELSGHKNIVGYLDCAVNSis 120
Cdd:cd05106  37 RDNLQFGKTLGAGAFGKVVEATAFGlgkednVLRVAVKMLKASAHTDeREALMSELKILSHLGQHKNIVNLLGACTHG-- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 121 dnvWEVLILMEYCRAGQVVNQMNKKLQT--------------------------------GF------TEPEVLQIFCDT 162
Cdd:cd05106 115 ---GPVLVITEYCCYGDLLNFLRKKAETflnfvmalpeisetssdyknitlekkyirsdsGFssqgsdTYVEMRPVSSSS 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 163 CEAVARLHQCKTP----------------------------IIHRDLKVENILLNDGGNYVLCDFGSAtnkflnpqKDGV 214
Cdd:cd05106 192 SQSSDSKDEEDTEdswpldlddllrfssqvaqgmdflasknCIHRDVAARNVLLTDGRVAKICDFGLA--------RDIM 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 215 NVVEEEIKKYTTL--SYRAPEMI--NLYggkpiTTKADIWALGCLLYKLcfFTLPFGESQVAICDGNF--TIPDNSRYSR 288
Cdd:cd05106 264 NDSNYVVKGNARLpvKWMAPESIfdCVY-----TVQSDVWSYGILLWEI--FSLGKSPYPGILVNSKFykMVKRGYQMSR 336
                       330       340       350
                ....*....|....*....|....*....|..
gi 38787904 289 ------NIHCLIRFMLEPDPEHRPDIFQVSYF 314
Cdd:cd05106 337 pdfappEIYSIMKMCWNLEPTERPTFSQISQL 368
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
157-233 2.07e-03

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: 40.88  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 157 QIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDG-GNYVLCDFGSATNkflnpQKDGVNVveeeIKKYTTLS--YRAPE 233
Cdd:cd14013 124 SIMRQILVALRKLH--STGIVHRDVKPQNIIVSEGdGQFKIIDLGAAAD-----LRIGINY----IPKEFLLDprYAPPE 192
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
176-259 2.38e-03

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: 40.84  E-value: 2.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGN----YVLCDFGSATNkflnpqkdgvnVVEEEIKKY-TTLSYRAPEMINlygGKPITTKADIW 250
Cdd:cd14227 138 LIHADLKPENIMLVDPSRqpyrVKVIDFGSASH-----------VSKAVCSTYlQSRYYRAPEIIL---GLPFCEAIDMW 203

                ....*....
gi 38787904 251 ALGCLLYKL 259
Cdd:cd14227 204 SLGCVIAEL 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
176-266 3.31e-03

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: 39.82  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDGGNYV--LCDFGSAtnkflnpQKdgvnvVEEEIKKYT--TLSYRAPEMINlyGGKPITTKADIWA 251
Cdd:cd14112 120 IAHLDVQPDNIMFQSVRSWQvkLVDFGRA-------QK-----VSKLGKVPVdgDTDWASPEFHN--PETPITVQSDIWG 185
                        90
                ....*....|....*
gi 38787904 252 LGCLLYKLCFFTLPF 266
Cdd:cd14112 186 LGVLTFCLLSGFHPF 200
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
163-264 3.42e-03

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: 40.00  E-value: 3.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 163 CEAVARLHQCKtpIIHRDLKVENILLNDGgNYVL--------------------CDFGSATNKFlnpqkdgvnvvEEEIK 222
Cdd:cd14215 126 CQAVKFLHDNK--LTHTDLKPENILFVNS-DYELtynlekkrdersvkstairvVDFGSATFDH-----------EHHST 191
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 38787904 223 KYTTLSYRAPEMINLYGGkpiTTKADIWALGCLLYKLCF-FTL 264
Cdd:cd14215 192 IVSTRHYRAPEVILELGW---SQPCDVWSIGCIIFEYYVgFTL 231
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
126-259 3.61e-03

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 39.84  E-value: 3.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 126 VLILMEYCRAGQVVNQMNKKLQtgftEPEVLQIFCDTCE------------------------AVARLHQckTPIIHRDL 181
Cdd:cd05576  66 VFLVLQHAEGGKLWSYLSKFLN----DKEIHQLFADLDErlaaasrfyipeeciqrwaaemvvALDALHR--EGIVCRDL 139
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 182 KVENILLNDGGNYVLCDFGSATNkfLNPQKDGvnvveEEIKKYttlsYRAPEMinlyGGKPITTKA-DIWALGCLLYKL 259
Cdd:cd05576 140 NPNNILLNDRGHIQLTYFSRWSE--VEDSCDS-----DAIENM----YCAPEV----GGISEETEAcDWWSLGALLFEL 203
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
60-324 4.10e-03

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: 39.38  E-value: 4.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  60 GGFSTVFLV--RTHGGIRcALKRMYVN-NMPDLnvcKREITIMKELSgHKNIVGYLDCAVNSisdnvWEVLILMEYCRAG 136
Cdd:cd14155   4 GFFSEVYKVrhRTSGQVM-ALKMNTLSsNRANM---LREVQLMNRLS-HPNILRFMGVCVHQ-----GQLHALTEYINGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 137 QVVNQMNKKLQTGFTEPevLQIFCDTCEAVARLHQckTPIIHRDLKVENILL---NDGGNYVLCDFGSAtnkflnpqkDG 213
Cdd:cd14155  74 NLEQLLDSNEPLSWTVR--VKLALDIARGLSYLHS--KGIFHRDLTSKNCLIkrdENGYTAVVGDFGLA---------EK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 214 VNVVEEEIKKYTTLS---YRAPEMINlygGKPITTKADIWALGCLLyklcfftlpfgesqvaicdgnftipdnsrysrni 290
Cdd:cd14155 141 IPDYSDGKEKLAVVGspyWMAPEVLR---GEPYNEKADVFSYGIIL---------------------------------- 183
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38787904 291 hCLIRFMLEPDPEHRP--DIFQVSYFAFKFAKKDCP 324
Cdd:cd14155 184 -CEIIARIQADPDYLPrtEDFGLDYDAFQHMVGDCP 218
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
177-306 4.34e-03

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 39.89  E-value: 4.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 177 IHRDLKVENILLNDGGNYVLCDFGSATNKflnpQKDGVNVVEEEIKkyTTLSYRAPEMI--NLYggkpiTTKADIWALGC 254
Cdd:cd05104 236 IHRDLAARNILLTHGRITKICDFGLARDI----RNDSNYVVKGNAR--LPVKWMAPESIfeCVY-----TFESDVWSYGI 304
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 38787904 255 LLYKLcfFTLpfGESQVAicdgnfTIPDNSRYSRNIHCLIRFMlepDPEHRP 306
Cdd:cd05104 305 LLWEI--FSL--GSSPYP------GMPVDSKFYKMIKEGYRMD---SPEFAP 343
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
176-259 6.83e-03

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: 39.30  E-value: 6.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 176 IIHRDLKVENILLNDG----GNYVLCDFGSATNkflnpqkdgvnVVEEEIKKY-TTLSYRAPEMINlygGKPITTKADIW 250
Cdd:cd14228 138 LIHADLKPENIMLVDPvrqpYRVKVIDFGSASH-----------VSKAVCSTYlQSRYYRAPEIIL---GLPFCEAIDMW 203

                ....*....
gi 38787904 251 ALGCLLYKL 259
Cdd:cd14228 204 SLGCVIAEL 212
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
51-259 7.38e-03

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: 38.83  E-value: 7.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904  51 VTLEESLAEGGFSTVFLVRTH-GGIR--CALKRMY-VNNMPDLNVCKREITIMKELSGHKNIV---------GYLDCAVN 117
Cdd:cd05088   9 IKFQDVIGEGNFGQVLKARIKkDGLRmdAAIKRMKeYASKDDHRDFAGELEVLCKLGHHPNIInllgacehrGYLYLAIE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38787904 118 SISDNVwevliLMEYCRAGQVVNQ-----MNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKtpIIHRDLKVENILLndGG 192
Cdd:cd05088  89 YAPHGN-----LLDFLRKSRVLETdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQ--FIHRDLAARNILV--GE 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38787904 193 NYV--LCDFGSATnkflnpqkdGVNVVEEEIKKYTTLSYRAPEMINLyggKPITTKADIWALGCLLYKL 259
Cdd:cd05088 160 NYVakIADFGLSR---------GQEVYVKKTMGRLPVRWMAIESLNY---SVYTTNSDVWSYGVLLWEI 216
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
127-200 9.01e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 37.96  E-value: 9.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38787904   127 LILMEYCRaGQVVNQMnkklqtgfTEPEVLQIFCDTCEAVARLHqcKTPIIHRDLKVENILLNDGGNYVLcDFG 200
Cdd:TIGR03724  73 TIVMEYIE-GKPLKDV--------IEENGDELAREIGRLVGKLH--KAGIVHGDLTTSNIIVRDDKVYLI-DFG 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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