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Conserved domains on  [gi|13928846|ref|NP_113805|]
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casein kinase I isoform epsilon [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
15-207 8.44e-33

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 123.12  E-value: 8.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL-GPSLE 90
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKiikKEDSSSLLEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEYCeGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  91 DLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDarthqhiPYREN 170
Cdd:cd00180  80 DLLKENEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENIL--LDSDNGKVKLADFGLSKLLTS-------DKSLL 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13928846 171 KNLTGTARYASINTHLGI-EQSRRDDLESLGYVLMYFN 207
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYELP 188
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
15-207 8.44e-33

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 123.12  E-value: 8.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL-GPSLE 90
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKiikKEDSSSLLEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEYCeGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  91 DLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDarthqhiPYREN 170
Cdd:cd00180  80 DLLKENEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENIL--LDSDNGKVKLADFGLSKLLTS-------DKSLL 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13928846 171 KNLTGTARYASINTHLGI-EQSRRDDLESLGYVLMYFN 207
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYELP 188
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 4.00e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 97.33  E-value: 4.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846    6 GNKYRLGRKIGSGSFGDIY---LGANIASGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13928846  219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
81-162 2.89e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 43.74  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   81 VMELL-GPSLEDLFNfcSRKFSLKTVLLLADQMISRIeyiHSKNFIHRDVKPDNFLMglgkKGNLVYIIDFGLAKKYRDA 159
Cdd:PRK14879  77 VMEYIeGEPLKDLIN--SNGMEELELSREIGRLVGKL---HSAGIIHGDLTTSNMIL----SGGKIYLIDFGLAEFSKDL 147

                 ...
gi 13928846  160 RTH 162
Cdd:PRK14879 148 EDR 150
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
119-155 1.90e-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: 234331  Cd Length: 199  Bit Score: 37.97  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13928846   119 IHSKNFIHRDVKPDNFLMGLGKkgnlVYIIDFGLAKK 155
Cdd:TIGR03724 106 LHKAGIVHGDLTTSNIIVRDDK----LYLIDFGLGKY 138
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]
3-201 5.38e-03

Predicted Ser/Thr protein kinase [Signal transduction mechanisms]


Pssm-ID: 225023  Cd Length: 201  Bit Score: 36.62  E-value: 5.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   3 LRVGNKYRLG--RKIGSGSFGDIYLGAniASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGaegdYNVM 80
Cdd:COG2112  16 NVEEGKYELRveKELAKGTTSVVYLGE--WRGGEVALKVRRRDSPRRNLEKEAKILEILAGEGVTPEVYFYG----EDFI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  81 VME-LLGPSLEDLFNFCSRKFSLKTV---LLLADQMISRIEyihsknfIHRdvkPDNFLMGLGKKgnlVYIIDFGLAKKY 156
Cdd:COG2112  90 RMEyIDGRPLGKLEIGGDRKHLLRVLekaYKLDRLGIEHGE-------LSR---PWKNVLVNDRD---VYIIDFDSATFK 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13928846 157 RDARthqhipyrenkNLTGTARYasinthLGIEQSRRDDLESLGY 201
Cdd:COG2112 157 KKPR-----------NVTQALSL------LFREGLRIEKTILRGY 184
Pkinase pfam00069
Protein kinase domain;
9-246 1.34e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 167.81  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846     9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHI----ESKFYKMMQGGVGIPSIKWCgAEGDYNVMVMEL 84
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQtarrEIRILRRLSHPNIVRLIDAF-EDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846    85 LGPSleDLFNFCSRK--FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKyrdarth 162
Cdd:pfam00069  80 CEGG--DLFDYLSRGgpLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENIL--LDENGV-VKIADFGLAKK------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   163 QHIPYRENKNLTGTARYASINTHL-GIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLC 241
Cdd:pfam00069 148 LTKSSSSLTTFVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDEPKSD 227

                  ....*
gi 13928846   242 KGYPS 246
Cdd:pfam00069 228 SGSEE 232
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
8-285 2.71e-36

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 137.18  E-value: 2.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIasgEEVAIK-----LECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVM 82
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR---KLVALKvlakkLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  83 ELL-GPSLEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDA 159
Cdd:COG0515  78 EYVdGGSLEDLLKKIGRkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIL--LDRDGRVVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 160 RTHQHIPYRENKNLtGTARYASINTHLGIEQ---SRRDDLESLGYVLMYFNLGSLPWQGLKAA-TKRQKYERISEKKMST 235
Cdd:COG0515 156 GSTSSIPALPSTSV-GTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSsATSQTLKIILELPTPS 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 13928846 236 PIEVLCKGYPSEFSTYLN--FCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYD 285
Cdd:COG0515 235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-238 2.27e-27

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 108.77  E-value: 2.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846      9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL 85
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKvikKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846     86 -GPSLEDLFNFCsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKKYRDARTHqh 164
Cdd:smart00220  80 eGGDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL--LDEDGH-VKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928846    165 ipyrenKNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY-FNLGSLPWQGlkAATKRQKYERISEKKMSTPIE 238
Cdd:smart00220 154 ------TTFVGTPEYMAPEVLLGKGYGKAVDIWSLG-VILYeLLTGKPPFPG--DDQLLELFKKIGKPKPPFPPP 219
pknD PRK13184
serine/threonine-protein kinase; Reviewed
8-239 9.68e-14

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 71.73  E-value: 9.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846    8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK-----LECVKTKHPQLHIESKFY-KMMQGGVgIPSIKWCgAEGDYNVMV 81
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKkiredLSENPLLKKRFLREAKIAaDLIHPGI-VPVYSIC-SDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   82 MELL-GPSLEDLFNFCSRKFSL----------KTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKgnlVYIIDF 150
Cdd:PRK13184  81 MPYIeGYTLKSLLKSVWQKESLskelaektsvGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGE---VVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  151 GLAK---KYRDARTHQHIPYREN--KNLT------GTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWqglkaa 219
Cdd:PRK13184 158 GAAIfkkLEEEDLLDIDVDERNIcySSMTipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY------ 231
                        250       260
                 ....*....|....*....|.
gi 13928846  220 tKRQKYERISEK-KMSTPIEV 239
Cdd:PRK13184 232 -RRKKGRKISYRdVILSPIEV 251
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
4-209 1.37e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 64.67  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846    4 RVGNK-YRLGRKIGSGSFGDIYLGANIASGEEVAIK--LECVKTKHPQLHIESKFykmmqGGVGIPSIK-----WCGAEG 75
Cdd:PTZ00036  62 RSPNKsYKLGNIIGNGSFGVVYEAICIDTSEKVAIKkvLQDPQYKNRELLIMKNL-----NHINIIFLKdyyytECFKKN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   76 DYNV---MVMELLGPSLEDLFNFCSRK---FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIID 149
Cdd:PTZ00036 137 EKNIflnVVMEFIPQTVHKYMKHYARNnhaLPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLL--IDPNTHTLKLCD 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13928846  150 FGLAKKYRDA-RTHQHIP---YRENKNLTGTARYasiNTHLgieqsrrdDLESLGYVLMYFNLG 209
Cdd:PTZ00036 215 FGSAKNLLAGqRSVSYICsrfYRAPELMLGATNY---TTHI--------DLWSLGCIIAEMILG 267
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
108-212 7.39e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 52.52  E-value: 7.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  108 LADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKgnlVYIIDFGLAKKYrdARTHQhiPYRENknlTGTARYAS---INT 184
Cdd:PLN00034 173 VARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRIL--AQTMD--PCNSS---VGTIAYMSperINT 242
                         90       100       110
                 ....*....|....*....|....*....|..
gi 13928846  185 HLgiEQSRRD----DLESLGYVLMYFNLGSLP 212
Cdd:PLN00034 243 DL--NHGAYDgyagDIWSLGVSILEFYLGRFP 272
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
91-154 5.72e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 49.47  E-value: 5.72e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928846   91 DLFNFC--SRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGnlVYIIDFGLAK 154
Cdd:PHA03390  95 DLFDLLkkEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDR--IYLCDYGLCK 158
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
15-207 8.44e-33

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 123.12  E-value: 8.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHIESKFYKMMQGgVGIPSIKWCGAEGDYNVMVMELL-GPSLE 90
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKiikKEDSSSLLEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEYCeGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  91 DLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYIIDFGLAKKYRDarthqhiPYREN 170
Cdd:cd00180  80 DLLKENEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENIL--LDSDNGKVKLADFGLSKLLTS-------DKSLL 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13928846 171 KNLTGTARYASINTHLGI-EQSRRDDLESLGYVLMYFN 207
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKgYYSEKSDIWSLGVILYELP 188
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
7-259 2.36e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 97.65  E-value: 2.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   7 NKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLeCVKT------KHPQLHIESKFYKMMQGGVGIpsIK-WCGAEGDYNV 79
Cdd:cd05581   1 DDFKFGKIIGEGSFSTVVLAKEKETNKEYAIKI-LDKRqlikekKVKYVKIEKEVLTRLNGHPGI--IKlYYTFQDEENL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  80 -MVMELL--GPSLEDLFNFCSrkFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVyIIDFGLAK-- 154
Cdd:cd05581  78 yFVLEYApnGELLQYIRKYGS--LDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENIL--LDKDMHIK-ITDFGTAKvl 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 155 -----------KYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY--------FNlGSLPWQG 215
Cdd:cd05581 153 dpnsspesnkgDATNIDSQIEKNRRRFASFVGTAEYVSPELLNEKPAGKSSDLWALG-CIIYqmltgkppFR-GSNEYLT 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 13928846 216 LKAATKRQ-KYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLR 259
Cdd:cd05581 231 FQKILKLEySFPPNFPPDAKDLIEKLLVLDPQDRLGVNEGYDELK 275
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
6-273 4.00e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 97.33  E-value: 4.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846    6 GNKYRLGRKIGSGSFGDIY---LGANIASGEEVAIKLECVKTKhpQLHIESKFYKMMQ--------------GGVGIPSI 68
Cdd:PHA02882  11 GKEWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENLENE--TIVMETLVYNNIYdidkialwknihniDHLGIPKY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   69 KWCGA----EGDYNVMVMELLGPSLEDLFN--FCSRKFSLKTVLLladQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKG 142
Cdd:PHA02882  89 YGCGSfkrcRMYYRFILLEKLVENTKEIFKriKCKNKKLIKNIMK---DMLTTLEYIHEHGISHGDIKPENIMVDGNNRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  143 nlvYIIDFGLAKKYrdARTHQHIPY-RENKNL-TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA-- 218
Cdd:PHA02882 166 ---YIIDYGIASHF--IIHGKHIEYsKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHng 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13928846  219 ----ATKRQKYERISEKKMStpIEVLCKGypseFSTYLNFCRSLRFDDKPDYSYLRQLF 273
Cdd:PHA02882 241 nlihAAKCDFIKRLHEGKIK--IKNANKF----IYDFIECVTKLSYEEKPDYDALIKIF 293
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
8-167 9.30e-23

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 95.35  E-value: 9.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKlecvktkhpQLHIESKF-YKMMQGGVGI------PSI-KWCGA--EGDY 77
Cdd:cd05122   1 LFEILEKIGKGGFGEVYKARHKRTGKEVAIK---------VIKLESKEkKEKIINEIQIlkkckhPNIvKYYGSylKKDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  78 NVMVMELL-GPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGnLVYIIDFGLAKKY 156
Cdd:cd05122  72 LWIVMEFCsGGSLKDLLKSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTS--DG-EVKLIDFGLSAQL 148
                       170
                ....*....|....
gi 13928846 157 RDARTHQHI---PY 167
Cdd:cd05122 149 SDTKARNTMvgtPY 162
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
8-155 9.77e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 89.92  E-value: 9.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKH-PQLHIESKFYKMMQGgvgiPSI-KWCGAEGD-----Y 77
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKsveLSGDSEEElEALEREIRILSSLQH----PNIvRYYGSERDeekntL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  78 NVmVMELL-GPSLEDLF-NFcsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKK 155
Cdd:cd06606  77 NI-FLEYVsGGSLSSLLkKF--GKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANIL--VDSDGV-VKLADFGCAKR 150
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
8-216 4.81e-20

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 87.78  E-value: 4.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVA---IKLECVKTK-HPQLHIESKFYKMMQGgvgiPSI-KWCGAEGDYNVMV- 81
Cdd:cd06626   1 RWQRGNKIGGGTFGKVYTAVNLDTGELMAvkeIRIQDNDPKtIKEIADEMKVLELLKH----PNLvKYYGVEVHREKVYi 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  82 -MELL-GPSLEDLFNFcSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVYiIDFGLAKKYRDA 159
Cdd:cd06626  77 fMEYCsGGTLEELLEH-GRILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIF--LDHNGVIKL-GDFGCAVKLKNN 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13928846 160 RThqhiPYREN-KNLTGTARYASINTHLGIEQS---RRDDLESLGYVLMYFNLGSLPWQGL 216
Cdd:cd06626 153 TT----TMGEEvQSLAGTPAYMAPEVITGGKGKghgRAADIWSLGCVVLEMATGKRPWSEL 209
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine ...
8-163 1.29e-19

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173736 [Multi-domain]  Cd Length: 286  Bit Score: 86.96  E-value: 1.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKH----PQLHIESKFYKMMQGGvGIPSIKWCGAEGDYNVMVME 83
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRRLEggipNQALREIKALQACQHP-YVVKLLDVFPHGSGFVLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  84 LLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKY----RDA 159
Cdd:cd07832  80 YMPSDLSEVLRDEERPLPEAQVKSYMRMLLKGVAYMHANGIMHRDLKPANLL--ISADGVL-KIADFGLARLFseeePRL 156

                ....
gi 13928846 160 RTHQ 163
Cdd:cd07832 157 YSHQ 160
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine ...
9-157 2.55e-19

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Male germ cell-Associated Kinase (MAK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAK-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. 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 (ECO), 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.


Pssm-ID: 173734 [Multi-domain]  Cd Length: 283  Bit Score: 86.05  E-value: 2.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKL---------ECVKTKhpqlhiESKFYKMMQGGVGIPSIKWCGAEGDYNV 79
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKmkkkfysweECMNLR------EVKSLRKLNEHPNIVKLKEVFRENDELY 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928846  80 MVMELLGPSLEDLF-NFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYR 157
Cdd:cd07830  75 FVFEYMEGNLYQLMkDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV---SGPEVVKIADFGLAREIR 150
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
15-236 1.11e-18

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 83.72  E-value: 1.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIKL----ECVKTKHpQLH----------IESKFykmmqggvgIPSIKWCGAEGDYNVM 80
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVlkkkKIIKRKE-VEHtlternilsrINHPF---------IVKLHYAFQTEEKLYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  81 VMELL--GpsleDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVyIIDFGLAKK- 155
Cdd:cd05123  71 VLEYApgG----ELFSHLSKegRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENIL--LDADGHIK-LTDFGLAKEl 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 156 -YRDARTHQhipyrenknLTGTARYASINTHLGIEQSRRDDLESLGyVLMYFNL-GSLPWQglkAATKRQKYERISEKKM 233
Cdd:cd05123 144 sSEGSRTNT---------FCGTPEYLAPEVLLGKGYGKAVDWWSLG-VLLYEMLtGKPPFY---AEDRKEIYEKILKDPL 210

                ...
gi 13928846 234 STP 236
Cdd:cd05123 211 RFP 213
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
8-156 1.13e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 77.92  E-value: 1.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK------------------LECVKT-KHPqlHIeskfykmmqggvgipsI 68
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKeidlsnmsekeredalneVKILKKlNHP--NI----------------I 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  69 KWCGA--EGDYNVMVMELL-GPSLEDLF---NFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDN-FLMglgkK 141
Cdd:cd08215  63 KYYESfeEKGKLCIVMEYAdGGDLSQKIkkqKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNiFLT----S 138
                       170
                ....*....|....*
gi 13928846 142 GNLVYIIDFGLAKKY 156
Cdd:cd08215 139 NGLVKLGDFGISKVL 153
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine ...
9-157 1.54e-16

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK-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. 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.


Pssm-ID: 173733 [Multi-domain]  Cd Length: 282  Bit Score: 77.91  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKLecvktkhpqlhieskfYKMMQGGVGIPS-----------------IKWc 71
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKARDKKTGEIVALKK----------------IRLDNEEEGIPStalreisllkelkhpniVKL- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  72 gaegdYNV--------MVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGlgkKGN 143
Cdd:cd07829  64 -----LDVihterklyLVFEYCDMDLKKYLDKRPGPLSPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNILIN---RDG 135
                       170
                ....*....|....
gi 13928846 144 LVYIIDFGLAKKYR 157
Cdd:cd07829 136 VLKLADFGLARAFG 149
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
7-153 2.00e-16

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, 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 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.


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 77.64  E-value: 2.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   7 NKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHI-ESKFYKMMQGGVGIPSIKwCGAEGDYNVMVMELL 85
Cdd:cd06614  19 ELYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIInEILIMKDCKHPNIVDYYD-SYLVGDELWVVMEYM 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13928846  86 -GPSLEDLFNFCSRKfslktvllLADQMISRI--------EYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLA 153
Cdd:cd06614  98 dGGSLTDIITQNFVR--------MNEPQIAYVcrevlqglEYLHSQNVIHRDIKSDNIL--LSKDGS-VKLADFGFA 163
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
8-155 1.39e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that 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. 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.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 74.77  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIK-----------LECVKtkhpQLHIESKFYKMMQGgvgiPSI-KWCGA-- 73
Cdd:cd06632   1 RWRKGELLGSGSFGSVYEGLNLDDGDFFAVKevsladdgqtgQEAVK----QLEQEIALLSKLQH----PNIvQYLGTer 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  74 EGDYNVMVMELL-GPSLEDLFnfcsRKF-SLKTVL--LLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGnLVYIID 149
Cdd:cd06632  73 EEDNLYIFLELVpGGSLAKLL----KKYgSFPEPVirLYTRQILLGLEYLHDRNTVHRDIKGANIL--VDTNG-VVKLAD 145

                ....*.
gi 13928846 150 FGLAKK 155
Cdd:cd06632 146 FGMAKQ 151
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; Protein Tyrosine ...
13-275 8.48e-15

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Spleen Tyrosine Kinase (Syk) subfamily; catalytic (c) domain. The Syk subfamily is composed of Syk, ZAP-70, Shark, 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. Syk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases 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 (BCR) signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) 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.


Pssm-ID: 133191 [Multi-domain]  Cd Length: 257  Bit Score: 72.38  E-value: 8.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLGA-NIASGEEVAIKLECVKTKHPQLHiESKFYK----MMQggVGIPSI-KWCG-AEGDYNVMVMEL- 84
Cdd:cd05060   1 KELGHGNFGSVVKGVyLMKSGKEVEVAVKTLKQEHIAAG-KKEFLReasvMAQ--LDHPCIvRLIGvCKGEPLMLVMELa 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  85 -LGPSLEDLFNfcSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAK------KYR 157
Cdd:cd05060  78 pLGPLLKYLKK--RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVL--LVNRHQ-AKISDFGMSRalgagsDYY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 158 DARTHQHIPYRenknltgtaRYA--SINTHlgiEQSRRDDLESLGyVLMY--FNLGSLPWQGLKAATKRQKYEriSEKKM 233
Cdd:cd05060 153 RATTAGRWPLK---------WYApeCINYG---KFSSKSDVWSYG-VTLWeaFSYGAKPYGEMKGAEVIAMLE--SGERL 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 13928846 234 STPIEvlCkgyPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRN 275
Cdd:cd05060 218 PRPEE--C---PQEIYSIMLSCWKYRPEDRPTFSELESTFRR 254
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family, catalytic ...
13-274 1.21e-14

Catalytic domain of Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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.


Pssm-ID: 173624  Cd Length: 262  Bit Score: 72.18  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLGA---NIASGEEVAIKleCVKTKHPQLHIEsKFYK---MMQG----------GVGIPSIKWCgaegd 76
Cdd:cd00192   1 KKLGEGAFGEVYKGKlkgKDGKTTEVAVK--TLKEDASEEERK-DFLKearVMKKlghpnvvrllGVCTEEEPLY----- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  77 ynvMVMEL---------LGPSLEDLFNFCSRKFSLKTVLLLADQmISR-IEYIHSKNFIHRDVKPDNFLMGlgkKGNLVY 146
Cdd:cd00192  73 ---LVLEYmeggdlldyLRKSRPVFPSPEKSTLSLKDLLSFAIQ-IAKgMEYLASKKFVHRDLAARNCLVG---EDLVVK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 147 IIDFGLAKK-----YRDARTHQHIPYR----EnknltgtaryaSINTHLGIEQSrrdDLESLGyVLMY--FNLGSLPWQG 215
Cdd:cd00192 146 ISDFGLSRDvydddYYRKKTGGKLPIRwmapE-----------SLKDGIFTSKS---DVWSFG-VLLWeiFTLGATPYPG 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 216 LKAatkRQKYERISE-KKMSTPievlcKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFR 274
Cdd:cd00192 211 LSN---EEVLEYLRKgYRLPKP-----EYCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
13-239 2.09e-14

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 71.36  E-value: 2.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLGANIASGEEVAIKL---ECVKTKHPQLHIESKFYKMMQGGVGIPSIK--WCGAEGDYNVMVMELL-G 86
Cdd:cd05611   2 KPISKGAFGSVYLAKKRSTGDYFAIKVlkkSDMIAKNQVTNVKAERAIMMIQGESPYVAKlyYSFQSKDYLYLVMEYLnG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  87 PSLEDLfnfcsrkfsLKTVLLLADQMISR--------IEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKyrd 158
Cdd:cd05611  82 GDCASL---------IKTLGGLPEDWAKQyiaevvlgVEDLHQRGIIHRDIKPENLL--IDQTGHL-KLTDFGLSRN--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 159 arthqhipYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQglkAATKRQKYERISEKKMSTPIE 238
Cdd:cd05611 147 --------GLENKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH---AETPDAVFDNILSRRINWPEE 215

                .
gi 13928846 239 V 239
Cdd:cd05611 216 V 216
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
9-249 6.85e-14

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a 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). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) 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 C 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.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 70.27  E-value: 6.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKL----ECVKTKhpQL-HIESKfyKMMQGGVGIPSI-KWCGA--EGDYNVM 80
Cdd:cd05580   3 FEFIKTLGTGSFGRVMLVRHKGSGKYYALKIlskaKIVKLK--QVeHVLNE--KRILQSIRHPFLvNLYGSfqDDSNLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  81 VMELL-GPSLEDLFNFCsRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKYRDa 159
Cdd:cd05580  79 VMEYVpGGELFSHLRKS-GRFPEPVARFYAAQVVLALEYLHSLDIVYRDLKPENLL--LDSDGYI-KITDFGFAKRVKG- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 160 RTHqhipyrenkNLTGTARYAS--INTHLGIEQSRrdDLESLGyVLMY-FNLGSLPWqglKAATKRQKYERISEKKMStp 236
Cdd:cd05580 154 RTY---------TLCGTPEYLApeIILSKGYGKAV--DWWALG-ILIYeMLAGYPPF---FDDNPIQIYEKILEGKVR-- 216
                       250
                ....*....|...
gi 13928846 237 ievlckgYPSEFS 249
Cdd:cd05580 217 -------FPSFFS 222
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ...
13-163 8.23e-14

Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC 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. 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 similar proteins. 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.


Pssm-ID: 143333 [Multi-domain]  Cd Length: 283  Bit Score: 70.05  E-value: 8.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLGANIASGEEVAIKLecVKTKHPQLHIESKFY---KMMQ--GGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd05118   5 GKIGEGTYGVVYKARDKLTGEIVAIKK--IKLRFESEGIPKTALreiKLLKelNHPNIIKLLDVFRHKGDLYLVFEFMDT 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928846  88 SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYR---DARTHQ 163
Cdd:cd05118  83 DLYKLIKDRQRGLPESLIKSYLYQLLQGLAFCHSHGILHRDLKPENLLI---NTEGVLKLADFGLARSFGspvRPYTHY 158
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs) ...
9-161 1.08e-13

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, PRKX-like kinases, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173703 [Multi-domain]  Cd Length: 291  Bit Score: 69.77  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKL----ECVKTKHPQ-LHIESKFYKMMQGGVgIPSIKWCGAEGDYNVMVME 83
Cdd:cd05612   3 LERIKTVGTGTFGRVHLVRDRISEHYYALKVmaipEVIRLKQEQhVHNEKRVLKEVSHPF-IIRLFWTEHDQRFLYMLME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  84 LLgPSLEdLFNF--CSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKYRDaRT 161
Cdd:cd05612  82 YV-PGGE-LFSYlrNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL--LDKEGHI-KLTDFGFAKKLRD-RT 155
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; Serine ...
8-168 1.31e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 7 (CDK7) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. 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.


Pssm-ID: 143346 [Multi-domain]  Cd Length: 298  Bit Score: 69.53  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKlecvKTKhpqlhiESKFYKMMQG--GVGIPSIKW--------------C 71
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIK----KIK------LGERKEAKDGinFTALREIKLlqelkhpniiglldV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  72 GAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglGKKGNLvYIIDFG 151
Cdd:cd07841  71 FGHKSNINLVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLI--ASDGVL-KLADFG 147
                       170       180
                ....*....|....*....|..
gi 13928846 152 LAKKYRDAR---THQHIP--YR 168
Cdd:cd07841 148 LARSFGSPNrkmTHQVVTrwYR 169
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; Protein Tyrosine ...
14-278 1.35e-13

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; Protein Tyrosine Kinase (PTK) family; Spleen tyrosine kinase (Syk); 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. Syk, together with Zap-70, form the Syk subfamily of kinases which are cytoplasmic (or nonreceptor) tyr kinases containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. Syk is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for epidermal growth factor receptor (EGFR) signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV).


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 68.84  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  14 KIGSGSFGDIYLG--ANIASGEEVAIKLECVKTKHP----QLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGP 87
Cdd:cd05116   2 ELGSGNFGTVKKGmyKMKKSEKTVAVKILKNDNNDPalkdELLREANVMQQLDNPYIVRMIGICEAESWMLVMELAELGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  88 sledLFNFC--SRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAK------KYRDA 159
Cdd:cd05116  82 ----LNKFLqkNKHVTEKNITELVHQVSMGMKYLEETNFVHRDLAARNVLL---VTQHYAKISDFGLSKalgadeNYYKA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 160 RTHQHIPYRenknltgtaRYAS--INTHlgiEQSRRDDLESLGyVLMY--FNLGSLPWQGLKAATKRQKYERisEKKMST 235
Cdd:cd05116 155 KTHGKWPVK---------WYAPecMNYY---KFSSKSDVWSFG-VLMWeaFSYGQKPYKGMKGNEVTQMIES--GERMEC 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 13928846 236 PievlcKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFH 278
Cdd:cd05116 220 P-----QRCPPEMYDLMKLCWTYGVDERPGFAVVELRLRNYYY 257
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
15-215 2.31e-13

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 68.41  E-value: 2.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIKleCVKTKH-----PQLHIES--------------KFYKMMQggvgipsikwcgaEG 75
Cdd:cd05572   1 LGVGGFGRVELVKVKSKNRTFALK--CVKKRHivetgQQEHIFSekeileecnhpfivKLYRTFK-------------DK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  76 DYNVMVMEL-LGpslEDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGnLVYIIDFGL 152
Cdd:cd05572  66 KYIYMLMEYcLG---GELWTILRDrgLFDEYTARFYIACVVLAFEYLHNRGIIYRDLKPENLL--LDSNG-YVKLVDFGF 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928846 153 AKK-YRDARTHqhipyrenkNLTGTARYASINTHLGIEQSRRDDLESLGyVLMY-FNLGSLPWQG 215
Cdd:cd05572 140 AKKlKSGQKTW---------TFCGTPEYVAPEIILNKGYDFSVDYWSLG-ILLYeLLTGRPPFGE 194
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Bypass ...
9-182 4.30e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Bypass UAS Requirement 1 and similar proteins; Serine/Threonine Kinases (STKs), Bypass UAS Requirement 1 (BUR1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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. BUR1, also called SGV1, is a yeast Cyclin-Dependent protein Kinase (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.


Pssm-ID: 143371 [Multi-domain]  Cd Length: 311  Bit Score: 68.11  E-value: 4.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHI----ESKFYKMMQGGVGIPSIKWCGAEGD-------- 76
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPItalrEIKILKKLKHPNVVPLIDMAVERPDkskrkrgs 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  77 -YnvMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKK 155
Cdd:cd07866  90 vY--MVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANIL--IDNQGIL-KIADFGLARP 164
                       170       180
                ....*....|....*....|....*..
gi 13928846 156 YRDArthqhIPYRENKNLTGTARYASI 182
Cdd:cd07866 165 YDGP-----PPNPKGGGGGGTRKYTNL 186
STKc_ROCK_NDR_like cd05573
Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine ...
15-267 4.36e-13

Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) and Nuclear Dbf2-Related (NDR)-like kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK- and NDR-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. 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.


Pssm-ID: 173664 [Multi-domain]  Cd Length: 350  Bit Score: 68.86  E-value: 4.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIKL--ECVKTKHPQ-LHIES--------------KFYKMMQggvgipsikwcgaEGDY 77
Cdd:cd05573   9 IGRGAFGEVWLVRDKDTGQVYAMKVlrKSDMIKRNQiAHVRAerdiladadspwivKLYYSFQ-------------DEEH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  78 NVMVMELLGPSleDLFNFCSRK--FSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLAKK 155
Cdd:cd05573  76 LYLVMEYMPGG--DLMNLLIRKdvFPEETARFYIAELVLALDSVHKLGFIHRDIKPDNIL--IDADGH-IKLADFGLCKK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 156 YRDA---------------------RTHQHIPYRENKNLT-GTARYASINTHLGIEQSRRDDLESLGyVLMYFNL-GSLP 212
Cdd:cd05573 151 MNKAkdreyylndshnllfrdnvlvRRRDHKQRRVRANSTvGTPDYIAPEVLRGTPYGLECDWWSLG-VILYEMLyGFPP 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13928846 213 wqgLKAATKRQKYERIsekkmstpievlckgypsefstyLNFCRSLRFDDKPDYS 267
Cdd:cd05573 230 ---FYSDTLQETYNKI-----------------------INWKESLRFPPDPPVS 258
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
13-271 4.83e-13

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


Pssm-ID: 173629 [Multi-domain]  Cd Length: 251  Bit Score: 67.10  E-value: 4.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLGAnIASGEEVAIKlECVKTKHPQLHIeskfyKMMQGGVGI-----PSI-KWCGAEGD-YNVM-VMEL 84
Cdd:cd05041   1 EKIGKGNFGDVYKGV-LKGNTEVAVK-TCRSTLPPDLKR-----KFLQEAEILkqydhPNIvKLIGVCVQkQPIYiVMEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  85 L-GPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLgkkGNLVYIIDFGLAKK-----YRD 158
Cdd:cd05041  74 VpGGSLLTFLRKKKNRLTVKKLLQMSLDAAAGMEYLESKNCIHRDLAARNCLVGE---NNVLKISDFGMSREeeggiYTV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 159 ARTHQHIPYR----ENKNltgTARYASinthlgieqsrRDDLESLGyVLMY--FNLGSLPWQGLkaaTKRQKYERI-SEK 231
Cdd:cd05041 151 SDGLKQIPIKwtapEALN---YGRYTS-----------ESDVWSYG-ILLWetFSLGDTPYPGM---SNQQTRERIeSGY 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13928846 232 KMSTPievlcKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQ 271
Cdd:cd05041 213 RMPAP-----QLCPEEIYRLMLQCWAYDPENRPSFSEIYN 247
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine ...
9-156 7.29e-13

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase 9 (CDK9)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK9-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. 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. 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.


Pssm-ID: 143345 [Multi-domain]  Cd Length: 287  Bit Score: 67.19  E-value: 7.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK---LECVKTKHPQLHI-ESKFYKMMQGG--VGIPSIKWCGAEGDYnVMVM 82
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkirMENEKEGFPITAIrEIKLLQKLRHPniVRLKEIVTSKGKGSI-YMVF 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13928846  83 ELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLvYIIDFGLAKKY 156
Cdd:cd07840  80 EYMDHDLTGLLDSPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIL--INNDGVL-KLADFGLARPY 150
STKc_MEKK3_like cd06625
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
7-218 7.32e-13

Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3-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. This subfamily is composed of MEKK3, MEKK2, and related proteins, all containing an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks), proteins that 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. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates extracellular signal-regulated kinase 5 (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.


Pssm-ID: 132956 [Multi-domain]  Cd Length: 263  Bit Score: 66.76  E-value: 7.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   7 NKYRLGRKIGSGSFGDIYLGANIASGEEVAIKL--ECVKTKHPQLHI-----ESKFYKMMQGgvgiPSI-KWCGAEGDYN 78
Cdd:cd06625   2 TNWRRGKLLGQGAFGRVYLCYDVDTGRELAVKQvpFDPDSPETKKEVnalecEIQLLKNLQH----ERIvQYYGCLRDDE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  79 VM--VMELL-GPSLED-------LFNFCSRKFSLktvllladQMISRIEYIHSKNFIHRDVKPDNFLMGLgkKGNlVYII 148
Cdd:cd06625  78 TLsiFMEYMpGGSVKDqlkaygaLTETVTRKYTR--------QILEGVEYLHSNMIVHRDIKGANILRDS--AGN-VKLG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 149 DFGLAKKYRDARTHQhipyRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKA 218
Cdd:cd06625 147 DFGASKRLQTICSSG----TGMKSVTGTPYWMSPEVISGEGYGRKADVWSVGCTVVEMLTEKPPWAEFEA 212
STKc_MAPKKK_Bck1_like cd06629
Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs) ...
12-264 3.44e-12

Catalytic domain of fungal Bck1-like MAP Kinase Kinase Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, fungal Bck1-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. 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. 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.


Pssm-ID: 132960 [Multi-domain]  Cd Length: 272  Bit Score: 65.20  E-value: 3.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  12 GRKIGSGSFGDIYLGANIASGEEVAIK-LECVKT---KHPQLH------IESKFyKMMQGGVGIPSIKWCGAEG---DYN 78
Cdd:cd06629   6 GELIGKGTYGRVYLALNVTTGEMMAVKqVELPATiagRHDSRQkdmvkaLRSEI-ETLKDLDHLNIVQYLGFETteeYLS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  79 VMVMELLGPSLEDlfnfCSR---KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLM---GLGKkgnlvyIIDFGL 152
Cdd:cd06629  85 IFLEYVPGGSIGS----CLRtygRFEEQLVRFFTEQVLEGLAYLHSKGILHRDLKADNLLVdadGICK------ISDFGI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846 153 AKKYRDARTHQhipyrENKNLTGT----ARYASINTHLGIeqSRRDDLESLGYVLMYFNLGSLPWQGLKAAtkrQKYERI 228
Cdd:cd06629 155 SKKSDDIYDND-----QNMSMQGSvfwmAPEVIHSYSQGY--SAKVDIWSLGCVVLEMFAGRRPWSDEEAI---AAMFKL 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 13928846 229 SEKKMSTPI-EVLCKGYPSEFSTYLNFCRSLRFDDKP 264
Cdd:cd06629 225 GNKRSAPPIpPDVSMNLSPVALDFLNACFTINPDNRP 261
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
8-164 7.54e-12

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. 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.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 63.81  E-value: 7.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   8 KYRLGRKIGSGSFGDIYLGANIASGEEVAIKleCVKTKHpqlhIESKFYKMMQGGVGI------PSI-KWCGA--EGDYN 78
Cdd:cd06627   1 NYQLGDLIGRGAFGVVYKGLNLETGDFVAIK--QISLEK----IKEEALKSIMQEIDLlknlkhPNIvKYIGSieTSDSL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  79 VMVMEL-LGPSLEDLFNfcsrKFSLKTVLLLAD---QMISRIEYIHSKNFIHRDVKPDNFLMGlgkKGNLVYIIDFGLAK 154
Cdd:cd06627  75 YIILEYaENGSLRQIIK----KFGPFPESLVAVyvyQVLQGLAYLHEQGVIHRDIKAANILTT---KDGVVKLADFGVAT 147
                       170
                ....*....|
gi 13928846 155 KYRDARTHQH 164
Cdd:cd06627 148 KLNDVSKDDA 157
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; Serine ...
9-169 8.49e-12

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; Serine/Threonine Kinases (STKs), MAPK/MAK/MRK Overlapping Kinase (MOK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173735 [Multi-domain]  Cd Length: 282  Bit Score: 63.83  E-value: 8.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   9 YRLGRKIGSGSFGDIYLGANIASGEEVAIK--------LECVK-----------TKHPQ-LHIESKFYKMMQGGVGipsi 68
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcmkkhfksLEQVNnlreiqalrrlSPHPNiLRLIEVLFDRKTGRLA---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  69 kwcgaegdynvMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgkKGNLVYII 148
Cdd:cd07831  77 -----------LVFELMDMNLYELIKGRKRPLPEKRVKSYMYQLLKSLDHMHRNGIFHRDIKPENILI----KDDILKLA 141
                       170       180
                ....*....|....*....|.
gi 13928846 149 DFGLAKKyrdarTHQHIPYRE 169
Cdd:cd07831 142 DFGSCRG-----IYSKPPYTE 157
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
7-153 1.23e-11

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. 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.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 63.40  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846   7 NKYRLGRKIGSGSFGDIYLGANIASGEEVAIKleCVKTKHPQLHIESkfykmMQGGVGIPS-------IKWCG-AEGDYN 78
Cdd:cd06609   1 ELFTLLECIGKGSFGEVYKAIDKRTNQVVAIK--VIDLEEAEDEIED-----IQQEIQFLSqcrspyiTKYYGsFLKGSK 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13928846  79 V-MVMELL-GPSLEDLFNfcSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFGLA 153
Cdd:cd06609  74 LwIIMEYCgGGSCLDLLK--PGKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANIL--LSEEGD-VKLADFGVS 145
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; Protein Tyrosine ...
13-154 2.31e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; Protein Tyrosine Kinase (PTK) family; Janus kinase (Jak) subfamily; catalytic (c) domain (repeat 2). The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, 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. Jak subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases 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.


Pssm-ID: 173628 [Multi-domain]  Cd Length: 284  Bit Score: 62.81  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDIYLG----ANIASGEEVAIKL---ECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNV-MVMEL 84
Cdd:cd05038  10 KQLGEGHFGKVELCrydpLGDNTGEQVAVKSlnhSGEEQHRSDFEREIEILRTLDHENIVKYKGVCEKPGGRSLrLIMEY 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13928846  85 LgP--SLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAK 154
Cdd:cd05038  90 L-PsgSLRDYLQRHRDQINLKRLLLFSSQICKGMDYLGSQRYIHRDLAARNILV---ESEDLVKISDFGLAK 157
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
15-215 2.35e-11

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 62.27  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  15 IGSGSFGDIYLGANIASGEEVAIKlecVKTKHpqlhieSKFYKMMQGGVGI----------PSI--KWCGAEGDYNV-MV 81
Cdd:cd05579   1 ISKGAYGRVFLAKKKSTGDIYAIK---VIKKA------DMIRKNQVDQVLTerdilsqaqsPYVvkLYYSFQGKKNLyLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  82 MELL-GPSLEDLF-NFCSrkFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNLVyIIDFGLAKK-YRD 158
Cdd:cd05579  72 MEYLpGGDLASLLeNVGS--LDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNIL--IDSNGHLK-LTDFGLSKVgLVR 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13928846 159 ARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQG 215
Cdd:cd05579 147 RQINLNDDEKEDKRIVGTPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPPFHG 203
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Protein ...
13-170 3.81e-11

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Protein Tyrosine Kinase (PTK) family; Tyrosine kinase 2 (Tyk2); catalytic (c) domain (repeat 2). 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. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) tyr kinases 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). 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.


Pssm-ID: 133211 [Multi-domain]  Cd Length: 283  Bit Score: 62.22  E-value: 3.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  13 RKIGSGSFGDI----YLGANIASGEEVAIKleCVKTKHPQLHIES--KFYKMMQGGVGIPSIKW---CGAEGDYNV-MVM 82
Cdd:cd05080  10 RVLGEGHFGKVslycYDPANDGTGEMVAVK--TLKRECGQQNTSGwkKEINILKTLYHENIVKYkgcCSEQGGKGLqLIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  83 ELLgpSLEDLFNFCSR-KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMglgKKGNLVYIIDFGLAKKYRDArt 161
Cdd:cd05080  88 EYV--PLGSLRDYLPKhKLNLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFGLAKAVPEG-- 160

                ....*....
gi 13928846 162 HQHIPYREN 170
Cdd:cd05080 161 HEYYRVRED 169
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
74-158 3.81e-11

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


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 61.56  E-value: 3.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  74 EGDYNVMVMELLGPSleDLFNFCSR--KFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLmgLGKKGNlVYIIDFG 151
Cdd:cd05578  71 DEENMYLVVDLLLGG--DLRYHLSQkvKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNIL--LDEQGH-VHITDFN 145

                ....*..
gi 13928846 152 LAKKYRD 158
Cdd:cd05578 146 IATKVTP 152
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
10-220 4.43e-11

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 61.45  E-value: 4.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928846  10 RLGRKIGSGSFGDIYLGANIASGEEVAIK-----------------LECV-KTKHPQLhieSKFYKM--MQGGVGIpsik 69
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKkihvdgdeefrkqllreLKTLrSCESPYV---VKCYGAfyKEG