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Conserved domains on  [gi|32477775|ref|NP_870769|]
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serine/threonine-protein kinase [Rhodopirellula baltica SH 1]

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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 ...
37-295 1.47e-32

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: 120.80  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFEHGITaKNQRILVMEYIAGVG 116
Cdd:cd00180   4 GGFGTVYLARDKKTGKKVAIKIIKKEDSSSLLEELL-----REIEILKKLNHPNIVKLYGVFED-ENHLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 117 IQDVIvRKKREVIDGKEML-LMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsGVRLIDFGLTVPATPPFMAP 195
Cdd:cd00180  78 LKDLL-KENEGKLSEDEILrILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG------KVKLADFGLSKLLTSDKSLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 196 GNRTGTPLYMCPEIVRRRAT-DKRVDVFSLGVTFYCLltfqhpwqgeivsgraalqhdtetatpilerrddihPKVARVI 274
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKGYySEKSDIWSLGVILYEL------------------------------------PELKDLI 194
                       250       260
                ....*....|....*....|.
gi 32477775 275 MRMIEPNVDDRLsSIKEFLSQ 295
Cdd:cd00180 195 RKMLQKDPEKRP-SAKEILEH 214
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
36-293 1.20e-40

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 143.44  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775     36 TGTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFEHGITaKNQRILVMEYIAGV 115
Cdd:smart00220   9 EGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERIL-----REIKILKKLKHPNIVRLYDVFED-EDKLYLVMEYCEGG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    116 GIQDVIVRKKRevIDGKEM-LLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVpatppFMA 194
Cdd:smart00220  83 DLFDLLKKRGR--LSEDEArFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGH-----VKLADFGLAR-----QLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    195 PGNRT----GTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEIvSGRAALQHDTETATPILERRDDIHPKV 270
Cdd:smart00220 149 PGEKLttfvGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDD-QLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|...
gi 32477775    271 ARVIMRMIEPNVDDRLsSIKEFL 293
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEAL 249
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
37-295 1.47e-32

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: 120.80  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFEHGITaKNQRILVMEYIAGVG 116
Cdd:cd00180   4 GGFGTVYLARDKKTGKKVAIKIIKKEDSSSLLEELL-----REIEILKKLNHPNIVKLYGVFED-ENHLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 117 IQDVIvRKKREVIDGKEML-LMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsGVRLIDFGLTVPATPPFMAP 195
Cdd:cd00180  78 LKDLL-KENEGKLSEDEILrILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG------KVKLADFGLSKLLTSDKSLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 196 GNRTGTPLYMCPEIVRRRAT-DKRVDVFSLGVTFYCLltfqhpwqgeivsgraalqhdtetatpilerrddihPKVARVI 274
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKGYySEKSDIWSLGVILYEL------------------------------------PELKDLI 194
                       250       260
                ....*....|....*....|.
gi 32477775 275 MRMIEPNVDDRLsSIKEFLSQ 295
Cdd:cd00180 195 RKMLQKDPEKRP-SAKEILEH 214
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
106-184 6.04e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 51.06  E-value: 6.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32477775  106 ILVMEYIAGVGIQDVIVRKKREVIDgkemlLMREMAESLAYVHEQGFIHRDVCPRNFICTppkDGeetvsGVRLIDFGL 184
Cdd:PRK14879  75 IIVMEYIEGEPLKDLINSNGMEELE-----LSREIGRLVGKLHSAGIIHGDLTTSNMILS---GG-----KIYLIDFGL 140
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
103-184 1.39e-07

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: 49.52  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   103 NQRILVMEYIAGvgiqdvivRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppkdGEETVsgvrLIDF 182
Cdd:TIGR03724  70 DNKTIVMEYIEG--------KPLKDVIEEGNDELLREIGRLVGKLHKAGIVHGDLTTSNIIVR----DDKLY----LIDF 133

                  ..
gi 32477775   183 GL 184
Cdd:TIGR03724 134 GL 135
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
106-184 1.02e-05

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 44.20  E-value: 1.02e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32477775 106 ILVMEYIAGVGIQDVIVRKKREvidgkemlLMREMAESLAYVHEQGFIHRDVCPRNFICTPpkdgeetvSGVRLIDFGL 184
Cdd:COG3642  75 LIVMEYIEGELLKDALEEARPD--------LLREVGRLVGKLHKAGIVHGDLTTSNIILSG--------GRIYFIDFGL 137
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
36-293 1.20e-40

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 143.44  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775     36 TGTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFEHGITaKNQRILVMEYIAGV 115
Cdd:smart00220   9 EGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERIL-----REIKILKKLKHPNIVRLYDVFED-EDKLYLVMEYCEGG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    116 GIQDVIVRKKRevIDGKEM-LLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVpatppFMA 194
Cdd:smart00220  83 DLFDLLKKRGR--LSEDEArFYLRQILSALEYLHSKGIVHRDLKPENILLD--EDGH-----VKLADFGLAR-----QLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    195 PGNRT----GTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEIvSGRAALQHDTETATPILERRDDIHPKV 270
Cdd:smart00220 149 PGEKLttfvGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDD-QLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|...
gi 32477775    271 ARVIMRMIEPNVDDRLsSIKEFL 293
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEAL 249
Pkinase pfam00069
Protein kinase domain;
28-293 2.22e-33

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 124.28  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    28 FERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKyelfESRFKGLNKPSEGEIAMQMKHPLIVKTFehGITAKNQRI- 106
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRS----EKSKKDQTARREIRILRRLSHPNIVRLI--DAFEDKDHLy 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   107 LVMEYIAGVGIQDVIVRKK----REVIDgkemlLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDF 182
Cdd:pfam00069  75 LVMEYCEGGDLFDYLSRGGplseDEAKK-----IALQILRGLEYLHSNGIIHRDLKPENILLD--ENGV-----VKIADF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   183 GLTVPATPPFMAPGNRTGTPLYMCPEIVR-RRATDKRVDVFSLGVTFYCLLTFQHPWQGEivSGRAALQHDTETATPILE 261
Cdd:pfam00069 143 GLAKKLTKSSSSLTTFVGTPEYMAPEVLLgGNGYGPKVDVWSLGVILYELLTGKPPFSGE--SILDQLQLIRRILGPPLE 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 32477775   262 R----RDDIHPKVARVIMRMIEPNVDDRLsSIKEFL 293
Cdd:pfam00069 221 FdepkSDSGSEEAKDLIKKCLNKDPSKRP-TAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
28-295 1.24e-28

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: 112.91  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  28 FERSRTAATGTMSNFFVAYDlerKENVGVKILDPE--KYELFESRFKglnkpSEGEIAMQMKHP-LIVKTFEHGITaKNQ 104
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD---RKLVALKVLAKKleSKSKEVERFL-----REIQILASLNHPpNIVKLYDFFQD-EGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 105 RILVMEYIAGVGIQDVIV-RKKREVIDGKEML-LMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsGVRLIDF 182
Cdd:COG0515  73 LYLVMEYVDGGSLEDLLKkIGRKGPLSESEALfILAQILSALEYLHSKGIIHRDIKPENILLDRDGR------VVKLIDF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 183 GL------TVPATPPFMAPGNRTGTPLYMCPEIVR---RRATDKRVDVFSLGVTFYCLLTFQHPWQGEIVSG--RAALQH 251
Cdd:COG0515 147 GLakllpdPGSTSSIPALPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSatSQTLKI 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32477775 252 DTETATPIL------ERRDDIHPKVARVIMRMIEPNVDDRLSSIKEFLSQ 295
Cdd:COG0515 227 ILELPTPSLasplspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHD 276
pknD PRK13184
serine/threonine-protein kinase; Reviewed
27-291 1.21e-16

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.04  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   27 RFERSRTAATGTMSNFFVAYDLERKENVGVKIL--DPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFehgiTAKNQ 104
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIreDLSENPLLKKRFL-----REAKIAADLIHPGIVPVY----SICSD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  105 RILV---MEYIAGVGIQDvIVRKKREvidgKEMLlMREMAE----------------SLAYVHEQGFIHRDVCPRNFI-- 163
Cdd:PRK13184  74 GDPVyytMPYIEGYTLKS-LLKSVWQ----KESL-SKELAEktsvgaflsifhkicaTIEYVHSKGVLHRDLKPDNILlg 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  164 -----------CTPPKDGEETVSGVrlIDFGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLL 232
Cdd:PRK13184 148 lfgevvildwgAAIFKKLEEEDLLD--IDVDERNICYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQML 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  233 TFQHPWQGEivSGRA-ALQHDTETATPILERRdDIHPKVARVIMRMIEPNVDDRLSSIKE 291
Cdd:PRK13184 226 TLSFPYRRK--KGRKiSYRDVILSPIEVAPYR-EIPPFLSQIAMKALAVDPAERYSSVQE 282
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
87-251 2.67e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.59  E-value: 2.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   87 KHPLIVKTFEHgITAKNQRILVMEYIAGVGIQDVIVRKKREVIDGKEM---LLMREMAESLAYVHEQGFIHRDVCPRNFI 163
Cdd:PTZ00267 123 DHFGIVKHFDD-FKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYevgLLFYQIVLALDEVHSRKMMHRDLKSANIF 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  164 CTPpkdgeetvSGV-RLIDFGLTVPATPPFM--APGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQG 240
Cdd:PTZ00267 202 LMP--------TGIiKLGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKG 273
                        170
                 ....*....|.
gi 32477775  241 EivSGRAALQH 251
Cdd:PTZ00267 274 P--SQREIMQQ 282
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
86-291 1.68e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 62.18  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   86 MK-HPLIVKTFeHGITAKNQRILVMEYIAGVGIQDVIvrKKREVIDGKEM-LLMREMAESLAYVHEQGFIHRDVCPRNFI 163
Cdd:PHA03390  65 MKdNPNFIKLY-YSVTTLKGHVLIMDYIKDGDLFDLL--KKEGKLSEAEVkKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  164 CTPPKDGeetvsgVRLIDFGLTVPATppfmAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGeiv 243
Cdd:PHA03390 142 YDRAKDR------IYLCDYGLCKIIG----TPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE--- 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32477775  244 sgraalqHDTETATP-ILERR--DDIH-----PKVAR-VIMRMIEPNVDDRLSSIKE 291
Cdd:PHA03390 209 -------DEDEELDLeSLLKRqqKKLPfiknvSKNANdFVQSMLKYNINYRLTNYNE 258
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
56-244 2.05e-11

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 63.33  E-value: 2.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775     56 VKILDPEKYELFeSRFKglnkpSEGEIAMQMKHPLIVKTFEHGITAKNQRILVMEYIAGvgiqdvivRKKREVIDGKEML 135
Cdd:TIGR03903   11 LRTDAPEEEHQR-ARFR-----RETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPG--------RTLREVLAADGAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775    136 -------LMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDGeetvSGVRLIDFGLTV-------PATPPFMAPGNRTGT 201
Cdd:TIGR03903   77 pagetgrLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVR----PHAKVLDFGIGTllpgvrdADVATLTRTTEVLGT 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 32477775    202 PLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEIVS 244
Cdd:TIGR03903  153 PTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVA 195
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
79-229 3.54e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 52.90  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775   79 EGEIAMQMKHPLIVKTfeHGITAKNQRI-LVMEYIAGVGIQDVIVRKKREVIDgkemlLMREMAESLAYVHEQGFIHRDV 157
Cdd:PLN00034 122 EIEILRDVNHPNVVKC--HDMFDHNGEIqVLLEFMDGGSLEGTHIADEQFLAD-----VARQILSGIAYLHRRHIVHRDI 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  158 CPRNFICTPPKDgeetvsgVRLIDFGLT--VPATppfMAPGNRT-GTPLYMCPEIVRRRATDKRV-----DVFSLGVT-- 227
Cdd:PLN00034 195 KPSNLLINSAKN-------VKIADFGVSriLAQT---MDPCNSSvGTIAYMSPERINTDLNHGAYdgyagDIWSLGVSil 264

                 ...
gi 32477775  228 -FY 229
Cdd:PLN00034 265 eFY 267
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
37-295 1.47e-32

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: 120.80  E-value: 1.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpSEGEIAMQMKHPLIVKTFEHGITaKNQRILVMEYIAGVG 116
Cdd:cd00180   4 GGFGTVYLARDKKTGKKVAIKIIKKEDSSSLLEELL-----REIEILKKLNHPNIVKLYGVFED-ENHLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 117 IQDVIvRKKREVIDGKEML-LMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsGVRLIDFGLTVPATPPFMAP 195
Cdd:cd00180  78 LKDLL-KENEGKLSEDEILrILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG------KVKLADFGLSKLLTSDKSLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 196 GNRTGTPLYMCPEIVRRRAT-DKRVDVFSLGVTFYCLltfqhpwqgeivsgraalqhdtetatpilerrddihPKVARVI 274
Cdd:cd00180 151 KTIVGTPAYMAPEVLLGKGYySEKSDIWSLGVILYEL------------------------------------PELKDLI 194
                       250       260
                ....*....|....*....|.
gi 32477775 275 MRMIEPNVDDRLsSIKEFLSQ 295
Cdd:cd00180 195 RKMLQKDPEKRP-SAKEILEH 214
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
78-295 1.78e-26

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: 104.89  E-value: 1.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  78 SEGEIAMQMKHPLIVKTFEHGITAKNQRIlVMEYIAGVGIQDVIVRKKREVIDGKE---MLLMREMAESLAYVHEQGFIH 154
Cdd:cd08215  48 NEVKILKKLNHPNIIKYYESFEEKGKLCI-VMEYADGGDLSQKIKKQKKEGKPFPEeqiLDWFVQLCLALKYLHSRKILH 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 155 RDVCPRN-FICtppKDGEetvsgVRLIDFGL------TVPATPPFmapgnrTGTPLYMCPEIVRRRATDKRVDVFSLGVT 227
Cdd:cd08215 127 RDIKPQNiFLT---SNGL-----VKLGDFGIskvlssTVDLAKTV------VGTPYYLSPELCQNKPYNYKSDIWSLGCV 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32477775 228 FYCLLTFQHPWQGE--------IVSGraalqhdteTATPILERRDDihpKVARVIMRMIEPNVDDRLsSIKEFLSQ 295
Cdd:cd08215 193 LYELCTLKHPFEGEnllelalkILKG---------QYPPIPSQYSS---ELRNLVSSLLQKDPEERP-SIAQILQS 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
28-227 3.34e-24

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: 98.43  E-value: 3.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  28 FERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYELFESRFKglnkpsegEIAM--QMKHPLIVKtFEHGITAKNQR 105
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKKEKIIN--------EIQIlkKCKHPNIVK-YYGSYLKKDEL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 106 ILVMEYIAGVGIQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLT 185
Cdd:cd05122  73 WIVMEFCSGGSLKDLLKSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLT--SDGE-----VKLIDFGLS 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 32477775 186 VPATPPfMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVT 227
Cdd:cd05122 146 AQLSDT-KARNTMVGTPYWMAPEVINGKPYDYKADIWSLGIT 186
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
79-295 3.38e-24

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: 98.40  E-value: 3.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  79 EGEIAM--QMKHPLIVKTFEHGIT-AKNQRILVMEYIAGVGIQDVIVRKKR---EVIdgkeMLLMREMAESLAYVHEQGF 152
Cdd:cd06606  47 EREIRIlsSLQHPNIVRYYGSERDeEKNTLNIFLEYVSGGSLSSLLKKFGKlpePVI----RKYTRQILEGLAYLHSNGI 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 153 IHRDVCPRNFICTPpkDGEetvsgVRLIDFGL--TVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYC 230
Cdd:cd06606 123 VHRDIKGANILVDS--DGV-----VKLADFGCakRLGDIETGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIE 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32477775 231 LLTFQHPWqgeivsgraalqHDTETATPILErrddihpkvaRVIMRMIEPNVDDRLSSI-KEFLSQ 295
Cdd:cd06606 196 MATGKPPW------------SELGNPMAALY----------KIGSSGEPPEIPEHLSEEaKDFLRK 239
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
79-287 3.53e-23

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: 95.46  E-value: 3.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  79 EGEIAMQMKHPLIVK---TFEhgitaKNQRI-LVMEYIAGVGIQDVIVRKKR---EVIDgkemLLMREMAESLAYVHEQG 151
Cdd:cd05578  50 ERRILQELNHPFLVNlwySFQ-----DEENMyLVVDLLLGGDLRYHLSQKVKfseEQVK----FWICEIVLALEYLHSKG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 152 FIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPGnRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCL 231
Cdd:cd05578 121 IIHRDIKPDNILLD--EQGH-----VHITDFNIATKVTPDTLTTS-TSGTPGYMAPEVLCRQGYSVAVDWWSLGVTAYEC 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32477775 232 LTFQHPWQGEIVSGRAALQHDTETATPILErrdDIHPKVAR-VIMRMIEPNVDDRLS 287
Cdd:cd05578 193 LRGKRPYRGHSRTIRDQIRAKQETADVLYP---ATWSTEAIdAINKLLERDPQKRLG 246
STKc_PAK2 cd06655
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 2; Serine ...
23-295 7.32e-21

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 89.01  E-value: 7.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  23 DVEKRFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYELFESRFkglnkpSEGEIAMQMKHPLIVkTFEHGITAK 102
Cdd:cd06655  16 DPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELII------NEILVMKELKNPNIV-NFLDSFLVG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 103 NQRILVMEYIAGVGIQDVIVRKKREviDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICtppkdGEEtvSGVRLIDF 182
Cdd:cd06655  89 DELFVVMEYLAGGSLTDVVTETCMD--EAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL-----GMD--GSVKLTDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 183 GLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEivSGRAALQHDTETATPILER 262
Cdd:cd06655 160 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE--NPLRALYLIATNGTPELQN 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 32477775 263 RDDIHPKVARVIMRMIEPNVDDRlSSIKEFLSQ 295
Cdd:cd06655 238 PEKLSPIFRDFLNRCLEMDVEKR-GSAKELLQH 269
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
27-301 1.81e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group I, 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. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others.


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 88.04  E-value: 1.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMsnfFVAYDLERKENVGVK---ILDPEKYELFesrfkgLNkpsEGEIAMQMKHPLIVKTFEHGITAkN 103
Cdd:cd06647  23 RFEKIGQGASGTV---YTAIDVATGQEVAIKqmnLQQQPKKELI------IN---EILVMRENKHPNIVNYLDSYLVG-D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 104 QRILVMEYIAGVGIQDVIVRKKREviDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFG 183
Cdd:cd06647  90 ELWVVMEYLAGGSLTDVVTETCMD--EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG--MDGS-----VKLTDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 184 LTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEivSGRAALQHDTETATPILERR 263
Cdd:cd06647 161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE--NPLRALYLIATNGTPELQNP 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 32477775 264 DDIHPKVARVIMRMIEPNVDDRLSSIK----EFLSQTRGLES 301
Cdd:cd06647 239 EKLSAIFRDFLNRCLEMDVEKRGSAKEllqhPFLKLAKPLSS 280
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
37-227 3.01e-20

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 87.03  E-value: 3.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYELFesrFKGLNKpsegEIAM--QMKHPLIVKTFEhGITAKNQRILVMEYIAG 114
Cdd:cd06610  12 GATAVVYAAICLPNNEKVAIKRIDLEKCQTS---VDELRK----EVQAmsQCNHPNVVKYYT-SFVVGDELWLVMPYLSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 115 VGIQDVIVRK-KREVIDgkEMLL---MREMAESLAYVHEQGFIHRDVCPRN-FICTppkDGeetvsGVRLIDFGltVPAT 189
Cdd:cd06610  84 GSLLDIMKSSyPRGGLD--EAIIatvLKEVLKGLEYLHSNGQIHRDIKAGNiLLGE---DG-----SVKIADFG--VSAS 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 32477775 190 ppFMAPGNRT--------GTPLYMCPEIV-RRRATDKRVDVFSLGVT 227
Cdd:cd06610 152 --LADGGDRTrkvrktfvGTPCWMAPEVMeQVHGYDFKADIWSFGIT 196
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
27-295 7.40e-20

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 86.31  E-value: 7.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMsnfFVAYDLERKENVGVKILDPE---KYELFesrfkglnkPSEGEIAMQMKHPLIVKTFEHGITAkN 103
Cdd:cd06656  23 RFEKIGQGASGTV---YTAIDIATGQEVAIKQMNLQqqpKKELI---------INEILVMRENKNPNIVNYLDSYLVG-D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 104 QRILVMEYIAGVGIQDVIVRKKREviDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFG 183
Cdd:cd06656  90 ELWVVMEYLAGGSLTDVVTETCMD--EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG--MDGS-----VKLTDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 184 LTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEivSGRAALQHDTETATPILERR 263
Cdd:cd06656 161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE--NPLRALYLIATNGTPELQNP 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 32477775 264 DDIHPKVARVIMRMIEPNVDDRlSSIKEFLSQ 295
Cdd:cd06656 239 ERLSAVFRDFLNRCLEMDVDRR-GSAKELLQH 269
STKc_myosinIII_like cd06608
Catalytic domain of Class III myosin-like Protein Serine/Threonine Kinases; Serine/threonine ...
27-227 4.49e-19

Catalytic domain of Class III myosin-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Class III myosin-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The class III myosin-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. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), mitogen-activated protein kinase (MAPK) kinase kinase kinase 4 (MAPKKKK4 or MAP4K4) and MAPKKKK6 (or MAP4K6). MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAPK signaling cascades are important in mediating cellular responses to extracellular signals.


Pssm-ID: 173725 [Multi-domain]  Cd Length: 275  Bit Score: 83.48  E-value: 4.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYELFESrfkglnkpsEGEIAMQMK---HPLIVkTFEHGITAKN 103
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKARHKKTGQLVAIKIMDIIEDEEEEI---------KEEYNILRKysnHPNIA-TFYGAFIKKN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 104 QRI------LVMEYIAGVGIQDVI--VRKKREVIDgKEML--LMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEet 173
Cdd:cd06608  77 PPGnddqlwLVMELCGGGSVTDLVkgLRKKGKRLK-EEWIayILRETLRGLAYLHENKVIHRDIKGQNILLT--KNAE-- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32477775 174 vsgVRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIV-----RRRATDKRVDVFSLGVT 227
Cdd:cd06608 152 ---VKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIacdeqPDASYDARSDVWSLGIT 207
STKc_PAK1 cd06654
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine ...
27-295 7.25e-19

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 1, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK1 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells.


Pssm-ID: 132985 [Multi-domain]  Cd Length: 296  Bit Score: 83.23  E-value: 7.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMsnfFVAYDLERKENVGVKILDPE---KYELFesrfkglnkPSEGEIAMQMKHPLIVKTFEHGITAkN 103
Cdd:cd06654  24 RFEKIGQGASGTV---YTAMDVATGQEVAIRQMNLQqqpKKELI---------INEILVMRENKNPNIVNYLDSYLVG-D 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 104 QRILVMEYIAGVGIQDVIVRKKREviDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFG 183
Cdd:cd06654  91 ELWVVMEYLAGGSLTDVVTETCMD--EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG--MDGS-----VKLTDFG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 184 LTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEivSGRAALQHDTETATPILERR 263
Cdd:cd06654 162 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNE--NPLRALYLIATNGTPELQNP 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 32477775 264 DDIHPKVARVIMRMIEPNVDDRlSSIKEFLSQ 295
Cdd:cd06654 240 EKLSAIFRDFLNRCLDMDVEKR-GSAKELLQH 270
STKc_SLK cd06643
Catalytic domain of the Protein Serine/Threonine Kinase, Ste20-like kinase; Serine/threonine ...
37-305 1.48e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Ste20-like kinase; Serine/threonine kinases (STKs), Ste20-like kinase (SLK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase (MAPKKK) by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration.


Pssm-ID: 132974 [Multi-domain]  Cd Length: 282  Bit Score: 82.37  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYELFESRFkglnkpSEGEIAMQMKHPLIVKTFEHGITAKNQRILVmEYIAGVG 116
Cdd:cd06643  16 GAFGKVYKAQNKETGVLAAAKVIDTKSEEELEDYM------VEIDILASCDHPNIVKLLDAFYYENNLWILI-EFCAGGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 117 IQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPG 196
Cdd:cd06643  89 VDAVMLELERPLTEPQIRVVCKQTLEALNYLHENKIIHRDLKAGNILFT--LDGD-----IKLADFGVSAKNTRTIQRRD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 197 NRTGTPLYMCPEIV-----RRRATDKRVDVFSLGVTFYCLLTFQHPwQGEIVSGRAALQhDTETATPILERRDDIHPKVA 271
Cdd:cd06643 162 SFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGITLIEMAQIEPP-HHELNPMRVLLK-IAKSEPPTLAQPSRWSSEFK 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 32477775 272 RVIMRMIEPNVDDRLSSikeflsqTRGLESAFVS 305
Cdd:cd06643 240 DFLKKCLEKNVDARWTT-------TQLLQHPFVT 266
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
78-240 7.12e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 2; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 2 (Nek2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma.


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 79.98  E-value: 7.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  78 SEGEIAMQMKHPLIVKTFEHGITAKNQRI-LVMEYIAGVGIQDVIVRKKREvidgKEML-------LMREMAESLAYVH- 148
Cdd:cd08217  48 SEVNILRELKHPNIVRYYDRIIDRSNQTLyIVMEYCEGGDLAQLIQKCKKE----RKYIeeefiwrILTQLLLALYECHn 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 149 ----EQGFIHRDVCPRN-FIctppkDGEETVsgvRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFS 223
Cdd:cd08217 124 rsdpGNTVLHRDLKPANiFL-----DANNNV---KLGDFGLAKILGHDSSFAKTYVGTPYYMSPEQLNHMSYDEKSDIWS 195
                       170
                ....*....|....*..
gi 32477775 224 LGVTFYCLLTFQHPWQG 240
Cdd:cd08217 196 LGCLIYELCALSPPFTA 212
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
43-295 7.34e-18

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: 79.97  E-value: 7.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  43 FVAYDLERKENVGVKILDPEKYE--LFEsrfkgLNKpsegEIAM--QMKHPLIVKTFehGITAKNQRI-LVMEYIAGVGI 117
Cdd:cd06609  18 YKAIDKRTNQVVAIKVIDLEEAEdeIED-----IQQ----EIQFlsQCRSPYITKYY--GSFLKGSKLwIIMEYCGGGSC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 118 QDVIvrkKREVIDGKEM-LLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPG 196
Cdd:cd06609  87 LDLL---KPGKLDETYIaFILREVLLGLEYLHEEGKIHRDIKAANILLS--EEGD-----VKLADFGVSGQLTSTMSKRN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 197 NRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYclltfqhpwqgEIVSGRAALQhdtetatpilerrdDIHP-KVARVIM 275
Cdd:cd06609 157 TFVGTPFWMAPEVIKQSGYDEKADIWSLGITAI-----------ELAKGEPPLS--------------DLHPmRVLFLIP 211
                       250       260
                ....*....|....*....|..
gi 32477775 276 RMIEPNVDDRLSS--IKEFLSQ 295
Cdd:cd06609 212 KNNPPSLEGNKFSkpFKDFVSL 233
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
27-240 1.11e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 5; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 5 (Nek5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek5 subfamily is one of a family of 11 different Neks (Nek1-11). 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. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 79.23  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYELFEsrfkglNKPSEGEIAM--QMKHPLIVkTFEHGITAKNQ 104
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKE------KEASKKEVILlaKMKHPNIV-TFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 105 RILVMEYIAGVGIQDVIVRKkREVIDGKEMLL--MREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEETvsgvRLIDF 182
Cdd:cd08225  74 LFIVMEYCDGGDLMKRINRQ-RGVLFSEDQILswFVQISLGLKHIHDRKILHRDIKSQNIFLS--KNGMVA----KLGDF 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32477775 183 GLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQG 240
Cdd:cd08225 147 GIARQLNDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEG 204
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
57-287 2.56e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii Never In Mitosis gene A (NIMA)-related kinase 1 (CNK2)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii CNK2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis.


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 78.26  E-value: 2.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  57 KILDPEKYELFESRFKGLNKP------SEGEIAMQMKHPLIVKTFEHGITAkNQRILVMEYIAGVGIQDVIVRKKREVID 130
Cdd:cd08530  21 RLSDNQFYALKEVDLGSMSQKeredavNEIRILASVNHPNIISYKEAFLDG-NKLCIVMEYAPFGDLSKAISKRKKKRKL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 131 GKEMLLMR---EMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsgVRLIDFGLTVPATPpfMAPGNRTGTPLYMCP 207
Cdd:cd08530 100 IPEQEIWRifiQLLRGLQALHEQKILHRDLKSANILLVANDL-------VKIGDLGISKVLKK--NMAKTQIGTPHYMAP 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 208 EIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQGEIVSG-RAALQHDTETATPILERRDdihpkVARVIMRMIEPNVDDRL 286
Cdd:cd08530 171 EVWKGRPYSYKSDIWSLGCLLYEMATFAPPFEARSMQDlRYKVQRGKYPPIPPIYSQD-----LQNFIRSMLQVKPKLRP 245

                .
gi 32477775 287 S 287
Cdd:cd08530 246 N 246
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
78-291 3.28e-17

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: 78.06  E-value: 3.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  78 SEGEIAMQMKHPLIVKTFEhGITAKNQRILVMEYIAG---------VGIQDVIVRKKrevidgkemlLMREMAESLAYVH 148
Cdd:cd05579  42 TERDILSQAQSPYVVKLYY-SFQGKKNLYLVMEYLPGgdlasllenVGSLDEDVARI----------YIAEIVLALEYLH 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 149 EQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGL----------TVPATPpfmAPGNRT-GTPLYMCPEIVRRRATDK 217
Cdd:cd05579 111 SNGIIHRDLKPDNILID--SNGH-----LKLTDFGLskvglvrrqiNLNDDE---KEDKRIvGTPDYIAPEVILGQGHSK 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 218 RVDVFSLGVTFYCLLTFQHPWQGEIVsgraalqhdTETATPILERR------DDIHPKVARVIMRMIEPNVDDRL--SSI 289
Cdd:cd05579 181 TVDWWSLGCILYEFLVGIPPFHGETP---------EEIFQNILNGKiewpedVEVSDEAIDLISKLLVPDPEKRLgaKSI 251

                ..
gi 32477775 290 KE 291
Cdd:cd05579 252 EE 253
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
82-288 4.62e-17

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: 77.56  E-value: 4.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  82 IAMQMKHPLIVKTFeHGITAKNQRILVMEYIAGVGIQDVIvrKKREVIDGKEMLL-MREMAESLAYVHEQGFIHRDVCPR 160
Cdd:cd05123  46 ILSRINHPFIVKLH-YAFQTEEKLYLVLEYAPGGELFSHL--SKEGRFSEERARFyAAEIVLALEYLHSLGIIYRDLKPE 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 161 NFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQG 240
Cdd:cd05123 123 NILLD--ADGH-----IKLTDFGLAKELSSEGSRTNTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYA 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 32477775 241 EivsGRAALQHDTETATPILERRDDihPKVARVIMRMIEPNVDDRLSS 288
Cdd:cd05123 196 E---DRKEIYEKILKDPLRFPEFLS--PEARDLISGLLQKDPTKRLGS 238
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ...
37-240 1.06e-16

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: 76.98  E-value: 1.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKYElfesrfKGLNKPSEGEIAM--QMKHPLIVKTFEhGITAKNQRILVMEYIAg 114
Cdd:cd05118  10 GTYGVVYKARDKLTGEIVAIKKIKLRFES------EGIPKTALREIKLlkELNHPNIIKLLD-VFRHKGDLYLVFEFMD- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 115 VGIQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsgVRLIDFGLTVPATPPFMA 194
Cdd:cd05118  82 TDLYKLIKDRQRGLPESLIKSYLYQLLQGLAFCHSHGILHRDLKPENLLINTEGV-------LKLADFGLARSFGSPVRP 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 32477775 195 PGNRTGTPLYMCPEI-VRRRATDKRVDVFSLGVTFYCLLTFQHPWQG 240
Cdd:cd05118 155 YTHYVVTRWYRAPELlLGDKGYSTPVDIWSVGCIFAELLSRRPLFPG 201
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
27-240 1.11e-16

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: 76.61  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  27 RFERSRTAATGTMSNFFVAYDLERKENVGVKI--LDPEKYELFEsrfkglNKPSEGEIAMQMKHPLIVKTfeHGITAKNQ 104
Cdd:cd06626   1 RWQRGNKIGGGTFGKVYTAVNLDTGELMAVKEirIQDNDPKTIK------EIADEMKVLELLKHPNLVKY--YGVEVHRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 105 RILV-MEYIAGVGIQDVIVRKKREvidgKEMLLMR---EMAESLAYVHEQGFIHRDVCPRNFICTPpkdgeetvSGV-RL 179
Cdd:cd06626  73 KVYIfMEYCSGGTLEELLEHGRIL----DEHVIRVytlQLLEGLAYLHSHGIVHRDIKPANIFLDH--------NGViKL 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32477775 180 IDFGLTV----PATPPFMAPGNRTGTPLYMCPEIVRRRATDKR---VDVFSLGVTFYCLLTFQHPWQG 240
Cdd:cd06626 141 GDFGCAVklknNTTTMGEEVQSLAGTPAYMAPEVITGGKGKGHgraADIWSLGCVVLEMATGKRPWSE 208
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
78-241 1.43e-16

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: 76.12  E-value: 1.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  78 SEGEIAMQMKHPLIVKTFEhgiTAKNQRIL--VMEYIAGVGIQDVIvRKKREVIDGKEMLLMREMAESLAYVHEQGFIHR 155
Cdd:cd05572  42 SEKEILEECNHPFIVKLYR---TFKDKKYIymLMEYCLGGELWTIL-RDRGLFDEYTARFYIACVVLAFEYLHNRGIIYR 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 156 DVCPRNFICTppKDGEetvsgVRLIDFGltvpaTPPFMAPGNRT----GTPLYMCPEIVRRRATDKRVDVFSLGVTFYCL 231
Cdd:cd05572 118 DLKPENLLLD--SNGY-----VKLVDFG-----FAKKLKSGQKTwtfcGTPEYVAPEIILNKGYDFSVDYWSLGILLYEL 185
                       170
                ....*....|
gi 32477775 232 LTFQHPWQGE 241
Cdd:cd05572 186 LTGRPPFGED 195
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
81-228 2.54e-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: 76.10  E-value: 2.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  81 EIAM--QMKHPLIVKTFEHGITaKNQRILVMEYIAGVGIQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVC 158
Cdd:cd06614  65 EILImkDCKHPNIVDYYDSYLV-GDELWVVMEYMDGGSLTDIITQNFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIK 143
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32477775 159 PRNFICTppKDGEetvsgVRLIDFGLTVPATPpfmAPGNRT---GTPLYMCPEIVRRRATDKRVDVFSLGVTF 228
Cdd:cd06614 144 SDNILLS--KDGS-----VKLADFGFAAQLTK---EKSKRNsvvGTPYWMAPEVIKRKDYGPKVDIWSLGIMC 206
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine ...
25-227 4.03e-16

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 3 (MAPKKKK3 or MAP4K3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K3-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 includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain, similar to MAP4K4/6. MAP4Ks are involved in some MAPK signaling pathways that are important in mediating cellular responses to extracellular signals by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK).


Pssm-ID: 173727 [Multi-domain]  Cd Length: 262  Bit Score: 75.02  E-value: 4.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  25 EKRFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYELFESrfkglnkpSEGEIAM--QMKHPLIVKTFehGITAK 102
Cdd:cd06613   2 QEDYELIQRIGSGTYGDVYKARDIATGELVAIKVIKLEPGDDFEI--------IQQEISMlkECRHPNIVAYF--GSYLR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 103 NQRI-LVMEYIAGVGIQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLID 181
Cdd:cd06613  72 RDKLwIVMEYCGGGSLQDIYQVTRGPLSELQIAYVCRETLKGLAYLHETGKIHRDIKGANILLT--EDGD-----VKLAD 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 32477775 182 FGLTVPATPPFMAPGNRTGTPLYMCPEIV---RRRATDKRVDVFSLGVT 227
Cdd:cd06613 145 FGVSAQLTATIAKRKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGIT 193
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
37-233 6.04e-16

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: 74.21  E-value: 6.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKILDPEKyeLFESRFKGLNkpSEGEIAMQMKHPLIVKTFEHgITAKNQRILVMEYIAGVG 116
Cdd:cd06627  11 GAFGVVYKGLNLETGDFVAIKQISLEK--IKEEALKSIM--QEIDLLKNLKHPNIVKYIGS-IETSDSLYIILEYAENGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 117 IQDVIvrKKRevidGK--EMLL---MREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVPATPp 191
Cdd:cd06627  86 LRQII--KKF----GPfpESLVavyVYQVLQGLAYLHEQGVIHRDIKAANILTT--KDGV-----VKLADFGVATKLND- 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32477775 192 fMAPGNRT--GTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLLT 233
Cdd:cd06627 152 -VSKDDASvvGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLT 194
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
23-227 6.71e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation.


Pssm-ID: 132972 [Multi-domain]  Cd Length: 277  Bit Score: 74.73  E-value: 6.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  23 DVEKRFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYElfeSRFKGLNKpsEGEIAMQMKHPLIVKTFehGITAK 102
Cdd:cd06641   1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAE---DEIEDIQQ--EITVLSQCDSPYVTKYY--GSYLK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 103 NQRI-LVMEYIAGVGIQDVIvrKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLID 181
Cdd:cd06641  74 DTKLwIIMEYLGGGSALDLL--EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS--EHGE-----VKLAD 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32477775 182 FGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVT 227
Cdd:cd06641 145 FGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGIT 190
STKc_myosinIIIA cd06638
Catalytic domain of the Protein Serine/Threonine Kinase, Class IIIA myosin; Serine/threonine ...
23-227 9.11e-16

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 74.28  E-value: 9.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  23 DVEKRFERSRTAATGTMSNFFVAYDLERKENVGVKILDP--EKYELFESRFKGLNKPSEgeiamqmkHPLIVK----TFE 96
Cdd:cd06638  15 DPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPihDIDEEIEAEYNILKALSD--------HPNVVKfygmYYK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  97 HGITAKNQRILVMEYIAGVGIQDVIvrkKREVIDGKEM------LLMREMAESLAYVHEQGFIHRDVCPRNFICTppkdg 170
Cdd:cd06638  87 KDVKNGDQLWLVLELCNGGSVTDLV---KGFLKRGERMeepiiaYILHEALMGLQHLHVNKTIHRDVKGNNILLT----- 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32477775 171 eeTVSGVRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIVR-----RRATDKRVDVFSLGVT 227
Cdd:cd06638 159 --TEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGIT 218
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
23-227 1.15e-15

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


Pssm-ID: 132973 [Multi-domain]  Cd Length: 277  Bit Score: 73.93  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  23 DVEKRFERSRTAATGTMSNFFVAYDLERKENVGVKILDPEKYElfeSRFKGLNKpsEGEIAMQMKHPLIVKTFehGITAK 102
Cdd:cd06642   1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAE---DEIEDIQQ--EITVLSQCDSPYITRYY--GSYLK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 103 NQRI-LVMEYIAGVGIQDVIvrKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTPPKDgeetvsgVRLID 181
Cdd:cd06642  74 GTKLwIIMEYLGGGSALDLL--KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD-------VKLAD 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32477775 182 FGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVT 227
Cdd:cd06642 145 FGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGIT 190
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
75-239 1.67e-15

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 73.08  E-value: 1.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  75 NKPSEGEIAMQMKHPLIVkTFEHGITAKNQRILVMEYIAGVGIQDVIvRKKREVIDGKEMLL--MREMAESLAYVHEQGF 152
Cdd:cd08219  44 DSRKEAVLLAKMKHPNIV-AFKESFEADGHLYIVMEYCDGGDLMQKI-KLQRGKLFPEDTILqwFVQMCLGVQHIHEKRV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 153 IHRDVCPRNFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIVRRRATDKRVDVFSLGVTFYCLL 232
Cdd:cd08219 122 LHRDIKSKNIFLT--QNGK-----VKLGDFGSARLLTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELC 194

                ....*..
gi 32477775 233 TFQHPWQ 239
Cdd:cd08219 195 TLKHPFQ 201
STKc_SLK_like cd06611
Catalytic domain of Ste20-like kinase-like Protein Serine/Threonine Kinases; Serine/threonine ...
79-227 2.54e-15

Catalytic domain of Ste20-like kinase-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Ste20-like kinase (SLK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SLK-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 the subfamily include SLK, STK10 (also called LOK for lymphocyte-oriented kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney (HEK) cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 73.24  E-value: 2.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  79 EGEIAMQMKHPLIVKTFEhGITAKNQRILVMEYIAGVGIQDVIVRKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVC 158
Cdd:cd06611  52 EIDILSECKHPNIVGLYE-AYFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLK 130
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32477775 159 PRNFICTppKDGEetvsgVRLIDFGLTVPATPPFMAPGNRTGTPLYMCPEIV-----RRRATDKRVDVFSLGVT 227
Cdd:cd06611 131 AGNILLT--LDGD-----VKLADFGVSAKNKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGIT 197
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
43-240 3.65e-15

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


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 73.21  E-value: 3.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  43 FVAYDLERKENVGVKILdpeKYELFESRFKGLNKPSEGEIAMQMKHPLIVKTFeHGITAKNQRILVMEYIAGvGIQDVIV 122
Cdd:cd05600  18 FLAKKKDTGEIVALKRM---KKSLLFKLNEVRHVLTERDILTTTKSEWLVKLL-YAFQDDEYLYLAMEYVPG-GDFRTLL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 123 RKKREVIDGKEMLLMREMAESLAYVHEQGFIHRDVCPRNFICTppKDGEetvsgVRLIDFGLtvpATPPFMAPGNRTGTP 202
Cdd:cd05600  93 NNLGVLSEDHARFYMAEMFEAVDALHELGYIHRDLKPENFLID--ASGH-----IKLTDFGL---SKGIVTYANSVVGSP 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 32477775 203 LYMCPEIVRRRATDKRVDVFSLGVTFYCLLTFQHPWQG 240
Cdd:cd05600 163 DYMAPEVLRGKGYDFTVDYWSLGCMLYEFLCGFPPFSG 200
STKc_MEKK3_like cd06625
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
37-288 4.46e-15

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: 72.15  E-value: 4.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775  37 GTMSNFFVAYDLERKENVGVKIL--DPEKYELfESRFKGLnkpsEGEIAM--QMKHPLIVKTFehGITAKNQRILV-MEY 111
Cdd:cd06625  13 GAFGRVYLCYDVDTGRELAVKQVpfDPDSPET-KKEVNAL----ECEIQLlkNLQHERIVQYY--GCLRDDETLSIfMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32477775 112 IAGVGIQDVIVRKK--REVIDGKemlLMREMAESLAYVHEQGFIHRDVCPRNFIctppkdgEETVSGVRLIDFGL----- 184
Cdd:cd06625  86 MPGGSVKDQLKAYGalTETVTRK---YTRQILEGVEYLHSNMIVHRDIKGANIL-------RDSAGNVKLGDFGAskrlq 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*