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Conserved domains on  [gi|5454096|ref|NP_006273|]
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serine/threonine-protein kinase 4 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase ...
26-281 0e+00

Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase 1 and 2; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 1 (MST1) and MST2 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 (a MAPK kinase) and MEKK1 (a MAPK kinase kinase) by acting as a MAPK kinase kinase kinase (MAPKKKK). Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress.


:

Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612   1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612  81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612 161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                       250
                ....*....|....*.
gi 5454096  266 PEQRATATQLLQHPFV 281
Cdd:cd06612 241 PEERPSAIQLLQHPFI 256
Mst1_SARAH pfam11629
C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH ...
432-480 9.90e-25

C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH domain of Mst1. SARAH controls apoptosis and cell cycle arrest via the Ras, RASSF, MST pathway. The Mst1 SARAH domain interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


:

Pssm-ID: 152065  Cd Length: 49  Bit Score: 96.65  E-value: 9.90e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5454096    432 DYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAK 480
Cdd:pfam11629   1 DFEFLKSLSVEELEQRLASLDPEMETEIEELRQRYQAKRQPILDAIEAK 49
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-281 1.39e-111

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 333.34  E-value: 1.39e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096      30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     107 AGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMaKRNTVIG 186
Cdd:smart00220  81 GGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPE-LWSDNFTDFVKQCLVKS 265
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 5454096     266 PEQRATATQLLQHPFV 281
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase ...
26-281 0e+00

Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase 1 and 2; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 1 (MST1) and MST2 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 (a MAPK kinase) and MEKK1 (a MAPK kinase kinase) by acting as a MAPK kinase kinase kinase (MAPKKKK). Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612   1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612  81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612 161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                       250
                ....*....|....*.
gi 5454096  266 PEQRATATQLLQHPFV 281
Cdd:cd06612 241 PEERPSAIQLLQHPFI 256
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
108-289 1.38e-40

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 144.47  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     108 GSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHfmrkihRDIKAGNILLNTEGHAKLadFGVAGQLTDTMAkrntvIGT 187
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELH------RQAKSGNILLTWDGLLKL--DGSVAFKTPEQS-----RPD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     188 PFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTF-----RKPELWSD--NFTDFVKQ 260
Cdd:smart00750  68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADdprdrSNLEGVSAarSFEDFMRL 147
                          170       180
                   ....*....|....*....|....*....
gi 5454096     261 CLVKSPEQRATATQLLQHPFVRSAKGVSI 289
Cdd:smart00750 148 CASRLPQRREAANHYLAHCRALFAETLEL 176
Mst1_SARAH pfam11629
C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH ...
432-480 9.90e-25

C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH domain of Mst1. SARAH controls apoptosis and cell cycle arrest via the Ras, RASSF, MST pathway. The Mst1 SARAH domain interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


Pssm-ID: 152065  Cd Length: 49  Bit Score: 96.65  E-value: 9.90e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 5454096    432 DYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAK 480
Cdd:pfam11629   1 DFEFLKSLSVEELEQRLASLDPEMETEIEELRQRYQAKRQPILDAIEAK 49
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
1-176 3.95e-09

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 57.32  E-value: 3.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    1 METVQLRNPP--RRQLKKLDEDSLTKQPEEVFDVLEK--LGEGSYGSVYKAIHKeTGQIVAIK-QVP-----VESDLQ-- 68
Cdd:COG0661  94 LAKLQDRVPPfpFEEAERIIEEELGRPIEELFSEFEPepIASASIAQVHRAVLK-SGEEVAVKvQRPgirerIEADLKll 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   69 --------------------EIIKEISIM--QQCDSPHVVKY---YGSYFKNTDL-------W-------IVMEYCGAGS 109
Cdd:COG0661 173 rrlarlikrlppggrrldlvEVVDEFEKRlrEELDYRREAANaerFRENFKDDPDvyvpkvyWeyttrrvLTMEWIDGIK 252
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5454096  110 VSDIIRLRNKTLTEDEIATIL-QSTLKGLEYLHFMrkiHRDIKAGNILLNTEGHAKLADFGVAGQLTD 176
Cdd:COG0661 253 ISDIAALKSAGIDRKELAELLvRAFLRQLLRDGFF---HADPHPGNILVRSDGRIVLLDFGIVGRLDP 317
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
32-171 5.81e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 46.87  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    32 VLEKL-GEGSYGSVY----KAIHKETGQIVA----------IKQVPVESDLQEIIKEISIMQQCDSPH--VVKYYG-SYF 93
Cdd:PHA02882  15 KIDKLiGCGGFGCVYetqcASDHCINNQAVAkienlenetiVMETLVYNNIYDIDKIALWKNIHNIDHlgIPKYYGcGSF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    94 KNTDLW---IVME--YCGAGSVSDIIRLRNKTLtedeIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADF 168
Cdd:PHA02882  95 KRCRMYyrfILLEklVENTKEIFKRIKCKNKKL----IKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIIDY 170

                 ...
gi 5454096   169 GVA 171
Cdd:PHA02882 171 GIA 173
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-281 1.39e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 333.34  E-value: 1.39e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096      30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     107 AGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMaKRNTVIG 186
Cdd:smart00220  81 GGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPE-LWSDNFTDFVKQCLVKS 265
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 5454096     266 PEQRATATQLLQHPFV 281
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
30-281 3.41e-90

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 278.36  E-value: 3.41e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESD----LQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEkskkDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    106 GAGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:pfam00069  81 EGGDLFDYLS-RGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSSSSLTTFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    186 GTPFWMAPEVIQE-IGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELW----SDNFTDFVKQ 260
Cdd:pfam00069 160 GTPEYMAPEVLLGgNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDEPKsdsgSEEAKDLIKK 239
                         250       260
                  ....*....|....*....|.
gi 5454096    261 CLVKSPEQRATATQLLQHPFV 281
Cdd:pfam00069 240 CLNKDPSKRPTAEEILQHPWF 260
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
30-307 3.00e-56

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: 193.81  E-value: 3.00e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   30 FDVLEKLGEGSYGSVYKAIHKetgQIVAIKQVPVE-----SDLQEIIKEISIMQQCDSP-HVVKYYGSYFKNTDLWIVME 103
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKlesksKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  104 YCGAGSVSDIIRLR--NKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGH-AKLADFGVAGQLTDTMAK 180
Cdd:COG0515  79 YVDGGSLEDLLKKIgrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  181 R------NTVIGTPFWMAPEVIQEIG---YNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMI----------PTNPP 241
Cdd:COG0515 159 SsipalpSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptpSLASP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5454096  242 PTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQES 307
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSL 304
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
35-286 2.19e-44

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 160.37  E-value: 2.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    35 KLGEGSYGSVYKAIHKETGQIVAIKQV---PVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVS 111
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLYALKVIygnHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   112 DiirlrNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWM 191
Cdd:PLN00034 161 G-----THIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYM 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   192 APEVI----QEIGYN-CVADIWSLGITAIEMAEGKPPYA-----DIHP-MRAIFMI-PTNPPPTFrkpelwSDNFTDFVK 259
Cdd:PLN00034 236 SPERIntdlNHGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrqgDWASlMCAICMSqPPEAPATA------SREFRHFIS 309
                        250       260
                 ....*....|....*....|....*..
gi 5454096   260 QCLVKSPEQRATATQLLQHPFVRSAKG 286
Cdd:PLN00034 310 CCLQREPAKRWSAMQLLQHPFILRAQP 336
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
30-304 1.41e-35

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 134.94  E-value: 1.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIK-----QVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEY 104
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKclkkrEILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   105 CGAGSVsdIIRLRNKTLTEDEIATILQSTLK-GLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDtmaKRNT 183
Cdd:PTZ00263 100 VVGGEL--FTHLRKAGRFPNDVAKFYHAELVlAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD---RTFT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   184 VIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNpppTFRKPELWSDNFTDFVKQCLV 263
Cdd:PTZ00263 175 LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFPNWFDGRARDLVKGLLQ 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 5454096   264 KSPEQRATATQ-----LLQHPFVRSAKGVSILRDLINEAMDVKLKR 304
Cdd:PTZ00263 252 TDHTKRLGTLKggvadVKNHPYFHGANWDKLYARYYPAPIPVRVKS 297
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
30-221 1.01e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 83.51  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQvpveSDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVME------ 103
Cdd:PHA03212  94 FSILETFTPGAEGFAFACIDNKTCEHVVIKA----GQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPryktdl 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   104 YCgagSVSDiirlrNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKR-N 182
Cdd:PHA03212 170 YC---YLAA-----KRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKyY 241
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 5454096   183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGK 221
Cdd:PHA03212 242 GWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
51-291 5.59e-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: 63.71  E-value: 5.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096      51 ETGQIVAIKQVPVESDLQE-----IIKEISIMQQCDSPHVVKYYGSYFKNTD-LWIVMEYCGAGSVSDIIRLRNKTLTED 124
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEhqrarFRRETALCARLYHPNIVALLDSGEAPPGlLFAVFEYVPGRTLREVLAADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     125 EIATILQsTLKGLEYLHFMRKIHRDIKAGNILLNTEG---HAKLADFGVAGQLTD-------TMAKRNTVIGTPFWMAPE 194
Cdd:TIGR03903   81 TGRLMLQ-VLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGvrdadvaTLTRTTEVLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096     195 VIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMiPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQ 274
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ-QLSPVDVSLPPWIAGHPLGQVLRKALNKDPRQRAASAP 238
                          250
                   ....*....|....*....
gi 5454096     275 LLQHPF--VRSAKGVSILR 291
Cdd:TIGR03903  239 ALAERFraLELCALVGILR 257
pknD PRK13184
serine/threonine-protein kinase; Reviewed
30-224 9.15e-11

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 62.87  E-value: 9.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096    30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVpvESDLQE-------IIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKI--REDLSEnpllkkrFLREAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   103 EYCGAGSVSDIIR-LRNKTLTEDEIA---------TILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVA- 171
Cdd:PRK13184  82 PYIEGYTLKSLLKsVWQKESLSKELAektsvgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAi 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   172 -----------------GQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPY 224
Cdd:PRK13184 162 fkkleeedlldidvderNICYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
 
Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase ...
26-281 0e+00

Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase 1 and 2; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 1 (MST1) and MST2 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 (a MAPK kinase) and MEKK1 (a MAPK kinase kinase) by acting as a MAPK kinase kinase kinase (MAPKKKK). Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612   1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612  81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612 161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                       250
                ....*....|....*.
gi 5454096  266 PEQRATATQLLQHPFV 281
Cdd:cd06612 241 PEERPSAIQLLQHPFI 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
29-280 1.91e-150

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: 432.40  E-value: 1.91e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   29 VFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES--DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:cd05122   1 LFEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESkeKKEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  107 AGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAkRNTVIG 186
Cdd:cd05122  81 GGSLKDLLKSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDTKA-RNTMVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSP 266
Cdd:cd05122 160 TPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPPGLRNPEKWSDEFKDFLKKCLQKNP 239
                       250
                ....*....|....
gi 5454096  267 EQRATATQLLQHPF 280
Cdd:cd05122 240 EKRPTAEQLLKHPF 253
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
28-294 7.11e-145

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: 418.94  E-value: 7.11e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   28 EVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEY 104
Cdd:cd06609   1 ELFTLLECIGKGSFGEVYKAIDKRTNQVVAIKVIDLEEaedEIEDIQQEIQFLSQCRSPYITKYYGSFLKGSKLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  105 CGAGSVSDIIRLRnkTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTV 184
Cdd:cd06609  81 CGGGSCLDLLKPG--KLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  185 IGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPElWSDNFTDFVKQCLVK 264
Cdd:cd06609 159 VGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNK-FSKPFKDFVSLCLNK 237
                       250       260       270
                ....*....|....*....|....*....|
gi 5454096  265 SPEQRATATQLLQHPFVRSAKGVSILRDLI 294
Cdd:cd06609 238 DPKERPSAKELLKHKFIKKAKKTSYLTLLI 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine ...
26-280 5.44e-142

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: 411.30  E-value: 5.44e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE--SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVME 103
Cdd:cd06613   1 PQEDYELIQRIGSGTYGDVYKARDIATGELVAIKVIKLEpgDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  104 YCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNT 183
Cdd:cd06613  81 YCGGGSLQDIYQVTRGPLSELQIAYVCRETLKGLAYLHETGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  184 VIGTPFWMAPEVIQE---IGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTN--PPPTFRKPELWSDNFTDFV 258
Cdd:cd06613 161 FIGTPYWMAPEVAAVerkGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLISKSnfPPPKLKDKEKWSPVFHDFI 240
                       250       260
                ....*....|....*....|..
gi 5454096  259 KQCLVKSPEQRATATQLLQHPF 280
Cdd:cd06613 241 KKCLTKDPKKRPTATKLLQHPF 262
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
15-280 5.92e-125

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: 368.85  E-value: 5.92e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   15 KKLDEDSLTKQ--PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQE-IIKEISIMQQCDSPHVVKYYGS 91
Cdd:cd06614   4 LKAALKDIVSEgdPRELYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKElIINEILIMKDCKHPNIVDYYDS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   92 YFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVA 171
Cdd:cd06614  84 YLVGDELWVVMEYMDGGSLTDIITQNFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  172 GQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWS 251
Cdd:cd06614 164 AQLTKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLREPPLRALFLITTKGIPPLKNPEKWS 243
                       250       260
                ....*....|....*....|....*....
gi 5454096  252 DNFTDFVKQCLVKSPEQRATATQLLQHPF 280
Cdd:cd06614 244 PEFKDFLNKCLVKDPEKRPSAEELLQHPF 272
STKc_myosinIII_like cd06608
Catalytic domain of Class III myosin-like Protein Serine/Threonine Kinases; Serine/threonine ...
24-281 4.30e-124

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: 366.22  E-value: 4.30e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   24 KQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIK-EISIMQQ-CDSPHVVKYYGSYFKNTD---- 97
Cdd:cd06608   2 PDPTGIFELVEVIGEGTYGKVYKARHKKTGQLVAIKIMDIIEDEEEEIKeEYNILRKySNHPNIATFYGAFIKKNPpgnd 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   98 --LWIVMEYCGAGSVSDII---RLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAG 172
Cdd:cd06608  82 dqLWLVMELCGGGSVTDLVkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTKNAEVKLVDFGVSA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  173 QLTDTMAKRNTVIGTPFWMAPEVIQ-----EIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKP 247
Cdd:cd06608 162 QLDSTLGRRNTFIGTPYWMAPEVIAcdeqpDASYDARSDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSP 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 5454096  248 ELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFV 281
Cdd:cd06608 242 ENWSKKFNDFISECLIKNYEQRPFMEELLEHPFI 275
STKc_SLK_like cd06611
Catalytic domain of Ste20-like kinase-like Protein Serine/Threonine Kinases; Serine/threonine ...
26-296 6.00e-111

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: 332.48  E-value: 6.00e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES--DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVME 103
Cdd:cd06611   3 PNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESeeELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  104 YCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNT 183
Cdd:cd06611  83 FCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  184 VIGTPFWMAPEVI-----QEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFV 258
Cdd:cd06611 163 FIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKWSSSFNDFL 242
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 5454096  259 KQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINE 296
Cdd:cd06611 243 KSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLAE 280
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
30-280 1.27e-102

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: 310.83  E-value: 1.27e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:cd06610   3 YELIEVIGVGATAVVYAAICLPNNEKVAIKRIDLEkcqTSVDELRKEVQAMSQCNHPNVVKYYTSFVVGDELWLVMPYLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  107 AGSVSDIIRLRNKT--LTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTM----AK 180
Cdd:cd06610  83 GGSLLDIMKSSYPRggLDEAIIATVLKEVLKGLEYLHSNGQIHRDIKAGNILLGEDGSVKIADFGVSASLADGGdrtrKV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  181 RNTVIGTPFWMAPEVIQEI-GYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTF---RKPELWSDNFTD 256
Cdd:cd06610 163 RKTFVGTPCWMAPEVMEQVhGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLetgADYKKYSKSFRK 242
                       250       260
                ....*....|....*....|....
gi 5454096  257 FVKQCLVKSPEQRATATQLLQHPF 280
Cdd:cd06610 243 MISLCLQKDPSKRPTAEELLKHKF 266
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
26-295 3.57e-102

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: 310.06  E-value: 3.57e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06642   2 PEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06642  82 EYLGGGSALDL--LKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06642 160 TFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQ--YSKPFKEFVEACL 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 5454096  263 VKSPEQRATATQLLQHPFV-RSAKGVSILRDLIN 295
Cdd:cd06642 238 NKDPRFRPTAKELLKHKFItRYTKKTSFLTELID 271
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
34-281 5.30e-102

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: 308.79  E-value: 5.30e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   34 EKLGEGSYGSVYKAIHKETGQIVAIKQVPV----ESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGS 109
Cdd:cd06627   6 DLIGRGAFGVVYKGLNLETGDFVAIKQISLekikEEALKSIMQEIDLLKNLKHPNIVKYIGSIETSDSLYIILEYAENGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  110 VSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPF 189
Cdd:cd06627  86 LRQIIK-KFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGVVKLADFGVATKLNDVSKDDASVVGTPY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  190 WMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFrkPELWSDNFTDFVKQCLVKSPEQR 269
Cdd:cd06627 165 WMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPYYDLNPMAALFRIVQDDHPPL--PEGISPELKDFLMQCFQKDPNLR 242
                       250
                ....*....|..
gi 5454096  270 ATATQLLQHPFV 281
Cdd:cd06627 243 PTAKQLLKHPWI 254
STKc_MST4 cd06640
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; ...
26-295 1.71e-100

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 4 (MST4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 305.82  E-value: 1.71e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06640   2 PEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06640  82 EYLGGGSALDL--LRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06640 160 TFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLTGE--FSKPFKEFIDACL 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 5454096  263 VKSPEQRATATQLLQHPF-VRSAKGVSILRDLIN 295
Cdd:cd06640 238 NKDPSFRPTAKELLKHKFiVKNAKKTSYLTELID 271
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
26-295 1.82e-99

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: 303.15  E-value: 1.82e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06641   2 PEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06641  82 EYLGGGSALDL--LEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096  183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06641 160 TFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPMKVLFLIPKNNPPTLEGN--YSKPLKEFVEACL 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 5454096  263 VKSPEQRATATQLLQHPFV-RSAKGVSILRDLIN 295
Cdd:cd06641 238 NKEPSFRPTAKELLKHKFIvRFAKKTSYLTELID 271
STKc_myosinIIIA cd06638
Catalytic domain of the Protein Serine/Threonine Kinase, Class IIIA myosin; Serine/threonine ...
26-281 7.81e-98

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: 299.23  E-value: 7.81e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5454096   26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQV-PVESDLQEIIKEISIMQQ-CDSPHVVKYYGSYFK----NTD-L 98
Cdd:cd06638  16 PSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILdPIHDIDEEIEAEYNILKAlSDHPNVVKFYGMYYKkdvkNGDqL 95