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Conserved domains on  [gi|281182886|ref|NP_001162203|]
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serine/threonine-protein kinase 4 [Papio anubis]

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List of domain hits

Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
26-281 0e+00

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612   81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612  161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                        250
                 ....*....|....*.
gi 281182886 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 ...
433-480 1.18e-23

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: 288481  Cd Length: 48  Bit Score: 93.83  E-value: 1.18e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 281182886  433 YEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAK 480
Cdd:pfam11629   1 FEFLKFLSYEELQQRLASLDPEMEQEIEELRKRYQAKRQPILDAIEAK 48
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-281 4.56e-111

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.80  E-value: 4.56e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886    30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   107 AGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMaKRNTVIG 186
Cdd:smart00220  81 GGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPE-LWSDNFTDFVKQCLVKS 265
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 281182886   266 PEQRATATQLLQHPFV 281
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
26-281 0e+00

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612   81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612  161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                        250
                 ....*....|....*.
gi 281182886 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 2.67e-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: 143.69  E-value: 2.67e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   108 GSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHfmrkihRDIKAGNILLNTEGQAKLadFGVAGQLTDTMAkrntvIGT 187
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELH------RQAKSGNILLTWDGLLKL--DGSVAFKTPEQS-----RPD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   188 PFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTF-----RKPELWSD--NFTDFVKQ 260
Cdd:smart00750  68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADdprdrSNLEGVSAarSFEDFMRL 147
                          170       180
                   ....*....|....*....|....*....
gi 281182886   261 CLVKSPEQRATATQLLQHPFVKSAKGVSI 289
Cdd:smart00750 148 CASRLPQRREAANHYLAHCRALFAETLEL 176
Mst1_SARAH pfam11629
C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH ...
433-480 1.18e-23

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: 288481  Cd Length: 48  Bit Score: 93.83  E-value: 1.18e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 281182886  433 YEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAK 480
Cdd:pfam11629   1 FEFLKFLSYEELQQRLASLDPEMEQEIEELRKRYQAKRQPILDAIEAK 48
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-281 4.56e-111

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 331.80  E-value: 4.56e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886    30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   107 AGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMaKRNTVIG 186
Cdd:smart00220  81 GGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPE-LWSDNFTDFVKQCLVKS 265
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 281182886   266 PEQRATATQLLQHPFV 281
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
30-281 3.05e-93

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 286.03  E-value: 3.05e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886   30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESD----LQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVKKIKKEKIkkkkDKNVLREIKILKKLNHPNIVRLYDVFEDKDHLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  106 GAGSVSDIIRlRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTmAKRNTVI 185
Cdd:pfam00069  81 EGGSLFDLLS-EKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAKQLSSG-SKLTTFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIH---PMRAIFMIPTNPPPTFRKPelwSDNFTDFVKQCL 262
Cdd:pfam00069 159 GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINgdtLYELIIDQLDLSSPRPSSI---SEEAKDLLKKLL 235
                         250
                  ....*....|....*....
gi 281182886  263 VKSPEQRATATQLLQHPFV 281
Cdd:pfam00069 236 KKDPSKRLTATQALQHPWF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-307 3.77e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 193.42  E-value: 3.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  30 FDVLEKLGEGSYGSVYKAIHKetgQIVAIKQVPVE-----SDLQEIIKEISIMQQCDSP-HVVKYYGSYFKNTDLWIVME 103
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKlesksKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 104 YCGAGSVSDIIRLR--NKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEG-QAKLADFGVAGQLTDTMAK 180
Cdd:COG0515   79 YVDGGSLEDLLKKIgrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAKLLPDPGST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 181 R------NTVIGTPFWMAPEVIQEIG---YNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMI----------PTNPP 241
Cdd:COG0515  159 SsipalpSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTlkiilelptpSLASP 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182886 242 PTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQES 307
Cdd:COG0515  239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSL 304
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
35-286 8.89e-45

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 161.53  E-value: 8.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  35 KLGEGSYGSVYKAIHKETGQIVAIKQV---PVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVS 111
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLYALKVIygnHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 112 DiirlrNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVIGTPFWM 191
Cdd:PLN00034 161 G-----THIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYM 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 192 APEVI----QEIGYN-CVADIWSLGITAIEMAEGKPPYA-----DIHP-MRAIFMI-PTNPPPTFrkpelwSDNFTDFVK 259
Cdd:PLN00034 236 SPERIntdlNHGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrqgDWASlMCAICMSqPPEAPATA------SREFRHFIS 309
                        250       260
                 ....*....|....*....|....*..
gi 281182886 260 QCLVKSPEQRATATQLLQHPFVKSAKG 286
Cdd:PLN00034 310 CCLQREPAKRWSAMQLLQHPFILRAQP 336
 
Name Accession Description Interval E-value
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
26-281 0e+00

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYC 105
Cdd:cd06612    1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 106 GAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVI 185
Cdd:cd06612   81 GAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 186 GTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKS 265
Cdd:cd06612  161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLVKD 240
                        250
                 ....*....|....*.
gi 281182886 266 PEQRATATQLLQHPFV 281
Cdd:cd06612  241 PEERPSAIQLLQHPFI 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
29-281 9.52e-150

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 430.86  E-value: 9.52e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  29 VFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES--DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESkeKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 107 AGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAkRNTVIG 186
Cdd:cd05122   81 GGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT-RNTFVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 187 TPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSP 266
Cdd:cd05122  160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQKDP 239
                        250
                 ....*....|....*
gi 281182886 267 EQRATATQLLQHPFV 281
Cdd:cd05122  240 EKRPTAEQLLKHPFI 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
28-294 1.81e-145

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 420.50  E-value: 1.81e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  28 EVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEY 104
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEaedEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 105 CGAGSVSDIIRLRnkTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTV 184
Cdd:cd06609   81 CGGGSVLDLLKPG--PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 185 IGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPElWSDNFTDFVKQCLVK 264
Cdd:cd06609  159 VGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNK-FSKPFKDFVELCLNK 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 281182886 265 SPEQRATATQLLQHPFVKSAKGVSILRDLI 294
Cdd:cd06609  238 DPKERPSAKELLKHKFIKKAKKTSYLTLLI 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
29-281 2.25e-138

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 402.07  E-value: 2.25e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  29 VFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE--SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEpgDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 107 AGSVSDIIrLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVIG 186
Cdd:cd06613   81 GGSLQDIY-QVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 187 TPFWMAPEVIQE---IGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIP--TNPPPTFRKPELWSDNFTDFVKQC 261
Cdd:cd06613  160 TPYWMAPEVAAVerkGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPksNFDPPKLKDKEKWSPDFHDFIKKC 239
                        250       260
                 ....*....|....*....|
gi 281182886 262 LVKSPEQRATATQLLQHPFV 281
Cdd:cd06613  240 LTKNPKKRPTATKLLQHPFV 259
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
29-282 1.03e-121

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 359.22  E-value: 1.03e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  29 VFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQE-IIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGA 107
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKElIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 108 GSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVIGT 187
Cdd:cd06614   81 GSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 188 PFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPE 267
Cdd:cd06614  161 PYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKDPE 240
                        250
                 ....*....|....*
gi 281182886 268 QRATATQLLQHPFVK 282
Cdd:cd06614  241 KRPSAEELLQHPFLK 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
24-281 1.39e-121

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 359.69  E-value: 1.39e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  24 KQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIK-EISIMQQ-CDSPHVVKYYGSYFKNTD---- 97
Cdd:cd06608    2 PDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKlEINILRKfSNHPNIATFYGAFIKKDPpggd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  98 --LWIVMEYCGAGSVSDII---RLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAG 172
Cdd:cd06608   82 dqLWLVMEYCGGGSVTDLVkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 173 QLTDTMAKRNTVIGTPFWMAPEVIQ-----EIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKP 247
Cdd:cd06608  162 QLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSP 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 281182886 248 ELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFV 281
Cdd:cd06608  242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
26-296 1.23e-111

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 334.40  E-value: 1.23e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES--DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVME 103
Cdd:cd06611    3 PNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESeeELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 104 YCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNT 183
Cdd:cd06611   83 FCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 184 VIGTPFWMAPEVI-----QEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFV 258
Cdd:cd06611  163 FIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKWSSSFNDFL 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 281182886 259 KQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINE 296
Cdd:cd06611  243 KSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLLAE 280
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
30-280 7.71e-103

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 311.21  E-value: 7.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  30 FDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVE---SDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCG 106
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEkcqTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 107 AGSVSDIIRLRNKT--LTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTM----AK 180
Cdd:cd06610   83 GGSLLDIMKSSYPRggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGdrtrKV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 181 RNTVIGTPFWMAPEVIQEI-GYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTF---RKPELWSDNFTD 256
Cdd:cd06610  163 RKTFVGTPCWMAPEVMEQVrGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLetgADYKKYSKSFRK 242
                        250       260
                 ....*....|....*....|....
gi 281182886 257 FVKQCLVKSPEQRATATQLLQHPF 280
Cdd:cd06610  243 MISLCLQKDPSKRPTAEELLKHKF 266
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
26-295 2.29e-101

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 307.75  E-value: 2.29e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06640    2 PEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06640   82 EYLGGGSALDL--LRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06640  160 TFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLTGE--FSKPFKEFIDACL 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 281182886 263 VKSPEQRATATQLLQHPF-VKSAKGVSILRDLIN 295
Cdd:cd06640  238 NKDPSFRPTAKELLKHKFiVKNAKKTSYLTELID 271
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
26-295 4.59e-101

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 306.98  E-value: 4.59e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06642    2 PEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06642   82 EYLGGGSALDL--LKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06642  160 TFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQ--HSKPFKEFVEACL 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 281182886 263 VKSPEQRATATQLLQHPFV-KSAKGVSILRDLIN 295
Cdd:cd06642  238 NKDPRFRPTAKELLKHKFItRYTKKTSFLTELID 271
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
26-295 5.40e-98

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 299.30  E-value: 5.40e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVES---DLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVM 102
Cdd:cd06641    2 PEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaedEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 103 EYCGAGSVSDIirLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRN 182
Cdd:cd06641   82 EYLGGGSALDL--LEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 183 TVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPelWSDNFTDFVKQCL 262
Cdd:cd06641  160 *FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGN--YSKPLKEFVEACL 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 281182886 263 VKSPEQRATATQLLQHPFV-KSAKGVSILRDLIN 295
Cdd:cd06641  238 NKEPSFRPTAKELLKHKFIlRNAKKTSYLTELID 271
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
26-281 7.09e-98

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 299.23  E-value: 7.09e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  26 PEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQV-PVESDLQEIIKEISIMQQ-CDSPHVVKYYGSYFK----NTD-L 98
Cdd:cd06638   16 PSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILdPIHDIDEEIEAEYNILKAlSDHPNVVKFYGMYYKkdvkNGDqL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886  99 WIVMEYCGAGSVSDIIR---LRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLT 175
Cdd:cd06638   96 WLVLELCNGGSVTDLVKgflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182886 176 DTMAKRNTVIGTPFWMAPEVI---QEI--GYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELW 250
Cdd:cd06638  176 STRLRRNTSVGTPFWMAPEVIaceQQLdsTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLHQPELW 255
                        250       260       270
                 ....*....|....*....|....*....|.
gi 281182886 251 SDNFTDFVKQCLVKSPEQRATATQLLQHPFV 281
Cdd:cd06638  256 SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
26-297 1.31e-95

Catalytic domain of the Serine/Threonine Kinas