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Conserved domains on  [gi|111225843|ref|YP_716637|]
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Serine/threonine protein kinase [Frankia alni ACN14a]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
10-252 2.13e-34

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 130.05  E-value: 2.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:cd00180    1 LGEGGFGTVYLARDkKTGKKVAIKIIKKED--SSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 YSSVAS-GGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP--KVIDFGIVAGLPGMMTASGVVMGSIG 165
Cdd:cd00180   79 KDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 166 YLAPELLTTTRRPRPACDIFSWGLTvcfaasgrppfgggpldalLYRtvhgeadlsgLPgPLRGVVAASLRKKPERRPDA 245
Cdd:cd00180  159 YMAPEVLLGKGYYSEKSDIWSLGVI-------------------LYE----------LP-ELKDLIRKMLQKDPEKRPSA 208

                 ....*..
gi 111225843 246 HRVLSQI 252
Cdd:cd00180  209 KEILEHL 215
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-249 5.94e-44

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 158.08  E-value: 5.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843     4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843    83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVm 161
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTTFV- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   162 GSIGYLAPELLtTTRRPRPACDIfsWGLTVCFA--ASGRPPFGGGPLDALLYRTVHGE-----ADLSGLPGPLRGVVAAS 234
Cdd:smart00220 158 GTPEYMAPEVL-LGKGYGKAVDI--WSLGVILYelLTGKPPFPGDDQLLELFKKIGKPkppfpPPEWDISPEAKDLIRKL 234
                          250
                   ....*....|....*
gi 111225843   235 LRKKPERRPDAHRVL 249
Cdd:smart00220 235 LVKDPEKRLTAEEAL 249
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
10-252 2.13e-34

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 130.05  E-value: 2.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:cd00180    1 LGEGGFGTVYLARDkKTGKKVAIKIIKKED--SSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 YSSVAS-GGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP--KVIDFGIVAGLPGMMTASGVVMGSIG 165
Cdd:cd00180   79 KDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 166 YLAPELLTTTRRPRPACDIFSWGLTvcfaasgrppfgggpldalLYRtvhgeadlsgLPgPLRGVVAASLRKKPERRPDA 245
Cdd:cd00180  159 YMAPEVLLGKGYYSEKSDIWSLGVI-------------------LYE----------LP-ELKDLIRKMLQKDPEKRPSA 208

                 ....*..
gi 111225843 246 HRVLSQI 252
Cdd:cd00180  209 KEILEHL 215
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
70-145 2.12e-09

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


Pssm-ID: 234331  Cd Length: 199  Bit Score: 56.46  E-value: 2.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111225843   70 DVDGDQPWIATEYVAGPTLYSSVASGGPlsgealwEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGPKVIDFG 145
Cdd:TIGR03724  66 DVDPDNKTIVMEYIEGKPLKDVIEEGND-------ELLREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKLYLIDFG 134
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
45-145 5.83e-09

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 54.98  E-value: 5.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  45 RHRFHREAAAVAA-----IDSPRVArllaaDVDGDQPWIATEYVAGPTLYSSVASGGPlsgealwEVARGLAEALCAIHD 119
Cdd:COG3642   43 RERTRREARILAKareagVPVPIVY-----DVDPDNGLIVMEYIEGELLKDALEEARP-------DLLREVGRLVGKLHK 110
                         90       100
                 ....*....|....*....|....*.
gi 111225843 120 ADVVHRDLKPGNVMLAADGPKVIDFG 145
Cdd:COG3642  111 AGIVHGDLTTSNIILSGGRIYFIDFG 136
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
7-145 6.95e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 54.91  E-value: 6.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   7 MGRLGSGGMGIVYLGvDDAGTRAAVKVMREE----HTADTAFRH-RFHREA-----AAVAAIDSPRVarlLAADVDGDQp 76
Cdd:PRK14879   1 MKLIKRGAEAEIYLG-DFLGIKAVIKWRIPKryrhPELDERIRReRTRREArimsrARKAGVNVPAV---YFVDPENFI- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111225843  77 wIATEYVAGPTLYSSVASGGPLSGEALWEVARglaeALCAIHDADVVHRDLKPGNVMLAADGPKVIDFG 145
Cdd:PRK14879  76 -IVMEYIEGEPLKDLINSNGMEELELSREIGR----LVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFG 139
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
95-200 9.01e-03

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: 36.22  E-value: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843    95 GGPLSGEALWEVARGLAEALcaihdaDVVHRDLKPGNVMLAADGpkvidfgiVAGLPGMMTASGVVMGSIG--YLAPELL 172
Cdd:smart00750  11 GRPLNEEEIWAVCLQCLGAL------RELHRQAKSGNILLTWDG--------LLKLDGSVAFKTPEQSRPDpyFMAPEVI 76
                           90       100
                   ....*....|....*....|....*...
gi 111225843   173 TTTRRPrPACDIFSWGLTVCFAASGRPP 200
Cdd:smart00750  77 QGQSYT-EKADIYSLGITLYEALDYELP 103
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-249 5.94e-44

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 158.08  E-value: 5.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843     4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843    83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVm 161
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTTFV- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   162 GSIGYLAPELLtTTRRPRPACDIfsWGLTVCFA--ASGRPPFGGGPLDALLYRTVHGE-----ADLSGLPGPLRGVVAAS 234
Cdd:smart00220 158 GTPEYMAPEVL-LGKGYGKAVDI--WSLGVILYelLTGKPPFPGDDQLLELFKKIGKPkppfpPPEWDISPEAKDLIRKL 234
                          250
                   ....*....|....*
gi 111225843   235 LRKKPERRPDAHRVL 249
Cdd:smart00220 235 LVKDPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
4-249 2.17e-40

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 148.16  E-value: 2.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843    4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFRHRFhREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHkGTGKIVAVKILKKRSEKSKKDQTAR-REIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADG-PKVIDFGIVAglpgMMTASGVVM 161
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGvVKIADFGLAK----KLTKSSSSL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  162 ----GSIGYLAPELLTTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLD---ALLYRTVHGEADLSGLPGP-----LRG 229
Cdd:pfam00069 156 ttfvGTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILdqlQLIRRILGPPLEFDEPKSDsgseeAKD 235
                         250       260
                  ....*....|....*....|
gi 111225843  230 VVAASLRKKPERRPDAHRVL 249
Cdd:pfam00069 236 LIKKCLNKDPSKRPTAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
4-251 2.35e-32

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: 128.32  E-value: 2.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDagTRAAVKVMREEHTADTAFRHRFHREAAAVAAIDSP-RVARLLAADVDGDQPWIATEY 82
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGG---PLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADG--PKVIDFGIVAGLPGMMTAS 157
Cdd:COG0515   80 VDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrvVKLIDFGLAKLLPDPGSTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 158 GV------VMGSIGYLAPELL--TTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVH--GEADLSGLPGP- 226
Cdd:COG0515  160 SIpalpstSVGTPGYMAPEVLlgLSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiiLELPTPSLASPl 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 111225843 227 -----------LRGVVAASLRKKPERRPDAHRVLSQ 251
Cdd:COG0515  240 spsnpeliskaASDLLKKLLAKDPKNRLSSSSDLSH 275
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
24-249 1.13e-24

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: 108.78  E-value: 1.13e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843    24 DAGTRAAVKVMREEHTADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIAT-EYVAGPTLYSSVASGGPLSGEA 102
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVfEYVPGRTLREVLAADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   103 LWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADG----PKVIDFGIVAGLPGM-------MTASGVVMGSIGYLAPEL 171
Cdd:TIGR03903   81 TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrphAKVLDFGIGTLLPGVrdadvatLTRTTEVLGTPTYCAPEQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   172 LtTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVhGEADLSgLPG-----PLRGVVAASLRKKPERRPDAH 246
Cdd:TIGR03903  161 L-RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL-SPVDVS-LPPwiaghPLGQVLRKALNKDPRQRAASA 237

                   ...
gi 111225843   247 RVL 249
Cdd:TIGR03903  238 PAL 240
pknD PRK13184
serine/threonine-protein kinase; Reviewed
1-189 3.43e-19

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 90.99  E-value: 3.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   1 MGPYRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMREEHTADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIA 79
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  80 TEYVAGPTLYSSVASggplsgeaLWE---VARGLAEA------------LCA----IHDADVVHRDLKPGNVMLAADGPK 140
Cdd:PRK13184  81 MPYIEGYTLKSLLKS--------VWQkesLSKELAEKtsvgaflsifhkICAtieyVHSKGVLHRDLKPDNILLGLFGEV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 111225843 141 VI-DFG--------------IVAGLPGM----MTASGVVMGSIGYLAPELLtttrRPRPA---CDIFSWGL 189
Cdd:PRK13184 153 VIlDWGaaifkkleeedlldIDVDERNIcyssMTIPGKIVGTPDYMAPERL----LGVPAsesTDIYALGV 219
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
9-249 5.46e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.39  E-value: 5.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   9 RLGSGGMGIVYLGVDDAGTRA-AVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPT 87
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLyALKVIYGNH--EDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  88 LyssvaSGGPLSGEA-LWEVARGLAEALCAIHDADVVHRDLKPGNVML-AADGPKVIDFGIVAGLPGMMTASGVVMGSIG 165
Cdd:PLN00034 159 L-----EGTHIADEQfLADVARQILSGIAYLHRRHIVHRDIKPSNLLInSAKNVKIADFGVSRILAQTMDPCNSSVGTIA 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 166 YLAPELLTTT----RRPRPACDIFSWGLTVCFAASGRPPFGGG------PLDALLYRTVHGEADLSGLPgPLRGVVAASL 235
Cdd:PLN00034 234 YMSPERINTDlnhgAYDGYAGDIWSLGVSILEFYLGRFPFGVGrqgdwaSLMCAICMSQPPEAPATASR-EFRHFISCCL 312
                        250
                 ....*....|....
gi 111225843 236 RKKPERRPDAHRVL 249
Cdd:PLN00034 313 QREPAKRWSAMQLL 326
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
10-201 1.66e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 64.84  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLG-VDDAGTRAAVKVMREEHTADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:PTZ00263  26 LGTGSFGRVRIAkHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 YSSVASGGPLSGEalweVARGL-AEALCA---IHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPgmmTASGVVMGS 163
Cdd:PTZ00263 106 FTHLRKAGRFPND----VAKFYhAELVLAfeyLHSKDIIYRDLKPENLLLDNKGHvKVTDFGFAKKVP---DRTFTLCGT 178
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 111225843 164 IGYLAPELLTTTRRPRpACDIFSWGLTVCFAASGRPPF 201
Cdd:PTZ00263 179 PEYLAPEVIQSKGHGK-AVDWWTMGVLLYEFIAGYPPF 215
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
88-202 5.61e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 51.00  E-value: 5.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  88 LYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGPKVI-DFGIVAGLpGMMTASGVVMGSIGY 166
Cdd:PHA03207 172 LFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLgDFGAACKL-DAHPDTPQCYGWSGT 250
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 111225843 167 L---APELLTTTrrprPAC---DIFSWGLtVCF--AASGRPPFG 202
Cdd:PHA03207 251 LetnSPELLALD----PYCaktDIWSAGL-VLFemSVKNVTLFG 289
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
10-252 2.13e-34

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 130.05  E-value: 2.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:cd00180    1 LGEGGFGTVYLARDkKTGKKVAIKIIKKED--SSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 YSSVAS-GGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP--KVIDFGIVAGLPGMMTASGVVMGSIG 165
Cdd:cd00180   79 KDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 166 YLAPELLTTTRRPRPACDIFSWGLTvcfaasgrppfgggpldalLYRtvhgeadlsgLPgPLRGVVAASLRKKPERRPDA 245
Cdd:cd00180  159 YMAPEVLLGKGYYSEKSDIWSLGVI-------------------LYE----------LP-ELKDLIRKMLQKDPEKRPSA 208

                 ....*..
gi 111225843 246 HRVLSQI 252
Cdd:cd00180  209 KEILEHL 215
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
4-251 7.21e-34

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: 129.63  E-value: 7.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMREEHTADtafRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd05122    2 FEILEKIGKGGFGEVYKARHKRtGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVAS-GGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGL-PGMMTASgv 159
Cdd:cd05122   79 CSGGSLKDLLKStNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEvKLIDFGLSAQLsDTKARNT-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 160 VMGSIGYLAPELLTTTRRpRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGeaDLSGLPGP------LRGVVAA 233
Cdd:cd05122  157 MVGTPYWMAPEVINGKPY-DYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATN--GPPGLRNPekwsdeFKDFLKK 233
                        250
                 ....*....|....*...
gi 111225843 234 SLRKKPERRPDAHRVLSQ 251
Cdd:cd05122  234 CLQKNPEKRPTAEQLLKH 251
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
10-245 1.85e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 103.02  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFRhRFHREAAAVAAIDSPRVARLLAADVD--GDQPWIATEYVAGP 86
Cdd:cd06606    8 LGRGSFGSVYLALDkDTGELMAVKSVELSGDSEEELE-ALEREIRILSSLQHPNIVRYYGSERDeeKNTLNIFLEYVSGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  87 TLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFG--IVAGLPGMMTASGVVMGS 163
Cdd:cd06606   87 SLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVvKLADFGcaKRLGDIETGEGTGSVRGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 164 IGYLAPELLTTTRRPRpACDIFSWGLTVCFAASGRPPFGG-GPLDALLYRTVHGE------ADLSglPGpLRGVVAASLR 236
Cdd:cd06606  167 PYWMAPEVIRGEEYGR-AADIWSLGCTVIEMATGKPPWSElGNPMAALYKIGSSGeppeipEHLS--EE-AKDFLRKCLR 242

                 ....*....
gi 111225843 237 KKPERRPDA 245
Cdd:cd06606  243 RDPKKRPTA 251
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
4-252 1.06e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 100.65  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKV-----MREEHTADTafrhrfHREAAAVAAIDSPRVARLLAADVDGDQPW 77
Cdd:cd08215    2 YEIIKQIGKGSFGKVYLVRRKSdGKLYVLKEidlsnMSEKEREDA------LNEVKILKKLNHPNIIKYYESFEEKGKLC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  78 IATEYVAGPTLY----SSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPG 152
Cdd:cd08215   76 IVMEYADGGDLSqkikKQKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLvKLGDFGISKVLSS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 153 MMTASGVVMGSIGYLAPELLttTRRP--RPAcDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGEAD--LSGLPGPLR 228
Cdd:cd08215  156 TVDLAKTVVGTPYYLSPELC--QNKPynYKS-DIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPpiPSQYSSELR 232
                        250       260
                 ....*....|....*....|....
gi 111225843 229 GVVAASLRKKPERRPDAHRVLSQI 252
Cdd:cd08215  233 NLVSSLLQKDPEERPSIAQILQSP 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
5-250 1.29e-23

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis. MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling, MKK2 is involved in cold and salt stress signaling, MKK4/MKK5 participates in innate immunity, and MKK7 regulates basal and systemic acquired resistance.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 100.36  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   5 RLMGRLGSGGMGIVYLGV-DDAGTRAAVKVMREEHtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYV 83
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRhKPTGKIYALKKIHVDG--DEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  84 AGPTLYSSVASGGPLSGEALWEVARGLAEALCAIH-DADVVHRDLKPGNVMLAADG-PKVIDFGIVAGLPGMM--TASGV 159
Cdd:cd06623   82 DGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGeVKIADFGISKVLENTLdqCNTFV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 160 vmGSIGYLAPELLtttrRPRP---ACDIFSWGLTVCFAASGRPPF---GGGPLDALLYRTVHGEADLsgLPG-----PLR 228
Cdd:cd06623  162 --GTVTYMSPERI----QGESysyAADIWSLGLTLLECALGKFPFlppGQPSFFELMQAICDGPPPS--LPAeefspEFR 233
                        250       260
                 ....*....|....*....|..
gi 111225843 229 GVVAASLRKKPERRPDAHRVLS 250
Cdd:cd06623  234 DFISACLQKDPKKRPSAAELLQ 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
4-249 2.57e-23

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: 99.74  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGV-DDAGTRAAVKVMREEhTADTAFRHrFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06610    3 YELIEVIGVGATAVVYAAIcLPNNEKVAIKRIDLE-KCQTSVDE-LRKEVQAMSQCNHPNVVKYYTSFVVGDELWLVMPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSG--EALWE-VARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGL--PGMMT- 155
Cdd:cd06610   81 LSGGSLLDIMKSSYPRGGldEAIIAtVLKEVLKGLEYLHSNGQIHRDIKAGNILLGEDGSvKIADFGVSASLadGGDRTr 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 156 -ASGVVMGSIGYLAPELLTTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHG-------EADLSGLPGPL 227
Cdd:cd06610  161 kVRKTFVGTPCWMAPEVMEQVHGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNdppsletGADYKKYSKSF 240
                        250       260
                 ....*....|....*....|..
gi 111225843 228 RGVVAASLRKKPERRPDAHRVL 249
Cdd:cd06610  241 RKMISLCLQKDPSKRPTAEELL 262
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
3-251 1.43e-22

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: 97.81  E-value: 1.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   3 PYRL---MGRLGSGGMGIVYLGVDDAGTRA-AVKVMREEHTADTAfrHRFHREAAAVAAIDSPRVARLLAADVDGDQPWI 78
Cdd:cd06642    2 PEELftkLERIGKGSFGEVYKGIDNRTKEVvAIKIIDLEEAEDEI--EDIQQEITVLSQCDSPYITRYYGSYLKGTKLWI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  79 ATEYVAGPTLYSsVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTAS 157
Cdd:cd06642   80 IMEYLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDvKLADFGVAGQLTDTQIKR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 158 GVVMGSIGYLAPELLTTTRRPRPAcDIFSWGLTVCFAASGRPPFGG-GPLDALLYRTVHGEADLSG-LPGPLRGVVAASL 235
Cdd:cd06642  159 NTFVGTPFWMAPEVIKQSAYDFKA-DIWSLGITAIELAKGEPPNSDlHPMRVLFLIPKNSPPTLEGqYSKPFKEFVEACL 237
                        250
                 ....*....|....*.
gi 111225843 236 RKKPERRPDAHRVLSQ 251
Cdd:cd06642  238 NKDPRFRPTAKELLKH 253
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
9-251 8.10e-22

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: 95.53  E-value: 8.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   9 RLGSGGMGIVYLGVDDAGTRA-AVKVMREEHTADTAfrHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPT 87
Cdd:cd06641   11 KIGKGSFGEVFKGIDNRTQKVvAIKIIDLEEAEDEI--EDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  88 LYSsVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVMGSIGY 166
Cdd:cd06641   89 ALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEvKLADFGVAGQLTDTQIKRNTFVGTPFW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 167 LAPELLTTTRRPRPAcDIFSWGLTVCFAASGRPPFGG-GPLDALLYRTVHGEADLSG-LPGPLRGVVAASLRKKPERRPD 244
Cdd:cd06641  168 MAPEVIKQSAYDSKA-DIWSLGITAIELAKGEPPHSElHPMKVLFLIPKNNPPTLEGnYSKPLKEFVEACLNKEPSFRPT 246

                 ....*..
gi 111225843 245 AHRVLSQ 251
Cdd:cd06641  247 AKELLKH 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
7-249 9.43e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 91.72  E-value: 9.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   7 MGRL-GSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFRH--RFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06632    4 KGELlGSGSFGSVYEGLNlDDGDFFAVKEVSLADDGQTGQEAvkQLEQEIALLSKLQHPNIVQYLGTEREEDNLYIFLEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVm 161
Cdd:cd06632   84 VPGGSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGANILVDTNGVvKLADFGMAKQVVEFSFAKSFK- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLTTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHgEADLSGLPGPL----RGVVAASLRK 237
Cdd:cd06632  163 GSPYWMAPEVIAQQGGYGLAADIWSLGCTVLEMATGKPPWSQLEGVAAVFKIGR-SKELPPIPDHLsdeaKDFILKCLQR 241
                        250
                 ....*....|..
gi 111225843 238 KPERRPDAHRVL 249
Cdd:cd06632  242 DPSLRPTAAELL 253
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
4-249 1.52e-20

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


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 91.35  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDAGTRA-AVKVMREEHTADtAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQFyALKEVDLGSMSQ-KEREDAVNEIRILASVNHPNIISYKEAFLDGNKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSV----ASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTAS 157
Cdd:cd08530   81 APFGDLSKAIskrkKKRKLIPEQEIWRIFIQLLRGLQALHEQKILHRDLKSANILLVANDLvKIGDLGISKVLKKNMAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 158 gvVMGSIGYLAPELLtttrRPRP---ACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGEADlsglPGP------LR 228
Cdd:cd08530  161 --QIGTPHYMAPEVW----KGRPysyKSDIWSLGCLLYEMATFAPPFEARSMQDLRYKVQRGKYP----PIPpiysqdLQ 230
                        250       260
                 ....*....|....*....|.
gi 111225843 229 GVVAASLRKKPERRPDAHRVL 249
Cdd:cd08530  231 NFIRSMLQVKPKLRPNCDKIL 251
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
4-251 4.44e-20

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 90.17  E-value: 4.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMREEHTADtafRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIAtGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEaLWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVM 161
Cdd:cd06656   98 LAGGSLTDVVTETCMDEGQ-IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSvKLTDFGFCAQITPEQSKRSTMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLtTTRRPRPACDIFSWGLTVCFAASGRPPF-GGGPLDALLYRTVHGEADLSG---LPGPLRGVVAASLRK 237
Cdd:cd06656  177 GTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGTPELQNperLSAVFRDFLNRCLEM 255
                        250
                 ....*....|....
gi 111225843 238 KPERRPDAHRVLSQ 251
Cdd:cd06656  256 DVDRRGSAKELLQH 269
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase-like Protein Serine ...
4-250 4.50e-20

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: 90.05  E-value: 4.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMREEHTADTAFrhrFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06613    5 YELIQRIGSGTYGDVYKARDIAtGELVAIKVIKLEPGDDFEI---IQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTL---YSsvASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASG 158
Cdd:cd06613   82 CGGGSLqdiYQ--VTRGPLSELQIAYVCRETLKGLAYLHETGKIHRDIKGANILLTEDGDvKLADFGVSAQLTATIAKRK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 159 VVMGSIGYLAPELLTTTRRPR--PACDIFSWGLTVCFAASGRPP-FGGGPLDALLYRTvhgeadLSGLPGP--------- 226
Cdd:cd06613  160 SFIGTPYWMAPEVAAVERKGGydGKCDIWALGITAIELAELQPPmFDLHPMRALFLIS------KSNFPPPklkdkekws 233
                        250       260
                 ....*....|....*....|....*.
gi 111225843 227 --LRGVVAASLRKKPERRPDAHRVLS 250
Cdd:cd06613  234 pvFHDFIKKCLTKDPKKRPTATKLLQ 259
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
10-201 4.93e-20

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK4 activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 89.70  E-value: 4.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFRhRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:cd06626    8 IGGGTFGKVYTAVNlDTGELMAVKEIRIQDNDPKTIK-EIADEMKVLELLKHPNLVKYYGVEVHREKVYIFMEYCSGGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 ySSVASGGPLSGEALWEV-ARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFG----IVAGLPGMMTASGVVMG 162
Cdd:cd06626   87 -EELLEHGRILDEHVIRVyTLQLLEGLAYLHSHGIVHRDIKPANIFLDHNGViKLGDFGcavkLKNNTTTMGEEVQSLAG 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 111225843 163 SIGYLAPELLTTTR---RPRpACDIFSWGLTVCFAASGRPPF 201
Cdd:cd06626  166 TPAYMAPEVITGGKgkgHGR-AADIWSLGCVVLEMATGKRPW 206
STKc_MAP4K3 cd06645
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-activated protein kinase ...
4-251 6.37e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 3 (MAPKKKK3 or MAP4K3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K3 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 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. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer.


Pssm-ID: 132976 [Multi-domain]  Cd Length: 267  Bit Score: 89.34  E-value: 6.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFrhrFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06645   11 FELIQRIGSGTYGDVYKARNvNTGELAAIKVIKLEPGEDFAV---VQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADG-PKVIDFGIVAGLPGMMTASGVVM 161
Cdd:cd06645   88 CGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGhVKLADFGVSAQITATIAKRKSFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLTTTRRP--RPACDIFSWGLTVCFAASGRPP-FGGGPLDALLYRTVHG-----EADLSGLPGPLRGVVAA 233
Cdd:cd06645  168 GTPYWMAPEVAAVERKGgyNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSNfqppkLKDKMKWSNSFHHFVKM 247
                        250
                 ....*....|....*...
gi 111225843 234 SLRKKPERRPDAHRVLSQ 251
Cdd:cd06645  248 ALTKNPKKRPTAEKLLQH 265
STKc_MAP4K5 cd06646
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-activated protein kinase ...
4-251 1.09e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase kinase 5 (MAPKKKK5 or MAP4K5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAP4K5 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 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. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity.


Pssm-ID: 132977 [Multi-domain]  Cd Length: 267  Bit Score: 88.94  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMREEHTADTAFrhrFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNlHTGELAAVKIIKLEPGDDFSL---IQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVM 161
Cdd:cd06646   88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDvKLADFGVAAKITATIAKRKSFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLTTTRRP--RPACDIFSWGLTVCFAASGRPP-FGGGPLDALLYRTVHG-----EADLSGLPGPLRGVVAA 233
Cdd:cd06646  168 GTPYWMAPEVAAVEKNGgyNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMSKSNfqppkLKDKTKWSSTFHNFVKI 247
                        250
                 ....*....|....*...
gi 111225843 234 SLRKKPERRPDAHRVLSQ 251
Cdd:cd06646  248 SLTKNPKKRPTAERLLTH 265
STKc_YSK4 cd06631
Catalytic domain of the Protein Serine/Threonine Kinase, Yeast Sps1/Ste20-related kinase 4; ...
10-249 3.95e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Yeast Sps1/Ste20-related kinase 4; Serine/threonine kinases (STKs), yeast Sps1/Ste20-related kinase 4 (YSK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The YSK4 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. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs (MKKKs or MAP3Ks) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.


Pssm-ID: 132962 [Multi-domain]  Cd Length: 265  Bit Score: 86.89  E-value: 3.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVDDAGTRAAVK-VMREEHTADTAFRH--RFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGP 86
Cdd:cd06631    8 LGKGAYGTVYCGLTNQGQLIAVKqVELDTSNVLAAEKEyeKLQEEVDLLKSLKHVNIVQYLGTCLDDNTISIFMEFVPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  87 TLYSSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLpGMMTASGV------ 159
Cdd:cd06631   88 SISSILNRFGPLPEPVFCKYTKQILDGVAYLHNNCVVHRDIKGNNVMLMPNGIiKLIDFGCARRL-AWVGLHGThsnmlk 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 160 -VMGSIGYLAPELLTTTRRPRPAcDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGEADLSGLPGPLRGV----VAAS 234
Cdd:cd06631  167 sMHGTPYWMAPEVINESGYGRKS-DIWSIGCTVFEMATGKPPLASMDRLAAMFYIGAHRGLMPRLPDSFSAAaidfVTSC 245
                        250
                 ....*....|....*
gi 111225843 235 LRKKPERRPDAHRVL 249
Cdd:cd06631  246 LTRDQHERPSALQLL 260
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
4-251 3.98e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group I, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others.


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 87.27  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMreeHTADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06647   21 YTRFEKIGQGASGTVYTAIDVAtGQEVAIKQM---NLQQQPKKELIINEILVMRENKHPNIVNYLDSYLVGDELWVVMEY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEaLWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVM 161
Cdd:cd06647   98 LAGGSLTDVVTETCMDEGQ-IAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSvKLTDFGFCAQITPEQSKRSTMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLtTTRRPRPACDIFSWGLTVCFAASGRPPF-GGGPLDALLYRTVHGEADLSG---LPGPLRGVVAASLRK 237
Cdd:cd06647  177 GTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGTPELQNpekLSAIFRDFLNRCLEM 255
                        250
                 ....*....|....
gi 111225843 238 KPERRPDAHRVLSQ 251
Cdd:cd06647  256 DVEKRGSAKELLQH 269
STKc_PAK1 cd06654
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine ...
4-251 5.10e-19

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


Pssm-ID: 132985 [Multi-domain]  Cd Length: 296  Bit Score: 87.09  E-value: 5.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDA-GTRAAVKVMREEHTADtafRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEY 82
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVAtGQEVAIRQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  83 VAGPTLYSSVASGGPLSGEaLWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTASGVVM 161
Cdd:cd06654   99 LAGGSLTDVVTETCMDEGQ-IAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSvKLTDFGFCAQITPEQSKRSTMV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 162 GSIGYLAPELLtTTRRPRPACDIFSWGLTVCFAASGRPPF-GGGPLDALLYRTVHGEADLSG---LPGPLRGVVAASLRK 237
Cdd:cd06654  178 GTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYLIATNGTPELQNpekLSAIFRDFLNRCLDM 256
                        250
                 ....*....|....
gi 111225843 238 KPERRPDAHRVLSQ 251
Cdd:cd06654  257 DVEKRGSAKELLQH 270
STKc_STK10_LOK cd06644
Catalytic domain of the Protein Serine/Threonine Kinase, STK10 or Lymphocyte-oriented kinase; ...
4-249 7.22e-19

Catalytic domain of the Protein Serine/Threonine Kinase, STK10 or Lymphocyte-oriented kinase; Serine/threonine kinases (STKs), STK10 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Other names for STK10 include lymphocyte-oriented kinase (LOK) and Xenopus polo-like kinase kinase 1 (xPlkk1). STK10 is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 86.62  E-value: 7.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVD-DAGTRAAVKVMR---EEHTADtafrhrFHREAAAVAAIDSPRVARLLAADVDGDQPWIA 79
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNkETGALAAAKVIEtksEEELED------YMVEIEILATCNHPYIVKLLGAFYWDGKLWIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  80 TEYVAGPTLYSSVAS-GGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGMMTAS 157
Cdd:cd06644   88 IEFCPGGAVDAIMLElDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDiKLADFGVSAKNVKTLQRR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 158 GVVMGSIGYLAPE-LLTTTRRPRP---ACDIFSWGLTVCFAASGRPPFGG-GPLDALLYRtvhGEADLSGLPGP------ 226
Cdd:cd06644  168 DSFIGTPYWMAPEvVMCETMKDTPydyKADIWSLGITLIEMAQIEPPHHElNPMRVLLKI---AKSEPPTLSQPskwsme 244
                        250       260
                 ....*....|....*....|...
gi 111225843 227 LRGVVAASLRKKPERRPDAHRVL 249
Cdd:cd06644  245 FRDFLKTALDKHPETRPSAAQLL 267
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
10-242 9.63e-19

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase (PI3K). Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 85.65  E-value: 9.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLgVDDAGTRA--AVKVMREEHTADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPT 87
Cdd:cd05123    1 LGKGSFGKVLL-VRKKDTGKlyAMKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYAPGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  88 LYSSVASGGPLSGEalwEVARGLAEALCAI---HDADVVHRDLKPGNVMLAADGP-KVIDFGIVA-GLPGMMTASGVVmG 162
Cdd:cd05123   80 LFSHLSKEGRFSEE---RARFYAAEIVLALeylHSLGIIYRDLKPENILLDADGHiKLTDFGLAKeLSSEGSRTNTFC-G 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 163 SIGYLAPELLttTRRPR-PACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGEADL-SGLPGPLRGVVAASLRKKPE 240
Cdd:cd05123  156 TPEYLAPEVL--LGKGYgKAVDWWSLGVLLYEMLTGKPPFYAEDRKEIYEKILKDPLRFpEFLSPEARDLISGLLQKDPT 233

                 ..
gi 111225843 241 RR 242
Cdd:cd05123  234 KR 235
STKc_ASK cd06624
Catalytic domain of the Protein Serine/Threonine Kinase, Apoptosis signal-regulating kinase; ...
10-249 1.74e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Apoptosis signal-regulating kinase; Serine/threonine kinases (STKs), Apoptosis signal-regulating kinase (ASK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ASK 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. Subfamily members are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) and include ASK1, ASK2, and MAPKKK15. 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. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species (ROS)-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown.


Pssm-ID: 173730 [Multi-domain]  Cd Length: 268  Bit Score: 85.27  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  10 LGSGGMGIVYLGVD-DAGTRAAVKVMREEhtaDTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATEYVAGPTL 88
Cdd:cd06624   16 LGKGTYGIVYAARDlSTQVRIAIKEIPER---DSRYVQPLHEEIALHSYLKHRNIVQYLGSDSENGFFKIFMEQVPGGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  89 YSSVASG-GPLSG--EALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP--KVIDFGIVAGLPGMMTASGVVMGS 163
Cdd:cd06624   93 SALLRSKwGPLKDneQTIIFYTKQILEGLKYLHDNQIVHRDIKGDNVLVNTYSGvvKISDFGTSKRLAGINPCTETFTGT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 164 IGYLAPELLTTTRRPR-PACDIFSWGLTVCFAASGRPPFG--GGPLDAL----LYRTvHGEADLSgLPGPLRGVVAASLR 236
Cdd:cd06624  173 LQYMAPEVIDKGPRGYgAPADIWSLGCTIVEMATGKPPFIelGEPQAAMfkvgMFKI-HPEIPES-LSAEAKNFILRCFE 250
                        250
                 ....*....|...
gi 111225843 237 KKPERRPDAHRVL 249
Cdd:cd06624  251 PDPDKRASAHDLL 263
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
3-249 3.02e-18

Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Nak1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nak1 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 Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also known as N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner.


Pssm-ID: 132991 [Multi-domain]  Cd Length: 277  Bit Score: 84.41  E-value: 3.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   3 PYRLMGRLGSGGMGIVYLGVDDAGTRA-AVKVMR----EEHTADtafrhrFHREAAAVAAI---DSPRVARLLAADVDGD 74
Cdd:cd06917    2 LYQRLELIGRGAYGAVYRGKHVPTGRVvALKIINldtpDDDVSD------IQREVALLSQLrqsQPPNITKYYGSYLKGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843  75 QPWIATEYVAGPTLySSVASGGPLSGEALWEVARGLAEALCAIHDADVVHRDLKPGNVMLAADGP-KVIDFGIVAGLPGM 153
Cdd:cd06917   76 RLWIIMEYAEGGSV-RTLMKAGPIAEKYISVIIREVLVALKYIHKVGVIHRDIKAANILVTNTGNvKLCDFGVAALLNQN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843 154 MTASGVVMGSIGYLAPELLTTTRRPRPACDIFSWGLTVCFAASGRPPFGGGPLDALLYRTVHGEA---DLSGLPGPLRGV 230
Cdd:cd06917  155 SSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITIYEMATGNPPYSDVDAFRAMMLIPKSKPprlEDNGYSKLLREF 234
                        250
                 ....*....|....*....
gi 111225843 231 VAASLRKKPERRPDAHRVL 249
Cdd:cd06917  235 VAACLDEEPKERLSAEELL 253
STKc_FA2-like cd08529
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and ...
4-251 3.38e-18

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


Pssm-ID: 173771 [Multi-domain]  Cd Length: 256  Bit Score: 84.10  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111225843   4 YRLMGRLGSGGMGIVYLGVDDAGTRaaVKVMREEH--TADTAFRHRFHREAAAVAAIDSPRVARLLAADVDGDQPWIATE 81
Cdd:cd08529    2 FEILNKIGKGSFGVVFKVVRKADKR--VYAMKQIDlsKMNRREREEAIDEARVLAKLDSSYIIRYYESFLDKGKLNIVME 79
                         90       100       110       120       130       140