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Conserved domains on  [gi|1346538|sp|P49137|]
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RecName: Full=MAP kinase-activated protein kinase 2; Short=MAPK-activated protein kinase 2; Short=MAPKAP kinase 2; Short=MAPKAP-K2; Short=MAPKAPK-2; Short=MK-2; Short=MK2 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
70-324 1.91e-57

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: 190.42  E-value: 1.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   70 LGLGINGKVLQIFNKRTQEKFALKML----------QDCPKARREVelhWRASQCPHIVRIV---DVYENLYagrkcllI 136
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLkkkkiikrkeVEHTLTERNI---LSRINHPFIVKLHyafQTEEKLY-------L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  137 VMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTS 216
Cdd:cd05123  71 VLEYAPGGELFSHLSKEG--RFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDAD---GHIKLTDFGLAKELSS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  217 HNSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLaispgMKTRIRMGQYEFPnpewSEV 294
Cdd:cd05123 146 EGSRTnTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYaEDRKE-----IYEKILKDPLRFP----EFL 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 1346538  295 SEEVKMLIRNLLKTEPTQRMT---ITEFMNHPW 324
Cdd:cd05123 217 SPEARDLISGLLQKDPTKRLGsggAEEIKAHPF 249
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-325 6.81e-94

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.81  E-value: 6.81e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538      68 QVLGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELHWRAsQCPHIVRIVDVYENlyagRKCLLIVMECL 141
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFED----EDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     142 DGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT 221
Cdd:smart00220  80 EGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPEWsEVSEEVKML 301
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 1346538     302 IRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
70-324 1.91e-57

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: 190.42  E-value: 1.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   70 LGLGINGKVLQIFNKRTQEKFALKML----------QDCPKARREVelhWRASQCPHIVRIV---DVYENLYagrkcllI 136
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLkkkkiikrkeVEHTLTERNI---LSRINHPFIVKLHyafQTEEKLY-------L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  137 VMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTS 216
Cdd:cd05123  71 VLEYAPGGELFSHLSKEG--RFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDAD---GHIKLTDFGLAKELSS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  217 HNSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLaispgMKTRIRMGQYEFPnpewSEV 294
Cdd:cd05123 146 EGSRTnTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYaEDRKE-----IYEKILKDPLRFP----EFL 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 1346538  295 SEEVKMLIRNLLKTEPTQRMT---ITEFMNHPW 324
Cdd:cd05123 217 SPEARDLISGLLQKDPTKRLGsggAEEIKAHPF 249
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
155-326 4.77e-06

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: 45.08  E-value: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     155 DQAFTEREASEIMKSIGEAIQYLHsiniahRDVKPENLLYTskrPNAILKLtdFGFAKETTSHNSLTTPcytpYYVAPEV 234
Cdd:smart00750  11 GRPLNEEEIWAVCLQCLGALRELH------RQAKSGNILLT---WDGLLKL--DGSVAFKTPEQSRPDP----YFMAPEV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     235 LGPEKYDKSCDMWSLGVIMYILLCGYPPFysNHGLAISPGMKTRI-RM---GQYEFPNPEWSEVSEEVKMLIRNLLKTEP 310
Cdd:smart00750  76 IQGQSYTEKADIYSLGITLYEALDYELPY--NEERELSAILEILLnGMpadDPRDRSNLEGVSAARSFEDFMRLCASRLP 153
                          170
                   ....*....|....*.
gi 1346538     311 TQRMTITEFMNHPWIM 326
Cdd:smart00750 154 QRREAANHYLAHCRAL 169
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
120-214 4.14e-05

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: 42.97  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    120 IVDVYENLYagrkclLIVMECLDGGELFSRIQDRGDqaftereasEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRP 199
Cdd:TIGR03724  64 VYDVDPDNK------TIVMEYIEGKPLKDVIEEGND---------ELLREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKL 128
                          90
                  ....*....|....*
gi 1346538    200 NAIlkltDFGFAKET 214
Cdd:TIGR03724 129 YLI----DFGLGKYS 139
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
117-212 4.56e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 42.97  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   117 IVRIVDVYEnlyagrkcLLIVMECLDGgELFSRIQDRGdqaftEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTS 196
Cdd:PRK14879  65 AVYFVDPEN--------FIIVMEYIEG-EPLKDLINSN-----GMEELELSREIGRLVGKLHSAGIIHGDLTTSNMILSG 130
                         90
                 ....*....|....*.
gi 1346538   197 KRpnaiLKLTDFGFAK 212
Cdd:PRK14879 131 GK----IYLIDFGLAE 142
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
119-212 1.85e-04

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 41.11  E-value: 1.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  119 RIVDVYENLYagrkclLIVMEcldggelfsRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKR 198
Cdd:COG3642  65 IVYDVDPDNG------LIVME---------YIEGELLKDALEEARPDLLREVGRLVGKLHKAGIVHGDLTTSNIILSGGR 129
                        90
                ....*....|....
gi 1346538  199 PNAIlkltDFGFAK 212
Cdd:COG3642 130 IYFI----DFGLGE 139
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
175-306 3.57e-04

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 258671  Cd Length: 289  Bit Score: 40.86  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    175 QYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFG-FAKETTSHNSLTTP-CYTPyyvaPEVLG--------PEKYDKSC 244
Cdd:pfam14531 160 AGLQHRGLVHGDFRPDNFFLDQKGG---VFLGGFTaLVRAGTKVVVSEVDvAFAP----PELFAsrgytgknTTTMTHKT 232
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346538    245 DMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRmgqyefpnpewsEVSEEVKMLIRNLL 306
Cdd:pfam14531 233 DAWQLGLVIYRIWCLRLPFTLDTPEGGSEWKFGRCV------------NMPEPVKALLAGFL 282
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
145-253 2.59e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 38.01  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   145 ELFSRIQdrgdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILkltDFGFAKETTSH------- 217
Cdd:PHA02882 115 EIFKRIK-----CKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYII---DYGIASHFIIHgkhieys 186
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 1346538   218 -NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIM 253
Cdd:PHA02882 187 kEQKDLHRGTLYYAGLDAHNGACVTRRGDLESLGYCM 223
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-325 6.81e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.81  E-value: 6.81e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538      68 QVLGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELHWRAsQCPHIVRIVDVYENlyagRKCLLIVMECL 141
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVFED----EDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     142 DGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT 221
Cdd:smart00220  80 EGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPEWsEVSEEVKML 301
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLE---LFKKIGKPKPPFPPPEW-DISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 1346538     302 IRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
65-325 1.52e-76

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 240.23  E-value: 1.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     65 VTSQVLGLGINGKVLQIFNKRTQEKFALKML-------QDCPKARREVELHwRASQCPHIVRIVDVYENlyagRKCLLIV 137
Cdd:pfam00069   2 ELLRKLGSGSFGTVYKAKHKGTGKIVAVKILkkrseksKKDQTARREIRIL-RRLSHPNIVRLIDAFED----KDHLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    138 MECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSH 217
Cdd:pfam00069  77 MEYCEGGDLFDYLSRGG--PLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDE---NGVVKIADFGLAKKLTKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    218 NS-LTTPCYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGYPPFYsNHGLAISPGMKTRIRMGQYEFPNPEWSEVS 295
Cdd:pfam00069 152 SSsLTTFVGTPEYMAPEVLlGGNGYGPKVDVWSLGVILYELLTGKPPFS-GESILDQLQLIRRILGPPLEFDEPKSDSGS 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 1346538    296 EEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:pfam00069 231 EEAKDLIKKCLNKDPSKRPTAEEILQHPWF 260
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
62-386 3.67e-42

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: 153.36  E-value: 3.67e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   62 DYKVTsQVLGLGINGKVLQIFNKRtqeKFALKML--------QDCPKARREVELHWRASQCPHIVRIVDVYENlyagRKC 133
Cdd:COG0515   1 SYRIL-RKLGEGSFGEVYLARDRK---LVALKVLakklesksKEVERFLREIQILASLNHPPNIVKLYDFFQD----EGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  134 LLIVMECLDGGELFSRIQDRGDQA-FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpNAILKLTDFGFAK 212
Cdd:COG0515  73 LYLVMEYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRD--GRVVKLIDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  213 ETTSHNS-------LTTPCYTPYYVAPEVLG---PEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMG 282
Cdd:COG0515 151 LLPDPGStssipalPSTSVGTPGYMAPEVLLglsLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILEL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  283 QYEFPNPEWS-----EVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ--STKVPQTPLHTSRVLKEDKERWEDVKEE 355
Cdd:COG0515 231 PTPSLASPLSpsnpeLISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHlkLKESDLSDLLKPDDSAPLRLSLPPSLEA 310
                       330       340       350
                ....*....|....*....|....*....|.
gi 1346538  356 MTSALATMRVDYEQIKIKKIEDASNPLLLKR 386
Cdd:COG0515 311 LISSLNSLAISGSDLKLDDSNFSKELAPNGV 341
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
70-324 2.69e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 138.41  E-value: 2.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    70 LGLGINGKVLQIFNKRTQEKFALKMLQdcpkaRREVelhWRASQCPHIVR------------IVDVYENLYAGRKcLLIV 137
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLK-----KREI---LKMKQVQHVAQeksilmelshpfIVNMMCSFQDENR-VYFL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   138 MECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 217
Cdd:PTZ00263  97 LEFVVGGELFTHLRKAG--RFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   218 NslTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaiSPgMKT--RIRMGQYEFPNpeWseVS 295
Cdd:PTZ00263 172 T--FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDD-----TP-FRIyeKILAGRLKFPN--W--FD 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 1346538   296 EEVKMLIRNLLKTEPTQRM-----TITEFMNHPW 324
Cdd:PTZ00263 240 GRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPY 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
115-325 1.10e-22

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 95.31  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   115 PHIVRIVDVYENLyagrKCLLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLY 194
Cdd:PHA03390  69 PNFIKLYYSVTTL----KGHVLIMDYIKDGDLFDLLKKEG--KLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   195 TSKRPNaiLKLTDFGFAKettshNSLTTPCY--TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAIS 272
Cdd:PHA03390 143 DRAKDR--IYLCDYGLCK-----IIGTPSCYdgTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELD 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1346538   273 PG-MKTRirmgqYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRM-TITEFMNHPWI 325
Cdd:PHA03390 216 LEsLLKR-----QQKKLPFIKNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFL 265
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
70-334 2.01e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 92.96  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538    70 LGLGINGKVLQIFNKRTQEKFALKML----------QDCpkarREVELhWRASQCPHIVRIVDVYEnlYAGRkcLLIVME 139
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIygnhedtvrrQIC----REIEI-LRDVNHPNVVKCHDMFD--HNGE--IQVLLE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   140 CLDGGELfsriqdRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFAKETtshNS 219
Cdd:PLN00034 153 FMDGGSL------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRIL---AQ 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   220 LTTPCY----TPYYVAPEVLGPE----KYDK-SCDMWSLGVIMYILLCGYPPF-YSNHGLAISpgMKTRIRMGQyefPNP 289
Cdd:PLN00034 221 TMDPCNssvgTIAYMSPERINTDlnhgAYDGyAGDIWSLGVSILEFYLGRFPFgVGRQGDWAS--LMCAICMSQ---PPE 295
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 1346538   290 EWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQT 334
Cdd:PLN00034 296 APATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQ 340
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
86-261 3.62e-12

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: 66.79  E-value: 3.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538      86 TQEKFALKMLQ-DCP-------KARREVELHWRASQcPHIVRIVDVYEnlyAGRKCLLIVMECLDGGELFSRIQDRGdqA 157
Cdd:TIGR03903    2 TGHEVAIKLLRtDAPeeehqraRFRRETALCARLYH-PNIVALLDSGE---APPGLLFAVFEYVPGRTLREVLAADG--A 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538     158 FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSK--RPNAilKLTDFGF------------AKETTSHNSLTTP 223
Cdd:TIGR03903   76 LPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTgvRPHA--KVLDFGIgtllpgvrdadvATLTRTTEVLGTP 153
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1346538     224 CYTpyyvAPEVLGPEKYDKSCDMWSLGVIMYILLCGYP 261
Cdd:TIGR03903  154 TYC----APEQLRGEPVTPNSDLYAWGLIFLECLTGQR 187
pknD PRK13184
serine/threonine-protein kinase; Reviewed
166-350 2.55e-09

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.86  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   166 IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIL-------------KLTDFGFAKETTSHNSLTTP---CYTPYY 229
Cdd:PRK13184 118 IFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILdwgaaifkkleeeDLLDIDVDERNICYSSMTIPgkiVGTPDY 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   230 VAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgMKTRIRMGQYEFPNPEWSEVSEEVKMlirNLLKTE 309
Cdd:PRK13184 198 MAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIS--YRDVILSPIEVAPYREIPPFLSQIAM---KALAVD 272
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1346538   310 PTQRM-TITEFMN--HPWIMQSTK-VPQTPLHTsrvlkEDKERWE 350
Cdd:PRK13184 273 PAERYsSVQELKQdlEPHLQGSPEwTVKATLMT-----KKKSCWK 312
 
Name Accession Description Interval E-value
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
70-324 1.91e-57

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: 190.42  E-value: 1.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   70 LGLGINGKVLQIFNKRTQEKFALKML----------QDCPKARREVelhWRASQCPHIVRIV---DVYENLYagrkcllI 136
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLkkkkiikrkeVEHTLTERNI---LSRINHPFIVKLHyafQTEEKLY-------L 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  137 VMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTS 216
Cdd:cd05123  71 VLEYAPGGELFSHLSKEG--RFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDAD---GHIKLTDFGLAKELSS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  217 HNSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLaispgMKTRIRMGQYEFPnpewSEV 294
Cdd:cd05123 146 EGSRTnTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYaEDRKE-----IYEKILKDPLRFP----EFL 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 1346538  295 SEEVKMLIRNLLKTEPTQRMT---ITEFMNHPW 324
Cdd:cd05123 217 SPEARDLISGLLQKDPTKRLGsggAEEIKAHPF 249
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
62-325 5.26e-53

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: 178.85  E-value: 5.26e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   62 DYKVTsQVLGLGINGKVLQIFNKRTQEKFALK------MLQDC-PKARREVELhWRASQCPHIVRIVDVYENlyagRKCL 134
Cdd:cd08215   1 KYEII-KQIGKGSFGKVYLVRRKSDGKLYVLKeidlsnMSEKErEDALNEVKI-LKKLNHPNIIKYYESFEE----KGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  135 LIVMECLDGGELFSRIQDRGDQA--FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAK 212
Cdd:cd08215  75 CIVMEYADGGDLSQKIKKQKKEGkpFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTS---NGLVKLGDFGISK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  213 ETTSH-NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkTRIRMGQYEfPNPew 291
Cdd:cd08215 152 VLSSTvDLAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELA----LKILKGQYP-PIP-- 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 1346538  292 SEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd08215 225 SQYSSELRNLVSSLLQKDPEERPSIAQILQSPFI 258
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
70-323 4.34e-52

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: 175.12  E-value: 4.34e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   70 LGLGINGKVLQIFNKRTQEKFALKML------QDCPKARREVELHwRASQCPHIVRIVDVYENlyagRKCLLIVMECLDG 143
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIkkedssSLLEELLREIEIL-KKLNHPNIVKLYGVFED----ENHLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  144 GELFSRIQDRGDQaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpNAILKLTDFGFAKETTSHNS-LTT 222
Cdd:cd00180  76 GSLKDLLKENEGK-LSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSD--NGKVKLADFGLSKLLTSDKSlLKT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  223 PCYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILlcgyppfysnhglaispgmktrirmgqyefpnpewsevsEEVKML 301
Cdd:cd00180 153 IVGTPAYMAPEVLlGKGYYSEKSDIWSLGVILYEL---------------------------------------PELKDL 193
                       250       260
                ....*....|....*....|..
gi 1346538  302 IRNLLKTEPTQRMTITEFMNHP 323
Cdd:cd00180 194 IRKMLQKDPEKRPSAKEILEHL 215
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
61-324 5.30e-51

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active C subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 174.66  E-value: 5.30e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   61 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKAR-REVElH-------WRASQCPHIVRIVDVYE---NLYa 129
Cdd:cd05580   1 DDFEFI-KTLGTGSFGRVMLVRHKGSGKYYALKILSKAKIVKlKQVE-HvlnekriLQSIRHPFLVNLYGSFQddsNLY- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  130 grkcllIVMECLDGGELFSRIqdRGDQAFTERE----ASEIMKsigeAIQYLHSINIAHRDVKPENLLYTSkrpNAILKL 205
Cdd:cd05580  78 ------LVMEYVPGGELFSHL--RKSGRFPEPVarfyAAQVVL----ALEYLHSLDIVYRDLKPENLLLDS---DGYIKI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  206 TDFGFAKETTSHNSltTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaiSPgMKT--RIRMGQ 283
Cdd:cd05580 143 TDFGFAKRVKGRTY--TLCGTPEYLAPEIILSKGYGKAVDWWALGILIYEMLAGYPPFFDD-----NP-IQIyeKILEGK 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 1346538  284 YEFPnpewSEVSEEVKMLIRNLLKTEPTQRM-----TITEFMNHPW 324
Cdd:cd05580 215 VRFP----SFFSPDAKDLIRNLLQVDLTKRLgnlknGVNDIKNHPW 256
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
68-325 2.06e-49

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: 169.28  E-value: 2.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   68 QVLGLGINGKVLQIFNKRTQEKFALK--MLQDCPKA-----RREVELHwRASQCPHIVRIVDVYENlyAGRKCLLIVMEC 140
Cdd:cd06606   6 ELLGRGSFGSVYLALDKDTGELMAVKsvELSGDSEEelealEREIRIL-SSLQHPNIVRYYGSERD--EEKNTLNIFLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  141 LDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAK---ETTSH 217
Cdd:cd06606  83 VSGGSLSSLLKKFG--KLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDS---DGVVKLADFGCAKrlgDIETG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  218 NSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKtrIRMGQYEFPNPEWseVSEE 297
Cdd:cd06606 158 EGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPW-SELGNPMAALYK--IGSSGEPPEIPEH--LSEE 232
                       250       260
                ....*....|....*....|....*...
gi 1346538  298 VKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd06606 233 AKDFLRKCLRRDPKKRPTADELLQHPFL 260
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
76-325 3.99e-49

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which also contains an insert relative to MAST kinases like MASTL. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 168.97  E-value: 3.99e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   76 GKVLQIFNKRTQEKFALK----------MLQDCPKARREVELHwraSQCPHIVRIvdvYENLyAGRKCLLIVMECLDGGE 145
Cdd:cd05579   7 GRVFLAKKKSTGDIYAIKvikkadmirkNQVDQVLTERDILSQ---AQSPYVVKL---YYSF-QGKKNLYLVMEYLPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  146 LFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAK-----ETTSHNSL 220
Cdd:cd05579  80 LASLLENVG--SLDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNILIDS---NGHLKLTDFGLSKvglvrRQINLNDD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  221 TTPCY----TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaiSPgMKT--RIRMGQYEFpnPEWSEV 294
Cdd:cd05579 155 EKEDKrivgTPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPPFHGE-----TP-EEIfqNILNGKIEW--PEDVEV 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 1346538  295 SEEVKMLIRNLLKTEPTQRM---TITEFMNHPWI 325
Cdd:cd05579 227 SDEAIDLISKLLVPDPEKRLgakSIEEIKNHPFF 260
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
69-324 1.15e-45

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: 159.29  E-value: 1.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   69 VLGLGINGKVLQIFNKRTQEKFALKMLQDCPKAR-----REVELHwraSQCPH--IVRIVDVYenLYAGRkcLLIVMECL 141
Cdd:cd05122   7 KIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKkekiiNEIQIL---KKCKHpnIVKYYGSY--LKKDE--LWIVMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  142 DGGELFSRIQDRGdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSHNSLT 221
Cdd:cd05122  80 SGGSLKDLLKSTN-QTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSD---GEVKLIDFGLSAQLSDTKARN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGvIMYI-LLCGYPPFYSNHGLAIspgMKTRIRMGQYEFPNPEWseVSEEVKM 300
Cdd:cd05122 156 TMVGTPYWMAPEVINGKPYDYKADIWSLG-ITAIeLAEGKPPYSELPPMKA---LFKIATNGPPGLRNPEK--WSDEFKD 229
                       250       260
                ....*....|....*....|....
gi 1346538  301 LIRNLLKTEPTQRMTITEFMNHPW 324
Cdd:cd05122 230 FLKKCLQKNPEKRPTAEQLLKHPF 253
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
70-324 5.15e-45

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 157.78  E-value: 5.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   70 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQ-------CPHIVRIVDVYENlyagRKCLLIVMECLD 142
Cdd:cd05572   1 LGVGGFGRVELVKVKSKNRTFALKCVKKRHIVETGQQEHIFSEKeileecnHPFIVKLYRTFKD----KKYIYMLMEYCL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  143 GGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLTT 222
Cdd:cd05572  77 GGELWTILRDRG--LFDEYTARFYIACVVLAFEYLHNRGIIYRDLKPENLLLDS---NGYVKLVDFGFAKKLKSGQKTWT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  223 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglAISPgMKT--RI--RMGQYEFPNpewsEVSEEV 298
Cdd:cd05572 152 FCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGED---DEDP-MEIynDIlkGNGKLEFPN----YIDKAA 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 1346538  299 KMLIRNLLKTEPTQRM-----TITEFMNHPW 324
Cdd:cd05572 224 KDLIKQLLRRNPEERLgnlkgGIKDIKKHKW 254
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
61-324 7.31e-40

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 144.26  E-value: 7.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   61 DDYKVtSQVLGLGINGKVLQIFNKRTQEKFALKMLQdcpKAR-----------REVELHWRASQCPHIVRIVDVY---EN 126
Cdd:cd05581   1 DDFKF-GKIIGEGSFSTVVLAKEKETNKEYAIKILD---KRQlikekkvkyvkIEKEVLTRLNGHPGIIKLYYTFqdeEN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  127 LYagrkcllIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLT 206
Cdd:cd05581  77 LY-------FVLEYAPNGELLQYIRKYG--SLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDK---DMHIKIT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  207 DFGFAK--ETTSHNSLTTPCY-------------------TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY- 264
Cdd:cd05581 145 DFGTAKvlDPNSSPESNKGDAtnidsqieknrrrfasfvgTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRg 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1346538  265 SNHGLAISpgmktRIRMGQYEFPNpewsEVSEEVKMLIRNLLKTEPTQRMTI----TEFMNHPW 324
Cdd:cd05581 225 SNEYLTFQ-----KILKLEYSFPP----NFPPDAKDLIEKLLVLDPQDRLGVnegyDELKAHPF 279
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
69-325 4.98e-39

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: 141.57  E-value: 4.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   69 VLGLGINGKVLQIFNKRTQEKFALKMLQ--DCPKARREV--ELH-WRASQCPHIVRIvdvYENLYAGRKcLLIVMECLDG 143
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKIHvdGDEEFRKQLlrELKtLRSCESPYVVKC---YGAFYKEGE-ISIVLEYMDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  144 GELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSI-NIAHRDVKPENLLYTSKrpNAIlKLTDFGFAK--ETTSHNSL 220
Cdd:cd06623  84 GSLADLLKKVG--KIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSK--GEV-KIADFGISKvlENTLDQCN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  221 TTpCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaISPGMKTRIRMGQY--EFPNPEWSE--VSE 296
Cdd:cd06623 159 TF-VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPF-------LPPGQPSFFELMQAicDGPPPSLPAeeFSP 230
                       250       260
                ....*....|....*....|....*....
gi 1346538  297 EVKMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd06623 231 EFRDFISACLQKDPKKRPSAAELLQHPFI 259
STKc_PKB cd05571
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine ...
68-324 1.07e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of PI3K and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis.


Pssm-ID: 173662 [Multi-domain]  Cd Length: 323  Bit Score: 142.26  E-value: 1.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   68 QVLGLGINGKVLQIFNKRTQEKFALKML-QDCPKARREVELHWRASQ----CPHIVRIVDVYENLYAGRKCLliVMECLD 142
Cdd:cd05571   1 KLLGKGTFGKVILVREKATGKYYAMKILkKEVIIAKDEVAHTLTESRvlqnTRHPFLTALKYSFQTHDRLCF--VMEYAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  143 GGELFSRIqdRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSH-NSLT 221
Cdd:cd05571  79 GGELFFHL--SRERVFSEDRARFYGAEIVSALGYLHSCDVVYRDLKLENLMLDK---DGHIKITDFGLCKEGISDgATMK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  222 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYS-NHGLaispgMKTRIRMGQYEFPnpewSEVSEEVKM 300
Cdd:cd05571 154 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNqDHEK-----LFELILMEEIRFP----RTLSPEAKS 224
                       250       260
                ....*....|....*....|....*....
gi 1346538  301 LIRNLLKTEPTQRM-----TITEFMNHPW 324
Cdd:cd05571 225 LLAGLLKKDPKQRLgggpeDAKEIMEHRF 253
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
68-325 1.63e-37

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


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 138.11  E-value: 1.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   68 QVLGLGINGKVLQIFNKRTQEKFALK-MLQDCPKARR---EVELhWRASQCPHIVRIVDVYenLYAGrkCLLIVMECLDG 143
Cdd:cd06614  25 EKIGEGASGEVYKATDRATGKEVAIKkMRLRKQNKELiinEILI-MKDCKHPNIVDYYDSY--LVGD--ELWVVMEYMDG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  144 GELfSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE-TTSHNSLTT 222
Cdd:cd06614 100 GSL-TDIITQNFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSK---DGSVKLADFGFAAQlTKEKSKRNS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538  223 PCYTPYYVAPEVLGPEKYDKSCDMWSLGvIMYILLC-GYPPFYSNhglaisPGMK--TRIRM-GQYEFPNPEwsEVSEEV 298
Cdd:cd06614 176 VVGTPYWMAPEVIKRKDYGPKVDIWSLG-IMCIEMAeGEPPYLRE------PPLRalFLITTkGIPPLKNPE--KWSPEF 246
                       250       260
                ....*....|....*....|....*..
gi 1346538  299 KMLIRNLLKTEPTQRMTITEFMNHPWI 325
Cdd:cd06614 247 KDFLNKCLVKDPEKRPSAEELLQHPFL 273
STKc_PKB_beta cd05595
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine ...
68-363 2.03e-37

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase B beta; Serine/Threonine Kinases (STKs), Protein Kinase B (PKB) or Akt subfamily, beta (or Akt2) isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKB 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. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 138.60  E-value: 2.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346538   68 QVLGLGINGKVLQIFNKRTQEKFALKMLqdcpkaRREVELhwRASQCPHIVRIVDVYENL-----------YAGRKCLLI 136
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKI