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Conserved domains on  [gi|226944428|ref|YP_002799501|]
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serine/threonine-kinase and phosphatase [Azotobacter vinelandii DJ]

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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 ...
267-511 6.19e-28

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: 111.17  E-value: 6.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 267 LAESRQSLVYRVRDSHERRWL-LKTLPPtrHSKAEAGQALLLEEWFLRRVASRYFPEI-APLPQRQHLYYVQREYPGKTL 344
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVaIKIIKK--EDSSSLLEELLREIEILKKLNHPNIVKLyGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 345 AEHLQAH-GPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGED-GELRLLDFGLAYCPGLSRDEPNSLPGTPS 422
Cdd:cd00180   79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDnGKVKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 423 HIAPEAFAGAAPDARQ-DLYAAGVTLYllltghypygEIEAFQhprfgtplpasryrpdlpawldECLQRALIADPEQRF 501
Cdd:cd00180  159 YMAPEVLLGKGYYSEKsDIWSLGVILY----------ELPELK----------------------DLIRKMLQKDPEKRP 206
                        250
                 ....*....|
gi 226944428 502 eTAEEWLLDL 511
Cdd:cd00180  207 -SAKEILEHL 215
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
6-227 2.64e-21

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


:

Pssm-ID: 238083  Cd Length: 254  Bit Score: 92.77  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   6 SIGEASAAGPRPENQDAirvVTPNPTLAASKGYLFALADGVSQCADGGLAARA-------SLQALAMDYYATPETW---A 75
Cdd:cd00143    2 SAGVSDKGGDRKTNEDA---VVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLlveelleELEETLTLSEEDIEEAlrkA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  76 VAQALDRLLLAQNRWLQANGGGqpllttltalvlRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQP----------- 144
Cdd:cd00143   79 FLRADEEILEEAQDEPDDARSGttav----valiRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEeereriekagg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 145 ---GMRH----VLKRALGlDQHLL------VDYRDGDLQEADAFLLV-SDGVWATLGDQGIRRILVDE---QDSSVASRA 207
Cdd:cd00143  155 rvsNGRVpgvlAVTRALG-DFDLKpgvsaePDVTVVKLTEDDDFLILaSDGLWDVLSNQEAVDIVRSElakEDLQEAAQE 233
                        250       260
                 ....*....|....*....|
gi 226944428 208 LVRAAHLAGSRDNASALLVR 227
Cdd:cd00143  234 LVDLALRRGSHDNITVVVVR 253
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
267-511 6.19e-28

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: 111.17  E-value: 6.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 267 LAESRQSLVYRVRDSHERRWL-LKTLPPtrHSKAEAGQALLLEEWFLRRVASRYFPEI-APLPQRQHLYYVQREYPGKTL 344
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVaIKIIKK--EDSSSLLEELLREIEILKKLNHPNIVKLyGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 345 AEHLQAH-GPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGED-GELRLLDFGLAYCPGLSRDEPNSLPGTPS 422
Cdd:cd00180   79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDnGKVKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 423 HIAPEAFAGAAPDARQ-DLYAAGVTLYllltghypygEIEAFQhprfgtplpasryrpdlpawldECLQRALIADPEQRF 501
Cdd:cd00180  159 YMAPEVLLGKGYYSEKsDIWSLGVILY----------ELPELK----------------------DLIRKMLQKDPEKRP 206
                        250
                 ....*....|
gi 226944428 502 eTAEEWLLDL 511
Cdd:cd00180  207 -SAKEILEHL 215
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
6-227 2.64e-21

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 92.77  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   6 SIGEASAAGPRPENQDAirvVTPNPTLAASKGYLFALADGVSQCADGGLAARA-------SLQALAMDYYATPETW---A 75
Cdd:cd00143    2 SAGVSDKGGDRKTNEDA---VVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLlveelleELEETLTLSEEDIEEAlrkA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  76 VAQALDRLLLAQNRWLQANGGGqpllttltalvlRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQP----------- 144
Cdd:cd00143   79 FLRADEEILEEAQDEPDDARSGttav----valiRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEeereriekagg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 145 ---GMRH----VLKRALGlDQHLL------VDYRDGDLQEADAFLLV-SDGVWATLGDQGIRRILVDE---QDSSVASRA 207
Cdd:cd00143  155 rvsNGRVpgvlAVTRALG-DFDLKpgvsaePDVTVVKLTEDDDFLILaSDGLWDVLSNQEAVDIVRSElakEDLQEAAQE 233
                        250       260
                 ....*....|....*....|
gi 226944428 208 LVRAAHLAGSRDNASALLVR 227
Cdd:cd00143  234 LVDLALRRGSHDNITVVVVR 253
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
1-237 1.00e-44

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 159.83  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   1 MTLQLSIGEASAAGP-RPENQDAIrvvTPNPTLAASKGYLFALADGVSQCADGGLAARASLQALAMDYYATPETWAVA-- 77
Cdd:COG0631    4 GILSLKVAGLSDVGTvRKHNEDAF---LIKPNENGNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNEsl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  78 -QALDRLLLAQNRWLQANGGGQPLLTTL----TALVLRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQ--------- 143
Cdd:COG0631   81 eELLKEAILKANEAIAEEGQLNEDVRGMgttlVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNrleqrgiit 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 144 PGM------RHVLKRALGLDQHLLVDYRDGDLQEADAFLLVSDGVWATLGDQGIRRILVDEQDSSVASRALVRAAHLAGS 217
Cdd:COG0631  161 PEEarshprRNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNSETPQEAADKLIELALEGGG 240
                        250       260
                 ....*....|....*....|
gi 226944428 218 RDNASALLVRAERLPEGSLA 237
Cdd:COG0631  241 PDNITVVLVRLNGEGETSRD 260
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
19-186 2.51e-16

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 257978  Cd Length: 210  Bit Score: 77.35  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   19 NQDAIRVVTpnptlaASKGYLFALADGVSQCADGGLAARASLQALAMDYYATPETWAVAQALDRLLLAQNRWLQ-----A 93
Cdd:pfam13672  12 CQDAFAYRV------LSDGWLIAVADGAGSAKYSDVGARLAVEAAVEALRELLDSGELPELEALVRQILNDILAlvrqeA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   94 NGGGQPLLTTL---TALVLRGRRFTLAHVGDCR-AYRWRDGQLQRLTEEHVWEQPGMRHVLKRAlglDQHLLVDYRDGDL 169
Cdd:pfam13672  86 AAQGLEPRDYAttlLLAVITPGGIVFFQIGDGAiVVRDRDGELQLLSEPDSGEYANETTFLTSP---DALEEFRIRRLTL 162
                         170
                  ....*....|....*..
gi 226944428  170 QEADAFLLVSDGVWATL 186
Cdd:pfam13672 163 EPGDALALMTDGLSDSL 179
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
3-226 5.40e-13

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625  Cd Length: 252  Bit Score: 67.79  E-value: 5.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428     3 LQLSIGEASAAGPRPENQDAIrVVTPNPTlaaSKGYLFALADGV--SQCADggLAARASLQALAM-DYYATPETWAVAQA 79
Cdd:smart00332   7 LGLRYGLSSMQGVRKPMEDAH-VITPDLS---DSGGFFGVFDGHggSEAAK--FLSKNLPEILAEeLIKEKDELEDVEEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428    80 LDRLLLAQN----RWLQANGGGqplltTLTALVLRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQPGMRHVLK---- 151
Cdd:smart00332  81 LRKAFLSTDeeilEELEALSGS-----TAVVALISGNKLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDERARIEaagg 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   152 --------------RALGlDQHL------LVDYRDGDLQEADAFL-LVSDGVWATLGDQGIRRILVD--EQDSSVASRAL 208
Cdd:smart00332 156 fvingrvngvlalsRAIG-DFFLkpyvsaEPDVTVVELTEKDDFLiLASDGLWDVLSNQEVVDIVRKhlSKDPKEAAKRL 234
                          250
                   ....*....|....*...
gi 226944428   209 VRAAHLAGSRDNASALLV 226
Cdd:smart00332 235 IDLALARGSKDNITVVVV 252
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
338-405 1.89e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 47.59  E-value: 1.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226944428 338 EY-PGKTLAEHLQAHGPLTLaqwlDLAPRLLRALGMLHRRNILHRDIKPENLLWgEDGELRLLDFGLAY 405
Cdd:PRK14879  79 EYiEGEPLKDLINSNGMEEL----ELSREIGRLVGKLHSAGIIHGDLTTSNMIL-SGGKIYLIDFGLAE 142
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
338-405 1.06e-04

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: 42.20  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226944428  338 EY-PGKTLAEHLQAHGpltlaqwLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGeLRLLDFGLAY 405
Cdd:TIGR03724  77 EYiEGKPLKDVIEEGN-------DELLREIGRLVGKLHKAGIVHGDLTTSNIIVRDDK-LYLIDFGLGK 137
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
341-461 2.47e-03

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: 38.55  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  341 GKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSrdepNSLPGT 420
Cdd:pfam14531 130 VKVLDSHSTFHKSLEHAARLLLTLQLIRLAAGLQHRGLVHGDFRPDNFFLDQKGGVFLGGFTALVRAGTK----VVVSEV 205
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 226944428  421 PSHIAPEAFAGAAPDARQ---------DLYAAGVTLYLLLTGHYPYGEIE 461
Cdd:pfam14531 206 DVAFAPPELFASRGYTGKntttmthktDAWQLGLVIYRIWCLRLPFTLDT 255
Pkinase pfam00069
Protein kinase domain;
329-506 2.59e-31

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 121.58  E-value: 2.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  329 RQHLYYVQrEY-PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCP 407
Cdd:pfam00069  70 KDHLYLVM-EYcEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  408 GLSRDEPNSLPGTPSHIAPEAFAGAAP-DARQDLYAAGVTLYLLLTGHYPY-GEIEAFQHPRF----GTPLPASryRPDL 481
Cdd:pfam00069 149 TKSSSSLTTFVGTPEYMAPEVLLGGNGyGPKVDVWSLGVILYELLTGKPPFsGESILDQLQLIrrilGPPLEFD--EPKS 226
                         170       180
                  ....*....|....*....|....*...
gi 226944428  482 PAWLDECLQ---RALIADPEQRFeTAEE 506
Cdd:pfam00069 227 DSGSEEAKDlikKCLNKDPSKRP-TAEE 253
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
260-536 4.63e-31

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: 123.31  E-value: 4.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 260 GWRVDGLLAESRQSLVYRVRDshERRWLLKTLPPTRHSKAEAGQALLLEEWFLRRVASRyfPEIAPL----PQRQHLYYV 335
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARD--RKLVALKVLAKKLESKSKEVERFLREIQILASLNHP--PNIVKLydffQDEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 336 QREYPGKTLAEHLQAHG---PLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDG-ELRLLDFGLA------Y 405
Cdd:COG0515   77 MEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGLAkllpdpG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 406 CPGLSRDEPNSLPGTPSHIAPEAFAG---AAPDARQDLYAAGVTLYLLLTGHYPY-------GEIEAFQHPR-FGTPLPA 474
Cdd:COG0515  157 STSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeknssATSQTLKIILeLPTPSLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226944428 475 SRYRPDLPA----WLDECLQRALIADPEQRFETAEEWLLDLERGERRPQELHPRPWLEREPLKVWR 536
Cdd:COG0515  237 SPLSPSNPEliskAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRL 302
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
329-506 2.07e-29

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 116.09  E-value: 2.07e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   329 RQHLYYVQrEY-PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCp 407
Cdd:smart00220  69 EDKLYLVM-EYcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ- 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   408 gLSRDEP-NSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYG----EIEAFQHPRFGTPLPasryRPDLP 482
Cdd:smart00220 147 -LDPGEKlTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPgddqLLELFKKIGKPKPPF----PPPEW 221
                          170       180
                   ....*....|....*....|....*..
gi 226944428   483 AWLDEC---LQRALIADPEQRFeTAEE 506
Cdd:smart00220 222 DISPEAkdlIRKLLVKDPEKRL-TAEE 247
pknD PRK13184
serine/threonine-protein kinase; Reviewed
374-532 3.37e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 96.76  E-value: 3.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 374 HRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDE------------------PNSLPGTPSHIAPEAFAGAAPD 435
Cdd:PRK13184 130 HSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEEDlldidvdernicyssmtiPGKIVGTPDYMAPERLLGVPAS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 436 ARQDLYAAGVTLYLLLTGHYPY----GEIEAFQHpRFGTPLPASRYRpDLPAWLDECLQRALIADPEQRFETAEEWLLDL 511
Cdd:PRK13184 210 ESTDIYALGVILYQMLTLSFPYrrkkGRKISYRD-VILSPIEVAPYR-EIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
                        170       180
                 ....*....|....*....|..
gi 226944428 512 ErgerrpQELHPRP-WLEREPL 532
Cdd:PRK13184 288 E------PHLQGSPeWTVKATL 303
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
342-505 1.10e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.97  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 342 KTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLA--YCPGLSRDEPNSLPG 419
Cdd:PTZ00267 154 KQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSkqYSDSVSLDVASSFCG 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 420 TPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQHPRFGT----PLPASryrPDLPAWLDECLQRa 492
Cdd:PTZ00267 234 TPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFkgpSQREIMQQVLYGKydpfPCPVS---SGMKALLDPLLSK- 309
                        170
                 ....*....|...
gi 226944428 493 liaDPEQRFETAE 505
Cdd:PTZ00267 310 ---NPALRPTTQQ 319
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
332-505 1.15e-13

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: 72.95  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   332 LYYVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELR---LLDFGL-AYCP 407
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPhakVLDFGIgTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   408 GLSRDEPNSLP------GTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY-GEIEAFQHPRFGTPLPASryrpd 480
Cdd:TIGR03903  134 GVRDADVATLTrttevlGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVqGASVAEILYQQLSPVDVS----- 208
                          170       180       190
                   ....*....|....*....|....*....|
gi 226944428   481 LPAW-----LDECLQRALIADPEQRFETAE 505
Cdd:TIGR03903  209 LPPWiaghpLGQVLRKALNKDPRQRAASAP 238
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
340-457 8.20e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 67.57  E-value: 8.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 340 PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLW-GEDGELRLLDFGLAYCPGLsrdePNSLP 418
Cdd:PHA03390  92 KDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYdRAKDRIYLCDYGLCKIIGT----PSCYD 167
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 226944428 419 GTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY 457
Cdd:PHA03390 168 GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF 206
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
361-458 1.93e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 61.38  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 361 DLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPGTPSHIAPEAFAGAAPDARQDL 440
Cdd:PLN00034 172 DVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLNHGAYDG 251
                         90       100
                 ....*....|....*....|...
gi 226944428 441 YAA-----GVTLYLLLTGHYPYG 458
Cdd:PLN00034 252 YAGdiwslGVSILEFYLGRFPFG 274
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
267-511 6.19e-28

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: 111.17  E-value: 6.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 267 LAESRQSLVYRVRDSHERRWL-LKTLPPtrHSKAEAGQALLLEEWFLRRVASRYFPEI-APLPQRQHLYYVQREYPGKTL 344
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVaIKIIKK--EDSSSLLEELLREIEILKKLNHPNIVKLyGVFEDENHLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 345 AEHLQAH-GPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGED-GELRLLDFGLAYCPGLSRDEPNSLPGTPS 422
Cdd:cd00180   79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDnGKVKLADFGLSKLLTSDKSLLKTIVGTPA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 423 HIAPEAFAGAAPDARQ-DLYAAGVTLYllltghypygEIEAFQhprfgtplpasryrpdlpawldECLQRALIADPEQRF 501
Cdd:cd00180  159 YMAPEVLLGKGYYSEKsDIWSLGVILY----------ELPELK----------------------DLIRKMLQKDPEKRP 206
                        250
                 ....*....|
gi 226944428 502 eTAEEWLLDL 511
Cdd:cd00180  207 -SAKEILEHL 215
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
6-227 2.64e-21

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 92.77  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   6 SIGEASAAGPRPENQDAirvVTPNPTLAASKGYLFALADGVSQCADGGLAARA-------SLQALAMDYYATPETW---A 75
Cdd:cd00143    2 SAGVSDKGGDRKTNEDA---VVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLlveelleELEETLTLSEEDIEEAlrkA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  76 VAQALDRLLLAQNRWLQANGGGqpllttltalvlRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQP----------- 144
Cdd:cd00143   79 FLRADEEILEEAQDEPDDARSGttav----valiRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEeereriekagg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 145 ---GMRH----VLKRALGlDQHLL------VDYRDGDLQEADAFLLV-SDGVWATLGDQGIRRILVDE---QDSSVASRA 207
Cdd:cd00143  155 rvsNGRVpgvlAVTRALG-DFDLKpgvsaePDVTVVKLTEDDDFLILaSDGLWDVLSNQEAVDIVRSElakEDLQEAAQE 233
                        250       260
                 ....*....|....*....|
gi 226944428 208 LVRAAHLAGSRDNASALLVR 227
Cdd:cd00143  234 LVDLALRRGSHDNITVVVVR 253
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
1-237 1.00e-44

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 159.83  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428   1 MTLQLSIGEASAAGP-RPENQDAIrvvTPNPTLAASKGYLFALADGVSQCADGGLAARASLQALAMDYYATPETWAVA-- 77
Cdd:COG0631    4 GILSLKVAGLSDVGTvRKHNEDAF---LIKPNENGNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNEsl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428  78 -QALDRLLLAQNRWLQANGGGQPLLTTL----TALVLRGRRFTLAHVGDCRAYRWRDGQLQRLTEEHVWEQ--------- 143
Cdd:COG0631   81 eELLKEAILKANEAIAEEGQLNEDVRGMgttlVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNrleqrgiit 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 144 PGM------RHVLKRALGLDQHLLVDYRDGDLQEADAFLLVSDGVWATLGDQGIRRILVDEQDSSVASRALVRAAHLAGS 217
Cdd:COG0631  161 PEEarshprRNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNSETPQEAADKLIELALEGGG 240
                        250       260
                 ....*....|....*....|
gi 226944428 218 RDNASALLVRAERLPEGSLA 237
Cdd:COG0631  241 PDNITVVLVRLNGEGETSRD 260
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
330-509 1.18e-22

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: 96.86  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 330 QHLYYVQREY-PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLA---- 404
Cdd:cd06606   73 KNTLNIFLEYvSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAkrlg 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 405 --YCPGLSRdepnSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYGEieafqhprFGTPLPA------SR 476
Cdd:cd06606  153 diETGEGTG----SVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSE--------LGNPMAAlykigsSG 220
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226944428 477 YRPDLPAWL-DEC---LQRALIADPEQRFeTAEEwLL 509
Cdd:cd06606  221 EPPEIPEHLsEEAkdfLRKCLRRDPKKRP-TADE-LL 255
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
331-457 4.90e-22

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: 94.89  E-value: 4.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 331 HLYYVQREYPGKTLAEHLQAHGPLT--LAQWLdlAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAyCPG 408
Cdd:cd05123   67 KLYLVLEYAPGGELFSHLSKEGRFSeeRARFY--AAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLA-KEL 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226944428 409 LSRDE-PNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY 457
Cdd:cd05123  144 SSEGSrTNTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF 193
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
318-457 6.46e-22

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, 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. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 94.86  E-value: 6.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 318 RYFPEIAPL----PQRQHLYYVQREYPGKTLAEHLQAHGPLTLaQWL-DLAPRLLRALGMLHRRNILHRDIKPENLLWGE 392
Cdd:cd05611   54 GESPYVAKLyysfQSKDYLYLVMEYLNGGDCASLIKTLGGLPE-DWAkQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQ 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226944428 393 DGELRLLDFGLAYCPGLSRDepnsLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY 457
Cdd:cd05611  133 TGHLKLTDFGLSRNGLENKK----FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPF 193
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
329-511 2.20e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs), Yank1 or STK32A subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily contains uncharacterized STKs with similarity to the human protein designated Yank1 or STK32A.


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 90.45  E-value: 2.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 329 RQHLYYVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAycPG 408
Cdd:cd05578   72 EENMYLVVDLLLGGDLRYHLSQKVKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILLDEQGHVHITDFNIA--TK 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 409 LSRDEP-NSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY--------GEIEAFQHprfgtplPASRYRP 479
Cdd:cd05578  150 VTPDTLtTSTSGTPGYMAPEVLCRQGYSVAVDWWSLGVTAYECLRGKRPYrghsrtirDQIRAKQE-------TADVLYP 222
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226944428 480 dlPAWLDEC---LQRALIADPEQRFETAEEWLLDL 511
Cdd:cd05578  223 --ATWSTEAidaINKLLERDPQKRLGDNLKDLKNH 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
338-508 6.44e-20

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: 88.80  E-value: 6.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 338 EY-PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHR-RNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPN 415
Cdd:cd06623   79 EYmDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 416 SLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY------GEIEAFQHPRFGTP--LPASRYRPDLPAWLDE 487
Cdd:cd06623  159 TFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFlppgqpSFFELMQAICDGPPpsLPAEEFSPEFRDFISA 238
                        170       180
                 ....*....|....*....|.
gi 226944428 488 CLQRaliaDPEQRfETAEEWL 508
Cdd:cd06623  239 CLQK----DPKKR-PSAAELL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
366-508 1.26e-19

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: 88.03  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 366 LLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEpNSLPGTPSHIAPEAFAGAAPDARQDLYAAGV 445
Cdd:cd05122  107 LLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDTKAR-NTMVGTPYWMAPEVINGKPYDYKADIWSLGI 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226944428 446 TLYLLLTGHYPYGEIEAF---------QHPRFGTPlpaSRYRPDLPAWLDECLQRaliaDPEQRfETAEEWL 508
Cdd:cd05122  186 TAIELAEGKPPYSELPPMkalfkiatnGPPGLRNP---EKWSDEFKDFLKKCLQK----NPEKR-PTAEQLL 249
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
329-511 2.50e-19

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: 87.17  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 329 RQHLYYVQrEY-PGKTLAEHLQ----AHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGL 403
Cdd:cd08215   71 KGKLCIVM-EYaDGGDLSQKIKkqkkEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGI 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 404 AYCpgLSRDEP--NSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYP-YGE--------IEAFQHPrfgtPL 472
Cdd:cd08215  150 SKV--LSSTVDlaKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPfEGEnllelalkILKGQYP----PI 223
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226944428 473 PaSRYRPDLPAWLDECLQRaliaDPEQRFETAEewLLDL 511
Cdd:cd08215  224 P-SQYSSELRNLVSSLLQK----DPEERPSIAQ--ILQS 255
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine ...
277-457 3.99e-19

Catalytic domain of Yeast Protein Kinase 1-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Yeast protein kinase 1 (YPK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development.


Pssm-ID: 173676 [Multi-domain]  Cd Length: 312  Bit Score: 87.30  E-value: 3.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 277 RVRDShERRWLLKTLPPTR-HSKAEAGQALLlEEWFLRRVASryfPEIAPLP----QRQHLYYVQREYPGKTLAEHLQAH 351
Cdd:cd05585   13 RKRDT-QRIYALKTIRKAHiVSRSEVTHTLA-ERTVLAQVNC---PFIVPLKfsfqSPEKLYLVLAFINGGELFHHLQRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 352 GPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPGTPSHIAPEAFAG 431
Cdd:cd05585   88 GRFDLSRARFYTAELLCALENLHKFNVIYRDLKPENILLDYQGHIALCDFGLCKLNMKDDDKTNTFCGTPEYLAPELLLG 167
                        170       180
                 ....*....|....*....|....*.
gi 226944428 432 AAPDARQDLYAAGVTLYLLLTGHYPY 457
Cdd:cd05585  168 HGYTKAVDWWTLGVLLYEMLTGLPPF 193
STKc_nPKC_theta_delta cd05592
Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and ...
329-500 4.96e-19

Catalytic domain of the Protein Serine/Threonine Kinases, Novel Protein Kinase C theta and delta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), theta and delta-like isoforms, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC 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. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types.


Pssm-ID: 173683 [Multi-domain]  Cd Length: 316  Bit Score: 86.77  E-value: 4.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 329 RQHLYYVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPG 408
Cdd:cd05592   68 KEHLFFVMEYLNGGDLMFHIQSSGRFDEARARFYAAEIICGLQFLHKKGIIYRDLKLDNVLLDKDGHIKIADFGMCKENM 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 409 LSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQHPRFGTPLpasryrpdLPAWL 485
Cdd:cd05592  148 NGEGKASTFCGTPDYIAPEILKGQKYNESVDWWSFGVLLYEMLIGQSPFhgeDEDELFDSILNDRPH--------FPRWI 219
                        170
                 ....*....|....*....
gi 226944428 486 D----ECLQRALIADPEQR 500
Cdd:cd05592  220 SkeakDCLSKLFERDPTKR 238
STKc_GRK cd05577
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; ...
289-523 8.05e-19

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK 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. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7. They are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems.


Pssm-ID: 173668 [Multi-domain]  Cd Length: 277  Bit Score: 85.63  E-value: 8.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 289 KTLPPTRHSKAEAGQALLLEEWFLRRVASRYFPEIA-PLPQRQHLYYVQREYPGKTLAEHLQAHGP--LTLAQWLDLAPR 365
Cdd:cd05577   24 KKLDKKRLKKRKGEQMALNEKKILEKVSSRFIVSLAyAFETKDDLCLVMTLMNGGDLKYHIYNVGEpgFPEARAIFYAAQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 366 LLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAyCPGLSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGV 445
Cdd:cd05577  104 IICGLEHLHQRRIVYRDLKPENVLLDDHGNVRISDLGLA-VELKGGKKIKGRAGTPGYMAPEVLQGEVYDFSVDWFALGC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 446 TLYLLLTGHYPYG------EIEAFQHPRFGTPLPAS-RYRPDLPAWLDECLQRaliaDPEQRfetaeewLLDLERGERRP 518
Cdd:cd05577  183 TLYEMIAGRSPFRqrkekvEKEELKRRTLEMAVEYPdKFSPEAKDLCEALLQK----DPEKR-------LGCRGGSADEV 251

                 ....*
gi 226944428 519 QElHP 523
Cdd:cd05577  252 RE-HP 255
STKc_nPKC_theta cd05619
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C theta; Serine ...
329-501 1.57e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C theta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), theta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC 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. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases.


Pssm-ID: 173709 [Multi-domain]  Cd Length: 316  Bit Score: 85.41  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 329 RQHLYYVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPG 408
Cdd:cd05619   68 KENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDTDGHIKIADFGMCKENM 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 409 LSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQHPRFGTPLpasryrpdLPAWL 485
Cdd:cd05619  148 LGDAKTCTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFhghDEEELFQSIRMDNPC--------YPRWL 219
                        170       180
                 ....*....|....*....|
gi 226944428 486 D----ECLQRALIADPEQRF 501
Cdd:cd05619  220 TreakDILVKLFVREPERRL 239
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
367-508 2.47e-18

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 84.22  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 367 LRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVT 446
Cdd:cd06627  109 LQGLAYLHEQGVIHRDIKAANILTTKDGVVKLADFGVATKLNDVSKDDASVVGTPYWMAPEVIEMSGASTASDIWSLGCT 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226944428 447 LYLLLTGHYPYGEIEAF---------QHPrfgtPLPaSRYRPDLPAWLDECLQRaliaDPEQRfETAEEWL 508
Cdd:cd06627  189 VIELLTGNPPYYDLNPMaalfrivqdDHP----PLP-EGISPELKDFLMQCFQK----DPNLR-PTAKQLL 249
STKc_ROCK_NDR_like cd05573
Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine ...
330-506 2.73e-18

Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) and Nuclear Dbf2-Related (NDR)-like kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK- and NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis.


Pssm-ID: 173664 [Multi-domain]  Cd Length: 350  Bit Score: 85.04  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 330 QHLYYVQREYPGKTLAEHLQAHGPLT--LAQWLdlAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLA--- 404
Cdd:cd05573   74 EHLYLVMEYMPGGDLMNLLIRKDVFPeeTARFY--IAELVLALDSVHKLGFIHRDIKPDNILIDADGHIKLADFGLCkkm 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 405 ------------------YCPGLSRDEP--------NSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYP-- 456
Cdd:cd05573  152 nkakdreyylndshnllfRDNVLVRRRDhkqrrvraNSTVGTPDYIAPEVLRGTPYGLECDWWSLGVILYEMLYGFPPfy 231
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226944428 457 -------YGEIEAFQHprfgtplpaSRYRPDLPAWLDEC--LQRALIADPEQRFETAEE 506
Cdd:cd05573  232 sdtlqetYNKIINWKE---------SLRFPPDPPVSPEAidLICRLLCDPEDRLGSFEE 281
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
332-501 3.92e-18

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: 83.78  E-value: 3.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 332 LYYVQrEY-PGKTLAEHLQAHGPL--TLAQWLdlAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLA--YC 406
Cdd:cd05581   77 LYFVL-EYaPNGELLQYIRKYGSLdeKCTRFY--AAEILLALEYLHSKGIIHRDLKPENILLDKDMHIKITDFGTAkvLD 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 407 PGLS------------------RDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQH 465
Cdd:cd05581  154 PNSSpesnkgdatnidsqieknRRRFASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFrgsNEYLTFQK 233
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226944428 466 --PRfgtplpASRYRPDLPAWLDECLQRALIADPEQRF 501
Cdd:cd05581  234 ilKL------EYSFPPNFPPDAKDLIEKLLVLDPQDRL 265
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
366-508 5.67e-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: 83.26  E-value: 5.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 366 LLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPGTPSHIAPEAFA-GAAPDARQDLYAAG 444
Cdd:cd06917  110 VLVALKYIHKVGVIHRDIKAANILVTNTGNVKLCDFGVAALLNQNSSKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLG 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226944428 445 VTLYLLLTGHYPYGEIEAFQH----PRFGTP-LPASRYRPDLPAWLDECLQraliADPEQRFeTAEEWL 508
Cdd:cd06917  190 ITIYEMATGNPPYSDVDAFRAmmliPKSKPPrLEDNGYSKLLREFVAACLD----EEPKERL-SAEELL 253
STKc_MST3 cd06641
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; ...
334-508 8.49e-18

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: 82.82  E-value: 8.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 334 YVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDE 413
Cdd:cd06641   78 WIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIK 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 414 PNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYGEIEA----FQHPRFGTPLPASRYRPDLPAWLDECL 489
Cdd:cd06641  158 RNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPmkvlFLIPKNNPPTLEGNYSKPLKEFVEACL 237
                        170
                 ....*....|....*....
gi 226944428 490 QRaliaDPEQRfETAEEWL 508
Cdd:cd06641  238 NK----EPSFR-PTAKELL 251
STKc_FA2-like cd08529
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii FA2 and ...
267-504 1.23e-17

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: 81.79  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 267 LAESRQSLVYR-VRDSHERRWLLKTLPPTRHSKAEAGQALLlEEWFLRRVAS----RYFPEIAplpQRQHLYYVQREYPG 341
Cdd:cd08529    8 IGKGSFGVVFKvVRKADKRVYAMKQIDLSKMNRREREEAID-EARVLAKLDSsyiiRYYESFL---DKGKLNIVMEYAEN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 342 KTLAE--HLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPG 419
Cdd:cd08529   84 GDLHKllKMQRGRPLPEDQVWRFFIQILLGLAHLHSKKILHRDIKSLNLFLDAYDNVKIGDLGVAKLLSDNTNFANTIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 420 TPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY------GEIEAFQHPRFgTPLPAsRYRPDLPAWLDECLQRal 493
Cdd:cd08529  164 TPYYLSPELCEDKPYNEKSDVWALGVVLYECCTGKHPFdannqgALILKIIRGVF-PPVSQ-MYSQQLAQLIDQCLTK-- 239
                        250
                 ....*....|.
gi 226944428 494 iaDPEQRFETA 504
Cdd:cd08529  240 --DYRQRPDTF 248
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
331-506 3.01e-17

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


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 80.75  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 331 HLYYVQrEY-PGKTLAEHLQAHGPLT-------LAQwldlaprLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFG 402
Cdd:cd05579   67 NLYLVM-EYlPGGDLASLLENVGSLDedvariyIAE-------IVLALEYLHSNGIIHRDLKPDNILIDSNGHLKLTDFG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 403 LAYCpGLSRDEPNSLP---------GTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYG---EIEAFQHPRFGt 470
Cdd:cd05579  139 LSKV-GLVRRQINLNDdekedkrivGTPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPPFHgetPEEIFQNILNG- 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226944428 471 plpaSRYRPDLPAWLDEC---LQRALIADPEQR--FETAEE 506
Cdd:cd05579  217 ----KIEWPEDVEVSDEAidlISKLLVPDPEKRlgAKSIEE 253
STKc_nPKC_delta cd05620
Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C delta; Serine ...
329-501 3.95e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Novel Protein Kinase C delta; Serine/Threonine Kinases (STKs), Novel Protein Kinase C (nPKC), delta isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nPKC 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. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 81.14  E-value: 3.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 329 RQHLYYVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPG 408
Cdd:cd05620   68 KEHLFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 409 LSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQHPRFGTplpasryrPDLPAWL 485
Cdd:cd05620  148 FGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFhgdDEDELFESIRVDT--------PHYPRWI 219
                        170       180
                 ....*....|....*....|
gi 226944428 486 ----DECLQRALIADPEQRF 501
Cdd:cd05620  220 tkesKDILEKLFERDPTRRL 239
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
366-510 5.68e-17

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: 80.07  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 366 LLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFG----LAYCPGLSRDEPNSLPGTPSHIAPEAFAGAAPDARQ--- 438
Cdd:cd06626  108 LLEGLAYLHSHGIVHRDIKPANIFLDHNGVIKLGDFGcavkLKNNTTTMGEEVQSLAGTPAYMAPEVITGGKGKGHGraa 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 439 DLYAAGVTLYLLLTGHYPYGEIE---------AFQHPrfgTPLPAS-RYRPDLPAWLDECLQRaliaDPEQRfETAEEWL 508
Cdd:cd06626  188 DIWSLGCVVLEMATGKRPWSELDnefqimfhvGAGHK---PPIPDSlQLSPEGKDFLDRCLES----DPKKR-PTASELL 259

                 ..
gi 226944428 509 LD 510
Cdd:cd06626  260 QH 261
STKc_beta_ARK cd05606
Catalytic domain of the Protein Serine/Threonine Kinase, beta-adrenergic receptor kinase; ...
341-457 7.35e-17

Catalytic domain of the Protein Serine/Threonine Kinase, beta-adrenergic receptor kinase; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, beta-adrenergic receptor kinase (beta-ARK) group, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK 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. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. There are seven types of GRKs, named GRK1 to GRK7. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism.


Pssm-ID: 173697 [Multi-domain]  Cd Length: 278  Bit Score: 79.98  E-value: 7.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 341 GKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAyCpGLSRDEPNSLPGT 420
Cdd:cd05606   81 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA-C-DFSKKKPHASVGT 158
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226944428 421 PSHIAPEAFA-GAAPDARQDLYAAGVTLYLLLTGHYPY 457
Cdd:cd05606  159 HGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPF 196
STKc_MST4 cd06640
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; ...
334-508 7.49e-17

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 79.71  E-value: 7.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 334 YVQREYPGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDE 413
Cdd:cd06640   78 WIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIK 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 414 PNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYGEIEA----FQHPRFGTPLPASRYRPDLPAWLDECL 489
Cdd:cd06640  158 RNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPmrvlFLIPKNNPPTLTGEFSKPFKEFIDACL 237
                        170
                 ....*....|....*....
gi 226944428 490 QRaliaDPEQRfETAEEWL 508
Cdd:cd06640  238 NK----DPSFR-PTAKELL 251
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
322-509 7.69e-17

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: 79.39  E-value: 7.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 322 EIAPLPQRQHLYYVQR--------------EY-PGKTLAEHLQAHGPLTLAQWLDLAPRLLRALGMLHRRNILHRDIKPE 386
Cdd:cd06632   52 EIALLSKLQHPNIVQYlgtereednlyiflELvPGGSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 387 NLLWGEDGELRLLDFGLAYcPGLSRDEPNSLPGTPSHIAPEAFAGAAP-DARQDLYAAGVTLYLLLTGHYPYGEIEAFQ- 464
Cdd:cd06632  132 NILVDTNGVVKLADFGMAK-QVVEFSFAKSFKGSPYWMAPEVIAQQGGyGLAADIWSLGCTVLEMATGKPPWSQLEGVAa 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226944428 465 ---------HPrfgtPLPASrYRPDLPAWLDECLQRaliaDPEQRfETAEEWLL 509
Cdd:cd06632  211 vfkigrskeLP----PIPDH-LSDEAKDFILKCLQR----DPSLR-PTAAELLE 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
366-508 8.86e-17

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


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 79.58  E-value: 8.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 366 LLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYCPGLSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGV 445
Cdd:cd06609  107 VLLGLEYLHEEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGI 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226944428 446 TLYLLLTGHYPYGEIEA----FQHPRFGTP-LPASRYRPDLPAWLDECLQRaliaDPEQRfETAEEWL 508
Cdd:cd06609  187 TAIELAKGEPPLSDLHPmrvlFLIPKNNPPsLEGNKFSKPFKDFVSLCLNK----DPKER-PSAKELL 249
STKc_PAK6 cd06659
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 6; Serine ...
354-508 1.06e-16

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 6; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 6, 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. PAK6 belongs to group II. Group II PAKs contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility.


Pssm-ID: 132990 [Multi-domain]  Cd Length: 297  Bit Score: 79.69  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 354 LTLAQWLDLAPRLLRALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGlaYCPGLSRDEPN--SLPGTPSHIAPEAFAG 431
Cdd:cd06659  114 LNEEQIATVCESVLQALCYLHSQGVIHRDIKSDSILLTLDGRVKLSDFG--FCAQISKDVPKrkSLVGTPYWMAPEVISR 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226944428 432 AAPDARQDLYAAGVTLYLLLTGHYPY---GEIEAFQHPRfGTPLPASRYRPDLPAWLDECLQRALIADPEQRfETAEEWL 508
Cdd:cd06659  192 TPYGTEVDIWSLGIMVIEMVDGEPPYfsdSPVQAMKRLR-DSPPPKLKNAHKISPVLRDFLERMLTREPQER-ATAQELL 269
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
329-464 1.31e-16

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


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 78.82  E-value: 1.31e-16
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gi 226944428 329 RQHLYYVQREYPGKTLAEHLQAHGPL--TLAQWLdLAPRLLrALGMLHRRNILHRDIKPENLLWGEDGELRLLDFGLAYC 406
Cdd:cd05572   65 KKYIYMLMEYCLGGELWTILRDRGLFdeYTARFY-IACVVL-AFEYLHNRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK 142
                         90       100       110       120       130
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gi 226944428 407 PGlSRDEPNSLPGTPSHIAPEAFAGAAPDARQDLYAAGVTLYLLLTGHYPYGEIEAFQ 464
Cdd:cd05572  143 LK-SGQKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGEDDEDP 199
STKc_GRK1 cd05608
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; ...
289-457 1.39e-16

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; Serine/Threonine Kinases (STKs), G protein-coupled Receptor Kinase (GRK) subfamily, GRK1 isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The GRK 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. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. There are seven types of GRKs, named GRK1 to GRK7. GRK1, also called rhodopsin kinase, belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease.


Pssm-ID: 173699 [Multi-domain]  Cd Length: 280  Bit Score: 79.12  E-value: 1.39e-16
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gi 226944428 289 KTLPPTRHSKAEAGQALLLEEWFLRRVASRYFPEIAPLPQ-----------------RQHL