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Conserved domains on  [gi|75908330|ref|YP_322626|]
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serine/threonine protein kinase with Chase2 sensor [Anabaena variabilis ATCC 29413]

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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 ...
489-682 1.06e-33

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: 129.28  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 489 LGYGGFSETYIAEDTQRpgNPQCVVKQLKPVNTQAKglqlaRRLFNLEAQSLEKLGSyQQIPQLLAYFEQEAEFYLVQEY 568
Cdd:cd00180   1 LGEGGFGTVYLARDKKT--GKKVAIKIIKKEDSSSL-----LEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 569 IIGHPLNQELPS-GKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEIslpqanNQE 647
Cdd:cd00180  73 CEGGSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLL------TSD 146
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75908330 648 PLPFTIGIGTKGYAPSEQCFGRPQYN--SDIYAVGMI 682
Cdd:cd00180 147 KSLLKTIVGTPAYMAPEVLLGKGYYSekSDIWSLGVI 183
COG4252 COG4252
Predicted transmembrane sensor domain [Signal transduction mechanisms]
37-432 4.13e-77

Predicted transmembrane sensor domain [Signal transduction mechanisms]


:

Pssm-ID: 226703  Cd Length: 400  Bit Score: 256.17  E-value: 4.13e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  37 QRLVRLGNILTVALTMGAALLTTSGLSLVQLLENQAISAFFQIRGPLIPPEDIVILAIDDQSISVpeqyyrtypqkyayl 116
Cdd:COG4252  10 SRVWRLRVILLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLES--------------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 117 epLSKFPFKRVAYAQVVEKLMQAGAKSVALDVVFDLPGSygnEDDRQLQAVLQKYSGKVTLAAqyeTSQSHQgfFTQLRL 196
Cdd:COG4252  75 --LGQWPWPRAALARLLDKLAAAQPRAIGLDIYRDLPSS---PGDRALAAVLQRAPNLIGVEK---LSGDPG--IAVNPP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 197 PYEKFrndEASIGTVNFPVEVDGKIHRLGSELTKILGEVDALTDKIPSFDQAVLAtAKVKYPRSP------GERIYFWGP 270
Cdd:COG4252 145 PELPR---QAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLASLG-ISPKYPDPErlrlgkTTLPRLLGN 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 271 AGTFATI----------------PFWHVLDPQNWNTYLQQgQVFQNKIVIIGATAQLANDYHAVAVSSAWLssEKMSGVE 334
Cdd:COG4252 221 SGGYQGAdaggyqillnyrssssDFRTVSLRDVLNGKVPA-ELIRGRIVLIGATAPSLNDYFATPYSSSLK--ELVPGVE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 335 IHANA----IATLMEGKAIAQGIPsqSLQALFVLVLVGGTSFIIT-RSKSGLQRFILSLAVASGWGSISYISFVYAQllF 409
Cdd:COG4252 298 IHANIvsqiLSALLDGRPLLPVWP--DGAELLWIFAWSLLGGLLAwRLRSPLRLLLAVGLALAGLLLISYLLFLAGW--W 373
                       410       420
                ....*....|....*....|...
gi 75908330 410 PTAIPMLAiAFCGISYLGTEVAK 432
Cdd:COG4252 374 IPLIPPLL-ALVGSGIWSTLFLK 395
Pkinase pfam00069
Protein kinase domain;
483-738 2.71e-35

Protein kinase domain;


:

Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 135.07  E-value: 2.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   483 YKILKVLGYGGFSETYIAedtQRPGNPQCV-VKQLKPVNTQAKGLQLARRlfnlEAQSLEKLGSyQQIPQLLAYFEQEAE 561
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKA---KHKGTGKIVaVKILKKRSEKSKKDQTARR----EIRILRRLSH-PNIVRLIDAFEDKDH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   562 FYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNI-IrrHSDHKLVLIDFGAVKEISL 640
Cdd:pfam00069  73 LYLVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENIlL--DENGVVKIADFGLAKKLTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   641 PQANnqeplpFTIGIGTKGYAPSEQCFGRPQYN--SDIYAVGMIGIKALTGIAP--HDLPRDENEEIK----------WR 706
Cdd:pfam00069 151 SSSS------LTTFVGTPEYMAPEVLLGGNGYGpkVDVWSLGVILYELLTGKPPfsGESILDQLQLIRrilgpplefdEP 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 75908330   707 DKALVSQGFAQILSKMVREDFKQRYqSASAVL 738
Cdd:pfam00069 225 KSDSGSEEAKDLIKKCLNKDPSKRP-TAEEIL 255
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
489-682 1.06e-33

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: 129.28  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 489 LGYGGFSETYIAEDTQRpgNPQCVVKQLKPVNTQAKglqlaRRLFNLEAQSLEKLGSyQQIPQLLAYFEQEAEFYLVQEY 568
Cdd:cd00180   1 LGEGGFGTVYLARDKKT--GKKVAIKIIKKEDSSSL-----LEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 569 IIGHPLNQELPS-GKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEIslpqanNQE 647
Cdd:cd00180  73 CEGGSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLL------TSD 146
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75908330 648 PLPFTIGIGTKGYAPSEQCFGRPQYN--SDIYAVGMI 682
Cdd:cd00180 147 KSLLKTIVGTPAYMAPEVLLGKGYYSekSDIWSLGVI 183
COG4252 COG4252
Predicted transmembrane sensor domain [Signal transduction mechanisms]
37-432 4.13e-77

Predicted transmembrane sensor domain [Signal transduction mechanisms]


Pssm-ID: 226703  Cd Length: 400  Bit Score: 256.17  E-value: 4.13e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  37 QRLVRLGNILTVALTMGAALLTTSGLSLVQLLENQAISAFFQIRGPLIPPEDIVILAIDDQSISVpeqyyrtypqkyayl 116
Cdd:COG4252  10 SRVWRLRVILLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLES--------------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 117 epLSKFPFKRVAYAQVVEKLMQAGAKSVALDVVFDLPGSygnEDDRQLQAVLQKYSGKVTLAAqyeTSQSHQgfFTQLRL 196
Cdd:COG4252  75 --LGQWPWPRAALARLLDKLAAAQPRAIGLDIYRDLPSS---PGDRALAAVLQRAPNLIGVEK---LSGDPG--IAVNPP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 197 PYEKFrndEASIGTVNFPVEVDGKIHRLGSELTKILGEVDALTDKIPSFDQAVLAtAKVKYPRSP------GERIYFWGP 270
Cdd:COG4252 145 PELPR---QAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLASLG-ISPKYPDPErlrlgkTTLPRLLGN 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 271 AGTFATI----------------PFWHVLDPQNWNTYLQQgQVFQNKIVIIGATAQLANDYHAVAVSSAWLssEKMSGVE 334
Cdd:COG4252 221 SGGYQGAdaggyqillnyrssssDFRTVSLRDVLNGKVPA-ELIRGRIVLIGATAPSLNDYFATPYSSSLK--ELVPGVE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 335 IHANA----IATLMEGKAIAQGIPsqSLQALFVLVLVGGTSFIIT-RSKSGLQRFILSLAVASGWGSISYISFVYAQllF 409
Cdd:COG4252 298 IHANIvsqiLSALLDGRPLLPVWP--DGAELLWIFAWSLLGGLLAwRLRSPLRLLLAVGLALAGLLLISYLLFLAGW--W 373
                       410       420
                ....*....|....*....|...
gi 75908330 410 PTAIPMLAiAFCGISYLGTEVAK 432
Cdd:COG4252 374 IPLIPPLL-ALVGSGIWSTLFLK 395
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
46-372 2.66e-59

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 253103  Cd Length: 305  Bit Score: 204.09  E-value: 2.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    46 LTVALTMGAALLTTSGLslVQLLENQAISAFFQIRGPLIPP----EDIVILAIDDQSIsvpeqyyrtypqkyaylEPLSK 121
Cdd:pfam05226   1 LALLLLLLLALLSLRPL--LQRLELALYDLLFRLRGPRAPPpepdPRIVIVAIDEASL-----------------AELGR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   122 FPFKRVAYAQVVEKLMQAGAKSVALDVVFDLPGSYGNEDDRQLQAVLQKYSGKVTLAAQYETSQSHQGFFTQLrlpyEKF 201
Cdd:pfam05226  62 WPWPRALLARLLDRLAAAGAKAIGLDILFDEPDRDSPAGDAALAAALARAGNPVVLGVFLEASEDGGGPLAPP----PAL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   202 RNDEASIGTVNFPVEVDGKIHRlgseltkILGEVDALTDKIPSFDQAVLATAKVKYPRSPGER----------------I 265
Cdd:pfam05226 138 AAAAAGLGFVNVVPDSDGVVRR-------VPLLLRYGGRLYPSLALALARVALGAPPIRAEADagggdrriptdggqllL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   266 YFWGPAGTFATIPFWHVLDpqnwntylqqGQV----FQNKIVIIGATAQLANDYHAVAVSSAwlssekMSGVEIHANAIA 341
Cdd:pfam05226 211 NFRGPAGTFPTVSAADVLE----------GRVppelLRGKIVLIGATAAGLGDLFPTPFSGR------MPGVEIHANAIS 274
                         330       340       350
                  ....*....|....*....|....*....|.
gi 75908330   342 TLMEGKAIAQGIPSQSLQALFVLVLVGGTSF 372
Cdd:pfam05226 275 NLLSGRLLRPWPDWVELLLILLLALLLGLLL 305
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
66-372 4.25e-58

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 200.67  E-value: 4.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330     66 QLLENQAISAFFQIRGPLIPPEDIVILAIDDQSisvpeqyyrtypqkyayLEPLSKFPFKRVAYAQVVEKLMQAGAKSVA 145
Cdd:smart01080   1 QRLELRLYDARFRLRPRRAPDPDIVIVAIDEAS-----------------LAALGRWPWPRSVLARLLDRLAAAGAKAIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    146 LDVVFDLPGSYGNEDDRQLQAVLQKYSGKVTLAAQYETSQ------SHQGFFTQLRLPYEKFRNDEASIGTVNFPVEvDG 219
Cdd:smart01080  64 FDILFDEPDRDSPDGDAALAAALARAPNVVLLAKLSREAGggvlpsPPLPLPELPLPPLPGLADAAAGLGHVNEPDA-DG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    220 KIHR--------------LGSELTKILGEVDALTDKIP--SFDQAVLATAKVKYPRSPGERIYFWGPAG--TFATIPFWH 281
Cdd:smart01080 143 VVRRvplllryggkaypsLALELARVALGTPPLRLRLGglGGPALTLGDGGYPGDRAGRLLIPFDGPGRggTFPTVSAAD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    282 VLDPQNWNtylqQGQVFQNKIVIIGATAQLANDYHAVAVSSAwlssekMSGVEIHANAIATLMEGKAIAQGIPSQSLQAL 361
Cdd:smart01080 223 VLDGEVPA----LPELLRGKIVLIGATAAGLGDLFPTPFSRV------MPGVEIHANAIDNLLDGRFLRPAPPWWALLLL 292
                          330
                   ....*....|.
gi 75908330    362 FVLVLVGGTSF 372
Cdd:smart01080 293 LLLWLLLGLLL 303
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
555-633 3.46e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 56.07  E-value: 3.46e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75908330  555 YFEQEAEFYLVQEYIIGHPLNQELPSGksisEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRrhSDHKLVLIDFG 633
Cdd:PRK14879  67 YFVDPENFIIVMEYIEGEPLKDLINSN----GMEELELSREIGRLVGKLHSAGIIHGDLTTSNMIL--SGGKIYLIDFG 139
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
486-633 7.57e-09

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 54.98  E-value: 7.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 486 LKVLGYGGFSETYIAEDTQRPgnpqCVVKQLKPvntqaKGL---QLARRLFN----LEAQSLEKLgSYQQIPQLLAYFEQ 558
Cdd:COG3642   1 MDLIKQGAEAIIYLTDFLGLP----AVVKERIP-----KRYrhpELDEKLRRertrREARILAKA-REAGVPVPIVYDVD 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75908330 559 EAEFYLVQEYIIGHPLNQELPSGKsiseaetVAIIREILEILVFVHENGVIHRDIKPSNIIrrHSDHKLVLIDFG 633
Cdd:COG3642  71 PDNGLIVMEYIEGELLKDALEEAR-------PDLLREVGRLVGKLHKAGIVHGDLTTSNII--LSGGRIYFIDFG 136
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
561-633 1.22e-07

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: 51.45  E-value: 1.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75908330   561 EFYLVQEYIIGHPLNQELPSGKsiseaetVAIIREILEILVFVHENGVIHRDIKPSNIIRRhsDHKLVLIDFG 633
Cdd:TIGR03724  71 NKTIVMEYIEGKPLKDVIEEGN-------DELLREIGRLVGKLHKAGIVHGDLTTSNIIVR--DDKLYLIDFG 134
YrbL-PhoP_reg pfam10707
PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. ...
496-634 1.11e-04

PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. PhoP protein controls the expression of a large number of genes that mediate adaptation to low Mg2+ environments and/or virulence in several bacterial species. YbrL is proposed to be acting in a loop activity with PhoP and PrmA analogous to the multicomponent loop in Salmonella where the PhoP-dependent PmrD protein activates the regulatory protein PmrA, and the activated PmrA then represses transcription from the PmrD promoter which harbours binding sites for both the PhoP and PmrA proteins. Expression of YrbL is induced in low Mg2+ in a PhoP-dependent fashion and repressed by Fe3+ in a PmrA-dependent manner.


Pssm-ID: 151200  Cd Length: 199  Bit Score: 42.63  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   496 ETYIAEDTQR-----PGNPQCVVKQLKPVNtqakglQLARRLFNLEAQSLEKLGSYQQIPQLLAYFEQ-----EAEFYLV 565
Cdd:pfam10707   6 SDLLAQGGQRlvyahPLDADLCIKVLRPAN------IAARRRFKGWLKRLLPTSRYRQNLRELKEYLRlskrrGIDWSPI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   566 QEYI------IGHPLNQELPSGKSISEAETV----------AIIREILEILV-FVHENGVIHRDIKPSNII---RRHSDH 625
Cdd:pfam10707  80 PRYYgfvetdLGLGLVTERIRDADGNISPTLedllknggltAALREALNEFKrYLLDNHIVARDLNPHNIVygrRSEGEY 159
                         170
                  ....*....|
gi 75908330   626 KLVLID-FGA 634
Cdd:pfam10707 160 ELVLVDgFGD 169
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
478-635 1.00e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 40.32  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  478 ILSGRYKILKVLGYGGFSETYiaeDTQRPGNpQCVVKQL--KPVNTQAKGLQLARRLFN--LEAQSLEKLGSYQQIPQL- 552
Cdd:PHA02882   9 ITGKEWKIDKLIGCGGFGCVY---ETQCASD-HCINNQAvaKIENLENETIVMETLVYNniYDIDKIALWKNIHNIDHLg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  553 ------LAYFEQEAEFYlvqEYIIGHPL----NQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRH 622
Cdd:PHA02882  85 ipkyygCGSFKRCRMYY---RFILLEKLventKEIFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIM-VD 160
                        170
                 ....*....|...
gi 75908330  623 SDHKLVLIDFGAV 635
Cdd:PHA02882 161 GNNRGYIIDYGIA 173
Pkinase pfam00069
Protein kinase domain;
483-738 2.71e-35

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 135.07  E-value: 2.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   483 YKILKVLGYGGFSETYIAedtQRPGNPQCV-VKQLKPVNTQAKGLQLARRlfnlEAQSLEKLGSyQQIPQLLAYFEQEAE 561
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKA---KHKGTGKIVaVKILKKRSEKSKKDQTARR----EIRILRRLSH-PNIVRLIDAFEDKDH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   562 FYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNI-IrrHSDHKLVLIDFGAVKEISL 640
Cdd:pfam00069  73 LYLVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENIlL--DENGVVKIADFGLAKKLTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   641 PQANnqeplpFTIGIGTKGYAPSEQCFGRPQYN--SDIYAVGMIGIKALTGIAP--HDLPRDENEEIK----------WR 706
Cdd:pfam00069 151 SSSS------LTTFVGTPEYMAPEVLLGGNGYGpkVDVWSLGVILYELLTGKPPfsGESILDQLQLIRrilgpplefdEP 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 75908330   707 DKALVSQGFAQILSKMVREDFKQRYqSASAVL 738
Cdd:pfam00069 225 KSDSGSEEAKDLIKKCLNKDPSKRP-TAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
483-777 1.21e-48

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: 176.09  E-value: 1.21e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQRpgnpqCVVKQLKPvntQAKGLQLARRLFNLEAQSLEKLGSYQQIPQLLAYFEQEAEF 562
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL-----VALKVLAK---KLESKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 563 YLVQEYIIGHPLNQEL---PSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEIS 639
Cdd:COG0515  74 YLVMEYVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 640 LPQANNQEPLPFTIGIGTKGYAPSEQCFG----RPQYNSDIYAVGMIGIKALTGIAPHDLPRDENEE------------- 702
Cdd:COG0515 154 DPGSTSSIPALPSTSVGTPGYMAPEVLLGlslaYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATsqtlkiilelptp 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 703 -----IKWRDKALVSQGFAQILSKMVREDFKQRYQSASAVLAALNKLANTPDKNFGQQNDSSMNTIISIDESDFPTAHWP 777
Cdd:COG0515 234 slaspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALIS 313
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
483-739 1.13e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 127.26  E-value: 1.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    483 YKILKVLGYGGFSETYIAEDtqRPGNPQCVVKQLKPVNtQAKGLQLARRlfnlEAQSLEKLGSyQQIPQLLAYFEQEAEF 562
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD--KKTGKLVAIKVIKKKK-IKKDRERILR----EIKILKKLKH-PNIVRLYDVFEDEDKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    563 YLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVKEIslpq 642
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LDEDGHVKLADFGLARQL---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    643 annQEPLPFTIGIGTKGYAPSEQCFGRPqYN--SDIYAVGMIGIKALTGIAPHDLPRDENEEIK---------WRDKALV 711
Cdd:smart00220 148 ---DPGEKLTTFVGTPEYMAPEVLLGKG-YGkaVDIWSLGVILYELLTGKPPFPGDDQLLELFKkigkpkppfPPPEWDI 223
                          250       260
                   ....*....|....*....|....*...
gi 75908330    712 SQGFAQILSKMVREDFKQRYqSASAVLA 739
Cdd:smart00220 224 SPEAKDLIRKLLVKDPEKRL-TAEEALQ 250
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
527-737 6.41e-16

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: 81.04  E-value: 6.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    527 QLARrlFNLEAQSLEKLgSYQQIPQLLAYFEQEAEF-YLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHE 605
Cdd:TIGR03903   21 QRAR--FRRETALCARL-YHPNIVALLDSGEAPPGLlFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    606 NGVIHRDIKPSNIIRRHSD---HKLVLiDFGavkeIS--LPQANNQEPLPFTIG---IGTKGYAPSEQCFGRP-QYNSDI 676
Cdd:TIGR03903   98 QGIVHRDLKPQNIMVSQTGvrpHAKVL-DFG----IGtlLPGVRDADVATLTRTtevLGTPTYCAPEQLRGEPvTPNSDL 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75908330    677 YAVGMIGIKALTG----------------IAPHD--LPrdeneeikwrdKALVSQGFAQILSKMVREDFKQRYQSASAV 737
Cdd:TIGR03903  173 YAWGLIFLECLTGqrvvqgasvaeilyqqLSPVDvsLP-----------PWIAGHPLGQVLRKALNKDPRQRAASAPAL 240
pknD PRK13184
serine/threonine-protein kinase; Reviewed
481-741 1.16e-14

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 76.73  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  481 GRYKILKVLGYGGFSETYIAEDtqrpgnPQCVVK-QLKPVNTQAKGLQLARRLFNLEAQSLEKLGSYQQIPQLLAYFEQE 559
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYD------PVCSRRvALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  560 AEFYlVQEYIIGHPLNQELPS-------GKSISEAETVA----IIREILEILVFVHENGVIHRDIKPSNI-IRRHSDhkL 627
Cdd:PRK13184  76 PVYY-TMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVGaflsIFHKICATIEYVHSKGVLHRDLKPDNIlLGLFGE--V 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  628 VLIDFGAVKEISLPQAN------NQEPLPF---TIG---IGTKGYAPSEQCFGRPQYNS-DIYAVGMIGIKALTGIAPHD 694
Cdd:PRK13184 153 VILDWGAAIFKKLEEEDlldidvDERNICYssmTIPgkiVGTPDYMAPERLLGVPASEStDIYALGVILYQMLTLSFPYR 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 75908330  695 lpRDENEEIKWRDKALVSQGFA----------QILSKMVREDFKQRYQSASAVLAAL 741
Cdd:PRK13184 233 --RKKGRKISYRDVILSPIEVApyreippflsQIAMKALAVDPAERYSSVQELKQDL 287
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
553-634 1.88e-10

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 62.89  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  553 LAYFEQEAEF-YLVQEYIIGHPlnQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLID 631
Cdd:PLN03225 222 LADLMQSKEFpYNVEPYLLGKV--QDLPKGLERENKIIQTIMRQILFALDGLHSTGIVHRDVKPQNIIFSEGSGSFKIID 299

                 ...
gi 75908330  632 FGA 634
Cdd:PLN03225 300 LGA 302
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
563-703 1.50e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 58.33  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  563 YLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEISLPq 642
Cdd:PHA03390  85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDRIYLCDYGLCKIIGTP- 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75908330  643 annqeplpfTIGIGTKGYAPSEQCFGRP-QYNSDIYAVGMIGIKALTGIAPHDlpRDENEEI 703
Cdd:PHA03390 164 ---------SCYDGTLDYFSPEKIKGHNyDVSFDWWAVGVLTYELLTGKHPFK--EDEDEEL 214
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
479-689 8.72e-05

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 43.98  E-value: 8.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  479 LSGRYKIL-KVLGYGGFSETYIAEDTQRpgNPQCVVKQLKpVNTQAKGLQLARRL-------FNL--EAQSLEKLgSYQQ 548
Cdd:PTZ00024   6 ISERYIQKgAHLGEGTYGKVEKAYDTLT--GKIVAIKKVK-IIEISNDVTKDRQLvgmcgihFTTlrELKIMNEI-KHEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  549 IPQLLAYFEQEAEFYLVQEYIIGHpLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNI-IRRHSDHKL 627
Cdd:PTZ00024  82 IMGLVDVYVEGDFINLVMDIMASD-LKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIfINSKGICKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75908330  628 VliDFGAVKEISLP--------QANNQEPLPFTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMIGIKALTG 689
Cdd:PTZ00024 161 A--DFGLARRYGYPpysdtlskDETMQRREEMTSKVVTLWYRAPELLMGAEKYHFavDMWSVGCIFAELLTG 230
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
489-682 1.06e-33

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: 129.28  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 489 LGYGGFSETYIAEDTQRpgNPQCVVKQLKPVNTQAKglqlaRRLFNLEAQSLEKLGSyQQIPQLLAYFEQEAEFYLVQEY 568
Cdd:cd00180   1 LGEGGFGTVYLARDKKT--GKKVAIKIIKKEDSSSL-----LEELLREIEILKKLNH-PNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 569 IIGHPLNQELPS-GKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEIslpqanNQE 647
Cdd:cd00180  73 CEGGSLKDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLL------TSD 146
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75908330 648 PLPFTIGIGTKGYAPSEQCFGRPQYN--SDIYAVGMI 682
Cdd:cd00180 147 KSLLKTIVGTPAYMAPEVLLGKGYYSekSDIWSLGVI 183
COG4252 COG4252
Predicted transmembrane sensor domain [Signal transduction mechanisms]
37-432 4.13e-77

Predicted transmembrane sensor domain [Signal transduction mechanisms]


Pssm-ID: 226703  Cd Length: 400  Bit Score: 256.17  E-value: 4.13e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330  37 QRLVRLGNILTVALTMGAALLTTSGLSLVQLLENQAISAFFQIRGPLIPPEDIVILAIDDQSISVpeqyyrtypqkyayl 116
Cdd:COG4252  10 SRVWRLRVILLLALLVALLVLLLRLLGLLQLLELAAFDQLLRLRPSEPPDDRILIVAIDEQDLES--------------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 117 epLSKFPFKRVAYAQVVEKLMQAGAKSVALDVVFDLPGSygnEDDRQLQAVLQKYSGKVTLAAqyeTSQSHQgfFTQLRL 196
Cdd:COG4252  75 --LGQWPWPRAALARLLDKLAAAQPRAIGLDIYRDLPSS---PGDRALAAVLQRAPNLIGVEK---LSGDPG--IAVNPP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 197 PYEKFrndEASIGTVNFPVEVDGKIHRLGSELTKILGEVDALTDKIPSFDQAVLAtAKVKYPRSP------GERIYFWGP 270
Cdd:COG4252 145 PELPR---QAQIGFSDLILDSDGKVRRLLLAATPGPEPKYSLALKLALQYLASLG-ISPKYPDPErlrlgkTTLPRLLGN 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 271 AGTFATI----------------PFWHVLDPQNWNTYLQQgQVFQNKIVIIGATAQLANDYHAVAVSSAWLssEKMSGVE 334
Cdd:COG4252 221 SGGYQGAdaggyqillnyrssssDFRTVSLRDVLNGKVPA-ELIRGRIVLIGATAPSLNDYFATPYSSSLK--ELVPGVE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 335 IHANA----IATLMEGKAIAQGIPsqSLQALFVLVLVGGTSFIIT-RSKSGLQRFILSLAVASGWGSISYISFVYAQllF 409
Cdd:COG4252 298 IHANIvsqiLSALLDGRPLLPVWP--DGAELLWIFAWSLLGGLLAwRLRSPLRLLLAVGLALAGLLLISYLLFLAGW--W 373
                       410       420
                ....*....|....*....|...
gi 75908330 410 PTAIPMLAiAFCGISYLGTEVAK 432
Cdd:COG4252 374 IPLIPPLL-ALVGSGIWSTLFLK 395
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
46-372 2.66e-59

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 253103  Cd Length: 305  Bit Score: 204.09  E-value: 2.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    46 LTVALTMGAALLTTSGLslVQLLENQAISAFFQIRGPLIPP----EDIVILAIDDQSIsvpeqyyrtypqkyaylEPLSK 121
Cdd:pfam05226   1 LALLLLLLLALLSLRPL--LQRLELALYDLLFRLRGPRAPPpepdPRIVIVAIDEASL-----------------AELGR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   122 FPFKRVAYAQVVEKLMQAGAKSVALDVVFDLPGSYGNEDDRQLQAVLQKYSGKVTLAAQYETSQSHQGFFTQLrlpyEKF 201
Cdd:pfam05226  62 WPWPRALLARLLDRLAAAGAKAIGLDILFDEPDRDSPAGDAALAAALARAGNPVVLGVFLEASEDGGGPLAPP----PAL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   202 RNDEASIGTVNFPVEVDGKIHRlgseltkILGEVDALTDKIPSFDQAVLATAKVKYPRSPGER----------------I 265
Cdd:pfam05226 138 AAAAAGLGFVNVVPDSDGVVRR-------VPLLLRYGGRLYPSLALALARVALGAPPIRAEADagggdrriptdggqllL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330   266 YFWGPAGTFATIPFWHVLDpqnwntylqqGQV----FQNKIVIIGATAQLANDYHAVAVSSAwlssekMSGVEIHANAIA 341
Cdd:pfam05226 211 NFRGPAGTFPTVSAADVLE----------GRVppelLRGKIVLIGATAAGLGDLFPTPFSGR------MPGVEIHANAIS 274
                         330       340       350
                  ....*....|....*....|....*....|.
gi 75908330   342 TLMEGKAIAQGIPSQSLQALFVLVLVGGTSF 372
Cdd:pfam05226 275 NLLSGRLLRPWPDWVELLLILLLALLLGLLL 305
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
66-372 4.25e-58

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 200.67  E-value: 4.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330     66 QLLENQAISAFFQIRGPLIPPEDIVILAIDDQSisvpeqyyrtypqkyayLEPLSKFPFKRVAYAQVVEKLMQAGAKSVA 145
Cdd:smart01080   1 QRLELRLYDARFRLRPRRAPDPDIVIVAIDEAS-----------------LAALGRWPWPRSVLARLLDRLAAAGAKAIG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    146 LDVVFDLPGSYGNEDDRQLQAVLQKYSGKVTLAAQYETSQ------SHQGFFTQLRLPYEKFRNDEASIGTVNFPVEvDG 219
Cdd:smart01080  64 FDILFDEPDRDSPDGDAALAAALARAPNVVLLAKLSREAGggvlpsPPLPLPELPLPPLPGLADAAAGLGHVNEPDA-DG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    220 KIHR--------------LGSELTKILGEVDALTDKIP--SFDQAVLATAKVKYPRSPGERIYFWGPAG--TFATIPFWH 281
Cdd:smart01080 143 VVRRvplllryggkaypsLALELARVALGTPPLRLRLGglGGPALTLGDGGYPGDRAGRLLIPFDGPGRggTFPTVSAAD 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330    282 VLDPQNWNtylqQGQVFQNKIVIIGATAQLANDYHAVAVSSAwlssekMSGVEIHANAIATLMEGKAIAQGIPSQSLQAL 361
Cdd:smart01080 223 VLDGEVPA----LPELLRGKIVLIGATAAGLGDLFPTPFSRV------MPGVEIHANAIDNLLDGRFLRPAPPWWALLLL 292
                          330
                   ....*....|.
gi 75908330    362 FVLVLVGGTSF 372
Cdd:smart01080 293 LLLWLLLGLLL 303
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
482-692 4.39e-19

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: 87.23  E-value: 4.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDTQrpGNPQCVVKQlkpVNTQAKGLQLARRLFNlEAQSLEKLGSyqqiPQLLAYF----- 556
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKD--TGELMAVKS---VELSGDSEEELEALER-EIRILSSLQH----PNIVRYYgserd 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 557 EQEAEFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDH-KLVliDFGAV 635
Cdd:cd06606  71 EEKNTLNIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVvKLA--DFGCA 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75908330 636 KEISLPQANNQEPLPftigIGTKGY-APsEQCFGRPQ-YNSDIYAVGMIGIKALTGIAP 692
Cdd:cd06606 149 KRLGDIETGEGTGSV----RGTPYWmAP-EVIRGEEYgRAADIWSLGCTVIEMATGKPP 202
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
483-692 4.65e-19

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: 87.63  E-value: 4.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAedTQRPGNPQCVVKQL--KPVNTQAKGLQLarrlfNLEAQSLEKLGSYQQIPQLLAYFEQEA 560
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLA--KEKETNKEYAIKILdkRQLIKEKKVKYV-----KIEKEVLTRLNGHPGIIKLYYTFQDEE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 561 EFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHsDHKLVLIDFGAVK---E 637
Cdd:cd05581  76 NLYFVLEYAPNGELLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDK-DMHIKITDFGTAKvldP 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 638 ISLPQANNQEPLPFTIGI-----------GTKGY-AP---SEQCFGrpqYNSDIYAVGMIGIKALTGIAP 692
Cdd:cd05581 155 NSSPESNKGDATNIDSQIeknrrrfasfvGTAEYvSPellNEKPAG---KSSDLWALGCIIYQMLTGKPP 221
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
483-697 9.66e-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: 86.11  E-value: 9.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKPVNTQAKglqlaRRLFNlEAQSLEKLgSYQQIPQLLAYFEQEAE 561
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKR---TGKEVaIKVIKLESKEKK-----EKIIN-EIQILKKC-KHPNIVKYYGSYLKKDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 562 FYLVQEYIIGHPLNQEL-PSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHsDHKLVLIDFGAVKEISL 640
Cdd:cd05122  72 LWIVMEFCSGGSLKDLLkSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTS-DGEVKLIDFGLSAQLSD 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 641 PQANNqeplpfTIgIGTKGYAPSEQCFGRPqYN--SDIYAVGMIGIKALTGIAPH-DLPR 697
Cdd:cd05122 151 TKARN------TM-VGTPYWMAPEVINGKP-YDykADIWSLGITAIELAEGKPPYsELPP 202
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
482-682 1.10e-17

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: 82.93  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDTqRPGNpQCVVKQLKPVNTQAKGLQLARRlfnlEAQSLEKLgsyqQIPQLLAY---FEQ 558
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRK-SDGK-LYVLKEIDLSNMSEKEREDALN----EVKILKKL----NHPNIIKYyesFEE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 559 EAEFYLVQEYIIGHPLNQEL----PSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRhSDHKLVLIDFG- 633
Cdd:cd08215  71 KGKLCIVMEYADGGDLSQKIkkqkKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLT-SNGLVKLGDFGi 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75908330 634 -AVKEISLPQANnqeplpfTIgIGTKGYAPSEQCFGRPqYN--SDIYAVGMI 682
Cdd:cd08215 150 sKVLSSTVDLAK-------TV-VGTPYYLSPELCQNKP-YNykSDIWSLGCV 192
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine ...
482-682 1.78e-17

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CCRK 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. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed, this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure.


Pssm-ID: 173736 [Multi-domain]  Cd Length: 286  Bit Score: 82.72  E-value: 1.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDTQrpgNPQCVVKQLKPVNTQAKG--LQLARrlfnlEAQSLEKLGSyQQIPQLLAYFEQE 559
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRE---TGETVALKKVALRRLEGGipNQALR-----EIKALQACQH-PYVVKLLDVFPHG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 560 AEFYLVQEYIiGHPLNQEL-PSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHkLVLIDFGavkeI 638
Cdd:cd07832  72 SGFVLVMEYM-PSDLSEVLrDEERPLPEAQVKSYMRMLLKGVAYMHANGIMHRDLKPANLLISADGV-LKIADFG----L 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75908330 639 SLPQaNNQEPLPFTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMI 682
Cdd:cd07832 146 ARLF-SEEEPRLYSHQVATRWYRAPELLYGARKYDPgvDLWAVGCI 190
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
563-730 2.80e-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: 81.91  E-value: 2.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 563 YLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHkLVLIDFGAVKEISLPQ 642
Cdd:cd05579  69 YLVMEYLPGGDLASLLENVGSLDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNILIDSNGH-LKLTDFGLSKVGLVRR 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 643 ANNQEPLPFTIG--IGTKGYAPSEQCFGRPQ-YNSDIYAVGMIGIKALTGIAP-HDLPRDE------NEEIKWRDKALVS 712
Cdd:cd05579 148 QINLNDDEKEDKriVGTPDYIAPEVILGQGHsKTVDWWSLGCILYEFLVGIPPfHGETPEEifqnilNGKIEWPEDVEVS 227
                       170
                ....*....|....*...
gi 75908330 713 QGFAQILSKMVREDFKQR 730
Cdd:cd05579 228 DEAIDLISKLLVPDPEKR 245
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine ...
483-682 3.61e-17

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Male germ cell-Associated Kinase (MAK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAK-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 human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia (ECO), suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I.


Pssm-ID: 173734 [Multi-domain]  Cd Length: 283  Bit Score: 81.43  E-value: 3.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKpvntqakglqlaRRLFNL-------EAQSLEKLGSYQQIPQLLA 554
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKE---TGELVaIKKMK------------KKFYSWeecmnlrEVKSLRKLNEHPNIVKLKE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 555 YFEQEAEFYLVQEYIIGHpLNQELPS--GKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRrhSDHKLV-LID 631
Cdd:cd07830  66 VFRENDELYFVFEYMEGN-LYQLMKDrkGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLV--SGPEVVkIAD 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75908330 632 FGAVKEI-SLPqannqeplPFTIGIGTKGY-APsEQCFGRPQYNS--DIYAVGMI 682
Cdd:cd07830 143 FGLAREIrSRP--------PYTDYVSTRWYrAP-EILLRSTSYSSpvDIWALGCI 188
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ...
483-682 4.53e-16

Catalytic domain of CMGC family Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), CMGC family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC 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 CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and similar proteins. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation.


Pssm-ID: 143333 [Multi-domain]  Cd Length: 283  Bit Score: 78.14  E-value: 4.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKPVNTQAKGLQLARRlfnlEAQSLEKLgSYQQIPQLLAYFEQEAE 561
Cdd:cd05118   1 YQKLGKIGEGTYGVVYKARDKL---TGEIVaIKKIKLRFESEGIPKTALR----EIKLLKEL-NHPNIIKLLDVFRHKGD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 562 FYLVQEYIiGHPLNQELP-SGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNI-IRRHSDHKLVliDFGAVKEIS 639
Cdd:cd05118  73 LYLVFEFM-DTDLYKLIKdRQRGLPESLIKSYLYQLLQGLAFCHSHGILHRDLKPENLlINTEGVLKLA--DFGLARSFG 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75908330 640 LPQAnnqeplPFTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMI 682
Cdd:cd05118 150 SPVR------PYTHYVVTRWYRAPELLLGDKGYSTpvDIWSVGCI 188
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
482-682 1.11e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 5; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 5 (Nek5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek5 subfamily is one of a family of 11 different Neks (Nek1-11). 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. Neks 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. The specific function of Nek5 is unknown.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 76.92  E-value: 1.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDtqRPGNPQCVVKQLKPVNTQAKGLQLARRlfnlEAQSLEKLgSYQQIPQLLAYFEQEAE 561
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKA--KSDSEHCVIKEIDLTKMPVKEKEASKK----EVILLAKM-KHPNIVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 562 FYLVQEYIIGHPLNQEL--PSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKeis 639
Cdd:cd08225  74 LFIVMEYCDGGDLMKRInrQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIAR--- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75908330 640 lpQANNQEPLPFTIgIGTKGYAPSEQCFGRPQYN-SDIYAVGMI 682
Cdd:cd08225 151 --QLNDSMELAYTC-VGTPYYLSPEICQNRPYNNkTDIWSLGCV 191
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
483-694 1.90e-14

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: 73.12  E-value: 1.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAE--DTQRPGNPQCVVKQlKPVNTQAkglqlARRLFNlEAQSLEKLgSYQQIPQLLAYFEQEA 560
Cdd:cd05578   2 FELLRVIGKGAFGKVCIVQkrDTKKMFAMKYMNKQ-KCVEKGS-----VRNVLN-ERRILQEL-NHPFLVNLWYSFQDEE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 561 EFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHkLVLIDFGaVKEISL 640
Cdd:cd05578  74 NMYLVVDLLLGGDLRYHLSQKVKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILLDEQGH-VHITDFN-IATKVT 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75908330 641 PQANNQEplpftiGIGTKGY-APseQCFGRPQYNS--DIYAVGMIGIKALTGIAPHD 694
Cdd:cd05578 152 PDTLTTS------TSGTPGYmAP--EVLCRQGYSVavDWWSLGVTAYECLRGKRPYR 200
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine ...
481-682 2.28e-13

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-dependent protein kinase like (CDKL) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDKL 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. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory.


Pssm-ID: 143338 [Multi-domain]  Cd Length: 288  Bit Score: 70.04  E-value: 2.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 481 GRYKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKPVNTQAKGLQLARRlfnlEAQSLEKLgSYQQIPQLLAYFEQE 559
Cdd:cd07833   1 NKYEVLGVVGEGAYGVVLKCRNKA---TGEIVaIKKFKESEDDEDVKKTALR----EVKVLRQL-RHENIVNLKEAFRRK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 560 AEFYLVQEYIiGHPLNQEL---PSGksISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDhKLVLIDFGAVK 636
Cdd:cd07833  73 GRLYLVFEYV-ERTLLELLeasPGG--LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESG-VLKLCDFGFAR 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75908330 637 eiSLPQANNQeplPFTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMI 682
Cdd:cd07833 149 --ALRARPAS---PLTDYVATRWYRAPELLVGDTNYGKpvDVWAIGCI 191
STKc_MEKK3_like cd06625
Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine ...
487-692 5.94e-13

Catalytic domain of MAP/ERK kinase kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 3 (MEKK3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK3-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 MEKK3, MEKK2, and related proteins, all containing an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks), proteins that 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. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates extracellular signal-regulated kinase 5 (ERK5). The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs.


Pssm-ID: 132956 [Multi-domain]  Cd Length: 263  Bit Score: 68.30  E-value: 5.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 487 KVLGYGGFSETYIAED--TQRpgnpQCVVKQlkpVNTQAKGLQLARRLFNLEaQSLEKLGSYQ--QIPQLLAYFEQEAEF 562
Cdd:cd06625   8 KLLGQGAFGRVYLCYDvdTGR----ELAVKQ---VPFDPDSPETKKEVNALE-CEIQLLKNLQheRIVQYYGCLRDDETL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 563 YLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVKEISLPQ 642
Cdd:cd06625  80 SIFMEYMPGGSVKDQLKAYGALTETVTRKYTRQILEGVEYLHSNMIVHRDIKGANIL-RDSAGNVKLGDFGASKRLQTIC 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75908330 643 ANNQEPLPFTigiGTKGYAPSE----QCFGRpqyNSDIYAVGMIGIKALTGIAP 692
Cdd:cd06625 159 SSGTGMKSVT---GTPYWMSPEvisgEGYGR---KADVWSVGCTVVEMLTEKPP 206
STKc_myosinIII_like cd06608
Catalytic domain of Class III myosin-like Protein Serine/Threonine Kinases; Serine/threonine ...
480-633 7.96e-13

Catalytic domain of Class III myosin-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Class III myosin-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), mitogen-activated protein kinase (MAPK) kinase kinase kinase 4 (MAPKKKK4 or MAP4K4) and MAPKKKK6 (or MAP4K6). MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase (MAPKKK or MAP3K or MKKK). Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. MAPK signaling cascades are important in mediating cellular responses to extracellular signals.


Pssm-ID: 173725 [Multi-domain]  Cd Length: 275  Bit Score: 68.07  E-value: 7.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 480 SGRYKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKPVNTQAKGLQLarrlfnlEAQSLEKLGSYQQIPQLL-AYFE 557
Cdd:cd06608   5 TGIFELVEVIGEGTYGKVYKARHKK---TGQLVaIKIMDIIEDEEEEIKE-------EYNILRKYSNHPNIATFYgAFIK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 558 Q-----EAEFYLVQEYIIGHP----LNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDH-KL 627
Cdd:cd06608  75 KnppgnDDQLWLVMELCGGGSvtdlVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTKNAEvKL 154

                ....*.
gi 75908330 628 VliDFG 633
Cdd:cd06608 155 V--DFG 158
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK ...
485-633 1.42e-12

Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). The family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine.


Pssm-ID: 240159  Cd Length: 155  Bit Score: 66.27  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 485 ILKVLGYGGFSETYIAEDTQRPgnpqcVVkqLKPVNTQAKGLQLARrlfnlEAQSLEKLGSYQ-QIPQLLAYFEQEAEFY 563
Cdd:cd05120   2 SIKLLKGGLTNRVYLLGTKDED-----YV--LKINPSREKGADRER-----EVAILQLLARKGlPVPKVLASGESDGWSY 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75908330 564 LVQEYIIGHPLNQElpsgksiSEAETVAIIREILEILVFVHE---NGVIHRDIKPSNIIrRHSDHKLVLIDFG 633
Cdd:cd05120  70 LLMEWIEGETLDEV-------SEEEKEDIAEQLAELLAKLHQlplLVLCHGDLHPGNIL-VDDGKILGIIDWE 134
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine ...
487-692 2.00e-12

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 1 (MEKK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The 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. MEKK1 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. MEKK1 activates the extracellular signal-regulated kinase 1/2 (ERK1/2) and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing.


Pssm-ID: 132961 [Multi-domain]  Cd Length: 268  Bit Score: 66.81  E-value: 2.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 487 KVLGYGGFSETYIAEDTQRpgNPQCVVKQLKPVNTQAKGLQLARRLFNLEAQSLEKLgSYQQIPQLLAYFEQEAEFYLVQ 566
Cdd:cd06630   6 QQLGTGAFSSCYQARDVKT--GTLMAVKQVTYVRNTSSEQEEVVEALRKEIRLMARL-NHPHIIRMLGATCEDSHFNLFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 567 EYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHKLVLIDFGAVKEIS--LPQAN 644
Cdd:cd06630  83 EWMAGGSVSHLLSKYGAFKEAVIINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLAakGTGAG 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75908330 645 N-QEPLpftigIGTKGYAPSE----QCFGRpqyNSDIYAVGMIGIKALTGIAP 692
Cdd:cd06630 163 EfQGQL-----LGTIAFMAPEvlrgEQYGR---SCDVWSVGCVIIEMATAKPP 207
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
482-695 2.17e-12

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: 66.50  E-value: 2.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDTQrpgNPQCV-VKQLKPVNTQAKGLQLARRLFNLeaqsLEKLgSYQQIPQLLAYFEQEA 560
Cdd:cd06627   1 NYQLGDLIGRGAFGVVYKGLNLE---TGDFVaIKQISLEKIKEEALKSIMQEIDL----LKNL-KHPNIVKYIGSIETSD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 561 EFYLVQEYIIGHPLNQEL-PSGKsISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDH-KLVliDFG-AVKe 637
Cdd:cd06627  73 SLYIILEYAENGSLRQIIkKFGP-FPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGVvKLA--DFGvATK- 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 638 islpqANNQEPLPFTIgIGTKGYAPSEQCFGRP-QYNSDIYAVGMIGIKALTGIAP-HDL 695
Cdd:cd06627 149 -----LNDVSKDDASV-VGTPYWMAPEVIEMSGaSTASDIWSLGCTVIELLTGNPPyYDL 202
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
549-736 3.24e-12

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: 66.00  E-value: 3.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 549 IPQLLAYFEQEAEFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLV 628
Cdd:cd05123  55 IVKLHYAFQTEEKLYLVLEYAPGGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENIL-LDADGHIK 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 629 LIDFGAVKEISlpqanNQEPLPFTIgIGTKGY-AP---SEQCFGrpqYNSDIYAVGMIGIKALTGIAPHdlpRDENEE-- 702
Cdd:cd05123 134 LTDFGLAKELS-----SEGSRTNTF-CGTPEYlAPevlLGKGYG---KAVDWWSLGVLLYEMLTGKPPF---YAEDRKei 201
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75908330 703 ----IKWRDK--ALVSQGFAQILSKMVREDFKQRYQSASA 736
Cdd:cd05123 202 yekiLKDPLRfpEFLSPEARDLISGLLQKDPTKRLGSGGA 241
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
489-692 3.25e-12

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: 66.10  E-value: 3.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 489 LGYGGFSETYIAEDtqRPGNPQCVVKQLKPVNTQAKGLQlaRRLFNlEAQSLEKLGSyQQIPQLLAYFEQEAEFYLVQEY 568
Cdd:cd05572   1 LGVGGFGRVELVKV--KSKNRTFALKCVKKRHIVETGQQ--EHIFS-EKEILEECNH-PFIVKLYRTFKDKKYIYMLMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 569 IIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrrhSDHK--LVLIDFGAVKEISLPQANnq 646
Cdd:cd05572  75 CLGGELWTILRDRGLFDEYTARFYIACVVLAFEYLHNRGIIYRDLKPENLL---LDSNgyVKLVDFGFAKKLKSGQKT-- 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75908330 647 eplpFTIgIGTKGYAPSEQCFGRpQYN--SDIYAVGMIGIKALTGIAP 692
Cdd:cd05572 150 ----WTF-CGTPEYVAPEIILNK-GYDfsVDYWSLGILLYELLTGRPP 191
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
552-691 3.70e-12

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; Serine/Threonine Kinases (STKs), Cyclin-dependent protein kinase like 1 (CDKL1) and CDKL4 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDKL1 and CDKL4 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. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown.


Pssm-ID: 173744 [Multi-domain]  Cd Length: 286  Bit Score: 66.24  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 552 LLAYFEQEAEFYLVQEYIiGHPLNQEL---PSGksISEAETVAIIREILEILVFVHENGVIHRDIKPSNI-IRRHSDHKL 627
Cdd:cd07847  65 LIEVFRRKRKLHLVFEYC-DHTVLNELeknPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENIlITKQGQIKL 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75908330 628 VliDFGAVKEISLPQANnqeplpFTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMIGIKALTGIA 691
Cdd:cd07847 142 C--DFGFARILTGPGDD------YTDYVATRWYRAPELLVGDTQYGPpvDVWAIGCVFAELLTGQP 199
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
483-696 4.49e-12

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


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 65.84  E-value: 4.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTqrPGNPQCVVKQLkpvntqakglQLARRLFNLEAQSLE-KLGSYQQIPQLLAY---FEQ 558
Cdd:cd06610   3 YELIEVIGVGATAVVYAAICL--PNNEKVAIKRI----------DLEKCQTSVDELRKEvQAMSQCNHPNVVKYytsFVV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 559 EAEFYLVQEYIIG----HPLNQELPSGkSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRrhSDHKLVLI-DFG 633
Cdd:cd06610  71 GDELWLVMPYLSGgsllDIMKSSYPRG-GLDEAIIATVLKEVLKGLEYLHSNGQIHRDIKAGNILL--GEDGSVKIaDFG 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75908330 634 AVKEISLPqANNQEPLPFTIgIGTKGY-APS--EQCFGrpqYNS--DIYAVGMIGIKALTGIAP-HDLP 696
Cdd:cd06610 148 VSASLADG-GDRTRKVRKTF-VGTPCWmAPEvmEQVHG---YDFkaDIWSFGITAIELATGAAPySKYP 211
STKc_PAK1 cd06654
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 1; Serine ...
523-693 4.62e-12

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


Pssm-ID: 132985 [Multi-domain]  Cd Length: 296  Bit Score: 66.29  E-value: 4.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 523 AKGLQLARRLFNLEAQSLEKL-------GSYQQIPQLLAYFEQEA---EFYLVQEYIIGHPLNqELPSGKSISEAETVAI 592
Cdd:cd06654  43 ATGQEVAIRQMNLQQQPKKELiineilvMRENKNPNIVNYLDSYLvgdELWVVMEYLAGGSLT-DVVTETCMDEGQIAAV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 593 IREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVKEISLPQANNQEPL--PFTIG---IGTKGYAPseqcf 667
Cdd:cd06654 122 CRECLQALEFLHSNQVIHRDIKSDNIL-LGMDGSVKLTDFGFCAQITPEQSKRSTMVgtPYWMApevVTRKAYGP----- 195
                       170       180
                ....*....|....*....|....*.
gi 75908330 668 grpqyNSDIYAVGMIGIKALTGIAPH 693
Cdd:cd06654 196 -----KVDIWSLGIMAIEMIEGEPPY 216
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
483-734 5.65e-12

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK2, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK 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. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis.


Pssm-ID: 173705 [Multi-domain]  Cd Length: 332  Bit Score: 66.51  E-value: 5.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQRP-GNPQCVVKQLK--PVNTQAKGLQLARRlfnlEAQSLEKLgsyQQIPQL--LAY-F 556
Cdd:cd05614   2 FELLKVLGTGAYGKVFLVRKVTGHdTGKLYAMKVLQkaALVQKAKTVEHTRT----ERNVLEHV---RQSPFLvtLHYaF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 557 EQEAEFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVK 636
Cdd:cd05614  75 QTEAKLHLILDYVSGGEMFTHLYQRDNFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENIL-LDSEGHVVLTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 637 EIslpqANNQEPLPFTIgIGTKGYAPSEQCFGRPQYNS--DIYAVGMIGIKALTGIAPHDLPRDENEEIKWRDKAL-VSQ 713
Cdd:cd05614 154 EF----LSEEKERTYSF-CGTIEYMAPEIIRGKGGHGKavDWWSLGILIFELLTGASPFTLEGERNTQSEVSRRILkCDP 228
                       250       260
                ....*....|....*....|....*....
gi 75908330 714 GFAQILS--------KMVREDFKQRYQSA 734
Cdd:cd05614 229 PFPSFIGpeaqdllhKLLRKDPKKRLGAG 257
STKc_MSK_N cd05583
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
483-730 9.46e-12

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK 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. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2.


Pssm-ID: 173674 [Multi-domain]  Cd Length: 288  Bit Score: 65.20  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAED-TQRPGNPQCVVKQLKP--VNTQAKGLQLARRlfnlEAQSLEKLgsyQQIPQL--LAY-F 556
Cdd:cd05583   2 FELLRVLGTGAYGKVFLVRKvGGHDAGKLYAMKVLKKatIVQKAKTAEHTRT----ERQVLEAV---RRCPFLvtLHYaF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 557 EQEAEFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHkLVLIDFGAVK 636
Cdd:cd05583  75 QTDTKLHLILDYVNGGELFTHLYQREHFTESEVRVYIAEIVLALDHLHQLGIIYRDIKLENILLDSEGH-VVLTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 637 EISLPqaNNQEPLPFTigiGTKGY-APSEQCFGRPQYNS--DIYAVGMIGIKALTGIAPHDLPRDENEEIKWRDKALVSQ 713
Cdd:cd05583 154 EFLAE--EEERAYSFC---GTIEYmAPEVIRGGSGGHDKavDWWSLGVLTFELLTGASPFTVDGEQNSQSEISRRILKSK 228
                       250
                ....*....|....*...
gi 75908330 714 -GFAQILSKMVReDFKQR 730
Cdd:cd05583 229 pPFPKTMSAEAR-DFIQK 245
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
483-730 1.04e-11

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK1, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK 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. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkappaB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MEK1 is associated with the development of cerebral ischemic/hypoxic preconditioning.


Pssm-ID: 173704 [Multi-domain]  Cd Length: 290  Bit Score: 65.02  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 483 YKILKVLGYGGFSETYIAEDTQRPGNPQC-VVKQLKPVN--TQAKGLQLARRlfnlEAQSLEKLgsyQQIPQL--LAY-F 556
Cdd:cd05613   2 FELLKVLGTGAYGKVFLVRKVSGHDSGKLyAMKVLKKATivQKAKTTEHTRT----ERQVLEHI---RQSPFLvtLHYaF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 557 EQEAEFYLVQEYIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHSDHkLVLIDFGAVK 636
Cdd:cd05613  75 QTDTKLHLILDYINGGELFTHLSQRERFKEQEVQIYSGEIVLALEHLHKLGIIYRDIKLENILLDSNGH-VVLTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 637 EISlpQANNQEPLPFTigiGTKGY-APSEQCFGRPQYNS--DIYAVGMIGIKALTGIAPHDLPRDENEEIKWRDKALVSQ 713
Cdd:cd05613 154 EFH--EDEVERAYSFC---GTIEYmAPDIVRGGDGGHDKavDWWSMGVLMYELLTGASPFTVDGEKNSQAEISRRILKSE 228
                       250
                ....*....|....*...
gi 75908330 714 -GFAQILSKMVReDFKQR 730
Cdd:cd05613 229 pPYPQEMSALAK-DIIQR 245
STKc_PAK_I cd06647
Catalytic domain of the Protein Serine/Threonine Kinase, Group I p21-activated kinase; Serine ...
561-693 1.53e-11

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


Pssm-ID: 132978 [Multi-domain]  Cd Length: 293  Bit Score: 64.54  E-value: 1.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 561 EFYLVQEYIIGHPLNqELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVKEISl 640
Cdd:cd06647  90 ELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNIL-LGMDGSVKLTDFGFCAQIT- 166
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75908330 641 PQANNQEPLpftigIGTKgYAPSEQCFGRPQYNS--DIYAVGMIGIKALTGIAPH 693
Cdd:cd06647 167 PEQSKRSTM-----VGTP-YWMAPEVVTRKAYGPkvDIWSLGIMAIEMVEGEPPY 215
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
482-682 2.39e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 3; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 3 (Nek3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek3 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. 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. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 63.45  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEdtQRPGNPQCVVKQLK-PVNTQAkgLQLARRlfnlEAQSLEKLgsyqQIPQLLAY---FE 557
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQ--HVNSDQKYAMKEIRlPKSSSA--VEDSRK----EAVLLAKM----KHPNIVAFkesFE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 558 QEAEFYLVQEYIIGHPLNQELP--SGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRHsDHKLVLIDFGAV 635
Cdd:cd08219  69 ADGHLYIVMEYCDGGDLMQKIKlqRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQ-NGKVKLGDFGSA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75908330 636 KEISLPQANNqeplpfTIGIGTKGYAPSEQCFGRPQYN-SDIYAVGMI 682
Cdd:cd08219 148 RLLTSPGAYA------CTYVGTPYYVPPEIWENMPYNNkSDIWSLGCI 189
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
482-688 3.09e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 1; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 1 (Nek1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek1 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. 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. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair.


Pssm-ID: 173758 [Multi-domain]  Cd Length: 256  Bit Score: 62.93  E-value: 3.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDtqRPGNPQCVVKQLKPVNTQAKGLQLARRlfnlEAQSLEKLgSYQQIPQLLAYFEQEAE 561
Cdd:cd08218   1 KYVKVKKIGEGSFGKAILVKS--KEDGKQYVIKEINISKMSPKEREESRK----EVAVLSNM-KHPNIVQYQESFEENGN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 562 FYLVQEYIIGHPLNQELPSGKSI--SEAETVAIIREILEILVFVHENGVIHRDIKPSNIIRRhSDHKLVLIDFGAVKEIs 639
Cdd:cd08218  74 LYIVMDYCEGGDLYKKINAQRGVlfPEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLT-KDGTIKLGDFGIARVL- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75908330 640 lpqaNNQEPLPFTIgIGTKGYAPSEQCFGRPQYN-SDIYAVGMIGIKALT 688
Cdd:cd08218 152 ----NSTVELARTC-IGTPYYLSPEICENRPYNNkSDIWALGCVLYEMCT 196
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
482-682 4.60e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; Serine/Threonine Kinases (STKs), Fungal Mitogen-Activated Protein Kinase (MAPK) MPK1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MPK1 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 the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MAPKs are important mediators of cellular responses to extracellular signals. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity (CWI) pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 63.58  E-value: 4.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 482 RYKILKVLGYGGFSETYIAEDTQRPGNPQCVVKqlKPVNTQAKGLqLARRLFNlEAQSLEKLGSYQQIPQL----LAYFE 557
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETSEEETVAIK--KITNVFSKKI-LAKRALR-ELKLLRHFRGHKNITCLydmdIVFPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75908330 558 QEAEFYLVQEyIIGHPLNQELPSGKSISEAETVAIIREILEILVFVHENGVIHRDIKPSNIIrRHSDHKLVLIDFGAVKE 637
Cdd:cd07857  77 NFNELYLYEE-LMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLL-VNADCELKICDFGLARG 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75908330 638 ISLPQANNQEPLpfTIGIGTKGYAPSEQCFGRPQYNS--DIYAVGMI 682
Cdd:cd07857 155 FSENPGENAGFM--TEYVATRWYRAPEIMLSFQSYTKaiDVWSVGCI 199
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
482-693 4.84e-11

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 cel