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Conserved domains on  [gi|86742726|ref|YP_483126|]
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hypothetical protein Francci3_4047 [Frankia sp. CcI3]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-273 1.36e-42

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


:

Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 156.59  E-value: 1.36e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  21 PYTVERKLvdAR--TGPVFLARNGE-ARPVLVKTITAPFGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVV 97
Cdd:cd14014   1 RYRLVRLL--GRggMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  98 AEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNP 176
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 177 GgppSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDLSVFCP----ELREL 251
Cdd:cd14014 159 G---SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPaAVLAKHLQEAPPPPSPLNPdvppALDAI 235
                       250       260
                ....*....|....*....|...
gi 86742726 252 VAAAMRKDPKRRP-AAAELLEQL 273
Cdd:cd14014 236 ILRALAKDPEERPqSAAELLAAL 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
539-834 3.38e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 106.65  E-value: 3.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 539 TGAIRDLLITPDGRYLIIVGDFGG-SVWNIIGPGRVRYITdlpavaaamGDRSPLaagvapaaavkglLAVALIPASgpa 617
Cdd:cd00200  51 TGPVRDVAASADGTYLASGSSDKTiRLWDLETGECVRTLT---------GHTSYV-------------SSVAFSPDG--- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 618 tgvrasTIMVTAGTDGVIRLWRlaqpgstddgdlqsaINTGQrvsLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRL 697
Cdd:cd00200 106 ------RILSSSSRDKTIKVWD---------------VETGK---CLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 698 WDIghpQNPRALAELPQP-AEVTSLAFTPDGDSLAVGGV-GHLSVWDvTAAGQPRrrAQLTA-PATVRKLLVSPDGRWLA 774
Cdd:cd00200 162 WDL---RTGKCVATLTGHtGEVNSVAFSPDGEKLLSSSSdGTIKLWD-LSTGKCL--GTLRGhENGVNSVAFSPDGYLLA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 775 vaSTSDGGSLtEIYGLDSPRGLHRLTAIASRpgqAGSIALSADGRVLAVSTPAGQVTLWD 834
Cdd:cd00200 236 --SGSEDGTI-RVWDLRTGECVQTLSGHTNS---VTSLAWSPDGKRLASGSADGTIRIWD 289
Pkinase pfam00069
Protein kinase domain;
22-271 2.06e-19

Protein kinase domain;


:

Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 88.84  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    22 YTVERKLVDARTGPVFLARN-GEARPVLVKTITAPfGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVVAEF 100
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHkGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   101 IDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGP 179
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGvVKIADFGL-----AKKLTKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   180 PSGI-GTLAFITPEQALGQT-ATVASDVftWG-GMLLFA-ATGRPPFGAGTPRVLLQRAV--------YAEPDLSVFCPE 247
Cdd:pfam00069 155 LTTFvGTPEYMAPEVLLGGNgYGPKVDV--WSlGVILYElLTGKPPFSGESILDQLQLIRrilgppleFDEPKSDSGSEE 232
                         250       260
                  ....*....|....*....|....
gi 86742726   248 LRELVAAAMRKDPKRRPAAAELLE 271
Cdd:pfam00069 233 AKDLIKKCLNKDPSKRPTAEEILQ 256
COG2319 COG2319
FOG: WD40 repeat [General function prediction only]
532-843 4.88e-19

FOG: WD40 repeat [General function prediction only]


:

Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 89.76  E-value: 4.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 532 IRQIGPATGAIRDLLITPDGRYLIIVGDFGGSV--WNIIGPGRVRYITDLPAVAAAMgDRSPLAAGVAPAAAVKGLLAVA 609
Cdd:COG2319 148 IRTLEGHSESVTSLAFSPDGKLLASGSSLDGTIklWDLRTGKPLSTLAGHTDPVSSL-AFSPDGGLLIASGSSDGTIRLW 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 610 LIPASGPATGVRA-------------STIMVTAGTDGVIRLWRLAQPGStddgdlqsaintgqrvsLLAELRGHTGAVAS 676
Cdd:COG2319 227 DLSTGKLLRSTLSghsdsvvssfspdGSLLASGSSDGTIRLWDLRSSSS-----------------LLRTLSGHSSSVLS 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 677 VAVSGDGRTLASAGADRVVRLWDIGHPQNPRALAELPQPAEVTSLAFTPDGDSLAVGGV--GHLSVWDVtaaGQPRRRAQ 754
Cdd:COG2319 290 VAFSPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKGHEGPVSSLSFSPDGSLLVSGGSddGTIRLWDL---RTGKPLKT 366
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 755 LTAPATVRKLLVSPDGRWLAVASTSDggsltEIYGLDSPRGLhRLTAIASRPGQAGSIALSADGRVLAVSTPAGQVTLWD 834
Cdd:COG2319 367 LEGHSNVLSVSFSPDGRVVSSGSTDG-----TVRLWDLSTGS-LLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWD 440

                ....*....
gi 86742726 835 MRSPSRPVQ 843
Cdd:COG2319 441 LKTSLKSVS 449
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-273 1.36e-42

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 156.59  E-value: 1.36e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  21 PYTVERKLvdAR--TGPVFLARNGE-ARPVLVKTITAPFGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVV 97
Cdd:cd14014   1 RYRLVRLL--GRggMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  98 AEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNP 176
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 177 GgppSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDLSVFCP----ELREL 251
Cdd:cd14014 159 G---SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPaAVLAKHLQEAPPPPSPLNPdvppALDAI 235
                       250       260
                ....*....|....*....|...
gi 86742726 252 VAAAMRKDPKRRP-AAAELLEQL 273
Cdd:cd14014 236 ILRALAKDPEERPqSAAELLAAL 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
539-834 3.38e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 106.65  E-value: 3.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 539 TGAIRDLLITPDGRYLIIVGDFGG-SVWNIIGPGRVRYITdlpavaaamGDRSPLaagvapaaavkglLAVALIPASgpa 617
Cdd:cd00200  51 TGPVRDVAASADGTYLASGSSDKTiRLWDLETGECVRTLT---------GHTSYV-------------SSVAFSPDG--- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 618 tgvrasTIMVTAGTDGVIRLWRlaqpgstddgdlqsaINTGQrvsLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRL 697
Cdd:cd00200 106 ------RILSSSSRDKTIKVWD---------------VETGK---CLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 698 WDIghpQNPRALAELPQP-AEVTSLAFTPDGDSLAVGGV-GHLSVWDvTAAGQPRrrAQLTA-PATVRKLLVSPDGRWLA 774
Cdd:cd00200 162 WDL---RTGKCVATLTGHtGEVNSVAFSPDGEKLLSSSSdGTIKLWD-LSTGKCL--GTLRGhENGVNSVAFSPDGYLLA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 775 vaSTSDGGSLtEIYGLDSPRGLHRLTAIASRpgqAGSIALSADGRVLAVSTPAGQVTLWD 834
Cdd:cd00200 236 --SGSEDGTI-RVWDLRTGECVQTLSGHTNS---VTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 pfam00400
WD domain, G-beta repeat;
662-699 3.59e-09

WD domain, G-beta repeat;


Pssm-ID: 249832  Cd Length: 39  Bit Score: 53.90  E-value: 3.59e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 86742726   662 SLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRLWD 699
Cdd:pfam00400   2 KLLRTLKGHTGPVTSVAFSPDGNLLASGSDDGTVRVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
662-699 9.57e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651  Cd Length: 40  Bit Score: 52.70  E-value: 9.57e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 86742726    662 SLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRLWD 699
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
97-164 5.39e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 44.13  E-value: 5.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86742726   97 VAEFIDAPTLAATVAGGaalsGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQGVRLVDFGL 164
Cdd:PRK14879  77 VMEYIEGEPLKDLINSN----GMEELELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGL 140
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
37-164 4.41e-04

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


Pssm-ID: 234331  Cd Length: 199  Bit Score: 41.05  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    37 FLARNGEA---------RPVLVKT-ITAPFgRDAEFRRRLRVD--------LDNIRRL---APsclaAILDLDTGARppY 95
Cdd:TIGR03724   1 LIAKGAEAiiylgdflgLKAVIKErVPKSY-RHPELDERIRRErtrnearlLSRARKAgvnTP----VVYDVDPDNK--T 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726    96 VVAEFIDAPTLAATVAggaalSGPDTYRLAVGLAtaLAALHELEIFLGDLKPINVVLSGQGVRLVDFGL 164
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIE-----EGNDELLREIGRL--VGKLHKAGIVHGDLTTSNIIVRDDKLYLIDFGL 135
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
63-164 3.82e-03

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 38.42  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  63 RRRLRVDLDNIRRL--APSCLAAILDLDTGARppYVVAEFIDAPTLAATVAGGAalsgPDTYRlAVGLATALaaLHELEI 140
Cdd:COG3642  43 RERTRREARILAKAreAGVPVPIVYDVDPDNG--LIVMEYIEGELLKDALEEAR----PDLLR-EVGRLVGK--LHKAGI 113
                        90       100
                ....*....|....*....|....
gi 86742726 141 FLGDLKPINVVLSGQGVRLVDFGL 164
Cdd:COG3642 114 VHGDLTTSNIILSGGRIYFIDFGL 137
Pkinase pfam00069
Protein kinase domain;
22-271 2.06e-19

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 88.84  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    22 YTVERKLVDARTGPVFLARN-GEARPVLVKTITAPfGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVVAEF 100
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHkGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   101 IDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGP 179
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGvVKIADFGL-----AKKLTKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   180 PSGI-GTLAFITPEQALGQT-ATVASDVftWG-GMLLFA-ATGRPPFGAGTPRVLLQRAV--------YAEPDLSVFCPE 247
Cdd:pfam00069 155 LTTFvGTPEYMAPEVLLGGNgYGPKVDV--WSlGVILYElLTGKPPFSGESILDQLQLIRrilgppleFDEPKSDSGSEE 232
                         250       260
                  ....*....|....*....|....
gi 86742726   248 LRELVAAAMRKDPKRRPAAAELLE 271
Cdd:pfam00069 233 AKDLIKKCLNKDPSKRPTAEEILQ 256
COG2319 COG2319
FOG: WD40 repeat [General function prediction only]
532-843 4.88e-19

FOG: WD40 repeat [General function prediction only]


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 89.76  E-value: 4.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 532 IRQIGPATGAIRDLLITPDGRYLIIVGDFGGSV--WNIIGPGRVRYITDLPAVAAAMgDRSPLAAGVAPAAAVKGLLAVA 609
Cdd:COG2319 148 IRTLEGHSESVTSLAFSPDGKLLASGSSLDGTIklWDLRTGKPLSTLAGHTDPVSSL-AFSPDGGLLIASGSSDGTIRLW 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 610 LIPASGPATGVRA-------------STIMVTAGTDGVIRLWRLAQPGStddgdlqsaintgqrvsLLAELRGHTGAVAS 676
Cdd:COG2319 227 DLSTGKLLRSTLSghsdsvvssfspdGSLLASGSSDGTIRLWDLRSSSS-----------------LLRTLSGHSSSVLS 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 677 VAVSGDGRTLASAGADRVVRLWDIGHPQNPRALAELPQPAEVTSLAFTPDGDSLAVGGV--GHLSVWDVtaaGQPRRRAQ 754
Cdd:COG2319 290 VAFSPDGKLLASGSSDGTVRLWDLETGKLLSSLTLKGHEGPVSSLSFSPDGSLLVSGGSddGTIRLWDL---RTGKPLKT 366
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 755 LTAPATVRKLLVSPDGRWLAVASTSDggsltEIYGLDSPRGLhRLTAIASRPGQAGSIALSADGRVLAVSTPAGQVTLWD 834
Cdd:COG2319 367 LEGHSNVLSVSFSPDGRVVSSGSTDG-----TVRLWDLSTGS-LLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWD 440

                ....*....
gi 86742726 835 MRSPSRPVQ 843
Cdd:COG2319 441 LKTSLKSVS 449
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
22-326 7.08e-18

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: 85.56  E-value: 7.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  22 YTVERKLVDARTGPVFLARNgeARPVLVKTITAPFGRDAEFRRRLRVDLDNIRRLA-PSCLAAILDLDTGARPPYVVAEF 100
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD--RKLVALKVLAKKLESKSKEVERFLREIQILASLNhPPNIVKLYDFFQDEGSLYLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 101 IDAPTLAATVA---GGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG--VRLVDFGLFRAM--NAVSI 173
Cdd:COG0515  80 VDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrvVKLIDFGLAKLLpdPGSTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 174 NNPGGPPSGIGTLAFITPEQALGQT---ATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAV--------------Y 236
Cdd:COG0515 160 SIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslaspL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 237 AEPDLSVFCPELRELVAAAMRKDPKRRPAAAELLEQLMAYPtRSEAEPAVEPTRRLALPAGVIETLVPVQTRRTVESETK 316
Cdd:COG0515 240 SPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAH-LKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSL 318
                       330
                ....*....|
gi 86742726 317 PEVVGTSDLA 326
Cdd:COG0515 319 AISGSDLKLD 328
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
128-271 2.91e-17

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 82.19  E-value: 2.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    128 LATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGPPSGIGTLAFITPEQALGQTATVASDVf 206
Cdd:smart00220 106 ILSALEYLHSKGIVHRDLKPENILLDEDGhVKLADFGL-----ARQLDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDI- 179
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86742726    207 tWG-GMLLFA-ATGRPPF-GAGTPRVLLQRAVYAEPDL----SVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:smart00220 180 -WSlGVILYElLTGKPPFpGDDQLLELFKKIGKPKPPFpppeWDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
47-275 1.48e-13

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 73.73  E-value: 1.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726     47 VLVKTITAPFGRDAEFRRRLRVDLDNIRRLAPSCLAAILDldTGARPP---YVVAEFIDAPTLAATVAGGAALSGPDTYR 123
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLD--SGEAPPgllFAVFEYVPGRTLREVLAADGALPAGETGR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    124 LAVGLATALAALHELEIFLGDLKPINVVLSGQGVR----LVDFGL------FRAMNAVSINNPGgppSGIGTLAFITPEQ 193
Cdd:TIGR03903   84 LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphakVLDFGIgtllpgVRDADVATLTRTT---EVLGTPTYCAPEQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726    194 ALGQTATVASDVFTWGGMLLFAATGRPPF-GAGTPRVLLQRAVYAEPDL--SVFCPELRELVAAAMRKDPKRRPAAAELL 270
Cdd:TIGR03903  161 LRGEPVTPNSDLYAWGLIFLECLTGQRVVqGASVAEILYQQLSPVDVSLppWIAGHPLGQVLRKALNKDPRQRAASAPAL 240

                   ....*
gi 86742726    271 EQLMA 275
Cdd:TIGR03903  241 AERFR 245
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
96-295 1.65e-09

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 59.45  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   96 VVAEFIDAPTLAAT-VAGGAALSGpdtyrLAVGLATALAALHELEIFLGDLKPINVVL-SGQGVRLVDFGLFRAMNAVSi 173
Cdd:PLN00034 149 VLLEFMDGGSLEGThIADEQFLAD-----VARQILSGIAYLHRRHIVHRDIKPSNLLInSAKNVKIADFGVSRILAQTM- 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  174 nNPGGppSGIGTLAFITPEQA-----LGQTATVASDVFTWGGMLLFAATGRPPFGAGTP---RVLLQRAVYAEPDLS--V 243
Cdd:PLN00034 223 -DPCN--SSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQgdwASLMCAICMSQPPEApaT 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 86742726  244 FCPELRELVAAAMRKDPKRRPAAAELLEQ-LMAYPTRSEAEPAVEPTRRLALP 295
Cdd:PLN00034 300 ASREFRHFISCCLQREPAKRWSAMQLLQHpFILRAQPGQGQGGPNLHQLLPPP 352
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
131-270 2.50e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 56.03  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGlFRAMNAVSINNPGGPpSGIGTLAFITPEQALGQTATVASDVFTWG 209
Cdd:PTZ00283 155 AVHHVHSKHMIHRDIKSANILLCSNGlVKLGDFG-FSKMYAATVSDDVGR-TFCGTPYYVAPEIWRRKPYSKKADMFSLG 232
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86742726  210 GMLLFAATGRPPFGAGTPRVLLQRAVYA--EPDLSVFCPELRELVAAAMRKDPKRRPAAAELL 270
Cdd:PTZ00283 233 VLLYELLTLKRPFDGENMEEVMHKTLAGryDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
PTZ00421 PTZ00421
coronin; Provisional
623-700 1.61e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.73  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  623 STIMVTAGTDGVIRLWRLAQPGstddgdLQSAINtgqrvSLLAELRGHTGAVASVAV--SGDGrTLASAGADRVVRLWDI 700
Cdd:PTZ00421  88 PQKLFTASEDGTIMGWGIPEEG------LTQNIS-----DPIVHLQGHTKKVGIVSFhpSAMN-VLASAGADMVVNVWDV 155
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
662-824 2.17e-04

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 255877 [Multi-domain]  Cd Length: 344  Bit Score: 42.98  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   662 SLLAELRGHTGAVASVAVSGDGRTLASA----GADRVVRLWDIGHPQNPRALA------------ELPQPAEVTslaFTP 725
Cdd:pfam10282  76 TLLNQVPTGGASPCHLSVDPDGRFLFVAnyggGSVSVYPLDADGSLGEASQVVqhegsgpnperqEGPHAHSVV---FDP 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   726 DGDSLAVG--GVGHLSVWDVTAAGqprrrAQLTAPATV--------RKLLVSPDGRWLAVASTSDGgSLTeIYGLDSPRG 795
Cdd:pfam10282 153 DGKFLVVPdlGTDRVRVYRLDDAG-----GKLTPPASVktppgsgpRHLVFHPDGKYAYVVNELSS-TVT-VLSYDPATG 225
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 86742726   796 -LHRLTAIASRPG------QAGSIALSADGRVLAVS 824
Cdd:pfam10282 226 tFTELQTVSTLPEdftgtnGAAAIRISPDGRFLYVS 261
tolB PRK02889
translocation protein TolB; Provisional
704-819 2.63e-04

translocation protein TolB; Provisional


Pssm-ID: 235083 [Multi-domain]  Cd Length: 427  Bit Score: 43.05  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  704 QNPRALAELPQPaeVTSLAFTPDGDSLAvggvgHLS---------VWDVtAAGQPRRRAQL----TAPATvrkllvSPDG 770
Cdd:PRK02889 186 QNAQSALSSPEP--IISPAWSPDGTKLA-----YVSfeskkpvvyVHDL-ATGRRRVVANFkgsnSAPAW------SPDG 251
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 86742726  771 RWLAVASTSDGGSltEIYGLDSP-RGLHRLTaiasrpgQAGSI----ALSADGR 819
Cdd:PRK02889 252 RTLAVALSRDGNS--QIYTVNADgSGLRRLT-------QSSGIdtepFFSPDGR 296
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
674-846 8.30e-04

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear [Transport and binding proteins, Other, Cellular processes, Pathogenesis].


Pssm-ID: 234019 [Multi-domain]  Cd Length: 417  Bit Score: 41.48  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   674 VASVAVSGDGR--TLASAGADrvvrlwdiGHpqNPRALAELPQPaeVTSLAFTPDGDSLA----VGGVGHLSVWDVtaag 747
Cdd:TIGR02800 158 IAYVSKSGKGRryELQVADYD--------GA--NPQTITRSREP--ILSPAWSPDGQKLAyvsfESGKPEIYVQDL---- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726   748 QPRRRAQLT-------APAtvrkllVSPDGRWLAVASTSDGGSltEIYGLD-SPRGLHRLT---AIASRPgqagsiALSA 816
Cdd:TIGR02800 222 ATGQREKVAsfpgmngAPA------FSPDGSKLAVSLSKDGNP--DIYVMDlDGKQLTRLTngpGIDTEP------SWSP 287
                         170       180       190
                  ....*....|....*....|....*....|.
gi 86742726   817 DGRVLA-VSTPAGQVTLWDMRSPSRPVQRAT 846
Cdd:TIGR02800 288 DGKSIAfTSDRGGSPQIYMMDADGGEARRLT 318
pknD PRK13184
serine/threonine-protein kinase; Reviewed
144-276 4.65e-03

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 39.37  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  144 DLKPINVVLSGQG-VRLVDFGLFRAMNA-------VSINNPGG-------PPSGIGTLAFITPEQALGQTATVASDVFTW 208
Cdd:PRK13184 138 DLKPDNILLGLFGeVVILDWGAAIFKKLeeedlldIDVDERNIcyssmtiPGKIVGTPDYMAPERLLGVPASESTDIYAL 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86742726  209 GGMLLFAATGRPPFGAGTPRVLLQRAVYAEP-DLSVF---CPELRELVAAAMRKDPKRRPAAA-ELLEQLMAY 276
Cdd:PRK13184 218 GVILYQMLTLSFPYRRKKGRKISYRDVILSPiEVAPYreiPPFLSQIAMKALAVDPAERYSSVqELKQDLEPH 290
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-273 1.36e-42

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 156.59  E-value: 1.36e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  21 PYTVERKLvdAR--TGPVFLARNGE-ARPVLVKTITAPFGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVV 97
Cdd:cd14014   1 RYRLVRLL--GRggMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  98 AEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNP 176
Cdd:cd14014  79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 177 GgppSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDLSVFCP----ELREL 251
Cdd:cd14014 159 G---SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPaAVLAKHLQEAPPPPSPLNPdvppALDAI 235
                       250       260
                ....*....|....*....|...
gi 86742726 252 VAAAMRKDPKRRP-AAAELLEQL 273
Cdd:cd14014 236 ILRALAKDPEERPqSAAELLAAL 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
539-834 3.38e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 106.65  E-value: 3.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 539 TGAIRDLLITPDGRYLIIVGDFGG-SVWNIIGPGRVRYITdlpavaaamGDRSPLaagvapaaavkglLAVALIPASgpa 617
Cdd:cd00200  51 TGPVRDVAASADGTYLASGSSDKTiRLWDLETGECVRTLT---------GHTSYV-------------SSVAFSPDG--- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 618 tgvrasTIMVTAGTDGVIRLWRlaqpgstddgdlqsaINTGQrvsLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRL 697
Cdd:cd00200 106 ------RILSSSSRDKTIKVWD---------------VETGK---CLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 698 WDIghpQNPRALAELPQP-AEVTSLAFTPDGDSLAVGGV-GHLSVWDvTAAGQPRrrAQLTA-PATVRKLLVSPDGRWLA 774
Cdd:cd00200 162 WDL---RTGKCVATLTGHtGEVNSVAFSPDGEKLLSSSSdGTIKLWD-LSTGKCL--GTLRGhENGVNSVAFSPDGYLLA 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 775 vaSTSDGGSLtEIYGLDSPRGLHRLTAIASRpgqAGSIALSADGRVLAVSTPAGQVTLWD 834
Cdd:cd00200 236 --SGSEDGTI-RVWDLRTGECVQTLSGHTNS---VTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
623-881 5.25e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 100.10  E-value: 5.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 623 STIMVTAGTDGVIRLWRLaqpgstddgdlqsaiNTGQrvsLLAELRGHTGAVASVAVSGDGRTLASAGADRVVRLWDIgh 702
Cdd:cd00200  21 GKLLATGSGDGTIKVWDL---------------ETGE---LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 703 pQNPRALAELPQ-PAEVTSLAFTPDGDSLAVGGV-GHLSVWDVTAAGQprRRAQLTAPATVRKLLVSPDGRwLAVASTSD 780
Cdd:cd00200  81 -ETGECVRTLTGhTSYVSSVAFSPDGRILSSSSRdKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPDGT-FVASSSQD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 781 GgsLTEIYGLDSPRGLHRLTAiasRPGQAGSIALSADGRVLAVSTPAGQVTLWDMRSPSrpvQRATLPVGTAP-TATVFG 859
Cdd:cd00200 157 G--TIKLWDLRTGKCVATLTG---HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK---CLGTLRGHENGvNSVAFS 228
                       250       260
                ....*....|....*....|...
gi 86742726 860 PLGHegVLAVVAGD-AVRLWQLD 881
Cdd:cd00200 229 PDGY--LLASGSEDgTIRVWDLR 249
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
614-879 2.08e-22

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 98.18  E-value: 2.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 614 SGPATGVRA---STIMVTAGTDGVIRLWRLaqpgstddgdlqsaiNTGQRVSllaELRGHTGAVASVAVSGDGRTLASAG 690
Cdd:cd00200  51 TGPVRDVAAsadGTYLASGSSDKTIRLWDL---------------ETGECVR---TLTGHTSYVSSVAFSPDGRILSSSS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 691 ADRVVRLWDIghpQNPRALAELP-QPAEVTSLAFTPDGDSLAVGGV-GHLSVWDVTAAgqpRRRAQLTAP-ATVRKLLVS 767
Cdd:cd00200 113 RDKTIKVWDV---ETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQdGTIKLWDLRTG---KCVATLTGHtGEVNSVAFS 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 768 PDGRWLAVAStSDGgSLTeIYGLDSPRGLHRLTaiaSRPGQAGSIALSADGRVLAVSTPAGQVTLWDMRSPsRPVQraTL 847
Cdd:cd00200 187 PDGEKLLSSS-SDG-TIK-LWDLSTGKCLGTLR---GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQ--TL 257
                       250       260       270
                ....*....|....*....|....*....|....
gi 86742726 848 PVGTAP-TATVFGPLGheGVLAVVAGDA-VRLWQ 879
Cdd:cd00200 258 SGHTNSvTSLAWSPDG--KRLASGSADGtIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
663-881 1.23e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 86.62  E-value: 1.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 663 LLAELRGHTGAVASVAVSGDGRTLASAGADRVVRLWDIGHPQNPRALAELPQPaeVTSLAFTPDGDSLAVGGVGH-LSVW 741
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGP--VRDVAASADGTYLASGSSDKtIRLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 742 DVTaaGQPRRRAQLTAPATVRKLLVSPDGRWLavASTSDGGSLTeIYGLDSPRGLHRLTAIasrPGQAGSIALSADGRVL 821
Cdd:cd00200  79 DLE--TGECVRTLTGHTSYVSSVAFSPDGRIL--SSSSRDKTIK-VWDVETGKCLTTLRGH---TDWVNSVAFSPDGTFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86742726 822 AVSTPAGQVTLWDMRSpSRPVQRATLPVGTAPTATVFGPLGHegvLAVVAGD-AVRLWQLD 881
Cdd:cd00200 151 ASSSQDGTIKLWDLRT-GKCVATLTGHTGEVNSVAFSPDGEK---LLSSSSDgTIKLWDLS 207
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
36-273 1.97e-18

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation 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 more than 500 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. 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.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 85.01  E-value: 1.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  36 VFLARNGEA-RPVLVKTItaPFGRDAEFRRRLRVDLDNIRRLAPSCLAAILDLDTGARPPYVVAEFIDAPTLAATVA-GG 113
Cdd:cd00180   9 VYKARDKETgKKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKeNK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 114 AALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNPGGPpsGIGTLAFITPE 192
Cdd:cd00180  87 GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGtVKLADFGLAKDLDSDDSLLKTTG--GTTPPYYAPPE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 193 QALGQTATVASDVftWG-GMLLFAatgrppfgagtprvllqravyaepdlsvfCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd00180 165 LLGGRYYGPKVDI--WSlGVILYE-----------------------------LEELKDLIRRMLQYDPKKRPSAKELLE 213

                ..
gi 86742726 272 QL 273
Cdd:cd00180 214 HL 215
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
34-271 4.10e-18

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 84.95  E-value: 4.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  34 GPVFLARN-GEARPVLVKTItaPFGRDAEFRRRLRVDLDNIRRlAPS-----CLAAILDldtgARPPYVVAEFIDAPTLA 107
Cdd:cd06623  15 GVVYKVRHkPTGKIYALKKI--HVDGDEEFRKQLLRELKTLRS-CESpyvvkCYGAFYK----EGEISIVLEYMDGGSLA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 108 ATVAGGAALSGPDTYRLAVGLATALAALH-ELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNavsiNNPGGPPSGIGT 185
Cdd:cd06623  88 DLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGeVKIADFGISKVLE----NTLDQCNTFVGT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 186 LAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPF---GAGTPRVLLQRAVYAE-PDL--SVFCPELRELVAAAMRKD 259
Cdd:cd06623 164 VTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFlppGQPSFFELMQAICDGPpPSLpaEEFSPEFRDFISACLQKD 243
                       250
                ....*....|..
gi 86742726 260 PKRRPAAAELLE 271
Cdd:cd06623 244 PKKRPSAAELLQ 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
123-281 4.45e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 84.70  E-value: 4.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 123 RLAVGLATALAALHE-LEIFLGDLKPINVVLSGQG-VRLVDFGlframnaVS---INNPGGppSGIGTLAFITPEQALGQ 197
Cdd:cd06605 103 KIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGqVKLCDFG-------VSgqlVDSLAK--TFVGTRSYMAPERISGG 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 198 TATVASDVFTWGGMLLFAATGRPPF------GAGTPRVLLQRAVYAEPDL---SVFCPELRELVAAAMRKDPKRRPAAAE 268
Cdd:cd06605 174 KYTVKSDIWSLGLSLVELATGRFPYpppnakPSMMIFELLSYIVDEPPPLlpsGKFSPDFQDFVSQCLQKDPTERPSYKE 253
                       170
                ....*....|...
gi 86742726 269 LLEqlMAYPTRSE 281
Cdd:cd06605 254 LME--HPFIKRYE 264
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
34-276 1.24e-17

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 83.26  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  34 GPVFLARnGEARPVLVKTITAPFGRDA---EFRRRLRVDLDNIRRLAPSClaaildldTGARPPYVVAEFIDAPTLAATV 110
Cdd:cd14058   7 GVVCKAR-WRNQIVAVKIIESESEKKAfevEVRQLSRVDHPNIIKLYGAC--------SNQKPVCLVMEYAEGGSLYNVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 111 AGgaalSGPD---TYRLAVG----LATALAALHELE---IFLGDLKPINVVLSGQG--VRLVDFGLFRAMNAVSINNPGg 178
Cdd:cd14058  78 HG----KEPKpiyTAAHAMSwalqCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGtvLKICDFGTACDISTHMTNNKG- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 179 ppsgigTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPF-GAGTPRVLLQRAVY--AEPDLSVFCPE-LRELVAA 254
Cdd:cd14058 153 ------SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdHIGGPAFRIMWAVHngERPPLIKNCPKpIESLMTR 226
                       250       260
                ....*....|....*....|....*
gi 86742726 255 AMRKDPKRRPAAAEL---LEQLMAY 276
Cdd:cd14058 227 CWSKDPEKRPSMKEIvkiMSHLMQF 251
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
132-272 1.51e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or 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. The MAP3K8 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.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 73.50  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 132 LAALHELEIFLGDLKPINVVLSGQGVRLVDFGLFRAMNavsiNNPGGPPSGIGTLAFITPEQALGQTATVASDVFTWGGM 211
Cdd:cd13995 109 LDFLHSKNIIHHDIKPSNIVFMSTKAVLVDFGLSVQMT----EDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGAT 184
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726 212 LLFAATGRPPFGAGTPRVLLQRAVY-----AEP--DLSVFC-PELRELVAAAMRKDPKRRPAAAELLEQ 272
Cdd:cd13995 185 IIHMQTGSPPWVRRYPRSAYPSYLYiihkqAPPleDIAQDCsPAMRELLEAALERNPNHRSSAAELLKH 253
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
123-272 1.54e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 73.76  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 123 RLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAM-NAVSinnpggpPSGIGTLAFITPEQALGQTAT 200
Cdd:cd06619  99 RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGqVKLCDFGVSTQLvNSIA-------KTYVGTNAYMAPERISGEQYG 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 201 VASDVFTWGGMLLFAATGRPPF-------GAGTPRVLLQRAVYAEPDL---SVFCPELRELVAAAMRKDPKRRPAAAELL 270
Cdd:cd06619 172 IHSDVWSLGISFMELALGRFPYpqiqknqGSLMPLQLLQCIVDEDPPVlpvGQFSEKFVHFITQCMRKQPKERPAPENLM 251

                ..
gi 86742726 271 EQ 272
Cdd:cd06619 252 DH 253
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
95-271 3.16e-14

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 72.96  E-value: 3.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFIDAPTLAATVAGGAALSGPD-------TYRLAVGLATALaalHELEIFLGDLKPINVVLSGQG-VRLVDFGLFR 166
Cdd:cd06622  75 YMCMEYMDAGSLDKLYAGGVATEGIPedvlrriTYAVVKGLKFLK---EEHNIIHRDVKPTNVLVNGNGqVKLCDFGVSG 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 167 AMNAvSINNpggppSGIGTLAFITPEQALGQTA------TVASDVFTWGGMLLFAATGR---PPFGAGTPRVLLQRAVYA 237
Cdd:cd06622 152 NLVA-SLAK-----TNIGCQSYMAPERIKSGGPnqnptyTVQSDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVDG 225
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 86742726 238 EPDL--SVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd06622 226 DPPTlpSGYSDDAQDFVAKCLNKIPNRRPTYAQLLE 261
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
130-271 1.11e-13

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 70.69  E-value: 1.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 130 TALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGPPSGIGTLAFITPEQALGQTATVASDVFTW 208
Cdd:cd05122 109 KGLEYLHSHGIIHRDIKAANILLTSDGeVKLIDFGL-----SAQLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSL 183
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86742726 209 GGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDL---SVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd05122 184 GITAIEMAEGKPPYSELPPmKALFLIATNGPPGLrnpKKWSKEFKDFLKKCLQKDPEKRPTAEQLLK 250
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
128-271 1.35e-13

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora 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.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 70.58  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQGV-RLVDFGLframnavSINNPGGPPSGI-GTLAFITPEQALGQTATVASDV 205
Cdd:cd14007 109 LALALDYLHSKNIIHRDIKPENILLGSNGElKLADFGW-------SVHAPSNRRKTFcGTLDYLPPEMVEGKEYDYKVDI 181
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726 206 ftWG-GMLLFA-ATGRPPFGAGTPRVLLQRAVYAEPDL-SVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd14007 182 --WSlGVLCYElLVGKPPFESKSHQETYKRIQNVDIKFpSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
131-271 1.60e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 70.24  E-value: 1.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNavSINNPGGPPSGIGTLAFITPEQALGQTATVASDVFTWG 209
Cdd:cd06606 111 GLEYLHSNGIVHRDIKGANILVDSDGvVKLADFGCAKRLA--EIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLG 188
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726 210 GMLLFAATGRPPFGAGTPRV-LLQRAVYAE------PDLSvfcPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd06606 189 CTVIEMATGKPPWSELGNPVaALFKIGSSGepppipEHLS---EEAKDFLRKCLQRDPKKRPTADELLQ 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
128-272 1.82e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 70.18  E-value: 1.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMN-----AVSInnpggppsgIGTLAFITPEQALGQTATV 201
Cdd:cd08215 112 ICLALKYLHSRKILHRDLKTQNIFLTKDGvVKLGDFGISKVLEsttdlAKTV---------VGTPYYLSPELCENKPYNY 182
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86742726 202 ASDVftWG-GMLLFA-ATGRPPFGAGTPRVLLQRAVYAE--PDLSVFCPELRELVAAAMRKDPKRRPAAAELLEQ 272
Cdd:cd08215 183 KSDI--WAlGCVLYElCTLKHPFEANNLPALVYKIVKGQypPIPSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
116-273 3.45e-13

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or 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. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 69.10  E-value: 3.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 116 LSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNavsiNNPGGPPSGIGTLAFITPEQA 194
Cdd:cd13999  88 LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFtVKIADFGLSRIKN----STTEKMTGVVGTPRWMAPEVL 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 195 LGQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVY--AEPDLSVFCP-ELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd13999 164 RGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQkgLRPPIPPDCPpELSKLIKRCWNEDPEKRPSFSEIVK 243

                ..
gi 86742726 272 QL 273
Cdd:cd13999 244 RL 245
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
116-272 4.11e-13

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 69.68  E-value: 4.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 116 LSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLfRAMNAVSINNPGgppSGIGTLAFITPEQA 194
Cdd:cd06644 107 LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGdIKLADFGV-SAKNVKTLQRRD---SFIGTPYWMAPEVV 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 195 LGQTATVA-----SDVFTWGGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDL---SVFCPELRELVAAAMRKDPKRRPA 265
Cdd:cd06644 183 MCETMKDTpydykADIWSLGITLIEMAQIEPPHHELNPmRVLLKIAKSEPPTLsqpSKWSMEFRDFLKTALDKHPETRPS 262

                ....*..
gi 86742726 266 AAELLEQ 272
Cdd:cd06644 263 AAQLLEH 269
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
131-277 4.70e-13

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), 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 like in MASTL, also contains an insert relative to MAST kinases. 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. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 69.17  E-value: 4.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRA--------MNAVSINNPGGPP---SGIGTLAFITPEQALGQT 198
Cdd:cd05579 105 ALEYLHSHGIIHRDLKPDNILIDANGhLKLTDFGLSKVglvrrqikLSIQKKSNGAPEKedrRIVGTPDYLAPEILLGQG 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 199 ATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQR---AVYAEPDLSVFCPELRELVAAAMRKDPKRRPaAAELLEQLMA 275
Cdd:cd05579 185 HGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNilnGKIEWPEDPEVSDEAKDLISKLLTPDPEKRL-GAKGIEEIKN 263

                ..
gi 86742726 276 YP 277
Cdd:cd05579 264 HP 265
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
20-271 5.87e-13

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 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.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 68.66  E-value: 5.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  20 GPYTVERKLVDARTGPVFlarngeARPVLVKTITAPFGRDAE-FRRRLRVdldnIRRLAPSCLAAILDLDTGARPPYVVA 98
Cdd:cd14098  11 GTFAEVKKAVEVETGKMR------AIKQIVKRKVAGNDKNLQlFQREINI----LKSLEHPGIVRLIDWYEDDQHIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  99 EFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQGVRLV---DFGLFRAMNAVSINN 175
Cdd:cd14098  81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVkisDFGLAKVIHTGTFLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 176 pggppSGIGTLAFITPEQALGQTATVAS------DVFTWGGMLLFAATGRPPFGAGTPRVLLQ---RAVYAEPDLSVF-- 244
Cdd:cd14098 161 -----TFCGTMAYLAPEILMSKEQNLQGgysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKrirKGRYTQPPLVDFni 235
                       250       260
                ....*....|....*....|....*..
gi 86742726 245 CPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd14098 236 SEEAIDFILRLLDVDPEKRMTAAQALD 262
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
95-272 6.98e-13

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 68.19  E-value: 6.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFIDAPTLAATVAGGAALSGP----DTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMN 169
Cdd:cd08530  75 CIVMEYAPFGDLSKLISKRKKKRRLfpedDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDlVKIGDLGISKVLK 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 170 AVSINnpggppSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAV--YAEPDLSVFCPE 247
Cdd:cd08530 155 KNLAK------TQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCrgKFPPIPPVYSQD 228
                       170       180
                ....*....|....*....|....*
gi 86742726 248 LRELVAAAMRKDPKRRPAAAELLEQ 272
Cdd:cd08530 229 LQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
61-274 7.33e-13

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK 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.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 68.45  E-value: 7.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  61 EFRRRLRVDL----DNIRRLAPSCLaaildldtGARPPYVVAEFIDAPTLAAT---VAGGAALSGPDTYRLAVGLATALA 133
Cdd:cd14066  36 EFLTELEMLGrlrhPNLVRLLGYCL--------ESDEKLLVYEYMPNGSLEDRlhcHKGSPPLPWPQRLKIAKGIARGLE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 134 ALHE---LEIFLGDLKPINVVLSGQGV-RLVDFGLFRAMNAVSINNPGGPPSGigTLAFITPEQALGQTATVASDVFTWG 209
Cdd:cd14066 108 YLHEecpPPIIHGDIKSSNILLDEDFEpKLTDFGLARLIPPSESVSKTSAVKG--TIGYLAPEYIRTGRVSTKSDVYSFG 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 210 GMLLFAATGRPPFGAGTP--------------------RVLLQRAVYAEPDLSVFCPELRELVAAAMRKDPKRRPAAAEL 269
Cdd:cd14066 186 VVLLELLTGKPAVDENREnasrkdlvewveskgkeeleDILDKRLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEV 265

                ....*
gi 86742726 270 LEQLM 274
Cdd:cd14066 266 VQMLE 270
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
128-277 9.86e-13

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. 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. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 67.93  E-value: 9.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGL-----FRAMNAVSInnpggppsgIGTLAFITPEQALGQTATV 201
Cdd:cd05123 102 IVLALEYLHSLGIIYRDLKPENILLDSDGhIKLTDFGLakelsSDGDRTYTF---------CGTPEYLAPEVLLGKGYGK 172
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86742726 202 ASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYAEPDLSVFC-PELRELVAAAMRKDPKRRPAAAElLEQLMAYP 277
Cdd:cd05123 173 AVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVsPEAKSLISGLLQKDPTKRLGSGG-AEEIKAHP 248
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
123-271 2.07e-12

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 67.45  E-value: 2.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 123 RLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGlframnaVS---INNPGGppSGIGTLAFITPEQALGQT 198
Cdd:cd06621 109 KIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGqVKLCDFG-------VSgelVNSLAG--TFTGTSYYMAPERIQGGP 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 199 ATVASDVFTWGGMLLFAATGRPPFGA-GTPRV----LLQRAVYA-------EPDLSVFCPE-LRELVAAAMRKDPKRRPA 265
Cdd:cd06621 180 YSITSDVWSLGLTLLEVAQNRFPFPPeGEPPLgpieLLSYIVNMpnpelkdEPENGIKWSEsFKDFIEKCLEKDGTRRPG 259

                ....*.
gi 86742726 266 AAELLE 271
Cdd:cd06621 260 PWQMLA 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
128-277 2.98e-12

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 66.85  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNPGG-------------PPSGIGTLAFITPEQ 193
Cdd:cd05581 110 IVLALEYLHSKGIIHRDLKPENILLDEDMhIKITDFGTAKVLGPDSSPESTKgdadsqiaynqarAASFVGTAEYVSPEL 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 194 ALGQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYAEPDLSVFCPEL-RELVAAAMRKDPKRRPAAAEL--L 270
Cdd:cd05581 190 LNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPENFPPDaKDLIQKLLVLDPSKRLGVNENggY 269

                ....*..
gi 86742726 271 EQLMAYP 277
Cdd:cd05581 270 DELKAHP 276
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
123-270 3.79e-12

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 66.69  E-value: 3.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 123 RLAVGLATALAALH-ELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAM-NAVSinnpggpPSGIGTLAFITPEQALGQTA 199
Cdd:cd06620 108 KIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGqIKLCDFGVSGELiNSIA-------DTFVGTSTYMSPERIQGGKY 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 200 TVASDVFTWGGMLLFAATGRPPFGAGTPRV-----------LLQRAVYAE----PDLSVFCPELRELVAAAMRKDPKRRP 264
Cdd:cd06620 181 SVKSDVWSLGLSIIELALGEFPFAGSNDDDdgyngpmgildLLQRIVNEPpprlPKDRIFPKDLRDFVDRCLLKDPRERP 260

                ....*.
gi 86742726 265 AAAELL 270
Cdd:cd06620 261 SPQLLL 266
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
95-271 5.98e-12

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 65.79  E-value: 5.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQGV-RLVDFGlframNAVSI 173
Cdd:cd06626  75 YIFMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLiKLGDFG-----SAVKL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 174 NNPGGPPSG------IGTLAFITPEQALGQTAT---VASDVFTWGGMLLFAATGRPPF-------------GAGTPRVLl 231
Cdd:cd06626 150 KNNTTTMAPgevnslVGTPAYMAPEVITGNKGEghgRAADIWSLGCVVLEMATGKRPWseldnewaimyhvGMGHKPPI- 228
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86742726 232 qravyaePDLSVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd06626 229 -------PDSLQLSPEGKDFLSRCLESDPKKRPTASELLD 261
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
95-272 6.36e-12

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part 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 STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 65.37  E-value: 6.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFIDAPTLAA----TVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMN 169
Cdd:cd08224  76 NIVLELADAGDLSRlikhFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGvVKLGDLGLGRFFS 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 170 AVSInnpgGPPSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTPR--VLLQRAVYAE-PDLS--VF 244
Cdd:cd08224 156 SKTT----AAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEyPPLPadLY 231
                       170       180
                ....*....|....*....|....*...
gi 86742726 245 CPELRELVAAAMRKDPKRRPAAAELLEQ 272
Cdd:cd08224 232 SQELRDLVAACIQPDPEKRPDISYVLDV 259
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
45-273 9.82e-12

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos 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.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 65.10  E-value: 9.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  45 RPVLVKTI---TAPFGRDAEFRRRL---RVDLDNIRRLapscLAAILDLDtGARPPYVVAEFIDAPTLAATVAGGA-ALS 117
Cdd:cd13979  27 ETVAVKIVrrrRKNRASRQSFWAELnaaRLRHENIVRV----LAAETGTD-FASLGLIIMEYCGNGTLQQLIYEGSePLP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 118 GPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQGV-RLVDFGLFRAMNAVsiNNPGGPPSGI-GTLAFITPEQAL 195
Cdd:cd13979 102 LAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVcKLCDFGCSVKLGEG--NEVGTPRSHIgGTYTYRAPELLK 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 196 GQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYA-EPDL-----SVFCPELRELVAAAMRKDPKRRP-AAAE 268
Cdd:cd13979 180 GERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDlRPDLsgledSEFGQRLRSLISRCWSAQPAERPnADES 259

                ....*
gi 86742726 269 LLEQL 273
Cdd:cd13979 260 LLKSL 264
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
112-263 1.39e-11

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 64.86  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 112 GGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGPPSGIGTLAFIT 190
Cdd:cd05577  88 GTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGhVRISDLGL-----AVEFKGGKKIKGRVGTHGYMA 162
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726 191 PEQALGQTA-TVASDVFTWGGMLLFAATGRPPFGAGTPRV----LLQRAVYAEPDLS-VFCPELRELVAAAMRKDPKRR 263
Cdd:cd05577 163 PEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVdkeeLKRRTLEMAVEYPdSFSPEARSLCEGLLQKDPERR 241
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
95-277 2.15e-11

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 64.04  E-value: 2.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFI---DAPTLAATVaGGAALSGPDTYrlAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAmna 170
Cdd:cd05611  73 YLVMEYLnggDCASLIKTL-GGLPEDWAKQY--IAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGhLKLTDFGLSRN--- 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 171 VSINNPggPPSGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTP-----RVLLQRAVYAEPDLSVFC 245
Cdd:cd05611 147 GLEKRH--NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPdavfdNILSRRINWPEEVKEFCS 224
                       170       180       190
                ....*....|....*....|....*....|..
gi 86742726 246 PELRELVAAAMRKDPKRRpAAAELLEQLMAYP 277
Cdd:cd05611 225 PEAVDLINRLLCMDPAKR-LGANGYQEIKSHP 255
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
122-270 2.64e-11

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 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.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 63.85  E-value: 2.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 122 YRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRA------------MNAVSINNPGGPPSGIGTLAF 188
Cdd:cd14010  97 RKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGtLKLSDFGLARRegeilkelfgqfSDEGNVNKVSKKQAKRGTPYY 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 189 ITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYAEPDLSVFC------PELRELVAAAMRKDPKR 262
Cdd:cd14010 177 MAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKvsskpsPDFKSLLKGLLEKDPAK 256

                ....*...
gi 86742726 263 RPAAAELL 270
Cdd:cd14010 257 RLSWDELV 264
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
131-271 3.11e-11

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 63.34  E-value: 3.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGlframnaVSINNPGGPP---SGIGTLAFITPEQALGQTATV---AS 203
Cdd:cd14008 120 GLEYLHENGIVHRDIKPENLLLTADGtVKISDFG-------VSEMFEDGNDtlqKTAGTPAFLAPELCDGDSKTYsgkAA 192
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86742726 204 DVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYAE------PDLSvfcPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd14008 193 DIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNdefpipPELS---PELKDLLRRMLEKDPEKRITLKEIKE 263
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
131-270 3.44e-11

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 63.65  E-value: 3.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSIN-NPGGPPSGIGTLAFITPEQAL-GQTATVASDVFT 207
Cdd:cd06917 113 ALKFIHKDGIIHRDIKAANILVTNTGnVKLCDFGV-----AASLNqNSSKRSTFVGTPYWMAPEVITeGKYYDTKADIWS 187
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 208 WGGMLLFAATGRPPFGagtpRVLLQRAVYAEPD-------LSVFCPELRELVAAAMRKDPKRRPAAAELL 270
Cdd:cd06917 188 LGITTYEMATGNPPYS----DVDALRAVMLIPKskpprleGNGYSPLLKEFVAACLDEEPKDRLSADELL 253
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
117-270 4.81e-11

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 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.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 63.06  E-value: 4.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 117 SGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLS----GQGVRLV--DFGLFRAM--NAVSINNPGGPPsgiGTLAF 188
Cdd:cd13982  97 PGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnaHGNVRAMisDFGLCKKLdvGRSSFSRRSGVA---GTSGW 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 189 ITPEQALGQT---ATVASDVFTWGGMLLFAAT-GRPPFGAGTPR---VLLQRAVYAEP-DLSVFCPELRELVAAAMRKDP 260
Cdd:cd13982 174 IAPEMLSGSTkrrQTRAVDIFSLGCVFYYVLSgGSHPFGDKLEReanILKGKYSLDKLlSLGEHGPEAQDLIERMIDFDP 253
                       170
                ....*....|
gi 86742726 261 KRRPAAAELL 270
Cdd:cd13982 254 EKRPSAEEVL 263
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
73-263 5.28e-11

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 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.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 62.72  E-value: 5.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  73 IRRLAPSCLAAILDLDTGARPPYVVAEFIDAPTLAATVAGGAALSgPDTYRLAVG-LATALAALHELEIFLGDLKPINVV 151
Cdd:cd14202  55 LKELKHENIVALYDFQEIANSVYLVMEYCNGGDLADYLHTMRTLS-EDTIRLFLQqIAGAMKMLHSKGIIHRDLKPQNIL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 152 LSGQG----------VRLVDFGLFRAM--NAVSINNPGGPpsgigtlAFITPEQALGQTATVASDVFTWGGMLLFAATGR 219
Cdd:cd14202 134 LSYSGgrksnpnnirIKIADFGFARYLqnNMMAATLCGSP-------MYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGK 206
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 86742726 220 PPFGAGTP---RVLLQRAVYAEPDL--SVFCPeLRELVAAAMRKDPKRR 263
Cdd:cd14202 207 APFQASSPqdlRLFYEKNKSLSPNIprETSSH-LRQLLLGLLQRNQKDR 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
144-271 6.67e-11

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 62.56  E-value: 6.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 144 DLKPINVVLSGQG-VRLVDFGLFRAMN-AVSINNpggppSGIGTLAFITPEQALGQTATVASDVftWG-GMLLF-AATGR 219
Cdd:cd08217 135 DLKPANIFLDSDNnVKLGDFGLARVLShDSSFAK-----TYVGTPYYMSPELLNEQSYDEKSDI--WSlGCLIYeLCALH 207
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 86742726 220 PPFGAGTPRVLLQRAVYAE-PDL-SVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd08217 208 PPFQAANQLELAKKIKEGKfPRIpSRYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
92-288 1.40e-10

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 61.62  E-value: 1.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  92 RPPYVVAEFIDAPTLAATVAGGA--ALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVvLSGQGV--RLVDFGLFRA 167
Cdd:cd05070  76 EPIYIVTEYMSKGSLLDFLKDGEgrALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANI-LVGNGLicKIADFGLARL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 168 MNAVSINNPGGPPSGIgtlAFITPEQALGQTATVASDVFTWGGMLLFAAT-GRPPFGAGTPRVLLQRAvyaEPDLSVFCP 246
Cdd:cd05070 155 IEDNEYTARQGAKFPI---KWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV---ERGYRMPCP 228
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 86742726 247 E-----LRELVAAAMRKDPKRRPAAAELLEQLMAYPTRSeaEPAVEP 288
Cdd:cd05070 229 QdcpisLHELMIHCWKKDPEERPTFEYLQGFLEDYFTAT--EPQYQP 273
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
128-271 1.52e-10

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK 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.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 61.34  E-value: 1.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQG----VRLVDFGLframnAVSINNPGGPPSGIGTLAFITPEQALGQTATVAS 203
Cdd:cd05117 108 ILSAVAYLHSQGIVHRDLKPENILLASKDpdspIKIIDFGL-----AKIFEEGEKLKTVCGTPYYVAPEVLKGKGYGKKC 182
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86742726 204 DVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYA-----EPDLSVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd05117 183 DIWSLGVILYILLCGYPPFYGETEQELFEKILKGkysfdSPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALN 255
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
110-272 1.96e-10

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 61.22  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 110 VAGGAAL----SGP-DTYRLAVGLATALAAL---HELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSINNPggpp 180
Cdd:cd06640  84 LGGGSALdllrAGPfDEFQIATMLKEILKGLdylHSEKKIHRDIKAANVLLSEQGdVKLADFGVAGQLTDTQIKRN---- 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 181 SGIGTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTP-RVLLQRAVYAEPDLS-VFCPELRELVAAAMRK 258
Cdd:cd06640 160 TFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPmRVLFLIPKNNPPTLTgEFSKPFKEFIDACLNK 239
                       170
                ....*....|....
gi 86742726 259 DPKRRPAAAELLEQ 272
Cdd:cd06640 240 DPSFRPTAKELLKH 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
130-271 3.06e-10

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 60.49  E-value: 3.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 130 TALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnAVSINNPGGPPSGIGTLAFITPEQALGQTA--TVASDVF 206
Cdd:cd06632 113 SGLAYLHSRNTVHRDIKGANILVDTNGvVKLADFGM-----AKHVEAFSFAKSFKGSPYWMAPEVIMQKNSgyGLAVDIW 187
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86742726 207 TWGGMLLFAATGRPPFGAGTP-----RVLLQRAVYAEPD-LSvfcPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd06632 188 SLGCTVLEMATGKPPWSQYEGvaaifKIGNSGELPPIPDhLS---PDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
128-272 3.90e-10

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in 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 STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 60.14  E-value: 3.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSinnpGGPPSGIGTLAFITPEQALGQTATVASDVF 206
Cdd:cd08221 110 IVSAVSHIHKAGILHRDIKTLNIFLTKADlVKLGDFGISKVLDSES----SMAESIVGTPYYMSPELVQGVKYNFKSDIW 185
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86742726 207 TWGGMLLFAATGRPPFGAGTPRVLLQRAV---YAEPDlSVFCPELRELVAAAMRKDPKRRPAAAELLEQ 272
Cdd:cd08221 186 AVGCVLYELLTLKRTFDATNPLRLAVKIVqgeYEDID-EQYSEEIIQLVHDCLHQDPEDRPTAEELLER 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
131-271 5.07e-10

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, 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. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 59.55  E-value: 5.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 131 ALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLFRAMNAVSinnpGGPPSGIGTLAFITPEQALGQTATVASDVFTWG 209
Cdd:cd06627 111 GLAYLHEQGVIHRDIKGANILTTKDGlVKLADFGVATKLNEVE----KDENSVVGTPYWMAPEVIEMSGVTTASDIWSVG 186
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86742726 210 GMLLFAATGRPPFGAGTPRVLLQRAVYAE-----PDLSvfcPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd06627 187 CTVIELLTGNPPYYDLQPMAALFRIVQDDhpplpENIS---PELRDFLLQCFQKDPTLRPSAKELLK 250
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
96-271 5.26e-10

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like 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.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 59.59  E-value: 5.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  96 VVAEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLS---GQGVRLVDFGlframNAVS 172
Cdd:cd14006  66 LILELCSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrpSPQIKIIDFG-----LARK 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 173 INnPGGPPSGI-GTLAFITPEQALGQTATVASDVFTWGG---MLLfaaTGRPPFGAGTPRVLLQRAV-----YAEPDLSV 243
Cdd:cd14006 141 LN-PGEELKEIfGTPEFVAPEIVNGEPVSLATDMWSIGVltyVLL---SGLSPFLGEDDQETLANISacrvdFSEEYFSS 216
                       170       180
                ....*....|....*....|....*...
gi 86742726 244 FCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd14006 217 VSQEAKDFIRKLLVKEPRKRPTAQEALQ 244
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
95-273 5.62e-10

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 59.45  E-value: 5.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  95 YVVAEFIDAPTLAATVAGGA-ALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVL----SGQGVRLVDFGLFRAMN 169
Cdd:cd14156  64 HPILEYVSGGCLEELLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtpRGREAVVTDFGLAREVG 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 170 AVSINNPGGPPSGIGTLAFITPEQALGQTATVASDVFTWgGMLLFAATGRPPfgaGTPRVLLQRAVYAePDLSVF----- 244
Cdd:cd14156 144 EMPANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSF-GIVLCEILARIP---ADPEVLPRTGDFG-LDVQAFkemvp 218
                       170       180       190
                ....*....|....*....|....*....|.
gi 86742726 245 -CPE-LRELVAAAMRKDPKRRPAAAELLEQL 273
Cdd:cd14156 219 gCPEpFLDLAASCCRMDAFKRPSFAELLDEL 249
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
135-271 5.82e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI 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.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 59.83  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 135 LHELEIFLGDLKPINVVLSGQG--VRLVDFGL-----FRAMNAVSINNPGGPP---SGIGTLAFITPEQALGQTATVASD 204
Cdd:cd14049 136 IHSMGIVHRDLKPRNIFLHGSDihVRIGDFGLacpdiLQDGNDSTTMSRLNGLthtSGVGTCLYAAPEQLEGSHYDFKSD 215
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86742726 205 VFTWGGMLL--FAatgrpPFGAGTPRVLLQRAVYAEP---DLSVFCPELRELVAAAMRKDPKRRPAAAELLE 271
Cdd:cd14049 216 MYSIGVILLelFQ-----PFGTEMERAEVLTQLRNGQipkSLCKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
128-263 6.05e-10

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK 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.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 59.54  E-value: 6.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 128 LATALAALHELEIFLGDLKPINVVLSGQGVRLV----DFGLFRAMnavsinnpggPPSGI-----GTLAFITPEQALGQT 198
Cdd:cd14009 101 LASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVlkiaDFGFARSL----------QPASMaetlcGSPLYMAPEILQFQK 170
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 199 ATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQR-----AVYAEPDLSVFCPELRELVAAAMRKDPKRR 263
Cdd:cd14009 171 YDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNiersdAVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
22-272 7.29e-10

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora 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.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 59.20  E-value: 7.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  22 YTVERKLVDARTGPVFLARNGEAR-----PVLVKTITAPFGRDAEFRRRLRVDlDNIRRlaPSCLAAILDLDTGARPpYV 96
Cdd:cd14116   7 FEIGRPLGKGKFGNVYLAREKQSKfilalKVLFKAQLEKAGVEHQLRREVEIQ-SHLRH--PNILRLYGYFHDATRV-YL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  97 VAEFIDAPTLAATVAGGAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG-VRLVDFGLframnavSINN 175
Cdd:cd14116  83 ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGeLKIADFGW-------SVHA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 176 PGGPPSGI-GTLAFITPEQALGQTATVASDVFTWGGMLLFAATGRPPFGAGTPRVLLQRAVYAEPDLSVFCPE-LRELVA 253
Cdd:cd14116 156 PSSRRTTLcGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEgARDLIS 235
                       250
                ....*....|....*....
gi 86742726 254 AAMRKDPKRRPAAAELLEQ 272
Cdd:cd14116 236 RLLKHNPSQRPMLREVLEH 254
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
22-271 1.01e-09

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 other kinases. 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. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 58.79  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  22 YTVERKLVDARTGPVFLARNGEA-RPVLVKTITAPFG------RDAEFRRRLR--VDLDNIRRLapsclaaiLDL--DTG 90
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTgEKVAIKKIKNDFRhpkaalREIKLLKHLNdvEGHPNIVKL--------LDVfeHRG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726  91 ARPPYVVAEFIDaPTLAATVAG-GAALSGPDTYRLAVGLATALAALHELEIFLGDLKPINVVLSGQG--VRLVDFGLfra 167
Cdd:cd05118  73 GNHLCLVFELMG-MNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELgqLKLADFGL--- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86742726 168 mnAVSINNPGGPP