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Conserved domains on  [gi|15610217|ref|NP_217596|]
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serine/threonine-protein kinase PknK [Mycobacterium tuberculosis H37Rv]

Protein classification: serine/threonine-protein kinase PknK functions as a transcriptional and translational regulator in a phosphorylation-dependent manner

Graphical summary

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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 ...
25-284 1.91e-86

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: 281.01  E-value: 1.91e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   25 GFDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDL--DRDNLERFLREQRAMGRLSgHPHIVTVLQVGVLaGGRPFIV 102
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaeDEEFRERFLREARALARLS-HPNIVRVYDVGED-DGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  103 MPYHAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGG-FETAT 181
Cdd:cd14014   79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDsGLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  182 GVIAGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQPIPDLRKqGLPADVAAAIE 261
Cdd:cd14014  159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP-DVPPALDAIIL 237
                        250       260
                 ....*....|....*....|...
gi 15610217  262 RAMARHPADRPATAADVGEELRD 284
Cdd:cd14014  238 RALAKDPEERPQSAAELLAALRA 260
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
348-485 1.12e-08

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


:

Pssm-ID: 289934  Cd Length: 167  Bit Score: 54.85  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    348 RSRLTDILR--AGGRRRLILIHAPSGFGKSTLAAQWREELSRDGAAVAWLTIDNDDNNEVW--------FLSHLL----- 412
Cdd:pfam13191    9 LERLLDALErvRSGRPGSVLLTGPSGTGKTSLLRELARRLARDGGLFLRGKCDECIPYAPLlqaltrrgLLRQLLteees 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610217    413 ESIRRVRPTLAESLGHVLEEHGDDAGR--YVLTSLIDEIHENDDRIAVVIDDWHRvSDSRTQAALGFLLDNGCHH 485
Cdd:pfam13191   89 ALLEPWRARLLEALGPLPPLPPDEANRllDALLRLLDALARGERPLVLVLDDLQW-ADEASLDLLAALLRLLERL 162
MalT COG2909
ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];
333-1110 0e+00

ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];


:

Pssm-ID: 225461 [Multi-domain]  Cd Length: 894  Bit Score: 793.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  333 ATKYRPSVPTGSLVTRSRLTDILRAGGRRRLILIHAPSGFGKSTLAAQWREeLSRDGAAVAWLTIDNDDNNEVWFLSHLL 412
Cdd:COG2909    9 PSKLVRPVRPDNYVVRPRLLDRLRRANDYRLILISAPAGFGKTTLLAQWRE-LAADGAAVAWLSLDESDNDPARFLSYLI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  413 ESIRRVRPTLAESLGHVLEEHGDDAGRYVLTSLIDEIHENDDRIAVVIDDWHRVSDSRTQAALGFLLDNGCHHLQLIVTS 492
Cdd:COG2909   88 AALQQATPTLGDEAQTLLQKHQYVSLESLLSSLLNELASYEGPLYLVLDDYHLISDPALHEALRFLLKHAPENLTLVVTS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  493 WSRAGLPVGRLRIGDELAEIDSAALRFDTDEAAALLNDAGGLRLPRADVQALTTSTDGWAAALRLAALSLRGGGDATQLL 572
Cdd:COG2909  168 RSRPQLGLARLRLRDELLEIGSEELRFDTEEAAAFLNDRGSLPLDAADLKALYDRTEGWAAALQLIALALRNNTSAEQSL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  573 RGLSGASDVIHEFLSENVLDTLEPELREFLLVASVTERTCGGLASALAGITNGRAMLEEAEHRGLFLQRTEDDPNWFRFH 652
Cdd:COG2909  248 RGLSGAASHLSDYLVEEVLDRLPPELRDFLLQTSVLSRFNDELCNALTGEENGQAMLEELERRGLFLQRLDDEGQWFRYH 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  653 QMFADFLHRRLERGGSHRVAELHRRASAWFAENGYLHEAVDHALAAGDPARAVDLVEQDETNLPEQSKMTTLLAIVQKLP 732
Cdd:COG2909  328 HLFAEFLRQRLQRELAARLKELHRAAAEWFAEHGLPSEAIDHALAAGDPEMAADLLEQLEWQLFNGSELSLLLAWLKALP 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  733 TSMVVSRARLQLAIAWANILLQRPAPATGALNRFETALG-----RAELPEATQADLRAEADVLRAVAEVFADRVERVDDL 807
Cdd:COG2909  408 AELLASTPRLVLLQAWLLASQHRLAEAETLIARLEHFLKapmhsRQGDLLAEFQALRAQVALNRGDPEEAEDLARLALVQ 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  808 LAEAMSRPDTLPPRVPGTAG-----NTAALAAICRFE----FAEVYPLLDWAAP-------------YQEMMGPFGTVYA 865
Cdd:COG2909  488 LPEAAYRSRIVALSVLGEAAhirgeLTQALALMQQAEqmarQHDVYHLALWSLLqqseileaqgqvaRAEQEKAFNLIRE 567
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  866 Q------------CLRGMAARNRLDIVAALQNFRTAFEVGTAVGAHSHAARLAGSLLAELLYETGDLAGAGRLMDESYLL 933
Cdd:COG2909  568 QhleqkprheflvRIRAQLLRAWLRLDLAEAEARLGIEVGSVYTPQPLLSRLALSMLAELEFLRGDLDKALAQLDELERL 647
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  934 GSEGG-AVDYLAARYVIGARVKAAQGDHEGAADRLSTGGDTAVQLG-LPRLAAR-INNERIRLGIALPAAVAADLLAPRT 1010
Cdd:COG2909  648 LLNGQyHVDYLAAAYKVKLILWLAQGDKELAAEWLLKSGDPDKANAhFPQLQWRlIAREQILLGILLEAELALDELASRL 727
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217 1011 IPRDNGIATMTAELDEDSAVRLLSAGDSADRDQACQRAGALA-AAIDGTrRPLAALQAQILHIETLAATGRESDARNELA 1089
Cdd:COG2909  728 TEDLNRNLRLLGLLYEGEAVKGQLALDLLDALQLRERTGFLRhFAIEGE-ARMAEQLRQLILLGELPELERHRLQRILRE 806
                        810       820
                 ....*....|....*....|..
gi 15610217 1090 PVATKCAELG-LSRLLVDAGLA 1110
Cdd:COG2909  807 ILQTQRQKFIhLDEEFVEGLLN 828
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
26-280 1.79e-50

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 180.03  E-value: 1.79e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217      26 FDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDLDRDNLERFLREqRAMGRLSGHPHIVTVLQVgVLAGGRPFIVMPY 105
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILRE-IKILKKLKHPNIVRLYDV-FEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     106 HAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGGFETATGVIa 185
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV- 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     186 GSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRiTSQPIPDLRKQGLPADVAAAIERAMA 265
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG-KPKPPFPPPEWDISPEAKDLIRKLLV 236
                           250
                    ....*....|....*
gi 15610217     266 RHPADRPaTAADVGE 280
Cdd:smart00220  237 KDPEKRL-TAEEALQ 250
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-284 1.91e-86

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: 281.01  E-value: 1.91e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   25 GFDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDL--DRDNLERFLREQRAMGRLSgHPHIVTVLQVGVLaGGRPFIV 102
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaeDEEFRERFLREARALARLS-HPNIVRVYDVGED-DGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  103 MPYHAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGG-FETAT 181
Cdd:cd14014   79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDsGLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  182 GVIAGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQPIPDLRKqGLPADVAAAIE 261
Cdd:cd14014  159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP-DVPPALDAIIL 237
                        250       260
                 ....*....|....*....|...
gi 15610217  262 RAMARHPADRPATAADVGEELRD 284
Cdd:cd14014  238 RALAKDPEERPQSAAELLAALRA 260
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
348-485 1.12e-08

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 289934  Cd Length: 167  Bit Score: 54.85  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    348 RSRLTDILR--AGGRRRLILIHAPSGFGKSTLAAQWREELSRDGAAVAWLTIDNDDNNEVW--------FLSHLL----- 412
Cdd:pfam13191    9 LERLLDALErvRSGRPGSVLLTGPSGTGKTSLLRELARRLARDGGLFLRGKCDECIPYAPLlqaltrrgLLRQLLteees 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610217    413 ESIRRVRPTLAESLGHVLEEHGDDAGR--YVLTSLIDEIHENDDRIAVVIDDWHRvSDSRTQAALGFLLDNGCHH 485
Cdd:pfam13191   89 ALLEPWRARLLEALGPLPPLPPDEANRllDALLRLLDALARGERPLVLVLDDLQW-ADEASLDLLAALLRLLERL 162
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
110-224 6.81e-07

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 49.32  E-value: 6.81e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     110 SLETLIRRHG-PLDWRETLSIGVKLAGALEaahrvgTLHRDVKPGNILLTDYGepqltdfgIARIAGGFETATGVIAGS- 187
Cdd:smart00750    2 SLADILEVRGrPLNEEEIWAVCLQCLGALR------ELHRQAKSGNILLTWDG--------LLKLDGSVAFKTPEQSRPd 67
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 15610217     188 PAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAY 224
Cdd:smart00750   68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPY 104
MalT COG2909
ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];
333-1110 0e+00

ATP-, maltotriose- and DNA-dependent transcriptional regulator MalT [Transcription];


Pssm-ID: 225461 [Multi-domain]  Cd Length: 894  Bit Score: 793.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  333 ATKYRPSVPTGSLVTRSRLTDILRAGGRRRLILIHAPSGFGKSTLAAQWREeLSRDGAAVAWLTIDNDDNNEVWFLSHLL 412
Cdd:COG2909    9 PSKLVRPVRPDNYVVRPRLLDRLRRANDYRLILISAPAGFGKTTLLAQWRE-LAADGAAVAWLSLDESDNDPARFLSYLI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  413 ESIRRVRPTLAESLGHVLEEHGDDAGRYVLTSLIDEIHENDDRIAVVIDDWHRVSDSRTQAALGFLLDNGCHHLQLIVTS 492
Cdd:COG2909   88 AALQQATPTLGDEAQTLLQKHQYVSLESLLSSLLNELASYEGPLYLVLDDYHLISDPALHEALRFLLKHAPENLTLVVTS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  493 WSRAGLPVGRLRIGDELAEIDSAALRFDTDEAAALLNDAGGLRLPRADVQALTTSTDGWAAALRLAALSLRGGGDATQLL 572
Cdd:COG2909  168 RSRPQLGLARLRLRDELLEIGSEELRFDTEEAAAFLNDRGSLPLDAADLKALYDRTEGWAAALQLIALALRNNTSAEQSL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  573 RGLSGASDVIHEFLSENVLDTLEPELREFLLVASVTERTCGGLASALAGITNGRAMLEEAEHRGLFLQRTEDDPNWFRFH 652
Cdd:COG2909  248 RGLSGAASHLSDYLVEEVLDRLPPELRDFLLQTSVLSRFNDELCNALTGEENGQAMLEELERRGLFLQRLDDEGQWFRYH 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  653 QMFADFLHRRLERGGSHRVAELHRRASAWFAENGYLHEAVDHALAAGDPARAVDLVEQDETNLPEQSKMTTLLAIVQKLP 732
Cdd:COG2909  328 HLFAEFLRQRLQRELAARLKELHRAAAEWFAEHGLPSEAIDHALAAGDPEMAADLLEQLEWQLFNGSELSLLLAWLKALP 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  733 TSMVVSRARLQLAIAWANILLQRPAPATGALNRFETALG-----RAELPEATQADLRAEADVLRAVAEVFADRVERVDDL 807
Cdd:COG2909  408 AELLASTPRLVLLQAWLLASQHRLAEAETLIARLEHFLKapmhsRQGDLLAEFQALRAQVALNRGDPEEAEDLARLALVQ 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  808 LAEAMSRPDTLPPRVPGTAG-----NTAALAAICRFE----FAEVYPLLDWAAP-------------YQEMMGPFGTVYA 865
Cdd:COG2909  488 LPEAAYRSRIVALSVLGEAAhirgeLTQALALMQQAEqmarQHDVYHLALWSLLqqseileaqgqvaRAEQEKAFNLIRE 567
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  866 Q------------CLRGMAARNRLDIVAALQNFRTAFEVGTAVGAHSHAARLAGSLLAELLYETGDLAGAGRLMDESYLL 933
Cdd:COG2909  568 QhleqkprheflvRIRAQLLRAWLRLDLAEAEARLGIEVGSVYTPQPLLSRLALSMLAELEFLRGDLDKALAQLDELERL 647
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  934 GSEGG-AVDYLAARYVIGARVKAAQGDHEGAADRLSTGGDTAVQLG-LPRLAAR-INNERIRLGIALPAAVAADLLAPRT 1010
Cdd:COG2909  648 LLNGQyHVDYLAAAYKVKLILWLAQGDKELAAEWLLKSGDPDKANAhFPQLQWRlIAREQILLGILLEAELALDELASRL 727
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217 1011 IPRDNGIATMTAELDEDSAVRLLSAGDSADRDQACQRAGALA-AAIDGTrRPLAALQAQILHIETLAATGRESDARNELA 1089
Cdd:COG2909  728 TEDLNRNLRLLGLLYEGEAVKGQLALDLLDALQLRERTGFLRhFAIEGE-ARMAEQLRQLILLGELPELERHRLQRILRE 806
                        810       820
                 ....*....|....*....|..
gi 15610217 1090 PVATKCAELG-LSRLLVDAGLA 1110
Cdd:COG2909  807 ILQTQRQKFIhLDEEFVEGLLN 828
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
26-280 1.79e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 180.03  E-value: 1.79e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217      26 FDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDLDRDNLERFLREqRAMGRLSGHPHIVTVLQVgVLAGGRPFIVMPY 105
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILRE-IKILKKLKHPNIVRLYDV-FEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     106 HAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGGFETATGVIa 185
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV- 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     186 GSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRiTSQPIPDLRKQGLPADVAAAIERAMA 265
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG-KPKPPFPPPEWDISPEAKDLIRKLLV 236
                           250
                    ....*....|....*
gi 15610217     266 RHPADRPaTAADVGE 280
Cdd:smart00220  237 KDPEKRL-TAEEALQ 250
PRK04841 PRK04841
transcriptional regulator MalT; Provisional
337-820 3.39e-75

transcriptional regulator MalT; Provisional


Pssm-ID: 235315 [Multi-domain]  Cd Length: 903  Bit Score: 267.20  E-value: 3.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   337 RPSVPTGSLVtRSRLTDILRAGGRRRLILIHAPSGFGKSTLAAQWreelSRDGAAVAWLTIDNDDNNEVWFLSHLLESIR 416
Cdd:PRK04841    9 RPVRLHNTVV-RERLLAKLSGANNYRLVLVTSPAGYGKTTLISQW----AAGKNNLGWYSLDESDNQPERFASYLIAALQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   417 RVRPTLAESLGHVLEEHGDDAGRYVLTSLIDEIHENDDRIAVVIDDWHRVSDSRTQAALGFLLDNGCHHLQLIVTSWSRA 496
Cdd:PRK04841   84 QATNGHCSKSEALAQKRQYASLSSLFAQLFIELADWHQPLYLVIDDYHLITNPEIHEAMRFFLRHQPENLTLVVLSRNLP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   497 GLPVGRLRIGDELAEIDSAALRFDTDEAAALLNDAGGLRLPRADVQALTTSTDGWAAA-LRLAALSLRGGGDATQLLRGL 575
Cdd:PRK04841  164 PLGIANLRVRDQLLEIGSQQLAFDHQEAQQFFDQRLSSPIEAAESSRLCDDVEGWATAlQLIALSARQNNSSLHDSARRL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   576 SG--ASDvIHEFLSENVLDTLEPELREFLLVASVTERTCGGLASALAGITNGRAMLEEAEHRGLFLQRTEDDPNWFRFHQ 653
Cdd:PRK04841  244 AGinASH-LSDYLVEEVLDNVDLETRHFLLRCSVLRSMNDALIVRVTGEENGQMRLEELERQGLFIQRMDDSGEWFRYHP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   654 MFADFLHRRLERGGSHRVAELHRRASAWFAENGYLHEAVDHALAAGDPARAVDLVEQDETNLPEQSKMTTLLAIVQKLPT 733
Cdd:PRK04841  323 LFASFLRHRCQWELAQELPELHRAAAEAWLAQGFPSEAIHHALAAGDAQLLRDILLQHGWSLFNQGELSLLEECLNALPW 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   734 SMVVSRARLQLAIAWANILLQRPAPATGALNRFETALgrAELPEATQADLRAEADVLRavAEVfADRVERVDDLLAEAMS 813
Cdd:PRK04841  403 EVLLENPRLVLLQAWLAQSQHRYSEVNTLLARAEQEL--KDRNIELDGTLQAEFNALR--AQV-AINDGDPEEAERLAEL 477

                  ....*..
gi 15610217   814 RPDTLPP 820
Cdd:PRK04841  478 ALAELPL 484
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
25-350 1.96e-45

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 169.54  E-value: 1.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   25 GFDNVEEIGRGGFGVVYRCVQPsldRAVAVKVLSTDL--DRDNLERFLREQRAMGRLSGHPHIVTVLQVGVlAGGRPFIV 102
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLesKSKEVERFLREIQILASLNHPPNIVKLYDFFQ-DEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  103 MPYHAKNSLETLIR---RHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLT-DYGEPQLTDFGIARIAGGFE 178
Cdd:COG0515   77 MEYVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPDPG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  179 TA------TGVIAGSPAFTAPEVLEG---ASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQ------- 242
Cdd:COG0515  157 STssipalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKIILElptpsla 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  243 -PIPDLRKQGLPADVAAAIERAMARHPADRPATAADVGEELRDVQRRNGVSVDEMPLPVELGVERRRSPEAHAAHRHTGG 321
Cdd:COG0515  237 sPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLN 316
                        330       340
                 ....*....|....*....|....*....
gi 15610217  322 GTPTVPTPPTPATKYRPSVPTGSLVTRSR 350
Cdd:COG0515  317 SLAISGSDLKLDDSNFSKELAPNGVSSSP 345
Pkinase pfam00069
Protein kinase domain;
26-278 1.39e-44

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 163.15  E-value: 1.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     26 FDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDLDRDN-LERFLREQRAMGRLSgHPHIVTVLQVgVLAGGRPFIVMP 104
Cdd:pfam00069    1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVKKIKKEKIKKKkDKNVLREIKILKKLN-HPNIVRLYDV-FEDKDHLYLVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    105 YHAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGGFETATgVI 184
Cdd:pfam00069   79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAKQLSSGSKLT-TF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    185 AGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQPIPDLRKqgLPADVAAAIERAM 264
Cdd:pfam00069  158 VGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDTLYELIIDQLDLSSPRPSS--ISEEAKDLLKKLL 235
                          250
                   ....*....|....
gi 15610217    265 ARHPADRPaTAADV 278
Cdd:pfam00069  236 KKDPSKRL-TATQA 248
pknD PRK13184
serine/threonine-protein kinase; Reviewed
26-282 2.71e-26

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 115.25  E-value: 2.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    26 FDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDLDRDNL--ERFLREQRAMGRLSgHPHIVTVLQVgvLAGGRP-FIV 102
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLlkKRFLREAKIAADLI-HPGIVPVYSI--CSDGDPvYYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   103 MPYHAKNSLETLIRR-------HGPLDWRET----LSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIA 171
Cdd:PRK13184   81 MPYIEGYTLKSLLKSvwqkeslSKELAEKTSvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   172 RIAGGFE------------------TATGVIAGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVI 233
Cdd:PRK13184  161 IFKKLEEedlldidvdernicyssmTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 15610217   234 AQFLRITSQPIPDLRKqgLPADVAAAIERAMARHPADRPATAADVGEEL 282
Cdd:PRK13184  241 YRDVILSPIEVAPYRE--IPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
51-286 6.92e-25

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: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 111.09  E-value: 6.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217     51 AVAVKVLSTDLDRDNLE--RFLREQRAMGRLSgHPHIVTVLQVGVLAGGRPFIVMPYHAKNSLETLIRRHGPLDWRETLS 128
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQraRFRRETALCARLY-HPNIVALLDSGEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETGR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    129 IGVKLAGALEAAHRVGTLHRDVKPGNILLTDYG---EPQLTDFGIARIAGGFE-------TATGVIAGSPAFTAPEVLEG 198
Cdd:TIGR03903   84 LMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPGVRdadvatlTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217    199 ASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQPIPDLrKQGLPadVAAAIERAMARHPADRPATAADV 278
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSLPPW-IAGHP--LGQVLRKALNKDPRQRAASAPAL 240

                   ....*...
gi 15610217    279 GEELRDVQ 286
Cdd:TIGR03903  241 AERFRALE 248
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-284 1.91e-86

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: 281.01  E-value: 1.91e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   25 GFDNVEEIGRGGFGVVYRCVQPSLDRAVAVKVLSTDL--DRDNLERFLREQRAMGRLSgHPHIVTVLQVGVLaGGRPFIV 102
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaeDEEFRERFLREARALARLS-HPNIVRVYDVGED-DGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  103 MPYHAKNSLETLIRRHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGG-FETAT 181
Cdd:cd14014   79 MEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDsGLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  182 GVIAGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERRSGERVIAQFLRITSQPIPDLRKqGLPADVAAAIE 261
Cdd:cd14014  159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP-DVPPALDAIIL 237
                        250       260
                 ....*....|....*....|...
gi 15610217  262 RAMARHPADRPATAADVGEELRD 284
Cdd:cd14014  238 RALAKDPEERPQSAAELLAALRA 260
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
32-278 1.15e-45

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: 164.75  E-value: 1.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   32 IGRGGFGVVYRCVQPSLDRAVAVKVLSTDLDRDNLERFLREQRAMGRLSgHPHIVTVLQVgVLAGGRPFIVMPYHAKNSL 111
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLN-HPNIVKLYDV-FETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  112 ETLIRRH-GPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGGFETATGVIAGS--P 188
Cdd:cd00180   79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTtpP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  189 AFTAPEVLEGASPTPASDVYSLGATLFCaltghaayerrsgerviaqflritsqpIPDLRKqglpadvaaAIERAMARHP 268
Cdd:cd00180  159 YYAPPELLGGRYYGPKVDIWSLGVILYE---------------------------LEELKD---------LIRRMLQYDP 202
                        250
                 ....*....|
gi 15610217  269 ADRPaTAADV 278
Cdd:cd00180  203 KKRP-SAKEL 211
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
32-272 1.20e-38

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: 145.76  E-value: 1.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   32 IGRGGFGVVYRCVQpsLDRAVAVKVLSTDLDRDNLER-FLREQRAMGRLSgHPHIVTVLQVgVLAGGRPFIVMPYHAKNS 110
Cdd:cd13999    1 IGSGSFGEVYKGKW--RGTDVAIKKLKVEDDNDELLKeFRREVSILSKLR-HPNIVQFIGA-CLSPPPLCIVTEYMPGGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  111 LETLIR-RHGPLDWRETLSIGVKLAGALEAAHRVGTLHRDVKPGNILLTDYGEPQLTDFGIARIAGGFETATGVIAGSPA 189
Cdd:cd13999   77 LYDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  190 FTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYE----RRSGERVIAQFLRitsQPIPDlrkqGLPADVAAAIERAMA 265
Cdd:cd13999  157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKelspIQIAAAVVQKGLR---PPIPP----DCPPELSKLIKRCWN 229

                 ....*..
gi 15610217  266 RHPADRP 272
Cdd:cd13999  230 EDPEKRP 236
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
32-280 3.04e-35

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: 136.63  E-value: 3.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217   32 IGRGGFGVVYRCVQPSlDRAVAVKVLSTDLDRDNLERFLREQRAMGRLSgHPHIVTVLqvG-VLAGGRPFIVMPYHAKNS 110
Cdd:cd14066    1 IGSGGFGTVYKGVLEN-GTVVAVKRLNEMNCAASKKEFLTELEMLGRLR-HPNLVRLL--GyCLESDEKLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  111 LETLIRRHG---PLDWRETLSIGVKLAGALEAAHRVGTL---HRDVKPGNILLTDYGEPQLTDFGIARIAGGFETA--TG 182
Cdd:cd14066   77 LEDRLHCHKgspPLPWPQRLKIAKGIARGLEYLHEECPPpiiHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVskTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610217  183 VIAGSPAFTAPEVLEGASPTPASDVYSLGATLFCALTGHAAYERrsgERVIA