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Conserved domains on  [gi|21222873|ref|NP_628652|]
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Ser/Thr protein kinase [Streptomyces coelicolor A3(2)]

Protein Classification

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 ...
15-264 6.84e-81

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  Cd Length: 260  Bit Score: 258.29  E-value: 6.84e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  15 YRLLGRLGAGGMGRVFLGRSPG-GRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSY 93
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  94 IAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVDADSLTGSGHM 172
Cdd:cd14014  82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGSV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 173 AGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAP----DVAAVADPALRSLIADCLA 248
Cdd:cd14014 162 LGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILRALA 241
                       250
                ....*....|....*..
gi 21222873 249 KDPAHRP-APREILARI 264
Cdd:cd14014 242 KDPEERPqSAAELLAAL 258
LamGL smart00560
LamG-like jellyroll fold domain;
451-583 8.02e-34

LamG-like jellyroll fold domain;


:

Pssm-ID: 214722  Cd Length: 133  Bit Score: 126.38  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    451 RSFTVAAWVRLSAVPGVFA----TAVSQD--SADASGFYLQYSSeDQGWAFARPGlravgRTAPAAHVWTHLTGVCDGPA 524
Cdd:smart00560   1 GSFTLEAWVKLESAGGSQPiitgAAVAQPtiSEKALTFFLRAKS-VQGWQTARTG-----ATADWIGVWVHLAGVYDGGA 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    525 RKLHLYVNGVQEAVVEDTgPAPATGAFMIG-RASFDGQPRDFFPGAIRDVRAFDRALGPA 583
Cdd:smart00560  75 GKLSLYVNGVEVATSETQ-PSPSSGNLPQGgRILLGGAGGENFSGRLDEVRVYNRALTAR 133
DNA_pol3_gamma3 super family cl26386
DNA polymerase III subunits gamma and tau domain III; This domain family is found in bacteria, ...
202-336 1.83e-03

DNA polymerase III subunits gamma and tau domain III; This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00004. Domains I-III are shared between the tau and the gamma subunits, while most of the DnaB-binding Domain IV and all of the alpha-interacting Domain V are unique to tau.


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 331207  Cd Length: 618  Bit Score: 40.85  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  202 LAFAATGTNPFGAGPTPALLYRVVHNAPDVAAVADPALRSL--IADCLAKDPAHRPAPREILARIGPLGGESATALPHAQ 279
Cdd:PRK14951 362 LAFKPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPApaAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA 441
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21222873  280 QwTPAARPTRADAVPTrivPPVAAPPAHQHTRVDTSPAQVYP-PAPAPADVRPTATGD 336
Cdd:PRK14951 442 P-AAVALAPAPPAQAA---PETVAIPVRVAPEPAVASAAPAPaAAPAAARLTPTEEGD 495
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
15-264 6.84e-81

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  Cd Length: 260  Bit Score: 258.29  E-value: 6.84e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  15 YRLLGRLGAGGMGRVFLGRSPG-GRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSY 93
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  94 IAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVDADSLTGSGHM 172
Cdd:cd14014  82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGSV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 173 AGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAP----DVAAVADPALRSLIADCLA 248
Cdd:cd14014 162 LGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILRALA 241
                       250
                ....*....|....*..
gi 21222873 249 KDPAHRP-APREILARI 264
Cdd:cd14014 242 KDPEERPqSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
15-262 6.79e-47

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 166.94  E-value: 6.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873     15 YRLLGRLGAGGMGRVFLGRS-PGGRLVAVKVVHAELLRrpEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSY 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKKIK--KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873     94 IAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGP-RVIDFGIVRSVDADSLTGSghM 172
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    173 AGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNA----PDVAAVADPALRSLIADCLA 248
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPkppfPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 21222873    249 KDPAHRPAPREILA 262
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
15-262 1.40e-39

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 146.20  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    15 YRLLGRLGAGGMGRVFLGR-SPGGRLVAVKVVHAELlRRPEFRDRFRREVQAARMVS--------GAFTapvvdaDPDAP 85
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKIKKEK-IKKKKDKNILREIKILKKLNhpnivrlyDAFE------DKDNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    86 lpWLVTSYIAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVDAD 164
Cdd:pfam00069  74 --YLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   165 SLTGSghMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAPDVAAVAD--PALRSL 242
Cdd:pfam00069 152 SSLTS--FVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPSSisEEAKDL 229
                         250       260
                  ....*....|....*....|
gi 21222873   243 IADCLAKDPAHRPAPREILA 262
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
14-263 6.36e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 144.88  E-value: 6.36e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  14 EYRLLGRLGAGGMGRVFLGRSPggRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGA-FTAPVVDADPDAPLPWLVTS 92
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  93 YIAGPSLEQAVAERG---PFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGPRV--IDFGIVRSVDADSLT 167
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVklIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 168 GSGH-----MAGSPGFMSPEQVNG---DEVTWASDVFCLGAVLAFAATGTNPFGAGP---TPALLYRVVHNA-------- 228
Cdd:COG0515 159 SSIPalpstSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELptpslasp 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21222873 229 --PDVAAVADPALRSLIADCLAKDPAHRPAPREILAR 263
Cdd:COG0515 239 lsPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSH 275
LamGL smart00560
LamG-like jellyroll fold domain;
451-583 8.02e-34

LamG-like jellyroll fold domain;


Pssm-ID: 214722  Cd Length: 133  Bit Score: 126.38  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    451 RSFTVAAWVRLSAVPGVFA----TAVSQD--SADASGFYLQYSSeDQGWAFARPGlravgRTAPAAHVWTHLTGVCDGPA 524
Cdd:smart00560   1 GSFTLEAWVKLESAGGSQPiitgAAVAQPtiSEKALTFFLRAKS-VQGWQTARTG-----ATADWIGVWVHLAGVYDGGA 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    525 RKLHLYVNGVQEAVVEDTgPAPATGAFMIG-RASFDGQPRDFFPGAIRDVRAFDRALGPA 583
Cdd:smart00560  75 GKLSLYVNGVEVATSETQ-PSPSSGNLPQGgRILLGGAGGENFSGRLDEVRVYNRALTAR 133
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
432-586 2.91e-24

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 315949  Cd Length: 152  Bit Score: 100.54  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   432 DGTGSQIVTAGPVLQTGagrSFTVAAWVRLSAVPGvFATAVSQDSADASGFYLQYSSeDQGWAFARPGL-----RAVGRT 506
Cdd:pfam13385   1 DGGSDYVTLPDALLTTS---SFTVSAWVKPDSLPG-AARIIISSSGGGRGFSLGLDG-SGRLRFAVNGGnggwqTVTSGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   507 APAAHVWTHLTGVCDGpaRKLHLYVNGVQEAVVEDTGPAP--ATGAFMIGRASFDGqprDFFPGAIRDVRAFDRALGPAR 584
Cdd:pfam13385  76 PLPAGEWTHVAVTYDG--GTLRLYVNGVLVGSSTLTGGPPsgTGGPLYIGRSPGGD---DYFNGLIDEVRIYDRALTAAE 150

                  ..
gi 21222873   585 VA 586
Cdd:pfam13385 151 IA 152
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-289 1.16e-19

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 93.30  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   12 VGEYRLLGRLGAGGMGRVFLGRSPG-GRLVAVKVVHAELLRRPEFRDRFRREVQ-AARMVSGAFTaPVVDADPDAPLPWL 89
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENPLLKKRFLREAKiAADLIHPGIV-PVYSICSDGDPVYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   90 VTSYIAGPSLEQAVAERGPFDpqavlTLAAGLAE-----ALVSI-----------HAAHLVHRDLKPSNVLLAEDGPRVI 153
Cdd:PRK13184  80 TMPYIEGYTLKSLLKSVWQKE-----SLSKELAEktsvgAFLSIfhkicatieyvHSKGVLHRDLKPDNILLGLFGEVVI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  154 -DFGIVRSVDAD-----------------SLTGSGHMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAG 215
Cdd:PRK13184 155 lDWGAAIFKKLEeedlldidvdernicysSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  216 PTPALLYRVVHNAP-DVAAVAD--PALRSLIADCLAKDPAHRPAP-REILARIGP-LGGESatalphaqQWTP-AARPTR 289
Cdd:PRK13184 235 KGRKISYRDVILSPiEVAPYREipPFLSQIAMKALAVDPAERYSSvQELKQDLEPhLQGSP--------EWTVkATLMTK 306
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-285 5.22e-19

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  Cd Length: 1266  Bit Score: 91.44  E-value: 5.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873     37 GRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGAFTAPVVDADPDAP-LPWLVTSYIAGPSLEQAVAERGPFDPQAVL 115
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPgLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    116 TLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGPR----VIDFGI------VRSVDADSLTGSGHMAGSPGFMSPEQVN 185
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphakVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    186 GDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRvvHNAP-DVA---AVADPALRSLIADCLAKDPAHRPAPREIL 261
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ--QLSPvDVSlppWIAGHPLGQVLRKALNKDPRQRAASAPAL 240
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 21222873    262 A---------------RIGPLGGESATALPHAQQWTPAA 285
Cdd:TIGR03903  241 AerfralelcalvgilRMGEGAGREAIAAPLVASGTLDG 279
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
202-336 1.83e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865  Cd Length: 618  Bit Score: 40.85  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  202 LAFAATGTNPFGAGPTPALLYRVVHNAPDVAAVADPALRSL--IADCLAKDPAHRPAPREILARIGPLGGESATALPHAQ 279
Cdd:PRK14951 362 LAFKPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPApaAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA 441
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21222873  280 QwTPAARPTRADAVPTrivPPVAAPPAHQHTRVDTSPAQVYP-PAPAPADVRPTATGD 336
Cdd:PRK14951 442 P-AAVALAPAPPAQAA---PETVAIPVRVAPEPAVASAAPAPaAAPAAARLTPTEEGD 495
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
15-264 6.84e-81

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  Cd Length: 260  Bit Score: 258.29  E-value: 6.84e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  15 YRLLGRLGAGGMGRVFLGRSPG-GRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSY 93
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  94 IAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVDADSLTGSGHM 172
Cdd:cd14014  82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGSV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 173 AGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAP----DVAAVADPALRSLIADCLA 248
Cdd:cd14014 162 LGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILRALA 241
                       250
                ....*....|....*..
gi 21222873 249 KDPAHRP-APREILARI 264
Cdd:cd14014 242 KDPEERPqSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
15-262 6.79e-47

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 166.94  E-value: 6.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873     15 YRLLGRLGAGGMGRVFLGRS-PGGRLVAVKVVHAELLRrpEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSY 93
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKKIK--KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873     94 IAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGP-RVIDFGIVRSVDADSLTGSghM 172
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    173 AGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNA----PDVAAVADPALRSLIADCLA 248
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPkppfPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 21222873    249 KDPAHRPAPREILA 262
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
15-262 1.40e-39

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 146.20  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    15 YRLLGRLGAGGMGRVFLGR-SPGGRLVAVKVVHAELlRRPEFRDRFRREVQAARMVS--------GAFTapvvdaDPDAP 85
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKIKKEK-IKKKKDKNILREIKILKKLNhpnivrlyDAFE------DKDNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    86 lpWLVTSYIAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVDAD 164
Cdd:pfam00069  74 --YLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873   165 SLTGSghMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAPDVAAVAD--PALRSL 242
Cdd:pfam00069 152 SSLTS--FVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPSSisEEAKDL 229
                         250       260
                  ....*....|....*....|
gi 21222873   243 IADCLAKDPAHRPAPREILA 262
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
14-263 6.36e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 144.88  E-value: 6.36e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  14 EYRLLGRLGAGGMGRVFLGRSPggRLVAVKVVHAELLRRPEFRDRFRREVQAARMVSGA-FTAPVVDADPDAPLPWLVTS 92
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  93 YIAGPSLEQAVAERG---PFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGPRV--IDFGIVRSVDADSLT 167
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVklIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 168 GSGH-----MAGSPGFMSPEQVNG---DEVTWASDVFCLGAVLAFAATGTNPFGAGP---TPALLYRVVHNA-------- 228
Cdd:COG0515 159 SSIPalpstSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELptpslasp 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21222873 229 --PDVAAVADPALRSLIADCLAKDPAHRPAPREILAR 263
Cdd:COG0515 239 lsPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSH 275
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
21-264 1.49e-37

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  Cd Length: 245  Bit Score: 139.98  E-value: 1.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  21 LGAGGMGRVFLGRSpGGRLVAVKVVHAELLRRPEFRDrFRREVQAARMVS--------GAFTAPvvdadpdaPLPWLVTS 92
Cdd:cd13999   1 IGSGSFGEVYKGKW-RGTDVAIKKLKVEDDNDELLKE-FRREVSILSKLRhpnivqfiGACLSP--------PPLCIVTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  93 YIAGPSLEQAVAE-RGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSVdADSLTGSG 170
Cdd:cd13999  71 YMPGGSLYDLLHKkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFtVKIADFGLSRIK-NSTTEKMT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 171 HMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNA--PDVAAVADPALRSLIADCLA 248
Cdd:cd13999 150 GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGlrPPIPPDCPPELSKLIKRCWN 229
                       250
                ....*....|....*.
gi 21222873 249 KDPAHRPAPREILARI 264
Cdd:cd13999 230 EDPEKRPSFSEIVKRL 245
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
14-261 5.32e-37

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  Cd Length: 254  Bit Score: 138.88  E-value: 5.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  14 EYRLLGRLGAGGMGRVFLGRS-PGGRLVAVKVVHaelLRRPEFRDRFRREVQAARMVS--------GAFtapvVDADPda 84
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHkKTGQIVAIKKIN---LESKEKKESILNEIAILKKCKhpnivkyyGSY----LKKDE-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  85 plPWLVTSYIAGPSLEQAVAER-GPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGP-RVIDFGIvrSVD 162
Cdd:cd05122  72 --LWIVMEFCSGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEvKLIDFGL--SAQ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 163 ADSLTGSGHMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAPdvaavadPALRS- 241
Cdd:cd05122 148 LSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGP-------PGLRNp 220
                       250       260
                ....*....|....*....|....*....
gi 21222873 242 ---------LIADCLAKDPAHRPAPREIL 261
Cdd:cd05122 221 kkwskefkdFLKKCLQKDPEKRPTAEQLL 249
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
21-261 5.51e-37

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  Cd Length: 215  Bit Score: 137.79  E-value: 5.51e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  21 LGAGGMGRVFLGRSPG-GRLVAVKVVHAELLRRPefRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTSYIAGPSL 99
Cdd:cd00180   1 LGKGSFGKVYKARDKEtGKKVAVKVIPKEKLKKL--LEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 100 EQAVAER-GPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDG-PRVIDFGIVRSV-DADSLTGSGHMAGSP 176
Cdd:cd00180  79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGtVKLADFGLAKDLdSDDSLLKTTGGTTPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 177 GFMSPEQVNGDEVTWASDVFCLGAVLafaatgtnpfgagptpallYRVvhnapdvaavadPALRSLIADCLAKDPAHRPA 256
Cdd:cd00180 159 YYAPPELLGGRYYGPKVDIWSLGVIL-------------------YEL------------EELKDLIRRMLQYDPKKRPS 207

                ....*
gi 21222873 257 PREIL 261
Cdd:cd00180 208 AKELL 212
LamGL smart00560
LamG-like jellyroll fold domain;
451-583 8.02e-34

LamG-like jellyroll fold domain;


Pssm-ID: 214722  Cd Length: 133  Bit Score: 126.38  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    451 RSFTVAAWVRLSAVPGVFA----TAVSQD--SADASGFYLQYSSeDQGWAFARPGlravgRTAPAAHVWTHLTGVCDGPA 524
Cdd:smart00560   1 GSFTLEAWVKLESAGGSQPiitgAAVAQPtiSEKALTFFLRAKS-VQGWQTARTG-----ATADWIGVWVHLAGVYDGGA 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873    525 RKLHLYVNGVQEAVVEDTgPAPATGAFMIG-RASFDGQPRDFFPGAIRDVRAFDRALGPA 583
Cdd:smart00560  75 GKLSLYVNGVEVATSETQ-PSPSSGNLPQGgRILLGGAGGENFSGRLDEVRVYNRALTAR 133
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
15-264 1.76e-29

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  Cd Length: 258  Bit Score: 117.95  E-value: 1.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  15 YRLLGRLGAGGMGRVFLGRS-PGGRLVAVKVVHAELLRRPEfRDRFRREVQAARMVS--------GAFTAPVVdadpdap 85
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRkSDGKLYVLKEIDLSNMSEKE-REEALNEVKLLSKLKhpnivkyyESFEENGK------- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  86 lpwL--VTSYIAGPSLEQAVAER----GPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGprVI---DFG 156
Cdd:cd08215  74 ---LciVMEYADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG--VVklgDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 157 IVRSvdadsLTGSGHMA----GSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVH-NAPDV 231
Cdd:cd08215 149 ISKV-----LESTTDLAktvvGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKgQYPPI 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 21222873 232 AAVADPALRSLIADCLAKDPAHRPAPREILARI 264
Cdd:cd08215 224 PSQYSSELRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
15-262 3.82e-29

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-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: 270905  Cd Length: 252  Bit Score: 116.85  E-value: 3.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  15 YRLLGRLGAGGMGRVFLGR-SPGGRLVAVKVVHAELLRRPEFRdRFRREVQAARMVsgafTAP-------VVDaDPDAPl 86
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARhKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLL----NHPniiklyeVIE-TENKI- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  87 pWLVTSYIAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGP-RVIDFGIVRSVDADS 165
Cdd:cd14003  75 -YLVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNlKIIDFGLSNEFRGGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 166 LTGSghMAGSPGFMSPEQVNGDEV-TWASDVFCLGAVLAFAATGTNPFGAGPTPALLYRVVHNAPDVAAVADPALRSLIA 244
Cdd:cd14003 154 LLKT--FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIR 231
                       250
                ....*....|....*...
gi 21222873 245 DCLAKDPAHRPAPREILA 262
Cdd:cd14003 232 RMLVVDPSKRITIEEILN 249
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
14-261 4.08e-29

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  Cd Length: 258  Bit Score: 116.85  E-value: 4.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  14 EYRLLGRLGAGGMGRVFLGRSPG-GRLVAVKVVHAELlRRPEFRDRFRREVQAARMVSGAFTAPVVDADPDAPLPWLVTS 92
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDtGELMAVKEVELSG-DSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  93 YIAGPSLEQAVAERGPFDPQAVLTLAAGLAEALVSIHAAHLVHRDLKPSNVLLAEDGprVI---DFGIVRSV-DADSLTG 168
Cdd:cd06606  80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG--VVklaDFGCAKRLaEIATGEG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873 169 SGHMAGSPGFMSPEQVNGDEVTWASDVFCLGAVLAFAATGTNPFGA-GPTPALLYRVVH--NAPDVAAVADPALRSLIAD 245
Cdd:cd06606 158 TKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSsgEPPPIPEHLSEEAKDFLRK 237
                       250
                ....*....|....*.
gi 21222873 246 CLAKDPAHRPAPREIL 261
Cdd:cd06606 238 CLQRDPKKRPTADELL 253
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
21-267 1.48e-28

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  Cd Length: 272  Bit Score: 115.83  E-value: 1.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222873  21 LGAGGMGRVFLGRSPGGRLVAVKVVHAEllRRPEFRDRFRREVQaarmVSGAFTAP-VVD-----ADPDAPLpwLVTSYI 94
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEM--NCAASKKEFLTELE----ML