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Conserved domains on  [gi|15608884|ref|NP_216262|]
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serine/threonine-protein kinase PknF [Mycobacterium tuberculosis H37Rv]

Protein Classification

serine/threonine protein kinase (domain architecture ID 10195858)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

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 ...
11-274 6.94e-102

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: 309.13  E-value: 6.94e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMD 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  91 FVDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDpS 170
Cdd:cd14014  81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILL----TEDGRVKLTDFGIARALGD-S 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 171 GLTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTP-LD 249
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                       250       260
                ....*....|....*....|....*
gi 15608884 250 PVFAKALAKQPKDRYQRCVDFARAL 274
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAAL 258
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-274 6.94e-102

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: 309.13  E-value: 6.94e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMD 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  91 FVDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDpS 170
Cdd:cd14014  81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILL----TEDGRVKLTDFGIARALGD-S 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 171 GLTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTP-LD 249
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                       250       260
                ....*....|....*....|....*
gi 15608884 250 PVFAKALAKQPKDRYQRCVDFARAL 274
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAAL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-274 8.37e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 182.25  E-value: 8.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPrqdALKVLRADVSADGEYRARFNREADAAASL-WHPHIVAVHDRGEFDGQLWIDM 89
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  90 DFVDGTDTVSLLRDRYPNG-MPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpDSPDRRIMLADFGIAGWVDD 168
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL---DRDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 169 PSGLTATNMT----VGTVSYAAPEQLMGNEL---DGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLS--------A 233
Cdd:COG0515 155 PGSTSSIPALpstsVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptpS 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15608884 234 SPPAIGDRVPELTP--LDPVFAKALAKQPKDRYQRCVDFARAL 274
Cdd:COG0515 235 LASPLSPSNPELISkaASDLLKKLLAKDPKNRLSSSSDLSHDL 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-276 1.08e-51

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 178.11  E-value: 1.08e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRadVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     92 VDGTDTVSLLRDRypNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGWVDDPsg 171
Cdd:smart00220  79 CEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE----DGHVKLADFGLARQLDPG-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    172 lTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTP-LDP 250
Cdd:smart00220 151 -EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPeAKD 229
                          250       260
                   ....*....|....*....|....*.
gi 15608884    251 VFAKALAKQPKDRYqrcvDFARALGH 276
Cdd:smart00220 230 LIRKLLVKDPEKRL----TAEEALQH 251
Pkinase pfam00069
Protein kinase domain;
12-222 8.72e-37

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 137.34  E-value: 8.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADvSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    92 VDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDPSG 171
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI----DEDGNLKITDFGLARQLNSGSS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15608884   172 LTatnMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHAN 222
Cdd:pfam00069 154 LT---SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGIN 201
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-265 2.05e-31

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 128.35  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884   12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVH---DRGEfdgQLWID 88
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYsicSDGD---PVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884   89 MDFVDGTDTVSLLRDRYPNGMPGPEVTE---------IITAVAEALDYAHERRLLHRDVKPANILIANPDspdrRIMLAD 159
Cdd:PRK13184  81 MPYIEGYTLKSLLKSVWQKESLSKELAEktsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  160 FGIA----------GWVD-DPSGLTATNMT-----VGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANP 223
Cdd:PRK13184 157 WGAAifkkleeedlLDIDvDERNICYSSMTipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKG 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15608884  224 AVVISQHLSASPPAIGdrvP--ELTP-LDPVFAKALAKQPKDRYQ 265
Cdd:PRK13184 237 RKISYRDVILSPIEVA---PyrEIPPfLSQIAMKALAVDPAERYS 278
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
39-263 5.95e-29

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: 121.11  E-value: 5.95e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     39 ALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEF-DGQLWIDMDFVDGTDTVSLLRDRYPngMPGPEVTEI 117
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGA--LPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    118 ITAVAEALDYAHERRLLHRDVKPANILIANPDSpDRRIMLADFGIAGWV-----DDPSGLTATNMTVGTVSYAAPEQLMG 192
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGV-RPHAKVLDFGIGTLLpgvrdADVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608884    193 NELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLS----ASPPAIgdrvpELTPLDPVFAKALAKQPKDR 263
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSpvdvSLPPWI-----AGHPLGQVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-274 6.94e-102

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: 309.13  E-value: 6.94e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMD 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  91 FVDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDpS 170
Cdd:cd14014  81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILL----TEDGRVKLTDFGIARALGD-S 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 171 GLTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTP-LD 249
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                       250       260
                ....*....|....*....|....*
gi 15608884 250 PVFAKALAKQPKDRYQRCVDFARAL 274
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAAL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-274 8.37e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 182.25  E-value: 8.37e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPrqdALKVLRADVSADGEYRARFNREADAAASL-WHPHIVAVHDRGEFDGQLWIDM 89
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  90 DFVDGTDTVSLLRDRYPNG-MPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpDSPDRRIMLADFGIAGWVDD 168
Cdd:COG0515  78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL---DRDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 169 PSGLTATNMT----VGTVSYAAPEQLMGNEL---DGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLS--------A 233
Cdd:COG0515 155 PGSTSSIPALpstsVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptpS 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15608884 234 SPPAIGDRVPELTP--LDPVFAKALAKQPKDRYQRCVDFARAL 274
Cdd:COG0515 235 LASPLSPSNPELISkaASDLLKKLLAKDPKNRLSSSSDLSHDL 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-276 1.08e-51

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 178.11  E-value: 1.08e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRadVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     92 VDGTDTVSLLRDRypNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGWVDDPsg 171
Cdd:smart00220  79 CEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE----DGHVKLADFGLARQLDPG-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    172 lTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELTP-LDP 250
Cdd:smart00220 151 -EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPeAKD 229
                          250       260
                   ....*....|....*....|....*.
gi 15608884    251 VFAKALAKQPKDRYqrcvDFARALGH 276
Cdd:smart00220 230 LIRKLLVKDPEKRL----TAEEALQH 251
Pkinase pfam00069
Protein kinase domain;
12-222 8.72e-37

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 137.34  E-value: 8.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADvSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    92 VDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDPSG 171
Cdd:pfam00069  80 VEGGSLFDLLSEKGA--FSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI----DEDGNLKITDFGLARQLNSGSS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15608884   172 LTatnMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHAN 222
Cdd:pfam00069 154 LT---SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGIN 201
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-211 7.40e-36

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: 133.55  E-value: 7.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  18 LGSGGMGEVYLARHPRLPRQDALKVLraDVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDFVDGTDT 97
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  98 VSLLRdRYPNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGWVDDPSGLTATNM 177
Cdd:cd00180  79 KDLLK-ENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS----DGTVKLADFGLAKDLDSDDSLLKTTG 153
                       170       180       190
                ....*....|....*....|....*....|....
gi 15608884 178 TVGTVSYAAPEQLMGNELDGRADQYALAATAFHL 211
Cdd:cd00180 154 GTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-229 3.70e-35

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687  Cd Length: 258  Bit Score: 132.60  E-value: 3.70e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADvSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKK-KLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRDRypNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANPDsPDRRIMLADFGIAGWVDDPSG 171
Cdd:cd05117  81 CTGGELFDRIVKK--GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD-PDSPIKIIDFGLAKIFEEGEK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15608884 172 LTAtnmTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQ 229
Cdd:cd05117 158 LKT---VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEK 212
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-223 1.79e-34

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: 130.79  E-value: 1.79e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLraDVSADGEYRARFNrEADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKI--NLESKEKKESILN-EIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRDRyPNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGwvdDPSG 171
Cdd:cd05122  79 CSGGSLKDLLKNT-NKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILL----TSDGEVKLIDFGLSA---QLSD 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15608884 172 LTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANP 223
Cdd:cd05122 151 GKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPP 202
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-263 1.39e-33

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: 128.35  E-value: 1.39e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  11 GFTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNrEADAAASLWHPHIVAVHDRGEFDGQLWIDMD 90
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALN-EVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  91 FVDGTDTVSLLRDRYPNGMPGPE--VTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGWVDD 168
Cdd:cd08215  80 YADGGDLAQKIKKQKKKGQPFPEeqILDWFVQICLALKYLHSRKILHRDLKTQNIFLTK----DGVVKLGDFGISKVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 169 PSGLTATnmTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRV-PELTP 247
Cdd:cd08215 156 TTDLAKT--VVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYsSELRD 233
                       250
                ....*....|....*.
gi 15608884 248 LdpvFAKALAKQPKDR 263
Cdd:cd08215 234 L---VNSMLQKDPEKR 246
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-265 2.05e-31

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 128.35  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884   12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVH---DRGEfdgQLWID 88
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYsicSDGD---PVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884   89 MDFVDGTDTVSLLRDRYPNGMPGPEVTE---------IITAVAEALDYAHERRLLHRDVKPANILIANPDspdrRIMLAD 159
Cdd:PRK13184  81 MPYIEGYTLKSLLKSVWQKESLSKELAEktsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  160 FGIA----------GWVD-DPSGLTATNMT-----VGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANP 223
Cdd:PRK13184 157 WGAAifkkleeedlLDIDvDERNICYSSMTipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKG 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15608884  224 AVVISQHLSASPPAIGdrvP--ELTP-LDPVFAKALAKQPKDRYQ 265
Cdd:PRK13184 237 RKISYRDVILSPIEVA---PyrEIPPfLSQIAMKALAVDPAERYS 278
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-263 9.34e-31

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-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: 270786  Cd Length: 274  Bit Score: 120.43  E-value: 9.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLraDVSADGEYRARFNREADAAASLWHPHIVAVHdrGEF--DGQLWIDM 89
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI--DLEEAEDEIEDIQQEIQFLSQCDSPYITKYY--GSFlkGSKLWIIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  90 DFVDGTDTVSLLRdryPNGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGwvddp 169
Cdd:cd06609  79 EYCGGGSVLDLLK---PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSE----EGDVKLADFGVSG----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 170 sGLTAT----NMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRvpEL 245
Cdd:cd06609 147 -QLTSTmskrNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGN--KF 223
                       250
                ....*....|....*....
gi 15608884 246 TPLDPVF-AKALAKQPKDR 263
Cdd:cd06609 224 SKPFKDFvELCLNKDPKER 242
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-212 2.94e-30

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK 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: 270898  Cd Length: 273  Bit Score: 118.93  E-value: 2.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARfnREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd13996   8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVL--REVKALAKLNHPNIVRYYTAWVEEPPLYIQMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLL--RDRYPNGMPgPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpDSPDRRIMLADFGIAGWVDD- 168
Cdd:cd13996  86 CEGGTLRDWIdrRNSSSKNDR-KLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL---DNDDLQVKIGDFGLATSIGNq 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15608884 169 ----------PSGLTATNMT-VGTVSYAAPEQLMGNELDGRADQYALAATAFHLL 212
Cdd:cd13996 162 krelnnlnnnNNGNTSNNSVgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
12-218 6.28e-30

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909  Cd Length: 253  Bit Score: 117.58  E-value: 6.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFgiaGW-VDDPS 170
Cdd:cd14007  82 APNGELYKELKKQKR--FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGS----NGELKLADF---GWsVHAPS 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15608884 171 GLTATnmTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPF 218
Cdd:cd14007 153 NRRKT--FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPF 198
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-218 2.09e-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: 116.08  E-value: 2.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRaRFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRDRYPngMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpDSpDRRIMLADFGIAGWVDDPSG 171
Cdd:cd14003  81 ASGGELFDYIVNNGR--LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---DK-NGNLKIIDFGLSNEFRGGSL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15608884 172 LtatNMTVGTVSYAAPEQLMGNELDGR-ADQYALAATAFHLLTGSPPF 218
Cdd:cd14003 155 L---KTFCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPF 199
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
39-263 5.95e-29

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: 121.11  E-value: 5.95e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884     39 ALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHDRGEF-DGQLWIDMDFVDGTDTVSLLRDRYPngMPGPEVTEI 117
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGA--LPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884    118 ITAVAEALDYAHERRLLHRDVKPANILIANPDSpDRRIMLADFGIAGWV-----DDPSGLTATNMTVGTVSYAAPEQLMG 192
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGV-RPHAKVLDFGIGTLLpgvrdADVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608884    193 NELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLS----ASPPAIgdrvpELTPLDPVFAKALAKQPKDR 263
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSpvdvSLPPWI-----AGHPLGQVLRKALNKDPRQR 233
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
12-263 8.68e-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: 114.54  E-value: 8.68e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  12 FTIVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEYRArFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDF 91
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEA-LEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRdRYPnGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGWVDDPSG 171
Cdd:cd06606  81 VPGGSLASLLK-KFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILV----DSDGVVKLADFGCAKRLAEIAT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 172 LTATNMTVGTVSYAAPEQLMGNELDGRADQYALAATAFHLLTGSPPF-QHANPAVVISqHLSAS--PPAIGDRVPELTpL 248
Cdd:cd06606 155 GEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALF-KIGSSgePPPIPEHLSEEA-K 232
                       250
                ....*....|....*.
gi 15608884 249 DpvF-AKALAKQPKDR 263
Cdd:cd06606 233 D--FlRKCLQRDPKKR 246
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
14-236 4.83e-28

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK 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: 270787  Cd Length: 267  Bit Score: 112.45  E-value: 4.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  14 IVRQLGSGGMGEVYLARHprLPRQDALKVLRADVSADGEYRARFNREADAAASLWHPHIVAVHdrGEF--DGQLWIDMDF 91
Cdd:cd06610   5 LIEVIGSGATAVVYAAYC--LPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYY--TSFvvGDELWLVMPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  92 VDGTDTVSLLRDRYPNG-MPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIANpdspDRRIMLADFGIAGWVDDPS 170
Cdd:cd06610  81 LSGGSLLDIMKSSYPRGgLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE----DGSVKIADFGVSASLATGG 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608884 171 GLT--ATNMTVGTVSYAAPEQL-MGNELDGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPP 236
Cdd:cd06610 157 DRTrkVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPP 225
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
14-263 2.96e-27

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


Pssm-ID: 132975  Cd Length: 292  Bit Score: 110.89  E-value: 2.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  14 IVRQLGSGGMGEVYLARHPRLPRQDALKVLRADVSADGEyraRFNREADAAASLWHPHIVAVHDRGEFDGQLWIDMDFVD 93
Cdd:cd06644  16 IIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELE---DYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884  94 G--TDTVSLLRDRypnGMPGPEVTEIITAVAEALDYAHERRLLHRDVKPANILIanpdSPDRRIMLADFGIAGwvDDPSG 171
Cdd:cd06644  93 GgaVDAIMLELDR---GLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLL----TLDGDIKLADFGVSA--KNVKT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608884 172 LTATNMTVGTVSYAAPEQLMGNEL-----DGRADQYALAATAFHLLTGSPPFQHANPAVVISQHLSASPPAIGDRVPELT 246
Cdd:cd06644 164 LQRRDSFI