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Conserved domains on  [gi|15827075|ref|NP_301338|]
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serine-threonine protein kinase [Mycobacterium leprae TN]

Protein Classification

similar to serine/threonine-protein kinase PknG (domain architecture ID 12180975)

protein similar to serine/threonine-protein kinase PknG

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PknG_TPR pfam16918
Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein ...
426-765 3.84e-176

Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein kinase G and contains a tetratricopeptide repeat (TPR).


:

Pssm-ID: 319004  Cd Length: 340  Bit Score: 512.66  E-value: 3.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   426 AGLSTIFSPSRSTFGVDLLVAHTDVYLDGRLHSEKLTAKDIVTALQVPLVDPTDVAAPVLQATVLSQPVQTLDSLRAARH 505
Cdd:pfam16918   1 PGLSTVFSPQRGTFGTDLLVRQTDVYVDGVERDPKLSAREVAAALPVPLVDPTDPAAALLAATVHSDPAQTLDSLRAARE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   506 GMLDAQGIDLAESVELPLMEVRALLDLGDVVKANRKLDDLADRVSCQWRLVWYRAVADLLTGDYASATKHFTEVLNTFPG 585
Cdd:pfam16918  81 GALDADGVDASESLELPLAEVRAHLDLGDVAKARELLDRLAARIGGDWRLDWYRGLAALLEGDYETAFAHFDAVLAALPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   586 ELAPKLALAATAELAGESDEHKFYRTVWHTNDGVVSAAFGLARFQSAEGDRTGAVCTLDEVPPTSRHFTTARLTSAVTLL 665
Cdd:pfam16918 161 EIAPKLALAATAELAGETDAEKYYRTVWRTDRGVVSAAFGLARQLAAAGDRAGAVAALDQVPATSRHFTTARLTAVLTLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   666 SGRSTNEITEQQIRDAARRVETLPPTEPRVLQIRALVLGCAMDWLADNQASANHILGFPFTKHGLRLGVEASLRSLARVA 745
Cdd:pfam16918 241 SGRPPAELDEADLREAARRVEALPLDEPRALQLRALVLGAALDWLRAGGASTEHILGVPFTERGLRTGLEAALRALARNA 320
                         330       340
                  ....*....|....*....|
gi 15827075   746 PTQRHRYTLVDMANKVRPTS 765
Cdd:pfam16918 321 PDRTHRYALVDLANAIRPRS 340
PknG_rubred pfam16919
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ...
19-163 1.31e-77

Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of protein kinase G, and is essential for kinase activity.


:

Pssm-ID: 319005  Cd Length: 137  Bit Score: 248.86  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    19 QAAQRAD--PPSGTTEGRLQSTQAIFRPNFDDDddllHISVPSVDTEPQDRITPATRVLPPIRQLGGGLVEIRRVRDIDP 96
Cdd:pfam16919   1 PGTQPADdlPSASAATSRPMSTQAVFRPRFDDD----SISLGALDTEPSGRSTSATRSLSPRRRLGGGLVEIPRVPDIDP 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15827075    97 LEALMTNPVVPESKRFCWNCGRPVGRSELEGqeadgaQGAKEGWCPYCGSPYSFLPQLSPGDIVAGQ 163
Cdd:pfam16919  77 LTAVMTNPVVPESKRFCWNCGRPVGRSTGDG------PGRSEGWCPHCGSPYSFLPQLSPGDIVAGQ 137
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
163-409 1.25e-56

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: 195.88  E-value: 1.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVH--SGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHkdtsgDPV 240
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRPelAEDEEFRERFLREARALARLSHPNIVRVYDVGED-----DGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 GYIVMEYIGGRSLKRGSKKGNveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAV----- 314
Cdd:cd14014  75 PYIVMEYVEGGSLADLLRERG--PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDgRVKLTDFGIAralgd 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 315 SRINSFGCIYGTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL----------TLNLRTRNGRYMDGLPEDDPVLTTYDSF 383
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPvDPRSDIYSLGVVLYELltgrppfdgdSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*.
gi 15827075 384 ARLLHRAINPDPRRRFSSAEEMSAQL 409
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAAL 258
 
Name Accession Description Interval E-value
PknG_TPR pfam16918
Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein ...
426-765 3.84e-176

Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein kinase G and contains a tetratricopeptide repeat (TPR).


Pssm-ID: 319004  Cd Length: 340  Bit Score: 512.66  E-value: 3.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   426 AGLSTIFSPSRSTFGVDLLVAHTDVYLDGRLHSEKLTAKDIVTALQVPLVDPTDVAAPVLQATVLSQPVQTLDSLRAARH 505
Cdd:pfam16918   1 PGLSTVFSPQRGTFGTDLLVRQTDVYVDGVERDPKLSAREVAAALPVPLVDPTDPAAALLAATVHSDPAQTLDSLRAARE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   506 GMLDAQGIDLAESVELPLMEVRALLDLGDVVKANRKLDDLADRVSCQWRLVWYRAVADLLTGDYASATKHFTEVLNTFPG 585
Cdd:pfam16918  81 GALDADGVDASESLELPLAEVRAHLDLGDVAKARELLDRLAARIGGDWRLDWYRGLAALLEGDYETAFAHFDAVLAALPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   586 ELAPKLALAATAELAGESDEHKFYRTVWHTNDGVVSAAFGLARFQSAEGDRTGAVCTLDEVPPTSRHFTTARLTSAVTLL 665
Cdd:pfam16918 161 EIAPKLALAATAELAGETDAEKYYRTVWRTDRGVVSAAFGLARQLAAAGDRAGAVAALDQVPATSRHFTTARLTAVLTLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   666 SGRSTNEITEQQIRDAARRVETLPPTEPRVLQIRALVLGCAMDWLADNQASANHILGFPFTKHGLRLGVEASLRSLARVA 745
Cdd:pfam16918 241 SGRPPAELDEADLREAARRVEALPLDEPRALQLRALVLGAALDWLRAGGASTEHILGVPFTERGLRTGLEAALRALARNA 320
                         330       340
                  ....*....|....*....|
gi 15827075   746 PTQRHRYTLVDMANKVRPTS 765
Cdd:pfam16918 321 PDRTHRYALVDLANAIRPRS 340
PknG_rubred pfam16919
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ...
19-163 1.31e-77

Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of protein kinase G, and is essential for kinase activity.


Pssm-ID: 319005  Cd Length: 137  Bit Score: 248.86  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    19 QAAQRAD--PPSGTTEGRLQSTQAIFRPNFDDDddllHISVPSVDTEPQDRITPATRVLPPIRQLGGGLVEIRRVRDIDP 96
Cdd:pfam16919   1 PGTQPADdlPSASAATSRPMSTQAVFRPRFDDD----SISLGALDTEPSGRSTSATRSLSPRRRLGGGLVEIPRVPDIDP 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15827075    97 LEALMTNPVVPESKRFCWNCGRPVGRSELEGqeadgaQGAKEGWCPYCGSPYSFLPQLSPGDIVAGQ 163
Cdd:pfam16919  77 LTAVMTNPVVPESKRFCWNCGRPVGRSTGDG------PGRSEGWCPHCGSPYSFLPQLSPGDIVAGQ 137
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
163-409 1.25e-56

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: 195.88  E-value: 1.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVH--SGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHkdtsgDPV 240
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRPelAEDEEFRERFLREARALARLSHPNIVRVYDVGED-----DGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 GYIVMEYIGGRSLKRGSKKGNveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAV----- 314
Cdd:cd14014  75 PYIVMEYVEGGSLADLLRERG--PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDgRVKLTDFGIAralgd 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 315 SRINSFGCIYGTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL----------TLNLRTRNGRYMDGLPEDDPVLTTYDSF 383
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPvDPRSDIYSLGVVLYELltgrppfdgdSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*.
gi 15827075 384 ARLLHRAINPDPRRRFSSAEEMSAQL 409
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
164-405 3.72e-37

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 141.13  E-value: 3.72e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    164 YEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgYI 243
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKK-TGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-----YL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    244 VMEYIGGRSLKRGSKKGNveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSFGC 322
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDgHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    323 IY---GTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL----------TLNLRTRNGRYMDGLPEDDPVLTTYDSFARLLH 388
Cdd:smart00220 153 LTtfvGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELltgkppfpgdDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                          250
                   ....*....|....*..
gi 15827075    389 RAINPDPRRRFSSAEEM 405
Cdd:smart00220 233 KLLVKDPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
164-403 7.78e-34

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 131.57  E-value: 7.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   164 YEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQ-ASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgY 242
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRD-TGKIVAIKKIKKEKIKKKKdKNILREIKILKKLNHPNIVRLYDAFEDKDNL-----Y 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   243 IVMEYIGGRSLKRG-SKKGNvekLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSF 320
Cdd:pfam00069  75 LVLEYVEGGSLFDLlSEKGA---FSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDgNLKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   321 GCIY---GTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL-------------TLNLRTRNGRYMDGLPEDDPvlttyDSF 383
Cdd:pfam00069 152 SSLTsfvGTPWYMAPEVLRGNPyGPKVDVWSLGCILYELltgkppfpgingnEIYEKIIDQDFDSPRPSSIS-----EEA 226
                         250       260
                  ....*....|....*....|
gi 15827075   384 ARLLHRAINPDPRRRFSSAE 403
Cdd:pfam00069 227 KDLLKKLLKKDPSKRLTATE 246
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
164-410 9.55e-34

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 134.48  E-value: 9.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 164 YEVKGCIAHGGLGWVYLAFDHnvndRPVVLKGL--VHSGDAEAQASAVAERQFLAEVVHP-QIVQIFNFVEHKDTSgdpv 240
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR----KLVALKVLakKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 gYIVMEYIGGRSLKRGSKK-GNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE--QLKLIDLGAVSRI 317
Cdd:COG0515  74 -YLVMEYVDGGSLEDLLKKiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgrVVKLIDFGLAKLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 318 NSFGC----------IYGTPGYQAPEIVRTG----PTVATDIYTVGRTLAALTL-------------------NLRTRNG 364
Cdd:COG0515 153 PDPGStssipalpstSVGTPGYMAPEVLLGLslayASSSSDIWSLGITLYELLTglppfegeknssatsqtlkIILELPT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15827075 365 RYMDGLPEDDPVLTTYDSFARLLHRAINPDPRRRFSSAEEMSAQLM 410
Cdd:COG0515 233 PSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLL 278
pknD PRK13184
serine/threonine-protein kinase; Reviewed
162-409 1.72e-23

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 106.39  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  162 GQYEVKGCIAHGGLGWVYLAFDhNVNDRPVVLKGLVH--SGDAEAQASAVAERQFLAEVVHPQIVQIFNFVehkdTSGDP 239
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYD-PVCSRRVALKKIREdlSENPLLKKRFLREAKIAADLIHPGIVPVYSIC----SDGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  240 VgYIVMEYIGGRSLKR---------GSKKGNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIML--------- 301
Cdd:PRK13184  77 V-YYTMPYIEGYTLKSllksvwqkeSLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLglfgevvil 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  302 ----------TEEQLKLIDLGAV----SRINSFGCIYGTPGYQAPEIVRTGP-TVATDIYTVGRTL-AALTLNL--RTRN 363
Cdd:PRK13184 156 dwgaaifkklEEEDLLDIDVDERnicySSMTIPGKIVGTPDYMAPERLLGVPaSESTDIYALGVILyQMLTLSFpyRRKK 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15827075  364 GRYM---DGLP---EDDPVLTTYDSFARLLHRAINPDPRRRFSSAEEMSAQL 409
Cdd:PRK13184 236 GRKIsyrDVILspiEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
191-434 8.39e-15

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: 78.73  E-value: 8.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    191 VVLKGL--VHSGDAEAQASAVAERQFLAEVVHPQIVQIFNfvehKDTSGDPVGYIVMEYIGGRSLKrgSKKGNVEKLPVA 268
Cdd:TIGR03903    6 VAIKLLrtDAPEEEHQRARFRRETALCARLYHPNIVALLD----SGEAPPGLLFAVFEYVPGRTLR--EVLAADGALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    269 EAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQL----KLIDLG-----------AVSRINSFGCIYGTPGYQAPE 333
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphaKVLDFGigtllpgvrdaDVATLTRTTEVLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    334 IVRTGP-TVATDIYTVGRTLAALTLNLRTRNGR-----YMDGLPEDD----PVLTTYdSFARLLHRAINPDPRRRFSSAE 403
Cdd:TIGR03903  160 QLRGEPvTPNSDLYAWGLIFLECLTGQRVVQGAsvaeiLYQQLSPVDvslpPWIAGH-PLGQVLRKALNKDPRQRAASAP 238
                          250       260       270
                   ....*....|....*....|....*....|..
gi 15827075    404 EMSAQLMGV-LREVVAQDTGVPRAGLSTIFSP 434
Cdd:TIGR03903  239 ALAERFRALeLCALVGILRMGEGAGREAIAAP 270
 
Name Accession Description Interval E-value
PknG_TPR pfam16918
Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein ...
426-765 3.84e-176

Protein kinase G tetratricopeptide repeat; This domain is found at the C-terminus of protein kinase G and contains a tetratricopeptide repeat (TPR).


Pssm-ID: 319004  Cd Length: 340  Bit Score: 512.66  E-value: 3.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   426 AGLSTIFSPSRSTFGVDLLVAHTDVYLDGRLHSEKLTAKDIVTALQVPLVDPTDVAAPVLQATVLSQPVQTLDSLRAARH 505
Cdd:pfam16918   1 PGLSTVFSPQRGTFGTDLLVRQTDVYVDGVERDPKLSAREVAAALPVPLVDPTDPAAALLAATVHSDPAQTLDSLRAARE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   506 GMLDAQGIDLAESVELPLMEVRALLDLGDVVKANRKLDDLADRVSCQWRLVWYRAVADLLTGDYASATKHFTEVLNTFPG 585
Cdd:pfam16918  81 GALDADGVDASESLELPLAEVRAHLDLGDVAKARELLDRLAARIGGDWRLDWYRGLAALLEGDYETAFAHFDAVLAALPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   586 ELAPKLALAATAELAGESDEHKFYRTVWHTNDGVVSAAFGLARFQSAEGDRTGAVCTLDEVPPTSRHFTTARLTSAVTLL 665
Cdd:pfam16918 161 EIAPKLALAATAELAGETDAEKYYRTVWRTDRGVVSAAFGLARQLAAAGDRAGAVAALDQVPATSRHFTTARLTAVLTLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   666 SGRSTNEITEQQIRDAARRVETLPPTEPRVLQIRALVLGCAMDWLADNQASANHILGFPFTKHGLRLGVEASLRSLARVA 745
Cdd:pfam16918 241 SGRPPAELDEADLREAARRVEALPLDEPRALQLRALVLGAALDWLRAGGASTEHILGVPFTERGLRTGLEAALRALARNA 320
                         330       340
                  ....*....|....*....|
gi 15827075   746 PTQRHRYTLVDMANKVRPTS 765
Cdd:pfam16918 321 PDRTHRYALVDLANAIRPRS 340
PknG_rubred pfam16919
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ...
19-163 1.31e-77

Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of protein kinase G, and is essential for kinase activity.


Pssm-ID: 319005  Cd Length: 137  Bit Score: 248.86  E-value: 1.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    19 QAAQRAD--PPSGTTEGRLQSTQAIFRPNFDDDddllHISVPSVDTEPQDRITPATRVLPPIRQLGGGLVEIRRVRDIDP 96
Cdd:pfam16919   1 PGTQPADdlPSASAATSRPMSTQAVFRPRFDDD----SISLGALDTEPSGRSTSATRSLSPRRRLGGGLVEIPRVPDIDP 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15827075    97 LEALMTNPVVPESKRFCWNCGRPVGRSELEGqeadgaQGAKEGWCPYCGSPYSFLPQLSPGDIVAGQ 163
Cdd:pfam16919  77 LTAVMTNPVVPESKRFCWNCGRPVGRSTGDG------PGRSEGWCPHCGSPYSFLPQLSPGDIVAGQ 137
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
163-409 1.25e-56

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: 195.88  E-value: 1.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVH--SGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHkdtsgDPV 240
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRPelAEDEEFRERFLREARALARLSHPNIVRVYDVGED-----DGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 GYIVMEYIGGRSLKRGSKKGNveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAV----- 314
Cdd:cd14014  75 PYIVMEYVEGGSLADLLRERG--PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDgRVKLTDFGIAralgd 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 315 SRINSFGCIYGTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL----------TLNLRTRNGRYMDGLPEDDPVLTTYDSF 383
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPvDPRSDIYSLGVVLYELltgrppfdgdSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|....*.
gi 15827075 384 ARLLHRAINPDPRRRFSSAEEMSAQL 409
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAELLAAL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
164-405 3.72e-37

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 141.13  E-value: 3.72e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    164 YEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgYI 243
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKK-TGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-----YL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    244 VMEYIGGRSLKRGSKKGNveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSFGC 322
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDgHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075    323 IY---GTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL----------TLNLRTRNGRYMDGLPEDDPVLTTYDSFARLLH 388
Cdd:smart00220 153 LTtfvGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELltgkppfpgdDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIR 232
                          250
                   ....*....|....*..
gi 15827075    389 RAINPDPRRRFSSAEEM 405
Cdd:smart00220 233 KLLVKDPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
164-403 7.78e-34

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 131.57  E-value: 7.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   164 YEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQ-ASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgY 242
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRD-TGKIVAIKKIKKEKIKKKKdKNILREIKILKKLNHPNIVRLYDAFEDKDNL-----Y 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   243 IVMEYIGGRSLKRG-SKKGNvekLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSF 320
Cdd:pfam00069  75 LVLEYVEGGSLFDLlSEKGA---FSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDgNLKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075   321 GCIY---GTPGYQAPEIVRTGP-TVATDIYTVGRTLAAL-------------TLNLRTRNGRYMDGLPEDDPvlttyDSF 383
Cdd:pfam00069 152 SSLTsfvGTPWYMAPEVLRGNPyGPKVDVWSLGCILYELltgkppfpgingnEIYEKIIDQDFDSPRPSSIS-----EEA 226
                         250       260
                  ....*....|....*....|
gi 15827075   384 ARLLHRAINPDPRRRFSSAE 403
Cdd:pfam00069 227 KDLLKKLLKKDPSKRLTATE 246
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
164-410 9.55e-34

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 134.48  E-value: 9.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 164 YEVKGCIAHGGLGWVYLAFDHnvndRPVVLKGL--VHSGDAEAQASAVAERQFLAEVVHP-QIVQIFNFVEHKDTSgdpv 240
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR----KLVALKVLakKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 gYIVMEYIGGRSLKRGSKK-GNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE--QLKLIDLGAVSRI 317
Cdd:COG0515  74 -YLVMEYVDGGSLEDLLKKiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgrVVKLIDFGLAKLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 318 NSFGC----------IYGTPGYQAPEIVRTG----PTVATDIYTVGRTLAALTL-------------------NLRTRNG 364
Cdd:COG0515 153 PDPGStssipalpstSVGTPGYMAPEVLLGLslayASSSSDIWSLGITLYELLTglppfegeknssatsqtlkIILELPT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15827075 365 RYMDGLPEDDPVLTTYDSFARLLHRAINPDPRRRFSSAEEMSAQLM 410
Cdd:COG0515 233 PSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLL 278
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
173-403 4.30e-31

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: 122.76  E-value: 4.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 173 GGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTsgdpvGYIVMEYIGGRS 252
Cdd:cd00180   4 GSFGKVYKARDKE-TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENF-----LYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 253 LKRGSKKgNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSFG-----CIYGT 326
Cdd:cd00180  78 LKDLLKE-NKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDgTVKLADFGLAKDLDSDDsllktTGGTT 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15827075 327 PGYQAPEIVRTGP--TVATDIYTVGRTLAALtlnlrtrngrymdglpeddpvlttyDSFARLLHRAINPDPRRRFSSAE 403
Cdd:cd00180 157 PPYYAPPELLGGRyyGPKVDIWSLGVILYEL-------------------------EELKDLIRRMLQYDPKKRPSAKE 210
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
164-404 2.44e-30

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: 121.54  E-value: 2.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 164 YEVKGCIAHGGLGWVYLAFdHNVNDRPVVLKGLVHSgDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgYI 243
Cdd:cd05122   2 FEILEKIGKGGFGVVYKAR-HKKTGQIVAIKKINLE-SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDEL-----WI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 244 VMEYIGGRSLKRGSKKGNvEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSFGC 322
Cdd:cd05122  75 VMEFCSGGSLKDLLKNTN-KTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDgEVKLIDFGLSAQLSDGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 323 ---IYGTPGYQAPEIVRTGP-TVATDIYTVGRTLAALTlnlrtrNGRY---------------MDGLPE-DDPVLTTyDS 382
Cdd:cd05122 154 rntFVGTPYWMAPEVIQGKPyGFKADIWSLGITAIEMA------EGKPpyselppmkalfliaTNGPPGlRNPKKWS-KE 226
                       250       260
                ....*....|....*....|..
gi 15827075 383 FARLLHRAINPDPRRRfSSAEE 404
Cdd:cd05122 227 FKDFLKKCLQKDPEKR-PTAEQ 247
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
163-403 5.85e-25

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: 106.06  E-value: 5.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFdHNVNDRPVVLKGLVHSGDAEAQASAVA-ERQFLAEVVHPQIVQIFNFVEHKDTSgdpvg 241
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLAR-HKLTGEKVAIKIIDKSKLKEEIEEKIKrEIEIMKLLNHPNIIKLYEVIETENKI----- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 242 YIVMEYI-GGRSLKRGSKKGnveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAvSRINS 319
Cdd:cd14003  75 YLVMEYAsGGELFDYIVNNG---RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNgNLKIIDFGL-SNEFR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 320 FGC----IYGTPGYQAPEIVRTGP--TVATDIYTVGRTLAALTLnlrtrnGRymdgLP---EDDPVL------TTYD--- 381
Cdd:cd14003 151 GGSllktFCGTPAYAAPEVLLGRKydGPKADVWSLGVILYAMLT------GY----LPfddDNDSKLfrkilkGKYPips 220
                       250       260
                ....*....|....*....|....*.
gi 15827075 382 ---SFAR-LLHRAINPDPRRRFSSAE 403
Cdd:cd14003 221 hlsPDARdLIRRMLVVDPSKRITIEE 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
166-349 2.75e-24

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: 104.14  E-value: 2.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 166 VKG-CIAHGGLGWVYLAFDHNVNDRPVVLKGLVHSGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvgYIV 244
Cdd:cd06606   3 KKGeLLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTL-----NIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 245 MEYIGGRSLKRGSKKGnvEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINS---- 319
Cdd:cd06606  78 LEYVPGGSLASLLKKF--GKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDgVVKLADFGCAKRLAEiatg 155
                       170       180       190
                ....*....|....*....|....*....|...
gi 15827075 320 --FGCIYGTPGYQAPEIVR-TGPTVATDIYTVG 349
Cdd:cd06606 156 egTKSLRGTPYWMAPEVIRgEGYGRAADIWSLG 188
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
201-349 5.80e-24

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908  Cd Length: 247  Bit Score: 103.12  E-value: 5.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 201 DAEAQASAVAERQFLAEVVHPQIVQIFnfvehkDTSGDPVGYI-VMEYI-GGRSLKRGSKKGNVEKlpvAEAIAYLLEIL 278
Cdd:cd14006  29 RDKKKEAVLREISILNQLQHPRIIQLH------EAYESPTELVlILELCsGGELLDRLAERGSLSE---EEVRTYMRQLL 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15827075 279 PALSYLHSIGLVYNDLKPENIMLTE---EQLKLIDLGAVSRIN---SFGCIYGTPGYQAPEIVRTGP-TVATDIYTVG 349
Cdd:cd14006 100 EGLQYLHNHHILHLDLKPENILLADrpsPQIKIIDFGLARKLNpgeELKEIFGTPEFVAPEIVNGEPvSLATDMWSIG 177
pknD PRK13184
serine/threonine-protein kinase; Reviewed
162-409 1.72e-23

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 106.39  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  162 GQYEVKGCIAHGGLGWVYLAFDhNVNDRPVVLKGLVH--SGDAEAQASAVAERQFLAEVVHPQIVQIFNFVehkdTSGDP 239
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYD-PVCSRRVALKKIREdlSENPLLKKRFLREAKIAADLIHPGIVPVYSIC----SDGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  240 VgYIVMEYIGGRSLKR---------GSKKGNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIML--------- 301
Cdd:PRK13184  77 V-YYTMPYIEGYTLKSllksvwqkeSLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLglfgevvil 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075  302 ----------TEEQLKLIDLGAV----SRINSFGCIYGTPGYQAPEIVRTGP-TVATDIYTVGRTL-AALTLNL--RTRN 363
Cdd:PRK13184 156 dwgaaifkklEEEDLLDIDVDERnicySSMTIPGKIVGTPDYMAPERLLGVPaSESTDIYALGVILyQMLTLSFpyRRKK 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15827075  364 GRYM---DGLP---EDDPVLTTYDSFARLLHRAINPDPRRRFSSAEEMSAQL 409
Cdd:PRK13184 236 GRKIsyrDVILspiEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
163-403 5.56e-23

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: 100.23  E-value: 5.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAfDHNVNDRPVVLKGL-VHSGDAEAQASAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpvg 241
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLV-RRKSDGKLYVLKEIdLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKL----- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 242 YIVMEYIGGRSLKRGSKKGNVEKLPVAEA--IAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQ-LKLIDLGaVSRI- 317
Cdd:cd08215  75 CIVMEYADGGDLAQKIKKQKKKGQPFPEEqiLDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGvVKLGDFG-ISKVl 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 318 -NSFGC---IYGTPGYQAPEIVRTGP-TVATDIYTVGRTL---AALT----------LNLRTRNGRYmdglpedDPVLTT 379
Cdd:cd08215 154 eSTTDLaktVVGTPYYLSPELCENKPyNYKSDIWALGCVLyelCTLKhpfeannlpaLVYKIVKGQY-------PPIPSQ 226
                       250       260
                ....*....|....*....|....*
gi 15827075 380 YDS-FARLLHRAINPDPRRRFSSAE 403
Cdd:cd08215 227 YSSeLRDLVNSMLQKDPEKRPSANE 251
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
170-405 7.14e-23

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899  Cd Length: 252  Bit Score: 99.77  E-value: 7.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 170 IAHGGLGWVYLAFDhNVNDRPVVLKGLVHS--GDAEaQASAVAERQFLAEV-VHPQIVQIFNFVEHKDTSgdpvgYIVME 246
Cdd:cd13997   8 IGSGSFSEVFKVRS-KVDGCLYAVKKSKKPfrGPKE-RARALREVEAHAALgQHPNIVRYYSSWEEGGHL-----YIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 247 YIGGRSLKRG-SKKGNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLIDLGAVSRINSFGCIY 324
Cdd:cd13997  81 LCENGSLQDAlEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKgTCKIGDFGLATRLETSGDVE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 325 -GTPGYQAPEIVR--TGPTVATDIYTVGRTL--AALTLNLrTRNGRYMDGLPEDD----PVLTTYDSFARLLHRAINPDP 395
Cdd:cd13997 161 eGDSRYLAPELLNenYTHLPKADIFSLGVTVyeAATGEPL-PRNGQQWQQLRQGKlplpPGLVLSQELTRLLKVMLDPDP 239
                       250
                ....*....|
gi 15827075 396 RRRFSSAEEM 405
Cdd:cd13997 240 TRRPTADQLL 249
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
173-405 9.92e-23

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881  Cd Length: 265  Bit Score: 99.77  E-value: 9.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 173 GGLGWVYLAFDHnvnDRPVVLKGLvhsgdaEAQASAVAERQ-FLAEV-----VHPQIVQIFNfVEHKDTSGDPvGYIVME 246
Cdd:cd13979  14 GGFGSVYKATYK---GETVAVKIV------RRRRKNRASRQsFWAELnaarlRHENIVRVLA-AETGTDFASL-GLIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 247 YIGGRSLKRgSKKGNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQL-KLIDLGAVSRINSFGC--- 322
Cdd:cd13979  83 YCGNGTLQQ-LIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVcKLCDFGCSVKLGEGNEvgt 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 323 ----IYGTPGYQAPEIVR-TGPTVATDIYTVGRTLAALT--------------LNLRTRNGRYMDGLPEDDPVLTTYDSf 383
Cdd:cd13979 162 prshIGGTYTYRAPELLKgERVTPKADIYSFGITLWQMLtrelpyaglrqhvlYAVVAKDLRPDLSGLEDSEFGQRLRS- 240
                       250       260
                ....*....|....*....|..
gi 15827075 384 arLLHRAINPDPRRRFSSAEEM 405
Cdd:cd13979 241 --LISRCWSAQPAERPNADESL 260
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
170-404 2.84e-22

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731  Cd Length: 272  Bit Score: 98.44  E-value: 2.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 170 IAHGGLGWVYLAFDHNVND---------RPVVLKGLVHSgdaeaqasAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdpv 240
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDlyaikvikkRDMIRKNQVDS--------VLAERNILSQAQNPFVVKLYYSFQGKKNL---- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 241 gYIVMEYI-GG--RSLKRgskkgNVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLID-----L 311
Cdd:cd05579  69 -YLVMEYLpGGdlYSLLE-----NVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANgHLKLTDfglskV 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 312 GAVSRINSFGC--------------IYGTPGYQAPEIV-RTGPTVATDIYTVG---------------RTLAALTLNlrT 361
Cdd:cd05579 143 GLVRRQIKLSIqkksngapekedrrIVGTPDYLAPEILlGQGHGKTVDWWSLGvilyeflvgippfhaETPEEIFQN--I 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15827075 362 RNGRYMDglPEDDPVltTYDSFaRLLHRAINPDPRRR--FSSAEE 404
Cdd:cd05579 221 LNGKIEW--PEDPEV--SDEAK-DLISKLLTPDPEKRlgAKGIEE 260
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
163-403 7.74e-22

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797  Cd Length: 254  Bit Score: 96.91  E-value: 7.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQASAV-AERQFLAEVVHPQIVQIFNFVEHKDTSgdpvg 241
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLN-TGEFVAIKQISLEKIPKSDLKSVmGEIDLLKKLNHPNIVKYIGSVKTKDSL----- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 242 YIVMEYIGGRSLKRGSKKgnVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQL-KLIDLGAVSRINS- 319
Cdd:cd06627  75 YIILEYVENGSLASIIKK--FGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLvKLADFGVATKLNEv 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 320 ---FGCIYGTPGYQAPEIVR-TGPTVATDIYTVGRTLaaltLNLRTRNGRYMDGLP--------EDD-PVLTTYDS--FA 384
Cdd:cd06627 153 ekdENSVVGTPYWMAPEVIEmSGVTTASDIWSVGCTV----IELLTGNPPYYDLQPmaalfrivQDDhPPLPENISpeLR 228
                       250
                ....*....|....*....
gi 15827075 385 RLLHRAINPDPRRRFSSAE 403
Cdd:cd06627 229 DFLLQCFQKDPTLRPSAKE 247
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
163-336 7.43e-21

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: 93.69  E-value: 7.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 163 QYEVKGCIAHGGLGWVYLAFDHNVNDR---PVVLKGLVHSGDAEaqaSAVAERQFLAEVVHPQIVQIFNFVEHKDTSgdp 239
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEyavKIIDKKKLKSEDEE---MLRREIEILKRLDHPNIVKLYEVFEDDKNL--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 240 vgYIVMEYI-GGRSLKRGSKKGnveKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEE----QLKLIDLGAV 314
Cdd:cd05117  75 --YLVMELCtGGELFDRIVKKG---SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdsPIKIIDFGLA 149
                       170       180
                ....*....|....*....|....*
gi 15827075 315 SRINSFGCIY---GTPGYQAPEIVR 336
Cdd:cd05117 150 KIFEEGEKLKtvcGTPYYVAPEVLK 174
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
210-349 8.64e-21

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693  Cd Length: 250  Bit Score: 93.35  E-value: 8.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 210 AERQFLAEVVHPQIVQI-FNFVEHKDTsgdpvgYIVMEYIGGRSL-KRGSKKGnveKLPVAEAIAYLLEILPALSYLHSI 287
Cdd:cd05123  42 NERNILERVNHPFIVKLhYAFQTEEKL------YLVLDYVPGGELfSHLSKEG---RFPEERARFYAAEIVLALEYLHSL 112
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15827075 288 GLVYNDLKPENIMLTEE-QLKLIDLG-------AVSRINSFgCiyGTPGYQAPEIV-RTGPTVATDIYTVG 349
Cdd:cd05123 113 GIIYRDLKPENILLDSDgHIKLTDFGlakelssDGDRTYTF-C--GTPEYLAPEVLlGKGYGKAVDWWSLG 180
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
164-406 1.59e-20

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895  Cd Length: 267  Bit Score: 92.80  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 164 YEVKGCIAHGGLGWVYLAFDHNvNDRPVVLKGLVHSGDAEAQASAVAERQFLAEVV-------HPQIVQIFNFVEHKDTS 236
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLR-TGRKYAIKCLYKSGPNSKDGNDFQKLPQLREIDlhrrvsrHPNIITLHDVFETEVAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 237 gdpvgYIVMEYIGGRSLK---RGSKKGNVEKLPVAEAIaylLEILPALSYLHSIGLVYNDLKPENIMLT--EEQLKLIDL 311
Cdd:cd13993  81 -----YIVLEYCPNGDLFeaiTENRIYVGKTELIKNVF---LQLIDAVKHCHSLGIYHRDIKPENILLSqdEGTVKLCDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 312 G--AVSRINS-FGCiyGTPGYQAPE-------IVRTGPTVATDIYTVGRTLAALTL--------NLRTRNGRYMDGLPED 373
Cdd:cd13993 153 GlaTTEKISMdFGV--GSEFYMAPEcfdevgrSLKGYPCAAGDIWSLGIILLNLTFgrnpwkiaSESDPIFYDYYLNSPN 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15827075 374 --DPVLTTYDSFARLLHRAINPDPRRRfSSAEEMS 406
Cdd:cd13993 231 lfDVILPMSDDFYNLLRQIFTVNPNNR-ILLPELQ 264
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
220-403 2.64e-20

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


Pssm-ID: 270910  Cd Length: 267  Bit Score: 92.23  E-value: 2.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 220 HPQIVQIFNFVEhkdtsgDPVG---YIVMEYI-GGRSLKRGSKKGnVEKLPVAEAIAYLLEILPALSYLHSIGLVYNDLK 295
Cdd:cd14008  63 HPNIVRLYEVID------DPESdklYLVLEYCeGGPVMELDSGDR-VPPLPEETARKYFRDLVLGLEYLHENGIVHRDIK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 296 PENIMLTEE-QLKLIDLGaVSRINSFGCIY-----GTPGYQAPEIVRTGPTV----ATDIYTVGRTLAAL---TLNLRTR 362
Cdd:cd14008 136 PENLLLTADgTVKISDFG-VSEMFEDGNDTlqktaGTPAFLAPELCDGDSKTysgkAADIWALGVTLYCLvfgRLPFNGD 214
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15827075 363 NGRYM------DGLPEDDPVlTTYDSFARLLHRAINPDPRRRFSSAE 403
Cdd:cd14008 215 NILELyeaiqnQNDEFPIPP-ELSPELKDLLRRMLEKDPEKRITLKE 260
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
156-403 4.76e-19

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 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: 270803  Cd Length: 313  Bit Score: 88.94  E-value: 4.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 156 PGDIVAGQYEvkgcIAHGGLGWVYLAFDHNVNDrPVVLKGLVHSGDA--EAQASAVAERQFLAEVVHPqivqifNFVEHK 233
Cdd:cd06633  19 PEEIFVDLHE----IGHGSFGAVYFATNSHTNE-VVAIKKMSYSGKQtnEKWQDIIKEVKFLQQLKHP------NTIEYK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 234 DTS-GDPVGYIVMEYIGGRSlkrgSKKGNVEKLPVAEA-IAYLLE-ILPALSYLHSIGLVYNDLKPENIMLTEE-QLKLI 309
Cdd:cd06633  88 GCYlKDHTAWLVMEYCLGSA----SDLLEVHKKPLQEVeIAAITHgALQGLAYLHSHNMIHRDIKAGNILLTEPgQVKLA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15827075 310 DLGAVSRINSFGCIYGTPGYQAPEIVRTGPT----VATDIYTVGRTLAALT------LNLRTRNGRYMDGlPEDDPVLTT 379
Cdd:cd06633 164 DFGSASIASPANSFVGTPYWMAPEVILAMDEgqydGKVDIWSLGI