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Conserved domains on  [gi|77465476|ref|YP_354979|]
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serine/threonine protein kinase [Rhodobacter sphaeroides 2.4.1]

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 ...
20-273 1.18e-61

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: 208.98  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARaLARLSHPNIVRVYDVGE-DDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAM-EAGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGapERATIIDFGIAKDLSAGAQTIV 177
Cdd:cd14014  81 YVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED--GRVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 178 GNdFAGKYEYAAPEQIDG-RAEPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPEPLRGLID 250
Cdd:cd14014 159 GS-VLGTPAYMAPEQARGgPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeappppSPLNPDVPPALDAIIL 237
                       250       260
                ....*....|....*....|...
gi 77465476 251 RLAAPEAERRPASAAAVVEELDR 273
Cdd:cd14014 238 RALAKDPEERPQSAAELLAALRA 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
20-273 1.18e-61

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: 208.98  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARaLARLSHPNIVRVYDVGE-DDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAM-EAGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGapERATIIDFGIAKDLSAGAQTIV 177
Cdd:cd14014  81 YVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED--GRVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 178 GNdFAGKYEYAAPEQIDG-RAEPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPEPLRGLID 250
Cdd:cd14014 159 GS-VLGTPAYMAPEQARGgPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeappppSPLNPDVPPALDAIIL 237
                       250       260
                ....*....|....*....|...
gi 77465476 251 RLAAPEAERRPASAAAVVEELDR 273
Cdd:cd14014 238 RALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-261 3.46e-39

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 145.75  E-value: 3.46e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476     20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSgnDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKiLKKLKHPNIVRLYDVFE-DEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476     99 HIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILrgGAPERATIIDFGIAKDLSAGAQTiv 177
Cdd:smart00220  78 YCEGGDLFDLLKKrGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL--DEDGHVKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    178 gNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPEPLRGLID 250
Cdd:smart00220 154 -TTFVGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGkpkppfPPPEWDISPEAKDLIR 232
                          250
                   ....*....|.
gi 77465476    251 RLAAPEAERRP 261
Cdd:smart00220 233 KLLVKDPEKRL 243
Pkinase pfam00069
Protein kinase domain;
20-269 3.38e-33

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 129.26  E-value: 3.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRfSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKiLKKLNHPNIVRLYDAFE-DKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    99 HIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIIL-RGGAPEratIIDFGIAKDLSAGAQTi 176
Cdd:pfam00069  79 YVEGGSLFDLLSEkGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIdEDGNLK---ITDFGLARQLNSGSSL- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476   177 vgNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGRPLDTEGVP----EPLRGLIDR 251
Cdd:pfam00069 155 --TSFVGTPWYMAPEVLRGNPyGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPssisEEAKDLLKK 232
                         250
                  ....*....|....*...
gi 77465476   252 LAAPEAERRPaSAAAVVE 269
Cdd:pfam00069 233 LLKKDPSKRL-TATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
20-288 3.71e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 129.09  E-value: 3.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLisgRIVAVKALNRRFSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRSDGGHVFLVMD 98
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQiLASLNHPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAME----AGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGAPERAtIIDFGIAKDLSAGAQ 174
Cdd:COG0515  79 YVDGGSLEDLLKkigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVK-LIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 175 TIVG----NDFAGKYEYAAPEQIDG----RAEPRSDLYALGATLLAAFRGEAPFAGATP-------GEIVRRKGRPLDTE 239
Cdd:COG0515 158 TSSIpalpSTSVGTPGYMAPEVLLGlslaYASSSSDIWSLGITLYELLTGLPPFEGEKNssatsqtLKIILELPTPSLAS 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 77465476 240 GVPEPLRG--------LIDRLAAPEAERRPASAAAVVEELDRLLRPQAEPDRRRRVW 288
Cdd:COG0515 238 PLSPSNPEliskaasdLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKP 294
pknD PRK13184
serine/threonine-protein kinase; Reviewed
20-244 1.40e-19

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 93.30  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476   20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREEQL-RDVIDDAVVR-YTECSRSDGghVFLVM 97
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIaADLIHPGIVPvYSICSDGDP--VYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476   98 DHIEGPSLAQAMEAGR---IEARDL---------LIVAHRVAEGLRAAHRHGIVHRDLSPDNIILrgGAPERATIIDFGI 165
Cdd:PRK13184  82 PYIEGYTLKSLLKSVWqkeSLSKELaektsvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILL--GLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  166 AK----------DLSAGAQ-------TIVGNdFAGKYEYAAPEQIDGR-AEPRSDLYALGATLLAAFRGEAPFAgatpge 227
Cdd:PRK13184 160 AIfkkleeedllDIDVDERnicyssmTIPGK-IVGTPDYMAPERLLGVpASESTDIYALGVILYQMLTLSFPYR------ 232
                        250
                 ....*....|....*...
gi 77465476  228 ivRRKGRPL-DTEGVPEP 244
Cdd:PRK13184 233 --RKKGRKIsYRDVILSP 248
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
79-270 2.55e-14

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: 76.81  E-value: 2.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476     79 VVRYTECSRSDGGHVFLVMDHIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIIL--RGGAP 155
Cdd:TIGR03903   40 IVALLDSGEAPPGLLFAVFEYVPGRTLREVLAAdGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqTGVRP 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    156 ErATIIDFGIAKDLS----AGAQTIV-GNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPFAGATPGEIV 229
Cdd:TIGR03903  120 H-AKVLDFGIGTLLPgvrdADVATLTrTTEVLGTPTYCAPEQLRGEPvTPNSDLYAWGLIFLECLTGQRVVQGASVAEIL 198
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 77465476    230 RRKGRPLDTEGVP----EPLRGLIDRLAAPEAERRPASAAAVVEE 270
Cdd:TIGR03903  199 YQQLSPVDVSLPPwiagHPLGQVLRKALNKDPRQRAASAPALAER 243
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
20-273 1.18e-61

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: 208.98  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARaLARLSHPNIVRVYDVGE-DDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAM-EAGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGapERATIIDFGIAKDLSAGAQTIV 177
Cdd:cd14014  81 YVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED--GRVKLTDFGIARALGDSGLTQT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 178 GNdFAGKYEYAAPEQIDG-RAEPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPEPLRGLID 250
Cdd:cd14014 159 GS-VLGTPAYMAPEQARGgPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQeappppSPLNPDVPPALDAIIL 237
                       250       260
                ....*....|....*....|...
gi 77465476 251 RLAAPEAERRPASAAAVVEELDR 273
Cdd:cd14014 238 RALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-261 3.46e-39

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 145.75  E-value: 3.46e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476     20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSgnDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKiLKKLKHPNIVRLYDVFE-DEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476     99 HIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILrgGAPERATIIDFGIAKDLSAGAQTiv 177
Cdd:smart00220  78 YCEGGDLFDLLKKrGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL--DEDGHVKLADFGLARQLDPGEKL-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    178 gNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPEPLRGLID 250
Cdd:smart00220 154 -TTFVGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGkpkppfPPPEWDISPEAKDLIR 232
                          250
                   ....*....|.
gi 77465476    251 RLAAPEAERRP 261
Cdd:smart00220 233 KLLVKDPEKRL 243
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
26-269 5.43e-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: 135.86  E-value: 5.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  26 LGRGGTGEIYRARNLISGRIVAVKALNrrFSGNDDYIGLMRRE-EQLRDVIDDAVVRYTECSRsDGGHVFLVMDHIEGPS 104
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIP--KEKLKKLLEELLREiEILKKLNHPNIVKLYDVFE-TENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 105 LAQAME--AGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILrgGAPERATIIDFGIAKDLSAGAQTIVGNDFA 182
Cdd:cd00180  78 LKDLLKenKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL--DSDGTVKLADFGLAKDLDSDDSLLKTTGGT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 183 GKYEYAAPEQIDGRA-EPRSDLYALGATLLaafrgeapfagatpgEIvrrkgrpldtegvpEPLRGLIDRLAAPEAERRP 261
Cdd:cd00180 156 TPPYYAPPELLGGRYyGPKVDIWSLGVILY---------------EL--------------EELKDLIRRMLQYDPKKRP 206

                ....*...
gi 77465476 262 aSAAAVVE 269
Cdd:cd00180 207 -SAKELLE 213
Pkinase pfam00069
Protein kinase domain;
20-269 3.38e-33

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 129.26  E-value: 3.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRfSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRsDGGHVFLVMD 98
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKiLKKLNHPNIVRLYDAFE-DKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476    99 HIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIIL-RGGAPEratIIDFGIAKDLSAGAQTi 176
Cdd:pfam00069  79 YVEGGSLFDLLSEkGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIdEDGNLK---ITDFGLARQLNSGSSL- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476   177 vgNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGRPLDTEGVP----EPLRGLIDR 251
Cdd:pfam00069 155 --TSFVGTPWYMAPEVLRGNPyGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRPssisEEAKDLLKK 232
                         250
                  ....*....|....*...
gi 77465476   252 LAAPEAERRPaSAAAVVE 269
Cdd:pfam00069 233 LLKKDPSKRL-TATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
20-288 3.71e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 129.09  E-value: 3.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLisgRIVAVKALNRRFSGNDDYIGLMRREEQ-LRDVIDDAVVRYTECSRSDGGHVFLVMD 98
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQiLASLNHPPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAME----AGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGAPERAtIIDFGIAKDLSAGAQ 174
Cdd:COG0515  79 YVDGGSLEDLLKkigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVK-LIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 175 TIVG----NDFAGKYEYAAPEQIDG----RAEPRSDLYALGATLLAAFRGEAPFAGATP-------GEIVRRKGRPLDTE 239
Cdd:COG0515 158 TSSIpalpSTSVGTPGYMAPEVLLGlslaYASSSSDIWSLGITLYELLTGLPPFEGEKNssatsqtLKIILELPTPSLAS 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 77465476 240 GVPEPLRG--------LIDRLAAPEAERRPASAAAVVEELDRLLRPQAEPDRRRRVW 288
Cdd:COG0515 238 PLSPSNPEliskaasdLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKP 294
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
20-220 1.44e-29

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: 118.84  E-value: 1.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIglmRREEQ-LRDVIDDAVVRYtECSRSDGGHVFLVMD 98
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESI---LNEIAiLKKCKHPNIVKY-YGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAMEA--GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIIL--RGgapeRATIIDFGIAKDLSAGAQ 174
Cdd:cd05122  78 FCSGGSLKDLLKNtnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLtsDG----EVKLIDFGLSAQLSDGKT 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 77465476 175 TivgNDFAGKYEYAAPEQIDGRA-EPRSDLYALGATLLAAFRGEAPF 220
Cdd:cd05122 154 R---NTFVGTPYWMAPEVIQGKPyGFKADIWSLGITAIEMAEGKPPY 197
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
20-261 1.25e-27

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: 113.38  E-value: 1.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREE-----------QLRDVIDdavvrytecsrs 88
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEimkllnhpniiKLYEVIE------------ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  89 DGGHVFLVMDHIEGPSL-AQAMEAGRI---EARDLLivaHRVAEGLRAAHRHGIVHRDLSPDNIILrgGAPERATIIDFG 164
Cdd:cd14003  70 TENKIYLVMEYASGGELfDYIVNNGRLsedEARRFF---QQLISAVDYCHSNGIVHRDLKLENILL--DKNGNLKIIDFG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 165 IAKDLSAGAQTivgNDFAGKYEYAAPEQIDGRAE--PRSDLYALGATLLAAFRGEAPFAGATPGEIVRR--KGRPLDTEG 240
Cdd:cd14003 145 LSNEFRGGSLL---KTFCGTPAYAAPEVLLGRKYdgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKilKGKYPIPSH 221
                       250       260
                ....*....|....*....|.
gi 77465476 241 VPEPLRGLIDRLAAPEAERRP 261
Cdd:cd14003 222 LSPDARDLIRRMLVVDPSKRI 242
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
20-267 2.50e-26

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000  Cd Length: 265  Bit Score: 109.87  E-value: 2.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALN-RRFSGNDDYIGLMRRE-EQLRDVIDDAVVRYTECSRSDGgHVFLVM 97
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkRKVAGNDKNLQLFQREiNILKSLEHPGIVRLIDWYEDDQ-HIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  98 DHIEGPSLAQ-AMEAGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGAPERATIIDFGIAKDLSAGaqTI 176
Cdd:cd14098  81 EYVEGGDLMDfIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKVIHTG--TF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 177 VgNDFAGKYEYAAPEQI-------DGRAEPRSDLYALGATLLAAFRGEAPFAGATPGEIVRRKGR------PLDTEGVPE 243
Cdd:cd14098 159 L-VTFCGTMAYLAPEILmskeqnlQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKgrytqpPLVDFNISE 237
                       250       260
                ....*....|....*....|....
gi 77465476 244 PLRGLIDRLAAPEAERRPASAAAV 267
Cdd:cd14098 238 EAIDFILRLLDVDPEKRMTAAQAL 261
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
20-265 4.52e-26

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: 108.72  E-value: 4.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  20 YEIEGVLGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDyIGLMRRE-EQLRDVIDDAVVRYTECSrSDGGHVFLVMD 98
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSED-EEMLRREiEILKRLDHPNIVKLYEVF-EDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAM-EAGRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGAPErATI--IDFGIAKDLSagaQT 175
Cdd:cd05117  80 LCTGGELFDRIvKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPD-SPIkiIDFGLAKIFE---EG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 176 IVGNDFAGKYEYAAPEQIDGRA-EPRSDLYALGA---TLLAafrGEAPFAGATPGEIVR--RKGR----PLDTEGVPEPL 245
Cdd:cd05117 156 EKLKTVCGTPYYVAPEVLKGKGyGKKCDIWSLGVilyILLC---GYPPFYGETEQELFEkiLKGKysfdSPEWKNVSEEA 232
                       250       260
                ....*....|....*....|
gi 77465476 246 RGLIDRLAAPEAERRPaSAA 265
Cdd:cd05117 233 KDLIKRLLVVDPKKRL-TAA 251
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-260 2.66e-25

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: 106.45  E-value: 2.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  26 LGRGGTGEIYRARNLISGRIVAVKALNRRFsgnddyigLMRREEQL-----RDVIDDA----VVRyTECSRSDGGHVFLV 96
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKE--------IIKRKEVEhtlneRNILERVnhpfIVK-LHYAFQTEEKLYLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  97 MDHIEGPSLAQAMEA-GRI-EARDLLIVAhRVAEGLRAAHRHGIVHRDLSPDNIIL--RGgapeRATIIDFGIAKDLSAG 172
Cdd:cd05123  72 LDYVPGGELFSHLSKeGRFpEERARFYAA-EIVLALEYLHSLGIIYRDLKPENILLdsDG----HIKLTDFGLAKELSSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 173 AQTIvgNDFAGKYEYAAPEQIDGRAEPRS-DLYALGATLLAAFRGEAPFAGATPGEIVRR-KGRPLDT-EGVPEPLRGLI 249
Cdd:cd05123 147 GDRT--YTFCGTPEYLAPEVLLGKGYGKAvDWWSLGVLLYEMLTGKPPFYAENRKEIYEKiLKSPLKFpEYVSPEAKSLI 224
                       250
                ....*....|.
gi 77465476 250 DRLAAPEAERR 260
Cdd:cd05123 225 SGLLQKDPTKR 235
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
26-260 1.43e-24

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: 104.56  E-value: 1.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  26 LGRGGTGEIYRARNLISGRIVAVKALN------RRFSGNDDYIG-----LMRRE------------EQLRDVIDDavvry 82
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkRREGKNDRGKIknaldDVRREiaimkkldhpniVRLYEVIDD----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  83 tecsrSDGGHVFLVMDHIEG----------PSLAQAMEAGRIEARDLLivahrvaEGLRAAHRHGIVHRDLSPDNIILrg 152
Cdd:cd14008  76 -----PESDKLYLVLEYCEGgpvmeldsgdRVPPLPEETARKYFRDLV-------LGLEYLHENGIVHRDIKPENLLL-- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 153 GAPERATIIDFGIAKDLSAGAQTIVGNdfAGKYEYAAPE-------QIDGRAeprSDLYALGATLLAAFRGEAPFAGATP 225
Cdd:cd14008 142 TADGTVKISDFGVSEMFEDGNDTLQKT--AGTPAFLAPElcdgdskTYSGKA---ADIWALGVTLYCLVFGRLPFNGDNI 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 77465476 226 GE----IVRRKGRPLDTEGVPEPLRGLIDRLAAPEAERR 260
Cdd:cd14008 217 LElyeaIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKR 255
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
10-221 2.40e-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: 103.75  E-value: 2.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  10 FRRGEILnhtyeiegvlGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDYIGLMRREEQLRDVIDDAVVRYTECSRSD 89
Cdd:cd06606   2 WKKGELL----------GKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  90 GgHVFLVMDHIEGPSLAQAMEA-GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNIILRGGApeRATIIDFGIAKD 168
Cdd:cd06606  72 N-TLNIFLEYVPGGSLASLLKKfGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG--VVKLADFGCAKR 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 77465476 169 LSAGAQTIVGNDFAGKYEYAAPEQI-DGRAEPRSDLYALGATLLAAFRGEAPFA 221
Cdd:cd06606 149 LAEIATGEGTKSLRGTPYWMAPEVIrGEGYGRAADIWSLGCTVIEMATGKPPWS 202
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
26-268 4.67e-24

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: 102.85  E-value: 4.67e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  26 LGRGGTGEIYRARNLISGRIVAVKALNRRFSGNDDyiglmrREEQLRDVIDDA-------VVRYtECSRSDGGHVFLVMD 98
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKE------RARALREVEAHAalgqhpnIVRY-YSSWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  99 HIEGPSLAQAMEA----GRIEARDLLIVAHRVAEGLRAAHRHGIVHRDLSPDNI-ILRGGapeRATIIDFGIAKDLSAGa 173
Cdd:cd13997  81 LCENGSLQDALEElspiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIfISNKG---TCKIGDFGLATRLETS- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 174 qtivGNDFAGKYEYAAPEQIDGRAE--PRSDLYALGATLLAAFRGEaPFAGATPGEIVRRKGRPLDTEGVP--EPLRGLI 249
Cdd:cd13997 157 ----GDVEEGDSRYLAPELLNENYThlPKADIFSLGVTVYEAATGE-PLPRNGQQWQQLRQGKLPLPPGLVlsQELTRLL 231
                       250
                ....*....|....*....
gi 77465476 250 DRLAAPEAERRPaSAAAVV 268
Cdd:cd13997 232 KVMLDPDPTRRP-TADQLL 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
26-260 2.72e-23

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


Pssm-ID: 270911  Cd Length: 251  Bit Score: 100.37  E-value: 2.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  26 LGRGGTGEIYRARNLISGRIVAVKA-----LNRRFSGNddyigLMRREEQLRDVIDDAVVRYTECSRSDGgHVFLVMDHI 100
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEisrkkLNKKLQEN-----LESEIAILKSIKHPNIVRLYDVQKTED-FIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 101 EGPSLAQAMEA-GRIE---ARDLLivaHRVAEGLRAAHRHGIVHRDLSPDNIILrGGAPERAT--IIDFGIAKDLSAG-- 172
Cdd:cd14009  75 AGGDLSQYIRKrGRLPeavARHFM---QQLASGLKFLRSKNIIHRDLKPQNLLL-STSGDDPVlkIADFGFARSLQPAsm 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 173 AQTIVGNDFagkyeYAAPE-----QIDGRAeprsDLYALGATLLAAFRGEAPFAGATPGEIVRR------KGRPLDTEGV 241
Cdd:cd14009 151 AETLCGSPL-----YMAPEilqfqKYDAKA----DLWSVGAILFEMLVGKPPFRGSNHVQLLRNiersdaVIPFPIAAQL 221
                       250
                ....*....|....*....
gi 77465476 242 PEPLRGLIDRLAAPEAERR 260
Cdd:cd14009 222 SPDCKDLLRRLLRRDPAER 240
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
21-223 7.61e-23

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


Pssm-ID: 132954  Cd Length: 264  Bit Score: 99.59  E-value: 7.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  21 EIEGVLGRGGTGEIYRARNLISGRIVAVKALNrrFSGNDDYIGLMRRE-EQLRDVIDDAVVRYTEcSRSDGGHVFLVMDH 99
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRElKTLRSCESPYVVKCYG-AFYKEGEISIVLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 100 IEGPSLAQAM-EAGRIEARDLLIVAHRVAEGLRAAHR-HGIVHRDLSPDNIIL-RGGAPEratIIDFGIAKDLSAGAQti 176
Cdd:cd06623  81 MDGGSLADLLkKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLInSKGEVK---IADFGISKVLENTLD-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 77465476 177 VGNDFAGKYEYAAPEQIDGRAEPR-SDLYALGATLLAAFRGEAPFAGA 223
Cdd:cd06623 156 QCNTFVGTVTYMSPERIQGESYSYaADIWSLGLTLLECALGKFPFLPP 203
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
25-271 1.49e-22

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: 98.61  E-value: 1.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476  25 VLGRGGTGEIYRArnLISGRIVAVKALNRRfSGNDDYIGLMRREEQLRDVIDDAVVRY----TECSRSDGGhvFLVMDHI 100
Cdd:cd13979  10 PLGSGGFGSVYKA--TYKGETVAVKIVRRR-RKNRASRQSFWAELNAARLRHENIVRVlaaeTGTDFASLG--LIIMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 101 EGPSLAQAMEagriEARDLLIVAHR------VAEGLRAAHRHGIVHRDLSPDNIILRG-GAPEratIIDFGIAKDLSAG- 172
Cdd:cd13979  85 GNGTLQQLIY----EGSEPLPLAHRilisldIARALRFCHSHGIVHLDVKPANILISEqGVCK---LCDFGCSVKLGEGn 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77465476 173 AQTIVGNDFAGKYEYAAPEQIDG-RAEPRSDL