NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|66045341|ref|YP_235182|]
View 

protein kinase [Pseudomonas syringae pv. syringae B728a]

Protein Classification

PP2Cc and STKc_PknB_like domain-containing protein (domain architecture ID 10001919)

PP2Cc and STKc_PknB_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
269-509 1.07e-51

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: 179.70  E-value: 1.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 269 SIVYRVTDIH-EQPWLLKTLpasRHDETGAGQgllLEEWFLR--RVAGRFfpeIHP--------LPDRQHLYYVMREYPG 337
Cdd:cd14014  14 GEVYRARDTLlGRPVAIKVL---RPELAEDEE---FRERFLReaRALARL---SHPnivrvydvGEDDGRPYIVMEYVEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 338 HTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAFCPGLSAVN-TEDLPGT 416
Cdd:cd14014  85 GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTqTGSVLGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 417 PSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPYG---EIEAFQHRRFGAPIPASRYRPDLPQWLSHSLDKALHADP 493
Cdd:cd14014 165 PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDgdsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDP 244
                       250
                ....*....|....*.
gi 66045341 494 NQRYETAEQWLLELEQ 509
Cdd:cd14014 245 EERPQSAAELLAALRA 260
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
1-231 4.94e-48

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


:

Pssm-ID: 223704  Cd Length: 262  Bit Score: 169.84  E-value: 4.94e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   1 MTLQLQFAQFSASGP-RAENQDAVrlvTPVPALAASKGYLFALADGVSQCADGALAAQSTLQALALDYYATPETWGVA-- 77
Cdd:COG0631   4 GILSLKVAGLSDVGTvRKHNEDAF---LIKPNENGNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNEsl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  78 -QSLDRLLLAQNRWLLA--------NGLLTTLSALVLRGRRFTLAHVGDCRVYRWQTGTLKRISEDHVWEQADMQ----- 143
Cdd:COG0631  81 eELLKEAILKANEAIAEegqlnedvRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNRLEQrgiit 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 144 ----------HVLKRALGLDQYVVMDYLDGELCEGERLLLVSDGVWATLGDASIRSILSEQHDLDAAVKTLVSAAHLAGS 213
Cdd:COG0631 161 peearshprrNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNSETPQEAADKLIELALEGGG 240
                       250
                ....*....|....*...
gi 66045341 214 QDNASALLIQVDTLGEDD 231
Cdd:COG0631 241 PDNITVVLVRLNGEGETS 258
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
269-509 1.07e-51

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: 179.70  E-value: 1.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 269 SIVYRVTDIH-EQPWLLKTLpasRHDETGAGQgllLEEWFLR--RVAGRFfpeIHP--------LPDRQHLYYVMREYPG 337
Cdd:cd14014  14 GEVYRARDTLlGRPVAIKVL---RPELAEDEE---FRERFLReaRALARL---SHPnivrvydvGEDDGRPYIVMEYVEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 338 HTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAFCPGLSAVN-TEDLPGT 416
Cdd:cd14014  85 GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTqTGSVLGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 417 PSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPYG---EIEAFQHRRFGAPIPASRYRPDLPQWLSHSLDKALHADP 493
Cdd:cd14014 165 PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDgdsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDP 244
                       250
                ....*....|....*.
gi 66045341 494 NQRYETAEQWLLELEQ 509
Cdd:cd14014 245 EERPQSAAELLAALRA 260
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
1-231 4.94e-48

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 223704  Cd Length: 262  Bit Score: 169.84  E-value: 4.94e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   1 MTLQLQFAQFSASGP-RAENQDAVrlvTPVPALAASKGYLFALADGVSQCADGALAAQSTLQALALDYYATPETWGVA-- 77
Cdd:COG0631   4 GILSLKVAGLSDVGTvRKHNEDAF---LIKPNENGNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNEsl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  78 -QSLDRLLLAQNRWLLA--------NGLLTTLSALVLRGRRFTLAHVGDCRVYRWQTGTLKRISEDHVWEQADMQ----- 143
Cdd:COG0631  81 eELLKEAILKANEAIAEegqlnedvRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNRLEQrgiit 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 144 ----------HVLKRALGLDQYVVMDYLDGELCEGERLLLVSDGVWATLGDASIRSILSEQHDLDAAVKTLVSAAHLAGS 213
Cdd:COG0631 161 peearshprrNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNSETPQEAADKLIELALEGGG 240
                       250
                ....*....|....*...
gi 66045341 214 QDNASALLIQVDTLGEDD 231
Cdd:COG0631 241 PDNITVVLVRLNGEGETS 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
324-502 8.36e-33

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 126.49  E-value: 8.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA-F 401
Cdd:smart00220  68 DEDKLYLVM-EYcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLArQ 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    402 CPGLSAVNTEDlpGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY---GEIEAFQHRRFGAPIPASRYRPDLP 478
Cdd:smart00220 147 LDPGEKLTTFV--GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFpgdDQLLELFKKIGKPKPPFPPPEWDIS 224
                          170       180
                   ....*....|....*....|....
gi 66045341    479 QWLSHSLDKALHADPNQRYeTAEQ 502
Cdd:smart00220 225 PEAKDLIRKLLVKDPEKRL-TAEE 247
Pkinase pfam00069
Protein kinase domain;
324-502 1.96e-31

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 122.71  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA-F 401
Cdd:pfam00069  69 DKDNLYLVL-EYvEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLArQ 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   402 CPGLSAVNTEDlpGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY-GEIEAFQHRRFGAPIPASRYRPDLPQW 480
Cdd:pfam00069 148 LNSGSSLTSFV--GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFpGINGNEIYEKIIDQDFDSPRPSSISEE 225
                         170       180
                  ....*....|....*....|..
gi 66045341   481 LSHSLDKALHADPNQRYeTAEQ 502
Cdd:pfam00069 226 AKDLLKKLLKKDPSKRL-TATE 246
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
256-533 2.01e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 125.62  E-value: 2.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 256 GWKVGNVVAQSRQSIVYRVTDIheQPWLLKTLPASRHDETGAGQGLLLEEWFLRRVA--GRFFPEIHPLPDRQHLYYVMR 333
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNhpPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 334 EYPGHTLAERFT---GNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLL-ADDGELRLLDFGLA------FCP 403
Cdd:COG0515  79 YVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLdRDGRVVKLIDFGLAkllpdpGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 404 GLSAVNTEDLPGTPSYIAPEAFNG---AEPHPQQDLYAAGVTLYYLLTGQYPY-------GEIEAFQH-RRFGAPIPASR 472
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeknssATSQTLKIiLELPTPSLASP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66045341 473 YRPDLP----QWLSHSLDKALHADPNQRYETAEQWLLELEQAEHRPLVTKPRPLLEREPLKVWRT 533
Cdd:COG0515 239 LSPSNPelisKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLS 303
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
7-224 3.10e-21

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 93.93  E-value: 3.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   7 FAQFSASGPRAENQDAVrlvTPVPALAASKGYLFALADGVSQCADGALAAQSTLQALALDYYATPETWG--VAQSLDRLL 84
Cdd:cd00143   3 AGVSDKGGDRKTNEDAV---VIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLSEedIEEALRKAF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  85 LAQNRWLLANGLL--------TTLSALVLRGRRFTLAHVGDCRVYRWQTGTLKRISEDHVWEQADmqhVLKRALGLDQYV 156
Cdd:cd00143  80 LRADEEILEEAQDepddarsgTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEE---ERERIEKAGGRV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 157 VMDYLDGELC---------------------------EGERLLLVSDGVWATLGDASIRSILSE---QHDLDAAVKTLVS 206
Cdd:cd00143 157 SNGRVPGVLAvtralgdfdlkpgvsaepdvtvvklteDDDFLILASDGLWDVLSNQEAVDIVRSelaKEDLQEAAQELVD 236
                       250
                ....*....|....*...
gi 66045341 207 AAHLAGSQDNASALLIQV 224
Cdd:cd00143 237 LALRRGSHDNITVVVVRL 254
pknD PRK13184
serine/threonine-protein kinase; Reviewed
370-509 3.28e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 97.92  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  370 HRRNIIHRDIKPENLLLADDGELRLLDFGLA-FCPG-------LSAVNTEDL----------PGTPSYIAPEAFNGAEPH 431
Cdd:PRK13184 130 HSKGVLHRDLKPDNILLGLFGEVVILDWGAAiFKKLeeedlldIDVDERNICyssmtipgkiVGTPDYMAPERLLGVPAS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  432 PQQDLYAAGVTLYYLLTGQYPY----GEIEAFQHrRFGAPIPASRYRpDLPQWLSHSLDKALHADPNQRYETAEQWLLEL 507
Cdd:PRK13184 210 ESTDIYALGVILYQMLTLSFPYrrkkGRKISYRD-VILSPIEVAPYR-EIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287

                 ..
gi 66045341  508 EQ 509
Cdd:PRK13184 288 EP 289
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
328-502 2.06e-19

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 92.22  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    328 LYYVMREYPGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELR---LLDFGL-AFCP 403
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPhakVLDFGIgTLLP 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    404 G------LSAVNTEDLPGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY-GEIEAFQHRRFGAPIPASryrpd 476
Cdd:TIGR03903  134 GvrdadvATLTRTTEVLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVqGASVAEILYQQLSPVDVS----- 208
                          170       180       190
                   ....*....|....*....|....*....|.
gi 66045341    477 LPQW-----LSHSLDKALHADPNQRYETAEQ 502
Cdd:TIGR03903  209 LPPWiaghpLGQVLRKALNKDPRQRAASAPA 239
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
11-222 9.77e-15

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625  Cd Length: 252  Bit Score: 74.33  E-value: 9.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341     11 SASGPRAENQDAVRLVTPVPalaaSKGYLFALADG-----VSQ-CADGALAAQSTLQALALDYYATPETWGVA--QSLDR 82
Cdd:smart00332  15 SMQGVRKPMEDAHVITPDLS----DSGGFFGVFDGhggseAAKfLSKNLPEILAEELIKEKDELEDVEEALRKafLSTDE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341     83 LLLAQNRWLLAngllTTLSALVLRGRRFTLAHVGDCRVYRWQTGTLKRISEDHVWEQADmqhVLKRALGLDQYVVMDYLD 162
Cdd:smart00332  91 EILEELEALSG----STAVVALISGNKLYVANVGDSRAVLCRNGKAVQLTEDHKPSNED---ERARIEAAGGFVINGRVN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    163 GELC---------------------------EGERLLLVSDGVWATLGDASIRSILSEQH--DLDAAVKTLVSAAHLAGS 213
Cdd:smart00332 164 GVLAlsraigdfflkpyvsaepdvtvvelteKDDFLILASDGLWDVLSNQEVVDIVRKHLskDPKEAAKRLIDLALARGS 243

                   ....*....
gi 66045341    214 QDNASALLI 222
Cdd:smart00332 244 KDNITVVVV 252
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
19-178 6.32e-05

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 316216  Cd Length: 209  Bit Score: 44.24  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    19 NQDAVRLVTpvpalaASKGYLFALADGVSQCADGALAAQ-------STLQALALDYYATPETWgVAQSLDRLLL-----A 86
Cdd:pfam13672  12 CQDAFAVWV------LDGGWLIAVADGAGSAKRSDVGARiaveaavEALADLLESEEELIEAL-LRAILNDWLAlvkaeA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    87 QNRWLLANGLLTTLSALVLRGRRFTLAHVGDCR-VYRWQTGTLKRISEDHVWEQADMQHVLKRALGLDQyvvMDYLDGEL 165
Cdd:pfam13672  85 LAQDLEPRDYATTLLAAVVTPGGIVFFQIGDGAiVVRDRDGEVQVLSQPDSGEYANETTFLTSEDALDE---LRIRRLPL 161
                         170
                  ....*....|...
gi 66045341   166 CEGERLLLVSDGV 178
Cdd:pfam13672 162 EPGDALALMTDGL 174
PRK14559 PRK14559
putative protein serine/threonine phosphatase; Provisional
98-224 1.48e-04

putative protein serine/threonine phosphatase; Provisional


Pssm-ID: 237756  Cd Length: 645  Bit Score: 44.28  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   98 TTLSALVLRGRRFTLAHVGDCRVYRW-QTGTLKRISEDHVWEQADMQ--------------HVLKRALGL--DQYVVMDY 160
Cdd:PRK14559 486 TTLVMALVQDTQVAVAHVGDSRLYRVtRKGGLEQLTVDHEVGQREIQrgvepqiayarpdaYQLTQALGPrdNSAIQPDI 565
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66045341  161 LDGELCEGERLLLVSDGV---------WATLgdasIRSILSEQHDLDAAVKTLVSAAHLAGSQDNASALLIQV 224
Cdd:PRK14559 566 QFLEIEEDTLLLLCSDGLsdndllethWQTH----LLPLLSSSANLDQGLNKLIDLANQYNGHDNITAILVRL 634
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
269-509 1.07e-51

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: 179.70  E-value: 1.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 269 SIVYRVTDIH-EQPWLLKTLpasRHDETGAGQgllLEEWFLR--RVAGRFfpeIHP--------LPDRQHLYYVMREYPG 337
Cdd:cd14014  14 GEVYRARDTLlGRPVAIKVL---RPELAEDEE---FRERFLReaRALARL---SHPnivrvydvGEDDGRPYIVMEYVEG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 338 HTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAFCPGLSAVN-TEDLPGT 416
Cdd:cd14014  85 GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTqTGSVLGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 417 PSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPYG---EIEAFQHRRFGAPIPASRYRPDLPQWLSHSLDKALHADP 493
Cdd:cd14014 165 PAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDgdsPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDP 244
                       250
                ....*....|....*.
gi 66045341 494 NQRYETAEQWLLELEQ 509
Cdd:cd14014 245 EERPQSAAELLAALRA 260
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
1-231 4.94e-48

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 223704  Cd Length: 262  Bit Score: 169.84  E-value: 4.94e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   1 MTLQLQFAQFSASGP-RAENQDAVrlvTPVPALAASKGYLFALADGVSQCADGALAAQSTLQALALDYYATPETWGVA-- 77
Cdd:COG0631   4 GILSLKVAGLSDVGTvRKHNEDAF---LIKPNENGNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNEsl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341  78 -QSLDRLLLAQNRWLLA--------NGLLTTLSALVLRGRRFTLAHVGDCRVYRWQTGTLKRISEDHVWEQADMQ----- 143
Cdd:COG0631  81 eELLKEAILKANEAIAEegqlnedvRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNRLEQrgiit 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 144 ----------HVLKRALGLDQYVVMDYLDGELCEGERLLLVSDGVWATLGDASIRSILSEQHDLDAAVKTLVSAAHLAGS 213
Cdd:COG0631 161 peearshprrNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDILKNSETPQEAADKLIELALEGGG 240
                       250
                ....*....|....*...
gi 66045341 214 QDNASALLIQVDTLGEDD 231
Cdd:COG0631 241 PDNITVVLVRLNGEGETS 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
324-502 8.36e-33

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 126.49  E-value: 8.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA-F 401
Cdd:smart00220  68 DEDKLYLVM-EYcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLArQ 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341    402 CPGLSAVNTEDlpGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY---GEIEAFQHRRFGAPIPASRYRPDLP 478
Cdd:smart00220 147 LDPGEKLTTFV--GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFpgdDQLLELFKKIGKPKPPFPPPEWDIS 224
                          170       180
                   ....*....|....*....|....
gi 66045341    479 QWLSHSLDKALHADPNQRYeTAEQ 502
Cdd:smart00220 225 PEAKDLIRKLLVKDPEKRL-TAEE 247
Pkinase pfam00069
Protein kinase domain;
324-502 1.96e-31

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 122.71  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA-F 401
Cdd:pfam00069  69 DKDNLYLVL-EYvEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLArQ 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341   402 CPGLSAVNTEDlpGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY-GEIEAFQHRRFGAPIPASRYRPDLPQW 480
Cdd:pfam00069 148 LNSGSSLTSFV--GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFpGINGNEIYEKIIDQDFDSPRPSSISEE 225
                         170       180
                  ....*....|....*....|..
gi 66045341   481 LSHSLDKALHADPNQRYeTAEQ 502
Cdd:pfam00069 226 AKDLLKKLLKKDPSKRL-TATE 246
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
256-533 2.01e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 125.62  E-value: 2.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 256 GWKVGNVVAQSRQSIVYRVTDIheQPWLLKTLPASRHDETGAGQGLLLEEWFLRRVA--GRFFPEIHPLPDRQHLYYVMR 333
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNhpPNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 334 EYPGHTLAERFT---GNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLL-ADDGELRLLDFGLA------FCP 403
Cdd:COG0515  79 YVDGGSLEDLLKkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLdRDGRVVKLIDFGLAkllpdpGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 404 GLSAVNTEDLPGTPSYIAPEAFNG---AEPHPQQDLYAAGVTLYYLLTGQYPY-------GEIEAFQH-RRFGAPIPASR 472
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeknssATSQTLKIiLELPTPSLASP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66045341 473 YRPDLP----QWLSHSLDKALHADPNQRYETAEQWLLELEQAEHRPLVTKPRPLLEREPLKVWRT 533
Cdd:COG0515 239 LSPSNPelisKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLS 303
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
324-502 1.64e-27

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: 111.80  E-value: 1.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLA---DDGELRLLDFGL 399
Cdd:cd05117  70 DDKNLYLVM-ELcTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 400 A--FCPGLSAvntEDLPGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYP-YGEIEAFQHRRfgapIPASRYRPD 476
Cdd:cd05117 149 AkiFEEGEKL---KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPfYGETEQELFEK----ILKGKYSFD 221
                       170       180       190
                ....*....|....*....|....*....|..
gi 66045341 477 LPQW--LSHS----LDKALHADPNQRYeTAEQ 502
Cdd:cd05117 222 SPEWknVSEEakdlIKRLLVVDPKKRL-TAAE 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
323-496 4.75e-27

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: 110.72  E-value: 4.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 323 PDRQHLYYVMrEY-PGHTLAER--FTGNGPLPlaqwQDLATRLLR--ATGL--LHRRNIIHRDIKPENLLLADDGELRLL 395
Cdd:cd14008  76 PESDKLYLVL-EYcEGGPVMELdsGDRVPPLP----EETARKYFRdlVLGLeyLHENGIVHRDIKPENLLLTADGTVKIS 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 396 DFGLAFCPGLSAVNTEDLPGTPSYIAPEAFNGAEP--HPQQ-DLYAAGVTLYYLLTGQYP------YGEIEAFQHRRFGA 466
Cdd:cd14008 151 DFGVSEMFEDGNDTLQKTAGTPAFLAPELCDGDSKtySGKAaDIWALGVTLYCLVFGRLPfngdniLELYEAIQNQNDEF 230
                       170       180       190
                ....*....|....*....|....*....|
gi 66045341 467 PIPasryrPDLPQWLSHSLDKALHADPNQR 496
Cdd:cd14008 231 PIP-----PELSPELKDLLRRMLEKDPEKR 255
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
327-501 7.10e-26

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: 107.22  E-value: 7.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 327 HLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA-FCPG 404
Cdd:cd14003  73 KIYLVM-EYaSGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSnEFRG 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 405 LSAVNTedLPGTPSYIAPEAFNGAEPH-PQQDLYAAGVTLYYLLTGQYPY-GEIEAFQHRRfgapIpaSRYRPDLPQWLS 482
Cdd:cd14003 152 GSLLKT--FCGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFdDDNDSKLFRK----I--LKGKYPIPSHLS 223
                       170       180
                ....*....|....*....|...
gi 66045341 483 HS----LDKALHADPNQRYETAE 501
Cdd:cd14003 224 PDardlIRRMLVVDPSKRITIEE 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
324-506 1.03e-25

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: 106.84  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 324 DRQHLYYVMrEY-PGHTLAERFTGNGPLPLAQWQDLATRLLRatGL--LHRRNIIHRDIKPENLLLADDGELRLLDFGLA 400
Cdd:cd06606  70 TENTLNIFL-EYvPGGSLASLLKKFGKLPEPVVRKYTRQILE--GLeyLHSNGIVHRDIKGANILVDSDGVVKLADFGCA 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 401 FCPGLSAVNTEDLP--GTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPYGEieafqhrrFGAPIPA------SR 472
Cdd:cd06606 147 KRLAEIATGEGTKSlrGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSE--------LGNPVAAlfkigsSG 218
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66045341 473 YRPDLPQWLSHS----LDKALHADPNQRYeTAEQwLLE 506
Cdd:cd06606 219 EPPPIPEHLSEEakdfLRKCLQRDPKKRP-TADE-LLQ 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
271-446 1.66e-25

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: 105.43  E-value: 1.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 271 VYRVTDIH-EQPWLLKTLPASRHDEtgAGQGLLLEEWFLRRVAGRFFPEIH-PLPDRQHLYYVMREYPGHTLAE-RFTGN 347
Cdd:cd00180   9 VYKARDKEtGKKVAVKVIPKEKLKK--LLEELLREIEILKKLNHPNIVKLYdVFETENFLYLVMEYCEGGSLKDlLKENK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 348 GPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLA--FCPGLSAVNTEDLPGTPSYIAPEAF 425
Cdd:cd00180  87 GPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAkdLDSDDSLLKTTGGTTPPYYAPPELL 166
                       170       180
                ....*....|....*....|.
gi 66045341 426 NGAEPHPQQDLYAAGVTLYYL 446
Cdd:cd00180 167 GGRYYGPKVDIWSLGVILYEL 187
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
327-453 1.52e-24

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-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: 270762  Cd Length: 263  Bit Score: 103.71  E-value: 1.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 327 HLYYVMREYPGHTLAERFTGNGPLPLaQW-QDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAFCpGL 405
Cdd:cd05611  71 YLYLVMEYLNGGDCASLIKTLGGLPE-DWaKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN-GL 148
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66045341 406 SAVNTEDLPGTPSYIAPEAFNGAEPHPQQDLYAAGVTLYYLLTGQYPY 453
Cdd:cd05611 149 EKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPF 196
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
318-496 7.38e-24

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (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. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 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: 271021  Cd Length: 255  Bit Score: 101.56  E-value: 7.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 318 EIHPLPDRQHLYYVMrEYPGHTLAERFTgNGP---LPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRL 394
Cdd:cd14119  61 DVLYNEEKQKLYMVM-EYCVGGLQEMLD-SAPdkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKI 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 395 LDFGLAfcPGLSAVNTEDL----PGTPSYIAPEAFNGAE--PHPQQDLYAAGVTLYYLLTGQYP-YGEIeafQHRRFgAP 467
Cdd:cd14119 139 SDFGVA--EALDLFAEDDTcttsQGSPAFQPPEIANGQDsfSGFKVDIWSAGVTLYNMTTGKYPfEGDN---IYKLF-EN 212
                       170       180       190
                ....*....|....*....|....*....|.
gi 66045341 468 IPASRYR--PDLPQWLSHSLDKALHADPNQR 496
Cdd:cd14119 213 IGKGEYTipDDVDPDLQDLLRGMLEKDPEKR 243
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
324-496 1.50e-23

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901  Cd Length: 245  Bit Score: 100.30  E-value: 1.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 324 DRQHLYYVMrEY-PGHTLAERFTGN-GPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAF 401
Cdd:cd13999  61 SPPPLCIVT-EYmPGGSLYDLLHKKkIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 402 CPGLSAVNTEDLPGTPSYIAPEAFNGaEPHPQQ-DLYAAGVTLYYLLTGQYPYGEIEAFQHRRFGAPIPasrYRPDLPQW 480
Cdd:cd13999 140 IKNSTTEKMTGVVGTPRWMAPEVLRG-EPYTEKaDVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKG---LRPPIPPD 215
                       170       180
                ....*....|....*....|.
gi 66045341 481 LSHSLdKAL-----HADPNQR 496
Cdd:cd13999 216 CPPEL-SKLikrcwNEDPEKR 235
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
324-506 2.43e-23

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: 99.97  E-value: 2.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 324 DRQHLYYVMREYPGHTLAERFTG-NGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAfC 402
Cdd:cd05122  68 KKDELWIVMEFCSGGSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLS-A 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 403 PGLSAVNTEDLPGTPSYIAPEAFNGaEPH-PQQDLYAAGVTLYYLLTGQYPYGEIEAFQHRRFGAPIPASRYRpDLPQW- 480
Cdd:cd05122 147 QLSDGKTRNTFVGTPYWMAPEVIQG-KPYgFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLR-NPKKWs 224
                       170       180
                ....*....|....*....|....*...
gi 66045341 481 --LSHSLDKALHADPNQRYeTAEQwLLE 506
Cdd:cd05122 225 keFKDFLKKCLQKDPEKRP-TAEQ-LLK 250
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
331-508 3.37e-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: 96.68  E-value: 3.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66045341 331 VMREYPG-HTLAER-FTGNGPLPLAQWQDLATRLLRATGLLHRRNIIHRDIKPENLLLADDGELRLLDFGLAFcpGLSAV 408
Cdd:cd13979  79 IIMEYCGnGTLQQLiYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLD