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Conserved domains on  [gi|21222037|ref|NP_627816|]
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serine-threonine protein kinase [Streptomyces coelicolor A3(2)]

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 ...
25-274 8.65e-80

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: 259.83  E-value: 8.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLARSDR-GRTVAVKLVREELAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGY 103
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 104 VAGPSLQQVVGHdHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALQtvaDGGLTR 182
Cdd:cd14014  82 VEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALG---DSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 183 TGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGA---HALMFRIAQEEPDLEGVPEGIADLVR 259
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvlaKHLQEAPPPPSPLNPDVPPALDAIIL 237
                       250
                ....*....|....*
gi 21222037 260 DCLRKDPAARPALAD 274
Cdd:cd14014 238 RALAKDPEERPQSAA 252
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-274 8.65e-80

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: 259.83  E-value: 8.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLARSDR-GRTVAVKLVREELAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGY 103
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 104 VAGPSLQQVVGHdHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALQtvaDGGLTR 182
Cdd:cd14014  82 VEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALG---DSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 183 TGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGA---HALMFRIAQEEPDLEGVPEGIADLVR 259
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvlaKHLQEAPPPPSPLNPDVPPALDAIIL 237
                       250
                ....*....|....*
gi 21222037 260 DCLRKDPAARPALAD 274
Cdd:cd14014 238 RALAKDPEERPQSAA 252
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-277 1.17e-48

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 173.48  E-value: 1.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037     25 YRLLGRLGTGGMGHVYLARS-DRGRTVAVKLVReeLAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGY 103
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    104 VAGPSLQQVVgHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP-RVIDFGIARALQtvaDGGLTR 182
Cdd:smart00220  79 CEGGDLFDLL-KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLD---PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    183 TgaLVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSgaHALMFRIAQEE-----PDLEGVPEGIADL 257
Cdd:smart00220 155 T--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ--LLELFKKIGKPkppfpPPEWDISPEAKDL 230
                          250       260
                   ....*....|....*....|
gi 21222037    258 VRDCLRKDPAARPALADVLE 277
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
25-277 4.45e-40

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 149.67  E-value: 4.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    25 YRLLGRLGTGGMGHVYLAR-SDRGRTVAVKLVREELAaLEEFRERFRHEVESARRVGgHwtaP----VLDADTEAAVPWV 99
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLN-H---PnivrLYDAFEDKDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037   100 ATGYVAGPSLQQVVgHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALqtVADG 178
Cdd:pfam00069  76 VLEYVEGGSLFDLL-SEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARQL--NSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037   179 GLTrtgALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPF-GSANSGAHALMFRIAQEEPDLEGVPEGIADL 257
Cdd:pfam00069 153 SLT---SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFpGINGNEIYEKIIDQDFDSPRPSSISEEAKDL 229
                         250       260
                  ....*....|....*....|
gi 21222037   258 VRDCLRKDPAARPALADVLE 277
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
25-278 7.50e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 152.59  E-value: 7.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLARSDRgrTVAVKLVREELAALEEFRERFRHEVESARRVGGHWT-APVLDADTEAAVPWVATGY 103
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRK--LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNiVKLYDFFQDEGSLYLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 104 VAGPSLQQVVGHDH--GALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGPRV--IDFGIARALQ--TVAD 177
Cdd:COG0515  80 VDGGSLEDLLKKIGrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVklIDFGLAKLLPdpGSTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 178 GGLTRTGALVGSPGFMAPEQVRG---DRVTPACDVFCLGSVLAYAATGKLPF-GSANSGAHALMFRIAQEEPD------- 246
Cdd:COG0515 160 SIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFeGEKNSSATSQTLKIILELPTpslaspl 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21222037 247 ----LEGVPEGIADLVRDCLRKDPAARPALADVLER 278
Cdd:COG0515 240 spsnPELISKAASDLLKKLLAKDPKNRLSSSSDLSH 275
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
45-276 1.30e-22

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: 103.77  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037     45 DRGRTVAVKLVREELAALEEFRERFRHEVESARRVGGHWTAPVLDA-DTEAAVPWVATGYVAGPSLQQVVGHDhGALPER 123
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAAD-GALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    124 SVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGPR----VIDFGIARALQTVADGG---LTRTGALVGSPGFMAPE 196
Cdd:TIGR03903   80 ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphakVLDFGIGTLLPGVRDADvatLTRTTEVLGTPTYCAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    197 QVRGDRVTPACDVFCLGSVLAYAATGKlpfgSANSGAHALMFRIAQEEPDLEGVPEGIA-----DLVRDCLRKDPAARPA 271
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTGQ----RVVQGASVAEILYQQLSPVDVSLPPWIAghplgQVLRKALNKDPRQRAA 235

                   ....*
gi 21222037    272 LADVL 276
Cdd:TIGR03903  236 SAPAL 240
pknD PRK13184
serine/threonine-protein kinase; Reviewed
22-269 1.19e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 100.62  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037   22 IGVYRLLGRLGTGGMGHVYLARSDR-GRTVAVKLVREELAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVA 100
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  101 TGYVAGPSL---------QQVVGHDHGAlpERSVRTL-------GAGLAHalqdIHAAGIVHRDLKPSNVLVTIDGPRVI 164
Cdd:PRK13184  81 MPYIEGYTLksllksvwqKESLSKELAE--KTSVGAFlsifhkiCATIEY----VHSKGVLHRDLKPDNILLGLFGEVVI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  165 -DFGIARALQTVAD--------------GGLTRTGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFgsA 229
Cdd:PRK13184 155 lDWGAAIFKKLEEEdlldidvdernicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY--R 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 21222037  230 NSGAHALMFRIAQEEPD----LEGVPEGIADLVRDCLRKDPAAR 269
Cdd:PRK13184 233 RKKGRKISYRDVILSPIevapYREIPPFLSQIAMKALAVDPAER 276
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-274 8.65e-80

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: 259.83  E-value: 8.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLARSDR-GRTVAVKLVREELAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGY 103
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 104 VAGPSLQQVVGHdHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALQtvaDGGLTR 182
Cdd:cd14014  82 VEGGSLADLLRE-RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALG---DSGLTQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 183 TGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGA---HALMFRIAQEEPDLEGVPEGIADLVR 259
Cdd:cd14014 158 TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvlaKHLQEAPPPPSPLNPDVPPALDAIIL 237
                       250
                ....*....|....*
gi 21222037 260 DCLRKDPAARPALAD 274
Cdd:cd14014 238 RALAKDPEERPQSAA 252
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-277 1.17e-48

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 173.48  E-value: 1.17e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037     25 YRLLGRLGTGGMGHVYLARS-DRGRTVAVKLVReeLAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGY 103
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    104 VAGPSLQQVVgHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP-RVIDFGIARALQtvaDGGLTR 182
Cdd:smart00220  79 CEGGDLFDLL-KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLD---PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    183 TgaLVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSgaHALMFRIAQEE-----PDLEGVPEGIADL 257
Cdd:smart00220 155 T--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ--LLELFKKIGKPkppfpPPEWDISPEAKDL 230
                          250       260
                   ....*....|....*....|
gi 21222037    258 VRDCLRKDPAARPALADVLE 277
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
25-277 4.45e-40

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 149.67  E-value: 4.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037    25 YRLLGRLGTGGMGHVYLAR-SDRGRTVAVKLVREELAaLEEFRERFRHEVESARRVGgHwtaP----VLDADTEAAVPWV 99
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLN-H---PnivrLYDAFEDKDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037   100 ATGYVAGPSLQQVVgHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALqtVADG 178
Cdd:pfam00069  76 VLEYVEGGSLFDLL-SEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARQL--NSGS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037   179 GLTrtgALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPF-GSANSGAHALMFRIAQEEPDLEGVPEGIADL 257
Cdd:pfam00069 153 SLT---SFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFpGINGNEIYEKIIDQDFDSPRPSSISEEAKDL 229
                         250       260
                  ....*....|....*....|
gi 21222037   258 VRDCLRKDPAARPALADVLE 277
Cdd:pfam00069 230 LKKLLKKDPSKRLTATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
25-278 7.50e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 152.59  E-value: 7.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLARSDRgrTVAVKLVREELAALEEFRERFRHEVESARRVGGHWT-APVLDADTEAAVPWVATGY 103
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRK--LVALKVLAKKLESKSKEVERFLREIQILASLNHPPNiVKLYDFFQDEGSLYLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 104 VAGPSLQQVVGHDH--GALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGPRV--IDFGIARALQ--TVAD 177
Cdd:COG0515  80 VDGGSLEDLLKKIGrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVklIDFGLAKLLPdpGSTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 178 GGLTRTGALVGSPGFMAPEQVRG---DRVTPACDVFCLGSVLAYAATGKLPF-GSANSGAHALMFRIAQEEPD------- 246
Cdd:COG0515 160 SIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFeGEKNSSATSQTLKIILELPTpslaspl 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21222037 247 ----LEGVPEGIADLVRDCLRKDPAARPALADVLER 278
Cdd:COG0515 240 spsnPELISKAASDLLKKLLAKDPKNRLSSSSDLSH 275
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
31-270 6.68e-38

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: 143.43  E-value: 6.68e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  31 LGTGGMGHVYLARSDR-GRTVAVKLVR------EELAALE-EFR--ERFRHE--VesaRRVGGHWTAPVLDADTEaavpw 98
Cdd:cd06606   8 LGKGSFGSVYLALNLDtGELMAVKEVElsgdseEELEALErEIRilSSLKHPniV---RYLGTERTENTLNIFLE----- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  99 vatgYVAGPSLQQVVGhDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGprVI---DFGIARALQTV 175
Cdd:cd06606  80 ----YVPGGSLASLLK-KFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG--VVklaDFGCAKRLAEI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 176 ADGGLTRTgaLVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFgSANSGAHALMFRIA--QEEPDL-EGVPE 252
Cdd:cd06606 153 ATGEGTKS--LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW-SELGNPVAALFKIGssGEPPPIpEHLSE 229
                       250
                ....*....|....*...
gi 21222037 253 GIADLVRDCLRKDPAARP 270
Cdd:cd06606 230 EAKDFLRKCLQRDPKKRP 247
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
24-277 3.65e-35

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: 135.79  E-value: 3.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  24 VYRLLGRLGTGGMGHVYLARSDR-GRTVAVKLVR-EELAALEE-FRERFRHEvesarrvggHWTAP--------VLDADT 92
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKtGQIVAIKKINlESKEKKESiLNEIAILK---------KCKHPnivkyygsYLKKDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  93 eaavPWVATGYVAGPSLQQVVGHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP-RVIDFGIAra 171
Cdd:cd05122  72 ----LWIVMEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEvKLIDFGLS-- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 172 lQTVADGGLTRTgaLVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGsaNSGAHALMFRIAQEEP----DL 247
Cdd:cd05122 146 -AQLSDGKTRNT--FVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS--ELPPMKALFLIATNGPpglrNP 220
                       250       260       270
                ....*....|....*....|....*....|
gi 21222037 248 EGVPEGIADLVRDCLRKDPAARPALADVLE 277
Cdd:cd05122 221 KKWSKEFKDFLKKCLQKDPEKRPTAEQLLK 250
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
31-277 5.54e-35

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622  Cd Length: 215  Bit Score: 133.94  E-value: 5.54e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  31 LGTGGMGHVYLAR-SDRGRTVAVKLVREELaaLEEFRERFRHEVESARRVGGHWTAPVLDADTEAAVPWVATGYVAGPSL 109
Cdd:cd00180   1 LGKGSFGKVYKARdKETGKKVAVKVIPKEK--LKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 110 QQVVGHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALQTvaDGGLTRTGALVG 188
Cdd:cd00180  79 KDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGtVKLADFGLAKDLDS--DDSLLKTTGGTT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 189 SPGFMAPEQVRGDRVTPACDVFCLGsvlayaatgklpfgsansgahALMFRIAQeepdlegvpegIADLVRDCLRKDPAA 268
Cdd:cd00180 157 PPYYAPPELLGGRYYGPKVDIWSLG---------------------VILYELEE-----------LKDLIRRMLQYDPKK 204

                ....*....
gi 21222037 269 RPALADVLE 277
Cdd:cd00180 205 RPSAKELLE 213
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
31-278 1.38e-32

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: 128.04  E-value: 1.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  31 LGTGGMGHVYLARSdRGRTVAVKLVREELAALEEFRErFRHEVESARR---------VGghwtapvldADTEAAVPWVAT 101
Cdd:cd13999   1 IGSGSFGEVYKGKW-RGTDVAIKKLKVEDDNDELLKE-FRREVSILSKlrhpnivqfIG---------ACLSPPPLCIVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 102 GYVAGPSLQQVVgHD-HGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARalqtVADGG 179
Cdd:cd13999  70 EYMPGGSLYDLL-HKkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFtVKIADFGLSR----IKNST 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 180 LTRTGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGAHALMFRIAQEEPDL-EGVPEGIADLV 258
Cdd:cd13999 145 TEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIpPDCPPELSKLI 224
                       250       260
                ....*....|....*....|
gi 21222037 259 RDCLRKDPAARPALADVLER 278
Cdd:cd13999 225 KRCWNEDPEKRPSFSEIVKR 244
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
25-277 1.82e-30

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: 122.24  E-value: 1.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  25 YRLLGRLGTGGMGHVYLAR-SDRGRTVAVKLVREELAAlEEFRERFRHEVESARRVGgHwtaP-------VLDadTEAAV 96
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARhKLTGEKVAIKIIDKSKLK-EEIEEKIKREIEIMKLLN-H---PniiklyeVIE--TENKI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  97 pWVATGYVAGPSL-QQVVghDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP-RVIDFGIARalqT 174
Cdd:cd14003  75 -YLVMEYASGGELfDYIV--NNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNlKIIDFGLSN---E 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 175 VADGGLTRTgaLVGSPGFMAPEQVRGD-RVTPACDVFCLGSVLaYA-ATGKLPFGSANsgaHALMFR-IAQEEPDLEG-V 250
Cdd:cd14003 149 FRGGSLLKT--FCGTPAYAAPEVLLGRkYDGPKADVWSLGVIL-YAmLTGYLPFDDDN---DSKLFRkILKGKYPIPShL 222
                       250       260
                ....*....|....*....|....*..
gi 21222037 251 PEGIADLVRDCLRKDPAARPALADVLE 277
Cdd:cd14003 223 SPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
31-278 5.34e-30

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968  Cd Length: 272  Bit Score: 121.23  E-value: 5.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  31 LGTGGMGHVYLARSDRGRTVAVKLVREElaALEEFRERFRHEVESARRV---------GGHWtapvlDADTEAAVpwvaT 101
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEM--NCAASKKEFLTELEMLGRLrhpnlvrllGYCL-----ESDEKLLV----Y 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 102 GYVAGPSLQQVVGHDHG--ALPERSVRTLGAGLAHALQDIHAAG---IVHRDLKPSNVLVTIDG-PRVIDFGIARALQTV 175
Cdd:cd14066  70 EYMPNGSLEDRLHCHKGspPLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFePKLTDFGLARLIPPS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 176 ADGglTRTGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGAHALMF----------------- 238
Cdd:cd14066 150 ESV--SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLvewveskgkeeledild 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21222037 239 -RIAQEEPDLEGVPEGIADLVRDCLRKDPAARPALADVLER 278
Cdd:cd14066 228 kRLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSMKEVVQM 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
24-277 1.24e-29

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


Pssm-ID: 270797  Cd Length: 254  Bit Score: 119.64  E-value: 1.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  24 VYRLLGRLGTGGMGHVYLAR-SDRGRTVAVKLVR------EELAALE---EFRERFRHE--VesaRRVGGHWTAPVLdad 91
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLnLNTGEFVAIKQISlekipkSDLKSVMgeiDLLKKLNHPniV---KYIGSVKTKDSL--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  92 teaavpWVATGYVAGPSLQQVVgHDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP-RVIDFGIAR 170
Cdd:cd06627  75 ------YIILEYVENGSLASII-KKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLvKLADFGVAT 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 171 ALQTVADggltRTGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFgsANSGAHALMFRIAQ-EEPDLeg 249
Cdd:cd06627 148 KLNEVEK----DENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPY--YDLQPMAALFRIVQdDHPPL-- 219
                       250       260       270
                ....*....|....*....|....*....|..
gi 21222037 250 vPEGIADLVRD----CLRKDPAARPALADVLE 277
Cdd:cd06627 220 -PENISPELRDfllqCFQKDPTLRPSAKELLK 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
24-277 3.71e-29

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: 118.35  E-value: 3.71e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  24 VYRLLGRLGTGGMGHVYLARS-DRGRTVAVKLVREELAAlEEFRERFRHEVESARRVGgHwtaP----VLDA-DTEAAVp 97
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHkKTGEEYAVKIIDKKKLK-SEDEEMLRREIEILKRLD-H---PnivkLYEVfEDDKNL- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  98 WVATGYVAGPSL-QQVVghDHGALPERSVRTLGAGLAHALQDIHAAGIVHRDLKPSNVLVTIDGP----RVIDFGIARAL 172
Cdd:cd05117  75 YLVMELCTGGELfDRIV--KKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspiKIIDFGLAKIF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 173 QtvaDGGLTRTgaLVGSPGFMAPEQVRGDRVTPACDVFCLGsVLAYA-ATGKLPFGSANsgaHALMFRIAQ------EEP 245
Cdd:cd05117 153 E---EGEKLKT--VCGTPYYVAPEVLKGKGYGKKCDIWSLG-VILYIlLCGYPPFYGET---EQELFEKILkgkysfDSP 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 21222037 246 DLEGVPEGIADLVRDCLRKDPAARPALADVLE 277
Cdd:cd05117 224 EWKNVSEEAKDLIKRLLVVDPKKRLTAAEALN 255
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
26-278 1.71e-28

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: 116.71  E-value: 1.71e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  26 RLLGRLGTGGMGHVYLARSdRGRTVAVKLVREElAALEEFRERFRHEVESAR-------RVGGHWTApvldaDTEAAVPW 98
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATY-KGETVAVKIVRRR-RKNRASRQSFWAELNAARlrhenivRVLAAETG-----TDFASLGL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  99 VATGYVAGPSLQQVVGHDHGALP-ERSVRTLgAGLAHALQDIHAAGIVHRDLKPSNVLVTIDG-PRVIDFGIARALQTVA 176
Cdd:cd13979  79 IIMEYCGNGTLQQLIYEGSEPLPlAHRILIS-LDIARALRFCHSHGIVHLDVKPANILISEQGvCKLCDFGCSVKLGEGN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 177 DGGLTRTGaLVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSgaHALMFRIAQE-EPDLEGVPEG-- 253
Cdd:cd13979 158 EVGTPRSH-IGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQ--HVLYAVVAKDlRPDLSGLEDSef 234
                       250       260
                ....*....|....*....|....*....
gi 21222037 254 ---IADLVRDCLRKDPAARP-ALADVLER 278
Cdd:cd13979 235 gqrLRSLISRCWSAQPAERPnADESLLKS 263
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
31-276 4.19e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 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: 270800  Cd Length: 268  Bit Score: 115.60  E-value: 4.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037  31 LGTGGMGHVYLARsDR--GRTVAVKLV---REELAALEEFRERFRHEVESARRVGGHWTAPVLDADTEAA-----VPWVA 100
Cdd:cd06630   8 LGTGAFSSCYQAR-DVktGTLMAVKQVsfcRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKShfnifVEWMA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 101 TGYVAGpslqqvVGHDHGALPE----RSVRTLGAGLAHalqdIHAAGIVHRDLKPSNVLVTIDGP--RVIDFGIARALQT 174
Cdd:cd06630  87 GGSVAS------LLSKYGAFSEnviiNYTLQILRGLAY----LHDNQIIHRDLKGANLLVDSTGQrlRIADFGAAARLAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222037 175 VADGGLTRTGALVGSPGFMAPEQVRGDRVTPACDVFCLGSVLAYAATGKLPFGSANSGAH-ALMFRIA--QEEPDL