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Conserved domains on  [gi|21224924|ref|NP_630703|]
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protein kinase [Streptomyces coelicolor A3(2)]

Protein Classification

NERD and HHH_5 domain-containing protein (domain architecture ID 10551716)

protein containing domains NERD, PKc_like, and HHH_5

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
529-802 3.98e-25

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14014:

Pssm-ID: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 107.29  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDleaeTRRTRPLAVlKVALSD--SRGEI---LVREAEAMRRLRpHSGIIRLAEPEplHIG 603
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARD----TLLGRPVAI-KVLRPElaEDEEFrerFLREARALARLS-HPNIVRVYDVG--EDD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 GRTVLALEYVgderdddgpgaEGatrprrreETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAV 683
Cdd:cd14014   73 GRPYIVMEYV-----------EG--------GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  684 rirpNRTRELVLIDFSLAGYPAKNTD------AGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPkwgDGSV 757
Cdd:cd14014  134 ----TEDGRVKLTDFGIARALGDSGLtqtgsvLGTPAYMAP--EQARGGPVDPRSDIYSLGVVLYELLTGRPP---FDGD 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 21224924  758 LPRMTDPKEWPYPTIAAEAFDPAVRDGLVAFFQKALHRDAGKRFP 802
Cdd:cd14014  205 SPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQ 249
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
210-488 2.33e-21

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14014:

Pssm-ID: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 95.73  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  210 YLARHSDLPEAARVRIYLSERGSDASLRQSVenaaRREAAVLGRFKHPGAVQLKQYFPsgHAAGPALIFDYHPHtQKLDE 289
Cdd:cd14014   17 YRARDTLLGRPVAIKVLRPELAEDEEFRERF----LREARALARLSHPNIVRVYDVGE--DDGRPYIVMEYVEG-GSLAD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  290 YLVQYGeKLDILGRMALVRQLAETVRSAHASRIHHRALAARSVLVVPRsrggkGRAVgeeaawltpqlqISDWQIATQRS 369
Cdd:cd14014   90 LLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED-----GRVK------------LTDFGIARALG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  370 GDssqgqGMTRFAPTALSAmhladdadAYLAPE-LTALNPDPVYlDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGE 446
Cdd:cd14014  152 DS-----GLTQTGSVLGTP--------AYMAPEqARGGPVDPRS-DIYSLGVVLYELLTGRPPfdGDSPAAVLAKHLQEA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 21224924  447 GLRPSSLVDGLSEDVDELVQAATAYRPGQRLSSVDEFLELLE 488
Cdd:cd14014  218 PPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALR 259
NERD pfam08378
Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial ...
14-128 1.40e-17

Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial as well as archaeal and plant proteins. It has distant similarity to endonucleases (hence its name) and its predicted secondary structure is helix - sheet - sheet - sheet - sheet - weak sheet/long loop - helix - sheet - sheet. The majority of NERD-containing proteins are single-domain, but in several cases proteins containing NERD have additional domains which in 75% of cases are involved in DNA processing.


:

Pssm-ID: 285566  Cd Length: 110  Bit Score: 81.32  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     14 FEHERRGLEAIRQKLpdgDPWRAWSNFTFTANTGHVREVDLLVVAPGGLCMVELKDWHGSVT-SENGTWVQTTPGGRRrt 92
Cdd:pfam08378    3 AEGERRVAEYLKKLP---GEYIVLHNLRLPDGDGGTTEIDHLVISPKGIFVIEVKNYSGWIFgDENGQWTQKKGNGFK-- 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 21224924     93 hgNPLHLVNRKAKELAGLLAQPGaKRVWVAEAVCFT 128
Cdd:pfam08378   78 --NPLEQNKRHAKALKKLLLKLG-PRVPVESVVVFS 110
HHH_5 pfam14520
Helix-hairpin-helix domain;
872-924 5.44e-04

Helix-hairpin-helix domain;


:

Pssm-ID: 291205  Cd Length: 57  Bit Score: 39.81  E-value: 5.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21224924    872 LTVSGLTPAAQSFLYGLGITTVGELLDYSRRKLVNAPGLGAKTRNEVQQRQRE 924
Cdd:pfam14520    5 LSIPGIGPKTALALLSAGIGTVEDLAEADVEELAEIPGIGEKTAERIIEELRD 57
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
529-802 3.98e-25

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 [Multi-domain]  Cd Length: 260  Bit Score: 107.29  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDleaeTRRTRPLAVlKVALSD--SRGEI---LVREAEAMRRLRpHSGIIRLAEPEplHIG 603
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARD----TLLGRPVAI-KVLRPElaEDEEFrerFLREARALARLS-HPNIVRVYDVG--EDD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 GRTVLALEYVgderdddgpgaEGatrprrreETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAV 683
Cdd:cd14014   73 GRPYIVMEYV-----------EG--------GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  684 rirpNRTRELVLIDFSLAGYPAKNTD------AGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPkwgDGSV 757
Cdd:cd14014  134 ----TEDGRVKLTDFGIARALGDSGLtqtgsvLGTPAYMAP--EQARGGPVDPRSDIYSLGVVLYELLTGRPP---FDGD 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 21224924  758 LPRMTDPKEWPYPTIAAEAFDPAVRDGLVAFFQKALHRDAGKRFP 802
Cdd:cd14014  205 SPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQ 249
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
210-488 2.33e-21

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 [Multi-domain]  Cd Length: 260  Bit Score: 95.73  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  210 YLARHSDLPEAARVRIYLSERGSDASLRQSVenaaRREAAVLGRFKHPGAVQLKQYFPsgHAAGPALIFDYHPHtQKLDE 289
Cdd:cd14014   17 YRARDTLLGRPVAIKVLRPELAEDEEFRERF----LREARALARLSHPNIVRVYDVGE--DDGRPYIVMEYVEG-GSLAD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  290 YLVQYGeKLDILGRMALVRQLAETVRSAHASRIHHRALAARSVLVVPRsrggkGRAVgeeaawltpqlqISDWQIATQRS 369
Cdd:cd14014   90 LLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED-----GRVK------------LTDFGIARALG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  370 GDssqgqGMTRFAPTALSAmhladdadAYLAPE-LTALNPDPVYlDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGE 446
Cdd:cd14014  152 DS-----GLTQTGSVLGTP--------AYMAPEqARGGPVDPRS-DIYSLGVVLYELLTGRPPfdGDSPAAVLAKHLQEA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 21224924  447 GLRPSSLVDGLSEDVDELVQAATAYRPGQRLSSVDEFLELLE 488
Cdd:cd14014  218 PPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALR 259
NERD pfam08378
Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial ...
14-128 1.40e-17

Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial as well as archaeal and plant proteins. It has distant similarity to endonucleases (hence its name) and its predicted secondary structure is helix - sheet - sheet - sheet - sheet - weak sheet/long loop - helix - sheet - sheet. The majority of NERD-containing proteins are single-domain, but in several cases proteins containing NERD have additional domains which in 75% of cases are involved in DNA processing.


Pssm-ID: 285566  Cd Length: 110  Bit Score: 81.32  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     14 FEHERRGLEAIRQKLpdgDPWRAWSNFTFTANTGHVREVDLLVVAPGGLCMVELKDWHGSVT-SENGTWVQTTPGGRRrt 92
Cdd:pfam08378    3 AEGERRVAEYLKKLP---GEYIVLHNLRLPDGDGGTTEIDHLVISPKGIFVIEVKNYSGWIFgDENGQWTQKKGNGFK-- 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 21224924     93 hgNPLHLVNRKAKELAGLLAQPGaKRVWVAEAVCFT 128
Cdd:pfam08378   78 --NPLEQNKRHAKALKKLLLKLG-PRVPVESVVVFS 110
HHH_5 pfam14520
Helix-hairpin-helix domain;
872-924 5.44e-04

Helix-hairpin-helix domain;


Pssm-ID: 291205  Cd Length: 57  Bit Score: 39.81  E-value: 5.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21224924    872 LTVSGLTPAAQSFLYGLGITTVGELLDYSRRKLVNAPGLGAKTRNEVQQRQRE 924
Cdd:pfam14520    5 LSIPGIGPKTALALLSAGIGTVEDLAEADVEELAEIPGIGEKTAERIIEELRD 57
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
530-801 6.29e-20

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 91.44  E-value: 6.29e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     530 WEVRRRLGTGSTSRAFLVRDleaetRRT-RPLAVLKVALSDSRGEI--LVREAEAMRRLRpHSGIIRL--AEPEPLHIgg 604
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARD-----KKTgKLVAIKVIKKKKIKKDRerILREIKILKKLK-HPNIVRLydVFEDEDKL-- 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     605 rtVLALEYVgderdddgPGAEgatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVr 684
Cdd:smart00220   73 --YLVMEYC--------EGGD-----------LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL- 130
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     685 irpNRTRELVLIDFSLAGY----PAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDGS---- 756
Cdd:smart00220  131 ---DEDGHVKLADFGLARQldpgEKLTTFVGTPEYMAP--EVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQllel 205
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*..
gi 21224924     757 --VLPRMTDPKEWPYPTIAAEAFDpavrdglvaFFQKALHRDAGKRF 801
Cdd:smart00220  206 fkKIGKPKPPFPPPEWDISPEAKD---------LIRKLLVKDPEKRL 243
Pkinase pfam00069
Protein kinase domain;
530-800 2.87e-19

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 89.19  E-value: 2.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924    530 WEVRRRLGTGSTSRAFLVRdlEAETRRtrPLAVLKVALS---DSRGEILVREAEAMRRLRpHSGIIRLAE--PEPLHIgg 604
Cdd:pfam00069    1 YEVLEKLGSGSFGTVYKAK--HRDTGK--IVAVKKIKKEkikKKKDKNVLREIKILKKLN-HPNIVRLYDvfEDKDHL-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924    605 rtVLALEYV-GDErdddgpgaegatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAV 683
Cdd:pfam00069   74 --YLVLEYVeGGS--------------------LFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILI 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924    684 rirpNRTRELVLIDFSLAGY----PAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDG--SV 757
Cdd:pfam00069  132 ----DEDGNLKITDFGLAKQlssgSKLTTFVGTPWYMAP--EVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINgdTL 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 21224924    758 LPRMTDPKEWPYPTiaAEAFDPAVRDglvaFFQKALHRDAGKR 800
Cdd:pfam00069  206 YELIIDQLDLSSPR--PSSISEEAKD----LLKKLLKKDPSKR 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
530-801 1.77e-15

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 79.02  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLVRDLEAETRRtrplaVLKVALSDSRGEI--LVREAEAMRRLRPHSGIIRLAEPepLHIGGRTV 607
Cdd:COG0515    2 YRILRKLGEGSFGEVYLARDRKLVALK-----VLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDF--FQDEGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  608 LALEYV--GDERDddgpgaegatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRI 685
Cdd:COG0515   75 LVMEYVdgGSLED------------------LLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  686 RPNrtrELVLIDFSLA-----------GYPAKNTDAGTDGYLDP-FVDVITRGSYDSHAERYAVAVTLHQMASGELPKWG 753
Cdd:COG0515  137 DGR---VVKLIDFGLAkllpdpgstssIPALPSTSVGTPGYMAPeVLLGLSLAYASSSSDIWSLGITLYELLTGLPPFEG 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21224924  754 DGSVLPRM----------TDPKEWPYPTIAAEAFDPAVRDglvaFFQKALHRDAGKRF 801
Cdd:COG0515  214 EKNSSATSqtlkiilelpTPSLASPLSPSNPELISKAASD----LLKKLLAKDPKNRL 267
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
530-744 1.20e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 44.87  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924   530 WEVRRRLGTGSTSRAFLV-RDLEAETrrtrplAVLKVALsdsRGEILVrEAEAMRRLRpHSGIIRLAEPepLHIGGRTVL 608
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVAtKPGQPDP------VVLKIGQ---KGTTLI-EAMLLQNVN-HPSVIRMKDT--LVSGAITCM 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924   609 ALeyvgderdddgpgaegatrPRRREETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirpN 688
Cdd:PHA03209  135 VL-------------------PHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFI----N 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924   689 RTRELVLIDFSLAGYPAKNTD----AGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQM 744
Cdd:PHA03209  192 DVDQVCIGDLGAAQFPVVAPAflglAGTVETNAP--EVLARDKYNSKADIWSAGIVLFEM 249
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
529-802 3.98e-25

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 [Multi-domain]  Cd Length: 260  Bit Score: 107.29  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDleaeTRRTRPLAVlKVALSD--SRGEI---LVREAEAMRRLRpHSGIIRLAEPEplHIG 603
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARD----TLLGRPVAI-KVLRPElaEDEEFrerFLREARALARLS-HPNIVRVYDVG--EDD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 GRTVLALEYVgderdddgpgaEGatrprrreETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAV 683
Cdd:cd14014   73 GRPYIVMEYV-----------EG--------GSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  684 rirpNRTRELVLIDFSLAGYPAKNTD------AGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPkwgDGSV 757
Cdd:cd14014  134 ----TEDGRVKLTDFGIARALGDSGLtqtgsvLGTPAYMAP--EQARGGPVDPRSDIYSLGVVLYELLTGRPP---FDGD 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 21224924  758 LPRMTDPKEWPYPTIAAEAFDPAVRDGLVAFFQKALHRDAGKRFP 802
Cdd:cd14014  205 SPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQ 249
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
210-488 2.33e-21

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 [Multi-domain]  Cd Length: 260  Bit Score: 95.73  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  210 YLARHSDLPEAARVRIYLSERGSDASLRQSVenaaRREAAVLGRFKHPGAVQLKQYFPsgHAAGPALIFDYHPHtQKLDE 289
Cdd:cd14014   17 YRARDTLLGRPVAIKVLRPELAEDEEFRERF----LREARALARLSHPNIVRVYDVGE--DDGRPYIVMEYVEG-GSLAD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  290 YLVQYGeKLDILGRMALVRQLAETVRSAHASRIHHRALAARSVLVVPRsrggkGRAVgeeaawltpqlqISDWQIATQRS 369
Cdd:cd14014   90 LLRERG-PLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTED-----GRVK------------LTDFGIARALG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  370 GDssqgqGMTRFAPTALSAmhladdadAYLAPE-LTALNPDPVYlDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGE 446
Cdd:cd14014  152 DS-----GLTQTGSVLGTP--------AYMAPEqARGGPVDPRS-DIYSLGVVLYELLTGRPPfdGDSPAAVLAKHLQEA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 21224924  447 GLRPSSLVDGLSEDVDELVQAATAYRPGQRLSSVDEFLELLE 488
Cdd:cd14014  218 PPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELLAALR 259
NERD pfam08378
Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial ...
14-128 1.40e-17

Nuclease-related domain; The nuclease-related domain (NERD) is found in a range of bacterial as well as archaeal and plant proteins. It has distant similarity to endonucleases (hence its name) and its predicted secondary structure is helix - sheet - sheet - sheet - sheet - weak sheet/long loop - helix - sheet - sheet. The majority of NERD-containing proteins are single-domain, but in several cases proteins containing NERD have additional domains which in 75% of cases are involved in DNA processing.


Pssm-ID: 285566  Cd Length: 110  Bit Score: 81.32  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924     14 FEHERRGLEAIRQKLpdgDPWRAWSNFTFTANTGHVREVDLLVVAPGGLCMVELKDWHGSVT-SENGTWVQTTPGGRRrt 92
Cdd:pfam08378    3 AEGERRVAEYLKKLP---GEYIVLHNLRLPDGDGGTTEIDHLVISPKGIFVIEVKNYSGWIFgDENGQWTQKKGNGFK-- 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 21224924     93 hgNPLHLVNRKAKELAGLLAQPGaKRVWVAEAVCFT 128
Cdd:pfam08378   78 --NPLEQNKRHAKALKKLLLKLG-PRVPVESVVVFS 110
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
529-750 2.69e-14

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 [Multi-domain]  Cd Length: 252  Bit Score: 73.71  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDleaetRRTRPLAVLKVA----LSDSRGEILVREAEAMRRLRpHSGIIRLAEPepLHIGG 604
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARH-----KLTGEKVAIKIIdkskLKEEIEEKIKREIEIMKLLN-HPNIIKLYEV--IETEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  605 RTVLALEYV--GDERDddgpgaegatrprrreetvarQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIA 682
Cdd:cd14003   73 KIYLVMEYAsgGELFD---------------------YIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  683 VRIRPNrtreLVLIDFSLAGYPAKN----TDAGTDGYLDPfvDVITRGSYDshAERYAV---AVTLHQMASGELP 750
Cdd:cd14003  132 LDKNGN----LKIIDFGLSNEFRGGsllkTFCGTPAYAAP--EVLLGRKYD--GPKADVwslGVILYAMLTGYLP 198
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
531-748 3.45e-14

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC 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: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 73.42  E-value: 3.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  531 EVRRRLGTGSTSRAFLVRDLEAETRRtrplAVLKVALSDSRGEILVREAEAMRRLRPHSG---IIRLAEPEPLHIGGRTV 607
Cdd:cd05118    2 EVLRKIGEGAFGTVWLARDKVTGEKV----AIKKIKNDFRHPKAALREIKLLKHLNDVEGhpnIVKLLDVFEHRGGNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  608 LALEYVGderdddgpgaegatrprrreETVARQLREHGR-LPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRir 686
Cdd:cd05118   78 LVFELMG--------------------MNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILIN-- 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  687 pNRTRELVLIDFSLAGY---PAKNTDAGTDGYLDPFVdVITRGSYDSHAERYAVAVTLHQMASGE 748
Cdd:cd05118  136 -LELGQLKLADFGLARSftsPPYTPYVATRWYRAPEV-LLGAKPYGSSIDIWSLGCILAELLTGR 198
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
536-746 1.24e-12

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 [Multi-domain]  Cd Length: 215  Bit Score: 68.07  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  536 LGTGSTSRAFLVRDLEAETRRtrplaVLKVALSDSRGEI---LVREAEAMRRLRpHSGIIRLAEPepLHIGGRTVLALEY 612
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKV-----AVKVIPKEKLKKLleeLLREIEILKKLN-HPNIVKLYDV--FETENFLYLVMEY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  613 VGderdddgpgaegatrprrrEETVARQLREH-GRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirpNRTR 691
Cdd:cd00180   73 CE-------------------GGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL----DSDG 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  692 ELVLIDFSLA-----GYPAKNTDAGTDGYLDPFVDVITRGSYDSHAERYAVAVTLHQMAS 746
Cdd:cd00180  130 TVKLADFGLAkdldsDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYELEE 189
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
536-811 1.27e-12

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 [Multi-domain]  Cd Length: 267  Bit Score: 68.73  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  536 LGTGSTSRAFLVRDLE------------AETRRTR----PLAVLKVALSDSRGEILVreaeaMRRLRpHSGIIRLAE--- 596
Cdd:cd14008    1 LGRGSFGKVKLALDTEtgqlyaikifnkSRLRKRRegknDRGKIKNALDDVRREIAI-----MKKLD-HPNIVRLYEvid 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  597 -PEPLHIggrtVLALEYV--GD--ERDDDGPgaegatRPRRREETVARQLREhgrlpvdqleaygdyLFGAVDFLEGEGI 671
Cdd:cd14008   75 dPESDKL----YLVLEYCegGPvmELDSGDR------VPPLPEETARKYFRD---------------LVLGLEYLHENGI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  672 WHRDIKPDNIAVrirpNRTRELVLIDFSLAGYPAKNTD-----AGTDGYLDPFVDVITRGSYDSHA-ERYAVAVTLHQMA 745
Cdd:cd14008  130 VHRDIKPENLLL----TADGTVKISDFGVSEMFEDGNDtlqktAGTPAFLAPELCDGDSKTYSGKAaDIWALGVTLYCLV 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21224924  746 SGELPKWGD-GSVLPRMTDPKEWPYPtiaaeaFDPAVRDGLVAFFQKALHRDAGKRF--PELkpMRDAW 811
Cdd:cd14008  206 FGRLPFNGDnILELYEAIQNQNDEFP------IPPELSPELKDLLRRMLEKDPEKRItlKEI--KEHPW 266
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
529-811 2.69e-12

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to 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: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 67.43  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDLEaeTRRTRPLAVL-KVALSDSR-GEILVREAEAMRRLRpHSGIIRLAEPepLHIGGRT 606
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTK--TGESVAIKIIdKEQVAREGmVEQIKREIAIMKLLR-HPNIVELHEV--MATKTKI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  607 VLALEYVgderdddgPGAEGATRprrreetvarqLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIR 686
Cdd:cd14663   76 FFVMELV--------TGGELFSK-----------IAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDED 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  687 PNrtreLVLIDFSLAGYPAKN-------TDAGTDGYLDPfvDVITRGSYD-SHAERYAVAVTLHQMASGELPkWGDGSV- 757
Cdd:cd14663  137 GN----LKISDFGLSALSEQFrqdgllhTTCGTPNYVAP--EVLARRGYDgAKADIWSCGVILFVLLAGYLP-FDDENLm 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  758 -LPRMTDPKEWPYPTiaaeAFDPavrdGLVAFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14663  210 aLYRKIMKGEFEYPR----WFSP----GAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
529-811 3.58e-12

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 67.12  E-value: 3.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVrdLEAETRRTRPLAVL---KVALSDSRGEILVREAEAMRRLRpHSGIIRLAE--PEPLHIg 603
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKA--VEVETGKMRAIKQIvkrKVAGNDKNLQLFQREINILKSLE-HPGIVRLIDwyEDDQHI- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 grtVLALEYV--GDERD---DDGPGAEGATRPrrreetVARQLREhgrlpvdqleaygdylfgAVDFLEGEGIWHRDIKP 678
Cdd:cd14098   77 ---YLVMEYVegGDLMDfimAWGAIPEQHARE------LTKQILE------------------AMAYTHSMGITHRDLKP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  679 DNIAvrIRPNRTRELVLIDFSLA----GYPAKNTDAGTDGYLDPFV----DVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14098  130 ENIL--ITQDDPVIVKISDFGLAkvihTGTFLVTFCGTMAYLAPEIlmskEQNLQGGYSNLVDMWSVGCLVYVMLTGALP 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21224924  751 KWGDG--SVLPRMTDPKeWPYPTIAAEAFDPAVRDglvaFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14098  208 FDGSSqlPVEKRIRKGR-YTQPPLVDFNISEEAID----FILRLLDVDPEKRMTAAQALDHPW 265
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
536-801 5.61e-11

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 63.30  E-value: 5.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  536 LGTGSTSRAFLVRdlEAETRRTRPLAVLKVALSDSRGEILVREAEA--MRRLrPHSGIIRLA----EPEPLHiggrtvLA 609
Cdd:cd05123    1 LGKGSFGKVLLVR--KKDTGKLYAMKVLRKKEIIKRKEVEHTLNERniLERV-NHPFIVKLHyafqTEEKLY------LV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  610 LEYVgderdddgPGAEgatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirpNR 689
Cdd:cd05123   72 LDYV--------PGGE-----------LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL----DS 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  690 TRELVLIDFSLA-----GYPAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDGS-VLPRMTD 763
Cdd:cd05123  129 DGHIKLTDFGLAkelssDGDRTYTFCGTPEYLAP--EVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRkEIYEKIL 206
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21224924  764 PKEWPYPtiaaEAFDPAVRDglvaFFQKALHRDAGKRF 801
Cdd:cd05123  207 KSPLKFP----EYVSPEAKS----LISGLLQKDPTKRL 236
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
529-820 6.73e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK 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: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 60.81  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDLEaetrRTRPLAVLKVALSDSRGEI---LVREAEAMRRLRPHSGIIRLAEPEPlhIGGR 605
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRE----TGETVALKKVALRKLEGGIpnqALREIKALQACQGHPYVVKLRDVFP--HGTG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  606 TVLALEYVGDerdddgpgaegatrprrreeTVARQLREHGR-LPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVR 684
Cdd:cd07832   75 FVLVFEYMLS--------------------SLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  685 irpnRTRELVLIDFSLAGYPAKNTDA------GTDGYLDPfvdVITRGS--YDSHAERYAVAVTLHQMASGE--LPKWGD 754
Cdd:cd07832  135 ----STGVLKIADFGLARLFSEEDPRlyshqvATRWYRAP---ELLYGSrkYDEGVDLWAVGCIFAELLNGSplFPGEND 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  755 GSVLPR------MTDPKEWPyptiaaeafdpavrdglvaffqkALHR--DAGK-RFPELKPMRdaWRKVFLDASQ 820
Cdd:cd07832  208 IEQLAIvlrtlgTPNEKTWP-----------------------ELTSlpDYNKiTFPESKGIR--LEEIFPDCSP 257
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
529-801 8.43e-10

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 [Multi-domain]  Cd Length: 258  Bit Score: 59.80  E-value: 8.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDLEAETRRtrplAV---LKVALSDSRGEILVREAEAMRRLRpHSGIIRLAE----PEPLH 601
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEY----AVkiiDKKKLKSEDEEMLRREIEILKRLD-HPNIVKLYEvfedDKNLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  602 IggrtvlALEYVgderdddgPGAEG----ATRPRRREETVARQLREhgrlpvdqleaygdyLFGAVDFLEGEGIWHRDIK 677
Cdd:cd05117   76 L------VMELC--------TGGELfdriVKKGSFSEREAAKIMKQ---------------ILSAVAYLHSQGIVHRDLK 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  678 PDNIAVRiRPNRTRELVLIDFSLA-----GYPAKnTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKW 752
Cdd:cd05117  127 PENILLA-SKDPDSPIKIIDFGLAkifeeGEKLK-TVCGTPYYVAP--EVLKGKGYGKKCDIWSLGVILYILLCGYPPFY 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21224924  753 GDG--SVLPRMT------DPKEWpyPTIAAEAFDpavrdglvaFFQKALHRDAGKRF 801
Cdd:cd05117  203 GETeqELFEKILkgkysfDSPEW--KNVSEEAKD---------LIKRLLVVDPKKRL 248
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
529-750 1.05e-09

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 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: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 59.64  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRR--LGTGSTSRAFLVRDLEAETRRTRPLAVLKVALSDSRgEILVREAEAMRRLRpHSGIIRLAEPEplHIGGRT 606
Cdd:cd14202    1 KFEFSRKdlIGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKSQ-TLLGKEIKILKELK-HENIVALYDFQ--EIANSV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  607 VLALEYV--GDerdddgpgaegatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAV- 683
Cdd:cd14202   77 YLVMEYCngGD---------------------LADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLs 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21224924  684 -----RIRPNRTReLVLIDFSLAGYPAKNTDA----GTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14202  136 ysggrKSNPNNIR-IKIADFGFARYLQNNMMAatlcGSPMYMAP--EVIMSQHYDAKADLWSIGTIIYQCLTGKAP 208
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
662-750 1.10e-09

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 [Multi-domain]  Cd Length: 254  Bit Score: 59.52  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGEGIWHRDIKPDNIAVrirpNRTRELVLIDFSLAGY----PAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAV 737
Cdd:cd05122  110 GLEYLHSHGIIHRDIKAANILL----TSDGEVKLIDFGLSAQlsdgKTRNTFVGTPYWMAP--EVIQGKPYGFKADIWSL 183
                         90
                 ....*....|...
gi 21224924  738 AVTLHQMASGELP 750
Cdd:cd05122  184 GITAIEMAEGKPP 196
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
641-807 1.14e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 59.67  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  641 LREHGRLPVDQLEAYGDYLFGAVDFL-EGEGIWHRDIKPDNIAVrirpNRTRELVLIDFSLAGY---PAKNTDAGTDGYL 716
Cdd:cd06605   90 LKEVGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILV----NSRGQVKLCDFGVSGQlvdSLAKTFVGTRSYM 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  717 DPfvDVITRGSYDSHAERYAVAVTLHQMASGELP-----KWGDGSVLPRMTDPKEWPYPTIAAEAFDPAVRDglvaFFQK 791
Cdd:cd06605  166 AP--ERISGGKYTVKSDIWSLGLSLVELATGRFPypppnAKPSMMIFELLSYIVDEPPPLLPSGKFSPDFQD----FVSQ 239
                        170
                 ....*....|....*.
gi 21224924  792 ALHRDAGKRfPELKPM 807
Cdd:cd06605  240 CLQKDPTER-PSYKEL 254
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
210-477 5.68e-09

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 57.27  E-value: 5.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  210 YLARHSDLPEAARVRIYLSERGSDASlrqsVENAARREAAVLGRFKHPGAVQLKQYFPSghAAGPALIFDYHPHTQKLDE 289
Cdd:cd14116   22 YLAREKQSKFILALKVLFKAQLEKAG----VEHQLRREVEIQSHLRHPNILRLYGYFHD--ATRVYLILEYAPLGTVYRE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  290 ylVQYGEKLDILGRMALVRQLAETVRSAHASRIHHRALAARSVLVvprsrGGKGravgeeaawltpQLQISD--WQIATQ 367
Cdd:cd14116   96 --LQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL-----GSAG------------ELKIADfgWSVHAP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  368 RSGDSSqgqgmtrfaptalsamhLADDADaYLAPELTALNPDPVYLDVYGLGVLTYLLVTGKAP--AASQAELLARLEAG 445
Cdd:cd14116  157 SSRRTT-----------------LCGTLD-YLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPfeANTYQETYKRISRV 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 21224924  446 EGLRPsslvDGLSEDVDELVQAATAYRPGQRL 477
Cdd:cd14116  219 EFTFP----DFVTEGARDLISRLLKHNPSQRP 246
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
529-750 6.41e-09

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 57.16  E-value: 6.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVrdleaETRRTRPLAVLKVALSDSRG-EILVREAEAMRRLRpHSGIIRLAE----PEPLHIg 603
Cdd:cd14087    2 KYDIKALIGRGSFSRVVRV-----EHRVTRQPYAIKMIETKCRGrEVCESELNVLRRVR-HTNIIQLIEvfetKERVYM- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 grtVLALEYVGDERDddgpgaEGATRPRRREETVARQLRehgrlpvdqleaygdYLFGAVDFLEGEGIWHRDIKPDNIaV 683
Cdd:cd14087   75 ---VMELATGGELFD------RIIAKGSFTERDATRVLQ---------------MVLDGVKYLHGLGITHRDLKPENL-L 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21224924  684 RIRPNRTRELVLIDFSLAGYPAKN------TDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14087  130 YYHPGPDSKIMITDFGLASTRKKGpnclmkTTCGTPEYIAP--EILLRKPYTQSVDMWAVGVIAYILLSGTMP 200
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
528-811 1.46e-08

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 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: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 56.34  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  528 GRWEVRRRLGTGSTSRAFLVRDLEAETRRTRPLAVLKVALSDSRGEI-----LVREAEAMRRLRpHSGIIRLAEPEPL-- 600
Cdd:cd14076    1 GPYILGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDTQQENcqtskIMREINILKGLT-HPNIVRLLDVLKTkk 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  601 HIGgrtvLALEYVGDerdddGPGAEGATRPRRREETVARQLREHgrlpvdqleaygdyLFGAVDFLEGEGIWHRDIKPDN 680
Cdd:cd14076   80 YIG----IVLEFVSG-----GELFDYILARRRLKDSVACRLFAQ--------------LISGVAYLHKKGVVHRDLKLEN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  681 IAVrirpNRTRELVLIDFSLAG--YPAKN----TDAGTDGYLDPFVDVITRGSYDSHAERYAVAVTLHQMASGELPkWGD 754
Cdd:cd14076  137 LLL----DKNRNLVITDFGFANtfDHFNGdlmsTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLP-FDD 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21224924  755 GSVLPRMTD-PKEWPY----PTIAAEAFDPAVRDGLvaffQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14076  212 DPHNPNGDNvPRLYRYicntPLIFPEYVTPKARDLL----RRILVPNPRKRIRLSAIMRHAW 269
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
662-787 1.74e-08

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 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: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 56.33  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGEGIWHRDIKPDNIAVrirpNRTRELVLIDFSLAGYPAKN-----TDAGTDGYLDPfvDVITRG-SYDSHAERY 735
Cdd:cd06917  113 ALKFIHKDGIIHRDIKAANILV----TNTGNVKLCDFGVAASLNQNsskrsTFVGTPYWMAP--EVITEGkYYDTKADIW 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21224924  736 AVAVTLHQMASGELPKWGDGSVLPRMTDPKEWPyPTIAAEAFDPAVRDGLVA 787
Cdd:cd06917  187 SLGITTYEMATGNPPYSDVDALRAVMLIPKSKP-PRLEGNGYSPLLKEFVAA 237
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
238-481 1.76e-08

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 56.19  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  238 QSVENAARREAAVLGRFKHPGAVQL-------KQYFPSGHAAGPALIFDYhphtqKLDEYLvqYGEKldilGRMALVRQL 310
Cdd:cd14088   40 RKVRKAAKNEINILKMVKHPNILQLvdvfetrKEYFIFLELATGREVFDW-----ILDQGY--YSER----DTSNVIRQV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  311 AETVRSAHASRIHHRALAARSVLVVPRSRGGKgravgeeaawltpqLQISDWQIATQRSGDSSQGQGMTRfaptalsamh 390
Cdd:cd14088  109 LEAVAYLHSLKIVHRNLKLENLVYYNRLKNSK--------------IVISDFHLAKLENGLIKEPCGTPE---------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  391 laddadaYLAPELTALNPDPVYLDVYGLGVLTYLLVTGKAPAASQAE----------LLARLEAGEGLRPSSLVDGLSED 460
Cdd:cd14088  165 -------YLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyenhdknLFRKILAGDYEFDSPYWDDISQA 237
                        250       260
                 ....*....|....*....|.
gi 21224924  461 VDELVQAATAYRPGQRLSSVD 481
Cdd:cd14088  238 AKDLVTRLMEVEQDQRITAEE 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
246-478 1.83e-08

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 55.94  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  246 REAAVLGRFKHPGAVQLKQYF--PSGHAagpaLIFDYHPHTQKLDeYLVQYGEKLDILGRmALVRQLAETVRSAHASRIH 323
Cdd:cd14098   50 REINILKSLEHPGIVRLIDWYedDQHIY----LVMEYVEGGDLMD-FIMAWGAIPEQHAR-ELTKQILEAMAYTHSMGIT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  324 HRALAARSVLVVprsrggkgravgEEAAWLtpqLQISDWQIATQRSGDSsqgqgmtrFAPTALSAMhladdadAYLAPEL 403
Cdd:cd14098  124 HRDLKPENILIT------------QDDPVI---VKISDFGLAKVIHTGT--------FLVTFCGTM-------AYLAPEI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  404 ---TALNPDPVY---LDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGEGLRPSSLVDGLSEDVDELVQAATAYRPGQ 475
Cdd:cd14098  174 lmsKEQNLQGGYsnlVDMWSVGCLVYVMLTGALPfdGSSQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEK 253

                 ...
gi 21224924  476 RLS 478
Cdd:cd14098  254 RMT 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
529-800 1.96e-08

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 [Multi-domain]  Cd Length: 258  Bit Score: 55.99  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLvrdleAETRRT-RPLAVLKVALSDSRGEI---LVREAEAMRRLRpHSGIIRlaepeplhigg 604
Cdd:cd06606    1 RWKKGELLGKGSFGSVYL-----ALNLDTgELMAVKEVELSGDSEEEleaLEREIRILSSLK-HPNIVR----------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  605 rtvlaleYVGDERDDDG--------PGaeGatrprrreeTVARQLREHGRLPVDQLEAY-GDYLFGaVDFLEGEGIWHRD 675
Cdd:cd06606   64 -------YLGTERTENTlnifleyvPG--G---------SLASLLKKFGKLPEPVVRKYtRQILEG-LEYLHSNGIVHRD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  676 IKPDNIAVrirpNRTRELVLIDF-------SLAGYPAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGE 748
Cdd:cd06606  125 IKGANILV----DSDGVVKLADFgcakrlaEIATGEGTKSLRGTPYWMAP--EVIRGEGYGRAADIWSLGCTVIEMATGK 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21224924  749 LPkWGD----GSVLPRMTDPKEWPY--PTIAAEAFDpavrdglvaFFQKALHRDAGKR 800
Cdd:cd06606  199 PP-WSElgnpVAALFKIGSSGEPPPipEHLSEEAKD---------FLRKCLQRDPKKR 246
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
529-804 2.04e-08

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 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: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 55.72  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFlvrdlEAETRRTRPLAVLKVALSDSRGEI----LVREAEAMRRLRpHSGIIRLAE----PEPL 600
Cdd:cd14002    2 NYHVLELIGEGSFGKVY-----KGRRKYTGQVVALKFIPKRGKSEKelrnLRQEIEILRKLN-HPNIIEMLDsfetKKEF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  601 higgrtVLALEYvgderdddgpgAEGatrprrreeTVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDN 680
Cdd:cd14002   76 ------VVVTEY-----------AQG---------ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  681 IAVrirpNRTRELVLIDFSLAGYPAKNTDA-----GTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDG 755
Cdd:cd14002  130 ILI----GKGGVVKLCDFGFARAMSCNTLVltsikGTPLYMAP--ELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNS 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21224924  756 SV-LPRMT--DPKEWPyptiaaEAFDPAVRDglvaFFQKALHRDAGKR--FPEL 804
Cdd:cd14002  204 IYqLVQMIvkDPVKWP------SNMSPEFKS----FLQGLLNKDPSKRlsWPDL 247
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
673-807 2.15e-08

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 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: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 55.89  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  673 HRDIKPDNIAVrirpNRTRELVLIDFSLAGY----PAKNTDAGTDGYLDP-FVDVITRGS-YDSHAERYAVAVTLHQMAS 746
Cdd:cd06617  127 HRDVKPSNVLI----NRNGQVKLCDFGISGYlvdsVAKTIDAGCKPYMAPeRINPELNQKgYDVKSDVWSLGITMIELAT 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  747 GELP--KWGDgsVLPRMTDPKEWPYPTIAAEAFDPAVRDglvaFFQKALHRDAGKR--FPELKPM 807
Cdd:cd06617  203 GRFPydSWKT--PFQQLKQVVEEPSPQLPAEKFSPEFQD----FVNKCLKKNYKERpnYPELLQH 261
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
531-806 2.52e-08

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-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: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 56.05  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  531 EVRRRLGTGSTSRAFLVRdleaeTRRTRPLAVLKVAlsdSRGEIL--------VREAEAMRRLRpHSGIIRLaepeplhI 602
Cdd:cd05580    4 EFLKTLGTGSFGRVRLVK-----HKDSGKYYALKIL---KKAKIIklkqvehvLNEKRILSEVR-HPFIVNL-------L 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  603 GG-----RTVLALEYVgderdddgPGAEGATRprrreetvarqLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIK 677
Cdd:cd05580   68 GSfqddrNLYMVMEYV--------PGGELFSL-----------LRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  678 PDNIAVRirpnRTRELVLIDFSLAGYPAKNTDA--GTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDG 755
Cdd:cd05580  129 PENLLLD----SDGHIKITDFGFAKRVKDRTYTlcGTPEYLAP--EIILSKGHGKAVDWWALGILIYEMLAGYPPFFDEN 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21224924  756 svlPRMTDPKewpypTIAAEA-----FDPAVRDGLvaffQKALHRDAGKRFPELKP 806
Cdd:cd05580  203 ---PMKIYEK-----ILEGKIrfpsfFDPDAKDLI----KRLLVVDLTKRLGNLKN 246
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
573-748 7.09e-08

Catalytic domain of Cyclin-Dependent protein 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 of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL 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: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 54.63  E-value: 7.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  573 EILVREAEAMRRLRpHSGIIRLAEPepLHIGGRTVLALEYVgderdddgpgaegatrprrrEETVARQLREH-GRLPVDQ 651
Cdd:cd07833   45 KTALREVKVLRQLR-HENIVNLKEA--FRRKGRLYLVFEYV--------------------ERTLLELLEASpGGLPPDA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  652 LEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirpNRTRELVLIDFSLAGYPAKNTDAGTDGYldpfvdVITR------ 725
Cdd:cd07833  102 VRSYIWQLLQAIAYCHSHNIIHRDIKPENILV----SESGVLKLCDFGFARALTARPASPLTDY------VATRwyrape 171
                        170       180
                 ....*....|....*....|....*...
gi 21224924  726 -----GSYDSHAERYAVAVTLHQMASGE 748
Cdd:cd07833  172 llvgdTNYGKPVDVWAIGCIMAELLDGE 199
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
230-478 7.30e-08

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 54.61  E-value: 7.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  230 RGSDASLRQSVENaarrEAAVLGRFKHPGAVQLKQYFPSGHaagpalifDYHPHTQkldeyLVQYGEKLD-ILGR----- 303
Cdd:cd14166   37 KKSPLSRDSSLEN----EIAVLKRIKHENIVTLEDIYESTT--------HYYLVMQ-----LVSGGELFDrILERgvyte 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  304 ---MALVRQLAETVRSAHASRIHHRALAARSVLvvprsrggkgravgeeaaWLTP----QLQISDWqiatqrsgdssqgq 376
Cdd:cd14166  100 kdaSRVINQVLSAVKYLHENGIVHRDLKPENLL------------------YLTPdensKIMITDF-------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  377 GMTRFAPTALsaMHLADDADAYLAPELTALNPDPVYLDVYGLGVLTYLLVTGKAPAASQAE--LLARLEAGEGLRPSSLV 454
Cdd:cd14166  148 GLSKMEQNGI--MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETEsrLFEKIKEGYYEFESPFW 225
                        250       260
                 ....*....|....*....|....
gi 21224924  455 DGLSEDVDELVQAATAYRPGQRLS 478
Cdd:cd14166  226 DDISESAKDFIRHLLEKNPSKRYT 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
536-750 8.41e-08

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 53.77  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  536 LGTGSTSRAFLvrdleAETRRTRPLAVLKV----ALSDSRGEILVREAEAMRRLRpHSGIIRLAE--PEPLHIggrtVLA 609
Cdd:cd14009    1 IGRGSFATVWK-----GRHKQTGEVVAIKEisrkKLNKKLQENLESEIAILKSIK-HPNIVRLYDvqKTEDFI----YLV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  610 LEYV--GDerdddgpgaegatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIRP 687
Cdd:cd14009   71 LEYCagGD---------------------LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSG 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21224924  688 NRTrELVLIDFSLAGYPAKNTDA----GTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14009  130 DDP-VLKIADFGFARSLQPASMAetlcGSPLYMAP--EILQFQKYDAKADLWSVGAILFEMLVGKPP 193
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
662-804 8.91e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 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: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 54.30  E-value: 8.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFL-EGEGIWHRDIKPDNIAVRIRPNrtreLVLIDFSLAGY----PAKNTDAGTDGYLDP-FVDVITRGSYDSHAERY 735
Cdd:cd06618  126 ALHYLkEKHGVIHRDVKPSNILLDESGN----VKLCDFGISGRlvdsKAKTRSAGCAAYMAPeRIDPPDNPKYDIRADVW 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21224924  736 AVAVTLHQMASGELPKWG---DGSVLPRM--TDPKEWPYptiaAEAFDPAVRDglvaFFQKALHRDAGKR--FPEL 804
Cdd:cd06618  202 SLGISLVELATGQFPYRNcktEFEVLTKIlnEEPPSLPP----NEGFSPDFCS----FVDLCLTKDHRYRpkYREL 269
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
529-789 1.07e-07

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 53.54  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRD-----LEAETRRTRPLAvlkvalSDSRGEILVREAEAMRRLRPHSGIIRL----AEPEP 599
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSkvdgcLYAVKKSKKPFR------GPKERARALREVEAHAALGQHPNIVRYysswEEGGH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  600 LHIggrtvlALEYVGDERDDDGPGAEGATRpRRREETVARQLREHGRlpvdqleaygdylfgAVDFLEGEGIWHRDIKPD 679
Cdd:cd13997   75 LYI------QMELCENGSLQDALEELSPIS-KLSEAEVWDLLLQVAL---------------GLAFIHSKGIVHLDIKPD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  680 NIAVRIRPNrtreLVLIDFSLAGYPAKNTD--AGTDGYLDPFVdVITRGSYDSHAERYAVAVTLHQMASG-ELPKWGDGS 756
Cdd:cd13997  133 NIFISNKGT----CKIGDFGLATRLETSGDveEGDSRYLAPEL-LNENYTHLPKADIFSLGVTVYEAATGePLPRNGQQW 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 21224924  757 VLPRMTDPKEWPYPTIAAE---------AFDPAVR---DGLVAFF 789
Cdd:cd13997  208 QQLRQGKLPLPPGLVLSQEltrllkvmlDPDPTRRptaDQLLAHD 252
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
247-431 1.49e-07

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio 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: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 53.44  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  247 EAAVLGRFKHPGAVQLKQYFPSghAAGPALIFDYHPHTQKLDeYLVQYGEKLDilGRMAL-VRQLAETVRSAHASRIHHR 325
Cdd:cd14113   53 ELGVLQSLQHPQLVGLLDTFET--PTSYILVLEMADQGRLLD-YVVRWGNLTE--EKIRFyLREILEALQYLHNCRIAHL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  326 ALAARSVLVvprsrggkgravgeEAAWLTPQLQISDWqiatqrsGDSSQgQGMTRFAPTALSAMHLAddadaylAPELTA 405
Cdd:cd14113  128 DLKPENILV--------------DQSLSKPTIKLADF-------GDAVQ-LNTTYYIHQLLGSPEFA-------APEIIL 178
                        170       180
                 ....*....|....*....|....*.
gi 21224924  406 LNPDPVYLDVYGLGVLTYLLVTGKAP 431
Cdd:cd14113  179 GNPVSLTSDLWSIGVLTYVLLSGVSP 204
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
662-811 1.85e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 53.11  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGEGIWHRDIKPDNIAVRiRPNRTRELVLIDFSLAG------------YPAKNTDAGTDGYLDP-FVDVITRGS- 727
Cdd:cd14174  112 ALDFLHTKGIAHRDLKPENILCE-SPDKVSPVKICDFDLGSgvklnsactpitTPELTTPCGSAEYMAPeVVEVFTDEAt 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  728 -YDSHAERYAVAVTLHQMASGELP---------KWGDGSV--------LPRMTDPK-EWP---YPTIAAEAFDpavrdgl 785
Cdd:cd14174  191 fYDKRCDLWSLGVILYIMLSGYPPfvghcgtdcGWDRGEVcrvcqnklFESIQEGKyEFPdkdWSHISSEAKD------- 263
                        170       180
                 ....*....|....*....|....*.
gi 21224924  786 vaFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14174  264 --LISKLLVRDAKERLSAAQVLQHPW 287
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
577-698 2.02e-07

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK 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: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 53.04  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  577 REAEAMRRLRPHSGIIRLAEP--EPLHigGRTVLALEYVgderddDGPGAEgATRPRRR---EETVARQLREhgrlpvdq 651
Cdd:cd07831   46 REIQALRRLSPHPNILRLIEVlfDRKT--GRLALVFELM------DMNLYE-LIKGRKRplpEKRVKNYMYQ-------- 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 21224924  652 leaygdyLFGAVDFLEGEGIWHRDIKPDNIAVRIrpnrtRELVLIDF 698
Cdd:cd07831  109 -------LLKSLDHMHRNGIFHRDIKPENILIKD-----DILKLADF 143
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
534-760 3.02e-07

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-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: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 52.17  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  534 RRLGTGSTSRaflVRdLEAETRRTRPLAVLKV----ALSDSRGEILVREAEAMRRLRpHSGIIRLAEPEPLhIGGRTVLA 609
Cdd:cd14164    6 TTIGEGSFSK---VK-LATSQKYCCKVAIKIVdrrrASPDFVQKFLPRELSILRRVN-HPNIVQMFECIEV-ANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  610 LEYVgderdddgpgaegatrprrrEETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIRPNR 689
Cdd:cd14164   80 MEAA--------------------ATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21224924  690 TRelvLIDFSLA----GYPA-KNTDAGTDGYLDPfvDVITRGSYDSHA-ERYAVAVTLHQMASGELPKWGDGSVLPR 760
Cdd:cd14164  140 IK---IADFGFArfveDYPElSTTFCGSRAYTPP--EVILGTPYDPKKyDVWSLGVVLYVMVTGTMPFDETNVRRLR 211
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
647-811 3.17e-07

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 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: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 52.33  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  647 LPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIRPNrtreLVLIDFSLAG-YPAKNTD------AGTDGYLDPf 719
Cdd:cd14069   97 MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN----LKISDFGLATvFRYKGKErllnkmCGTLPYVAP- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  720 vDVITRGSYdsHAER---YAVAVTLHQMASGELPkW-----GDGSVLPRMTD--PKEWPYPTIAAEAfdpavrdglVAFF 789
Cdd:cd14069  172 -ELLAKKKY--RAEPvdvWSCGIVLFAMLAGELP-WdqpsdSCQEYSDWKENkkTYLTPWKKIDTAA---------LSLL 238
                        170       180
                 ....*....|....*....|....
gi 21224924  790 QKALHRDAGKR--FPELKpmRDAW 811
Cdd:cd14069  239 RKILTENPNKRitIEDIK--KHPW 260
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
531-750 3.17e-07

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


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 52.09  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  531 EVRRRLGTGSTSRAFLVRDleaetRRTRPLAVLKV----ALSDSRGE-ILVREAEAMRRLRpHSGIIRLaepeplhIG-- 603
Cdd:cd14007    3 EIGKPLGKGKFGNVYLARE-----KKSGFIVALKVisksQLQKSGLEhQLRREIEIQSHLR-HPNILRL-------YGyf 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 ---GRTVLALEYVgderdddgPGAEgatrprrreetVARQLREHGRLpvDQLEAYgDYLF---GAVDFLEGEGIWHRDIK 677
Cdd:cd14007   70 edkKRIYLILEYA--------PNGE-----------LYKELKKQKRF--DEKEAA-KYIYqlaLALDYLHSKNIIHRDIK 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21224924  678 PDNIAVrirpNRTRELVLIDFSLAGY-PAK--NTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14007  128 PENILL----GSNGELKLADFGWSVHaPSNrrKTFCGTLDYLPP--EMVEGKEYDYKVDIWSLGVLCYELLVGKPP 197
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
662-811 3.28e-07

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 52.31  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGEGIWHRDIKPDNIAVrirpnrTRELVL--IDFSLA---GYPAKNTD------AGTDGYLDPfvDVITRGSYDS 730
Cdd:cd13994  110 GVAYLHSHGIAHRDLKPENILL------DEDGVLklTDFGTAevfGMPAEKESpmsaglCGSEPYMAP--EVFTSGSYDG 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  731 HA-ERYAVAVTLHQMASGELP----KWGDGSVLPRMTDPKEWPYPTIAAEAFDPAvrdGLVAFFQKALHRDAGKRFPELK 805
Cdd:cd13994  182 RAvDVWSCGIVLFALFTGRFPwrsaKKSDSAYKAYEKSGDFTNGPYEPIENLLPS---ECRRLIYRMLHPDPEKRITIDE 258

                 ....*.
gi 21224924  806 PMRDAW 811
Cdd:cd13994  259 ALNDPW 264
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
526-701 4.32e-07

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 52.47  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  526 LAGRWEVRRRLGTGSTSRAFLVRDLEAETRrtrpLAVLKVALSDSRG-EILVREAEAMRRLRpHSGIIRLAE-------P 597
Cdd:cd07854    3 LGSRYMDLRPLGCGSNGLVFSAVDSDCDKR----VAVKKIVLTDPQSvKHALREIKIIRRLD-HDNIVKVYEvlgpsgsD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  598 EPLHIGGRTVLALEYVGDERdddgpgaegatrprrrEETVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIK 677
Cdd:cd07854   78 LTEDVGSLTELNSVYIVQEY----------------METDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLK 141
                        170       180
                 ....*....|....*....|....*.
gi 21224924  678 PDNIAVrirpnRTRELVLI--DFSLA 701
Cdd:cd07854  142 PANVFI-----NTEDLVLKigDFGLA 162
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
530-750 4.50e-07

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 51.88  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLVRdlEAETRRTRPLAVL-KVALSDSRGE-ILVREAEAMRRLRpHSGIIRLAEPepLHIGGRTV 607
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAR--EKQSKFILALKVLfKAQLEKAGVEhQLRREVEIQSHLR-HPNILRLYGY--FHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  608 LALEYvgderdddGPGAEgatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirp 687
Cdd:cd14116   82 LILEY--------APLGT-----------VYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL---- 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21224924  688 NRTRELVLIDFSLAGY-PA--KNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14116  139 GSAGELKIADFGWSVHaPSsrRTTLCGTLDYLPP--EMIEGRMHDEKVDLWSLGVLCYEFLVGKPP 202
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
241-478 4.83e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 51.57  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  241 ENAARREAAVLGRFKHPGAVQLKQYFPSGhaAGPALIFDYHPHTQKLDEYLVQ--YGEKldilGRMALVRQLAETVRSAH 318
Cdd:cd14167   45 ETSIENEIAVLHKIKHPNIVALDDIYESG--GHLYLIMQLVSGGELFDRIVEKgfYTER----DASKLIFQILDAVKYLH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  319 ASRIHHRALAARSVLVVprsrggkgrAVGEEAawltpQLQISDWQIAtqrsgdSSQGQGmtrfaptalSAMHLADDADAY 398
Cdd:cd14167  119 DMGIVHRDLKPENLLYY---------SLDEDS-----KIMISDFGLS------KIEGSG---------SVMSTACGTPGY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  399 LAPELTALNPDPVYLDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGEGLRPSSLVDGLSEDVDELVQAATAYRPGQR 476
Cdd:cd14167  170 VAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPfyDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKR 249

                 ..
gi 21224924  477 LS 478
Cdd:cd14167  250 FT 251
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
637-791 4.87e-07

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 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: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 51.93  E-value: 4.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  637 VARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIRPNRTRELVLI-----DFSLAGYPAKN---- 707
Cdd:cd14201   92 LADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVSGIrikiaDFGFARYLQSNmmaa 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  708 TDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDGSVLPRMTDPKEWPY-PTIAAEAfDPAVRDGLV 786
Cdd:cd14201  172 TLCGSPMYMAP--EVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLqPSIPRET-SPYLADLLL 248

                 ....*
gi 21224924  787 AFFQK 791
Cdd:cd14201  249 GLLQR 253
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
246-473 5.67e-07

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-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: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 51.40  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  246 REAAVLGRFKHPGAVQLKQYFpsgHAAGPALIFDYHPHTQKLDEYLVQYGEKLDILGRMALVrQLAETVRSAHASRIHHR 325
Cdd:cd14164   49 RELSILRRVNHPNIVQMFECI---EVANGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMFA-QMVGAVNYLHDMNIVHR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  326 ALAARSVLVVPRSRggkgravgeeaawltpQLQISDWQIATQRSGdssqgqgmtrfaPTALSamHLADDADAYLAPELTA 405
Cdd:cd14164  125 DLKCENILLSADDR----------------KIKIADFGFARFVED------------YPELS--TTFCGSRAYTPPEVIL 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21224924  406 LNP-DPVYLDVYGLGVLTYLLVTGKAPAASQAELLARLEAGEGLRPSSLvdGLSED----VDELVQAATAYRP 473
Cdd:cd14164  175 GTPyDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGV--ALEEPcralIRTLLQFNPSTRP 245
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
662-811 6.43e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 51.57  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGEGIWHRDIKPDNIAVRiRPNRTRELVLIDFSLAGYPAKNTDA------------GTDGYLDP-FVDVITRGS- 727
Cdd:cd14173  112 ALDFLHNKGIAHRDLKPENILCE-HPNQVSPVKICDFDLGSGIKLNSDCspistpelltpcGSAEYMAPeVVEAFNEEAs 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  728 -YDSHAERYAVAVTLHQMASGELP-----------KWGDG-----SVLPRMTDPKEWPYPTIAAEAFDPAVRDglvaFFQ 790
Cdd:cd14173  191 iYDKRCDLWSLGVILYIMLSGYPPfvgrcgsdcgwDRGEAcpacqNMLFESIQEGKYEFPEKDWAHISCAAKD----LIS 266
                        170       180
                 ....*....|....*....|.
gi 21224924  791 KALHRDAGKRFPELKPMRDAW 811
Cdd:cd14173  267 KLLVRDAKQRLSAAQVLQHPW 287
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
530-811 6.57e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 51.43  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLvrdleAETRRTRPLAVLKVALSDS-RG-EILVREAEAMRRLRPHSGIIRLAE--PEPLHIggr 605
Cdd:cd14169    5 YELKEKLGEGAFSEVVL-----AQERGSQRLVALKCIPKKAlRGkEAMVENEIAVLRRINHENIVSLEDiyESPTHL--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  606 tVLALEYVgderdddgPGAEGATRPRRR----EETVARQLREhgrlpvdqleaygdyLFGAVDFLEGEGIWHRDIKPDNI 681
Cdd:cd14169   77 -YLAMELV--------TGGELFDRIIERgsytEKDASQLIGQ---------------VLQAVKYLHQLGIVHRDLKPENL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  682 aVRIRPNRTRELVLIDFSLAGYPAKN---TDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDgsvl 758
Cdd:cd14169  133 -LYATPFEDSKIMISDFGLSKIEAQGmlsTACGTPGYVAP--ELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDE---- 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21224924  759 prmTDPKEWPYPTIAAEAFDPA----VRDGLVAFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14169  206 ---NDSELFNQILKAEYEFDSPywddISESAKDFIRHLLERDPEKRFTCEQALQHPW 259
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
241-465 6.81e-07

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 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: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 51.19  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  241 ENAARREAAVLGRFKHPGAVQLKQYFPSghaagPALIFdyhphtqkLDEYLVQYGEKLDILGRM---------ALVRQLA 311
Cdd:cd14184   43 EHLIENEVSILRRVKHPNIIMLIEEMDT-----PAELY--------LVMELVKGGDLFDAITSStkyterdasAMVYNLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  312 ETVRSAHASRIHHRALAARSVLVVPRSRGgkgravgeeaawlTPQLQISDWQIATQRSGDSSQGQGmtrfAPTalsamhl 391
Cdd:cd14184  110 SALKYLHGLCIVHRDIKPENLLVCEYPDG-------------TKSLKLGDFGLATVVEGPLYTVCG----TPT------- 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21224924  392 addadaYLAPELTALNPDPVYLDVYGLGVLTYLLVTGKAPAAS----QAELLARLEAGEGLRPSSLVDGLSEDVDELV 465
Cdd:cd14184  166 ------YVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSennlQEDLFDQILLGKLEFPSPYWDNITDSAKELI 237
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
240-481 6.96e-07

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 51.17  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  240 VENaarrEAAVLGRFKHPGAVQL-KQYFPSGHaagpalIFdyhphtqkLDEYLVQYGEKLDILG-------RMA--LVRQ 309
Cdd:cd14095   45 IEN----EVAILRRVKHPNIVQLiEEYDTDTE------LY--------LVMELVKGGDLFDAITsstkfteRDAsrMVTD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  310 LAETVRSAHASRIHHRALAARSVLVVPRSRGGKGravgeeaawltpqLQISDWQIATQRSGDSSQGQGmtrfAPTalsam 389
Cdd:cd14095  107 LAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKS-------------LKLADFGLATEVKEPLFTVCG----TPT----- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  390 hladdadaYLAPELTALNPDPVYLDVYGLGVLTYLLVTG----KAPAASQAELLARLEAGEGLRPSSLVDGLSEDVDELV 465
Cdd:cd14095  165 --------YVAPEILAETGYGLKVDIWAAGVITYILLCGfppfRSPDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                        250
                 ....*....|....*.
gi 21224924  466 QAATAYRPGQRLSSVD 481
Cdd:cd14095  237 SRMLVVDPEKRYSAGQ 252
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
246-479 7.53e-07

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; 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. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. 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. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 51.27  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  246 REAAVLGRFKHPGAVQLKQYFPSGHAAgpALIFDyhphtqkldeyLVQYGEKL-DILGR--------MALVRQLAETVRS 316
Cdd:cd14086   49 REARICRLLKHPNIVRLHDSISEEGFH--YLVFD-----------LVTGGELFeDIVARefyseadaSHCIQQILESVNH 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  317 AHASRIHHRALAARSVLVVPRSRGgkgravgeeAAwltpqLQISDWQIATQRSGDSSQGQGmtrFAPTAlsamhladdad 396
Cdd:cd14086  116 CHQNGIVHRDLKPENLLLASKSKG---------AA-----VKLADFGLAIEVQGDQQAWFG---FAGTP----------- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  397 AYLAPELTALNPDPVYLDVYGLGVLTYLLVTGKAP--AASQAELLARLEAGEGLRPSSLVDGLSEDVDELVQAATAYRPG 474
Cdd:cd14086  168 GYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPfwDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVNPA 247

                 ....*
gi 21224924  475 QRLSS 479
Cdd:cd14086  248 KRITA 252
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
666-800 8.08e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK 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: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 51.37  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  666 LEGEGIWHRDIKPDNIAVRIRPN-RTRELVL-IDFSlAGYPAKNTdAGTDGYLDPFVdVITRGSYDSHAERYAVAVTLHQ 743
Cdd:cd05577  111 LHNRFIVYRDLKPENILLDDHGHvRISDLGLaVEFK-GGKKIKGR-VGTHGYMAPEV-LQKEVAYDFSVDWFALGCMLYE 187
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21224924  744 MASGELP-----KWGDGSVLPRMTDPKEWPYPtiaaEAFDPAVRDGLVAFFQKALHRDAGKR 800
Cdd:cd05577  188 MIAGRSPfrqrkEKVDKEELKRRTLEMAVEYP----DSFSPEARSLCEGLLQKDPERRLGCR 245
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
662-752 9.14e-07

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 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: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 51.21  E-value: 9.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  662 AVDFLEGE-GIWHRDIKPDNIAVrirpNRTRELVLIDFSLAGY----PAKNTDAGTDGY-----LDPFVdviTRGSYDSH 731
Cdd:cd06616  121 ALNYLKEElKIIHRDVKPSNILL----DRNGNIKLCDFGISGQlvdsIAKTRDAGCRPYmaperIDPSA---SRDGYDVR 193
                         90       100
                 ....*....|....*....|...
gi 21224924  732 AERYAVAVTLHQMASGELP--KW 752
Cdd:cd06616  194 SDVWSLGITLYEVATGKFPypKW 216
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
237-485 1.03e-06

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 50.34  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  237 RQSVENAARREAAVLGRFKHPGAVQLKQYFPSghaaGPALIFdyhphtqkLDEyLVQYGEKLDILGR---------MALV 307
Cdd:cd14006   29 RDKKKEAVLREISILNQLQHPRIIQLHEAYES----PTELVL--------ILE-LCSGGELLDRLAErgslseeevRTYM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  308 RQLAETVRSAHASRIHHRALAARSVLVVPRSRggkgravgeeaawltPQLQISDWQIATQRSGDSSQGQGMtrfaptals 387
Cdd:cd14006   96 RQLLEGLQYLHNHHILHLDLKPENILLADRPS---------------PQIKIIDFGLARKLNPGEELKEIF--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  388 amhladDADAYLAPELtaLNPDPVYL--DVYGLGVLTYLLVTGKAP--AASQAELLARLEAGEgLRPSSLV-DGLSED-- 460
Cdd:cd14006  152 ------GTPEFVAPEI--VNGEPVSLatDMWSIGVLTYVLLSGLSPflGEDDQETLANISACR-VDFSEEYfSSVSQEak 222
                        250       260
                 ....*....|....*....|....*..
gi 21224924  461 --VDELVQAATAYRPgqrlsSVDEFLE 485
Cdd:cd14006  223 dfIRKLLVKEPRKRP-----TAQEALQ 244
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
663-811 1.21e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 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: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 50.78  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  663 VDFLEGEGIWHRDIKPDNIAVRIRPNRTRELVLIDFSLAG-YPAKNTDAGTDGYLDPFV--DVITRGSYDSHAERYAVAV 739
Cdd:cd14178  110 VEYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKqLRAENGLLMTPCYTANFVapEVLKRQGYDAACDIWSLGI 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21224924  740 TLHQMASGELPkWGDG------SVLPRMTDPKEwpypTIAAEAFDpAVRDGLVAFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14178  190 LLYTMLAGFTP-FANGpddtpeEILARIGSGKY----ALSGGNWD-SISDAAKDIVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
536-754 1.21e-06

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 [Multi-domain]  Cd Length: 255  Bit Score: 50.33  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  536 LGTGSTSRAFLVRDLEAETRRtrplAVLKVALSDSR----GEILV-REAEAMRRLRpHSGIIRLAEPEPLHIGGRTVLAL 610
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRR----AVKILKKRKLRripnGEANVkREIQILRRLN-HRNVIKLVDVLYNEEKQKLYMVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  611 EY-VGDERD--DDGPGAegatrprrreetvarqlrehgRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIavrirp 687
Cdd:cd14119   76 EYcVGGLQEmlDSAPDK---------------------RLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNL------ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  688 nrtreLVLIDFSLagypaKNTDAGTDGYLDPFV--DVITRgSYDSHA------------------ERYAVAVTLHQMASG 747
Cdd:cd14119  129 -----LLTTDGTL-----KISDFGVAEALDLFAedDTCTT-SQGSPAfqppeiangqdsfsgfkvDIWSAGVTLYNMTTG 197

                 ....*..
gi 21224924  748 ELPKWGD 754
Cdd:cd14119  198 KYPFEGD 204
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
210-483 1.23e-06

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 50.30  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  210 YLARHSDLPEAARVRIYLSERGSDAsLRQSVENaarrEAAVLGRFKHPGAVQLKqyfpsghaagpalifdyhpHTQKLDE 289
Cdd:cd14009   10 WKGRHKQTGEVVAIKEISRKKLNKK-LQENLES----EIAILKSIKHPNIVRLY-------------------DVQKTED 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  290 --YLV----------QYGEKLDILGRMA---LVRQLAETVRSAHASRIHHRALAARSVLVVPRSrggkgravgeeaawLT 354
Cdd:cd14009   66 fiYLVleycaggdlsQYIRKRGRLPEAVarhFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSG--------------DD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  355 PQLQISDWqiatqrsgdssqgqGMTRFaptalsaMHLADDADA------YLAPELTALNPDPVYLDVYGLGVLTYLLVTG 428
Cdd:cd14009  132 PVLKIADF--------------GFARS-------LQPASMAETlcgsplYMAPEILQFQKYDAKADLWSVGAILFEMLVG 190
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21224924  429 KAP--AASQAELLARLEAGEGLRPSSLVDGLSEDVDELVQAATAYRPGQRLsSVDEF 483
Cdd:cd14009  191 KPPfrGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAERI-SFEEF 246
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
244-450 1.30e-06

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK 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: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 50.69  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  244 ARREAAVLGRFKHPGAVQLkqyfpSGHAAGP-ALIFDYHPHTQkLDEYLVQYGEKLDILGRM---ALVRQLAETVRSAHA 319
Cdd:cd14000   57 LRQELTVLSHLHHPSIVYL-----LGIGIHPlMLVLELAPLGS-LDHLLQQDSRSFASLGRTlqqRIALQVADGLRYLHS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  320 SRIHHRALAARSVLVvprsrggkgravgeeaaWLTPQ-----LQISDWQIATQRSGDSSQGQGMTrfaptalsamhladd 394
Cdd:cd14000  131 AMIIYRDLKSHNVLV-----------------WTLYPnsaiiIKIADYGISRQCCRMGAKGSEGT--------------- 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21224924  395 aDAYLAPELTALNPdpVY---LDVYGLGVLTYLLVTGKAPAASQAELLARLEAGEGLRP 450
Cdd:cd14000  179 -PGFRAPEIARGNV--IYnekVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGLRP 234
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
534-801 1.39e-06

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 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: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 50.29  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  534 RRLGTGSTSRAFLVRDLEaeTRRTRPLAVL-KVALSDSRGEILV-REAEAMRRLRpHSGIIRLA----EPEPLHiggrtv 607
Cdd:cd05581    7 KPLGEGSYSTVVLAKEKE--TGKEYAIKVLdKRHIIKEKKVKYVtIEKEVLSRLA-HPGIVKLYytfqDESKLY------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  608 LALEYVgderdddgPGAEgatrprrreetVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirp 687
Cdd:cd05581   78 FVLEYA--------PNGD-----------LLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILL---- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  688 NRTRELVLIDF----------------------SLAGYPAKNTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMA 745
Cdd:cd05581  135 DEDMHIKITDFgtakvlgpdsspestkgdadsqIAYNQARAASFVGTAEYVSP--ELLNEKPAGKSSDLWALGCIIYQML 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21224924  746 SGELPKWGDGS--VLPRMTDpKEWPYPtiaaEAFDPAVRDglvaFFQKALHRDAGKRF 801
Cdd:cd05581  213 TGKPPFRGSNEylTFQKIVK-LEYEFP----ENFPPDAKD----LIQKLLVLDPSKRL 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
529-800 1.51e-06

Catalytic domain of the Serine/Threonine Kinase, Plant 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. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. 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. The plant 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: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 50.09  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLvrDLEAETRRTRPLAVLKVALSDSRGEI----LVREAEAMRRLRpHSGIIRlaepeplhigg 604
Cdd:cd06632    1 RWQKGQLLGSGSFGSVYE--GFNGDTGDFFAVKEVSLVDDDKKSREsvkqLEQEIALLSKLR-HPNIVQ----------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  605 rtvlaleYVGDERDDDG--------PGAegatrprrreeTVARQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDI 676
Cdd:cd06632   67 -------YYGTEREEDNlyifleyvPGG-----------SIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  677 KPDNIAVrirpNRTRELVLIDFSLAGYPAKNTDA----GTDGYLDPFVDVITRGSYDSHAERYAVAVTLHQMASGElPKW 752
Cdd:cd06632  129 KGANILV----DTNGVVKLADFGMAKHVEAFSFAksfkGSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGK-PPW 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21224924  753 GDGS---VLPRMTDPKEwpYPTIaAEAFDPAVRDglvaFFQKALHRDAGKR 800
Cdd:cd06632  204 SQYEgvaAIFKIGNSGE--LPPI-PDHLSPDAKD----FIRLCLQRDPEDR 247
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
530-811 1.75e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 50.03  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLvrdleAETRRTRPLAVLKV----ALSDSRGEIlVREAEAMRRLRpHSGIIRLAEPepLHIGGR 605
Cdd:cd14167    5 YDFREVLGTGAFSEVVL-----AEEKRTQKLVAIKCiakkALEGKETSI-ENEIAVLHKIK-HPNIVALDDI--YESGGH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  606 TVLALEYV-GDERDDdgpgaegatrprRREETVARQLREHGRLPVDQLEAygdylfgaVDFLEGEGIWHRDIKPDNIaVR 684
Cdd:cd14167   76 LYLIMQLVsGGELFD------------RIVEKGFYTERDASKLIFQILDA--------VKYLHDMGIVHRDLKPENL-LY 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  685 IRPNRTRELVLIDFSLAGYPAK----NTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDgsvlpr 760
Cdd:cd14167  135 YSLDEDSKIMISDFGLSKIEGSgsvmSTACGTPGYVAP--EVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE------ 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  761 mTDPKEWPYPTIAAEAFDPA----VRDGLVAFFQKALHRDAGKRFPELKPMRDAW 811
Cdd:cd14167  207 -NDAKLFEQILKAEYEFDSPywddISDSAKDFIQHLMEKDPEKRFTCEQALQHPW 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
530-801 2.24e-06

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 50.00  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLVRDLEA-ETRRTRPLAVLKVAlsdsrgeILVREAEAMRRLRPHSGIIRLAEPEP----LHIGG 604
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVSGhDAGKLYAMKVLKKA-------TIVQKAKTAEHTRTERQVLEHIRQSPflvtLHYAF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  605 RTVLALEYVGDERDddgpGAEGATRPRRREetvarqlrehgRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVr 684
Cdd:cd05613   75 QTDTKLHLILDYIN----GGELFTHLSQRE-----------RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  685 irpNRTRELVLIDFSLAG-YPAKNTD-----AGTDGYLDPfvDVITRGS--YDSHAERYAVAVTLHQMASGELPKWGDG- 755
Cdd:cd05613  139 ---DSSGHVVLTDFGLSKeFLLDENEraysfCGTIEYMAP--EIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDGe 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 21224924  756 ----SVLPRMTDPKEWPYPtiaaEAFDPAVRDglvaFFQKALHRDAGKRF 801
Cdd:cd05613  214 knsqAEISRRILKSEPPYP----QEMSALAKD----IIQRLLMKDPKKRL 255
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
529-747 2.38e-06

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 49.63  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  529 RWEVRRRLGTGSTSRAFLVRDleAETRRTRPLAVLKVALSDSRGEILVREAEAMRRLRpHSGIIRLAE--PEPLHIggrt 606
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRD--KATDKEYALKIIDKAKCKGKEHMIENEVAILRRVK-HPNIVQLIEeyDTDTEL---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  607 VLALEYV--GDERDDdgpgaegatrprrreetvarqLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVR 684
Cdd:cd14095   74 YLVMELVkgGDLFDA---------------------ITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVV 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21224924  685 IRPNRTRELVLIDFSLAGYPAK--NTDAGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASG 747
Cdd:cd14095  133 EHEDGSKSLKLADFGLATEVKEplFTVCGTPTYVAP--EILAETGYGLKVDIWAAGVITYILLCG 195
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
646-800 2.84e-06

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 49.60  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  646 RLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVRIrpnrTRELVLIDFSLAG-----YPAKNTDAGTDGYLDPfv 720
Cdd:cd06659  113 RLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL----DGRVKLSDFGFCAqiskdVPKRKSLVGTPYWMAP-- 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  721 DVITRGSYDSHAERYAVAVTLHQMASGELPKWGDGSV--LPRMTDPkewPYPTIA-AEAFDPAVRDglvaFFQKALHRDA 797
Cdd:cd06659  187 EVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVqaMKRLRDS---PPPKLKnSHKASPVLRD----FLERMLVRDP 259

                 ...
gi 21224924  798 GKR 800
Cdd:cd06659  260 QER 262
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
247-479 3.11e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 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: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 49.63  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  247 EAAVLGRF-KHPGAVQLKQYFPSGHAAgpALIFDYHPHTQKLDEYLVQ--YGEKldilGRMALVRQLAETVRSAHASRIH 323
Cdd:cd14176   62 EIEILLRYgQHPNIITLKDVYDDGKYV--YVVTELMKGGELLDKILRQkfFSER----EASAVLFTITKTVEYLHAQGVV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  324 HRALAARSVLVVPRSRGGKgravgeeaawltpQLQISDWQIATQRSGDSsqGQGMTrfaptalsAMHLADdadaYLAPEL 403
Cdd:cd14176  136 HRDLKPSNILYVDESGNPE-------------SIRICDFGFAKQLRAEN--GLLMT--------PCYTAN----FVAPEV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  404 TALNPDPVYLDVYGLGVLTYLLVTGKAPAA-----SQAELLARLEAGEGLRPSSLVDGLSEDVDELVQAATAYRPGQRLS 478
Cdd:cd14176  189 LERQGYDAACDIWSLGVLLYTMLTGYTPFAngpddTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLT 268

                 .
gi 21224924  479 S 479
Cdd:cd14176  269 A 269
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
531-805 3.23e-06

Catalytic domain of PRKX-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 human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-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: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 49.36  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  531 EVRRRLGTGSTSRAFLVRDleaetRRTRPLAVLKV-ALSD----SRGEILVREAEAMRRLRpHSGIIRLAEPEplHIGGR 605
Cdd:cd05612    4 ERIKTIGTGTFGRVHLVRD-----RISEHYYALKVmAIPEvirlKQEQHVHNEKRVLKEVS-HPFIIRLFWTE--HDQRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  606 TVLALEYVgderdddgPGAEGATrprrreetvarQLREHGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVri 685
Cdd:cd05612   76 LYMLMEYV--------PGGELFS-----------YLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  686 rpNRTRELVLIDFslaGYPAKNTD-----AGTDGYLDPfvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDG--SVL 758
Cdd:cd05612  135 --DKEGHIKLTDF---GFAKKLRDrtwtlCGTPEYLAP--EVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNpfGIY 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 21224924  759 PRMTDPK-EWPyptiaaEAFDPAVRDglvaFFQKALHRDAGKRFPELK 805
Cdd:cd05612  208 EKILAGKlEFP------RHLDLYAKD----LIKKLLVVDRTRRLGNMK 245
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
577-750 3.52e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 49.27  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  577 REAEAMRRLRPHSGIIRLAE--PEPLHiggrTVLALEYVGderdddgpGAEGATRPRRRE---ETVARQLREHgrlpvdq 651
Cdd:cd14179   50 REIAALKLCEGHPNIVKLHEvyHDQLH----TFLVMELLK--------GGELLERIKKKQhfsETEASHIMRK------- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  652 leaygdyLFGAVDFLEGEGIWHRDIKPDNIaVRIRPNRTRELVLIDFSLAGY-PAKN----TDAGTDGYLDPfvDVITRG 726
Cdd:cd14179  111 -------LVSAVSHMHDVGVVHRDLKPENL-LFTDESDNSEIKIIDFGFARLkPPDNqplkTPCFTLHYAAP--ELLNYN 180
                        170       180
                 ....*....|....*....|....
gi 21224924  727 SYDSHAERYAVAVTLHQMASGELP 750
Cdd:cd14179  181 GYDESCDLWSLGVILYTMLSGQVP 204
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
534-698 3.54e-06

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 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: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 49.42  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  534 RRLGTGSTSRAFLVRDLEAEtrrtRPLAVLKVaLSDSRgeILVREAEAMRRLRpHSGIIRL------AEPEP----LHig 603
Cdd:cd14137   10 KVIGSGSFGVVYQAKLLETG----EVVAIKKV-LQDKR--YKNRELQIMRRLK-HPNIVKLkyffysSGEKKdevyLN-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  604 grtvLALEYVgderdddgpgaegatrPrrreETVARQLREH--GRLPVDQLEA--YGDYLFGAVDFLEGEGIWHRDIKPD 679
Cdd:cd14137   80 ----LVMEYM----------------P----ETLYRVIRHYskNKQTIPIIYVklYSYQLFRGLAYLHSLGICHRDIKPQ 135
                        170
                 ....*....|....*....
gi 21224924  680 NIAVRIrpnRTRELVLIDF 698
Cdd:cd14137  136 NLLVDP---ETGVLKLCDF 151
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
644-802 3.89e-06

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK 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: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 48.98  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  644 HGRLPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPDNIAVrirpNRTRELVLIDFSLAG-----YPAKNTDAGTDGYLDP 718
Cdd:cd06648   97 HTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILL----TSDGRVKLSDFGFCAqvskeVPRRKSLVGTPYWMAP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  719 fvDVITRGSYDSHAERYAVAVTLHQMASGELPKWGDgSVLPRMTDPKEWPYPTIA-AEAFDPAVRDglvaFFQKALHRDA 797
Cdd:cd06648  173 --EVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNE-PPLQAMKRIRDNEPPKLKnLHKVSPRLRS----FLDRMLVRDP 245

                 ....*
gi 21224924  798 GKRFP 802
Cdd:cd06648  246 AQRAT 250
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
235-491 4.23e-06

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 48.92  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  235 SLRQSVENAAR----REAAVLGRFKHPGAVQLKQYFPSGHAAGPALIFDYHPHTQkLDEYLVQYGEKLDiLGRMAL-VRQ 309
Cdd:cd05038   40 SLQPSGEEQHMsdfkREIEILRTLDHEYIVKYKGVCESPGRRSLRLIMEYLPSGS-LRDYLQRHRDQID-LKRLLLfASQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  310 LAETVRSAHASRIHHRALAARSVLVvprsrggkgravgeEAAWLtpqLQISDWqiatqrsgdssqgqGMTRFAPTALSAM 389
Cdd:cd05038  118 ICKGMEYLGSQRYIHRDLAARNILV--------------ESEDL---VKISDF--------------GLAKVLPEDKEYY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  390 HLADDADA---YLAPELTALNPDPVYLDVYGLGVLTYLLVT----GKAPAA-------------SQAELLARLEAGEGL- 448
Cdd:cd05038  167 YVKEPGESpifWYAPECLRESRFSSASDVWSFGVTLYELFTygdpSQSPPAlflrmigiaqgqmIVTRLLELLKSGERLp 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 21224924  449 RPsslvDGLSEDVDELVQAATAYRPGQRLSsvdeFLELLEVVE 491
Cdd:cd05038  247 RP----PSCPDEVYDLMKECWEYEPQDRPS----FSDLILIID 281
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
530-701 4.34e-06

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-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: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 48.81  E-value: 4.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  530 WEVRRRLGTGSTSRAFLVRDLeaetRRTRPLAVLKVALSDSRGEI---LVREAEAMRRLRP--HSGIIRLAEPEPLHIGG 604
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDL----QDGRFVALKKVRVPLSEEGIplsTIREIALLKQLESfeHPNVVRLLDVCHGPRTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21224924  605 RTV---LALEYVgderDDDgpgaegatrprrreetVARQLREHGR--LPVDQLEAYGDYLFGAVDFLEGEGIWHRDIKPD 679
Cdd:cd07838   77 RELkltLVFEHV----DQD----------------LATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQ 136
                        170       180
                 ....*....|....*....|..
gi 21224924  680 NIAVrirpNRTRELVLIDFSLA 701
Cdd:cd07838  137 NILV----TSDGQVKLADFGLA 154
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
536-811 4.49e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 48.84  E-value: 4.49e-06
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gi 21224924  536 LGTGSTSRAFLVRDleaetRRTRPLAVLKV--ALSDSRGEILVREAEAMRRLRpHSGIIRLAE--PEPLHIggrtVLALE 611
Cdd:cd14166   11 LGSGAFSEVYLVKQ-----RSTGKLYALKCikKSPLSR