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Conserved domains on  [gi|37520484|ref|NP_923861|]
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serine/threonine kinase [Gloeobacter violaceus PCC 7421]

Protein Classification

STKc_PknB_like and TolB_N domain-containing protein (domain architecture ID 10196526)

STKc_PknB_like and TolB_N domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
34-282 9.24e-81

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270916  Cd Length: 260  Bit Score: 254.82  E-value: 9.24e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAErdDGQFDKRAAVKILQPQLHG-PGLRERFIGERQILASLDHPYITRLLDGGTtEQGLPYLV 112
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 113 MDYVEGQPINLYCNERK-LDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLpadpeATA 191
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL-----GDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 192 VFSQSMTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEAT----------------PQQLTGKLAGPLA 255
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDspaavlakhlqeapppPSPLNPDVPPALD 233
                       250       260
                ....*....|....*....|....*..
gi 37520484 256 SLVLKALCEDPLDRFGSVAAFSLAIER 282
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAALRA 260
TolB_N super family cl21526
TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent ...
312-454 1.17e-31

TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent translocation system. This function of this amino terminal domain is uncertain.


The actual alignment was detected with superfamily member COG5616:

Pssm-ID: 328774  Cd Length: 152  Bit Score: 119.76  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 312 AAACLAVGLGWWSLQaavPPARRAIAVLPFENLSGDGRSAYFSKGVAVDLADQLGKTGRFTIIA--------GRAAtggS 383
Cdd:COG5616   6 FVESTTESLTAPGTS---IPAKPSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIArnssftykGKAV---D 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37520484 384 HHHLRRPFGTEAVLSGSVRRTGGHIRVVSQLIDARSGVQLWSESFDRPLQSGFADQTEVARQIVGALESQY 454
Cdd:COG5616  80 VREVGEELGVRYVLEGSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPY 150
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
34-282 9.24e-81

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916  Cd Length: 260  Bit Score: 254.82  E-value: 9.24e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAErdDGQFDKRAAVKILQPQLHG-PGLRERFIGERQILASLDHPYITRLLDGGTtEQGLPYLV 112
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 113 MDYVEGQPINLYCNERK-LDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLpadpeATA 191
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL-----GDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 192 VFSQSMTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEAT----------------PQQLTGKLAGPLA 255
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDspaavlakhlqeapppPSPLNPDVPPALD 233
                       250       260
                ....*....|....*....|....*..
gi 37520484 256 SLVLKALCEDPLDRFGSVAAFSLAIER 282
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-271 2.16e-55

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 188.12  E-value: 2.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484     34 YRIIRPVGQGGMGAVYLA-ERDDGQfdkRAAVKILQPQlHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTGK---LVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    113 MDYVEGQPI-NLYCNERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEATa 191
Cdd:smart00220  76 MEYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    192 vfsqsmTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRP--GEATPQQLTGKLAGP--------------LA 255
Cdd:smart00220 155 ------TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPfpGDDQLLELFKKIGKPkppfpppewdispeAK 228
                          250
                   ....*....|....*.
gi 37520484    256 SLVLKALCEDPLDRFG 271
Cdd:smart00220 229 DLIRKLLVKDPEKRLT 244
Pkinase pfam00069
Protein kinase domain;
34-271 3.59e-50

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 174.32  E-value: 3.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    34 YRIIRPVGQGGMGAVYLA-ERDDGQFdkrAAVKILQPQLHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAkHRDTGKI---VAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNL-YLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   113 MDYVEGQPINLYCNERKLDVDERLRLFLK-VCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEATA 191
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKqILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSSLTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   192 VFSqsmtrllTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEATPQQLTGK--------------LAGPLASL 257
Cdd:pfam00069 157 FVG-------TPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEkiidqdfdsprpssISEEAKDL 229
                         250
                  ....*....|....
gi 37520484   258 VLKALCEDPLDRFG 271
Cdd:pfam00069 230 LKKLLKKDPSKRLT 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
34-293 4.63e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 172.23  E-value: 4.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAERDdgqfdKRAAVKILQPQLHGPG-LRERFIGERQILASLDHP-YITRLLDGGTTEQGLpYL 111
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR-----KLVALKVLAKKLESKSkEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL-YL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 112 VMDYVEGQPINLYCNER----KLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGN-PRLLDFGIAKLLPAD 186
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIgrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 187 PEATAVFSQSMTRLLTPGYASPEQIKG---EAITPASDEYSLAVVLCELLSGRRPGEATP-------------QQLTGKL 250
Cdd:COG0515 156 GSTSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssatsqtlkiilELPTPSL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37520484 251 AGP------------LASLVLKALCEDPLDRFGSVAAFSLAIERHLTGQALPWPR 293
Cdd:COG0515 236 ASPlspsnpeliskaASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSD 290
pknD PRK13184
serine/threonine-protein kinase; Reviewed
31-297 9.34e-35

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 139.14  E-value: 9.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   31 LGAYRIIRPVGQGGMGAVYLAErdDGQFDKRAAVKILQPQLHG-PGLRERFIGERQILASLDHPYITRLLDggTTEQGLP 109
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAY--DPVCSRRVALKKIREDLSEnPLLKKRFLREAKIAADLIHPGIVPVYS--ICSDGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  110 -YLVMDYVEGQPINLY------CNERKLDVDER------LRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLD 176
Cdd:PRK13184  77 vYYTMPYIEGYTLKSLlksvwqKESLSKELAEKtsvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  177 FGIAK--------LLPADPEATAVFSQSMTR----LLTPGYASPEQIKGEAITPASDEYSLAVVLCELLS---------G 235
Cdd:PRK13184 157 WGAAIfkkleeedLLDIDVDERNICYSSMTIpgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTlsfpyrrkkG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37520484  236 RR---------PGEATPQQltgKLAGPLASLVLKALCEDPLDRFGSVAAFSLAIERHLTGQAlPWPRTGTL 297
Cdd:PRK13184 237 RKisyrdvilsPIEVAPYR---EIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP-EWTVKATL 303
TolBN COG5616
TolB amino-terminal domain (function unknown) [General function prediction only];
312-454 1.17e-31

TolB amino-terminal domain (function unknown) [General function prediction only];


Pssm-ID: 227903  Cd Length: 152  Bit Score: 119.76  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 312 AAACLAVGLGWWSLQaavPPARRAIAVLPFENLSGDGRSAYFSKGVAVDLADQLGKTGRFTIIA--------GRAAtggS 383
Cdd:COG5616   6 FVESTTESLTAPGTS---IPAKPSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIArnssftykGKAV---D 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37520484 384 HHHLRRPFGTEAVLSGSVRRTGGHIRVVSQLIDARSGVQLWSESFDRPLQSGFADQTEVARQIVGALESQY 454
Cdd:COG5616  80 VREVGEELGVRYVLEGSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPY 150
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
76-275 5.14e-30

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


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 124.57  E-value: 5.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484     76 LRERFIGERQILASLDHPYITRLLDGGTTEQGLPYLVMDYVEGQPI-NLYCNERKLDVDERLRLFLKVCEAVHYAHAHRV 154
Cdd:TIGR03903   21 QRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLrEVLAADGALPAGETGRLMLQVLDALACAHNQGI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    155 IHRDLKPANILI---DPEGNPRLLDFGIAKLLPADPEATAVFSQSMTRLL-TPGYASPEQIKGEAITPASDEYSLAVVLC 230
Cdd:TIGR03903  101 VHRDLKPQNIMVsqtGVRPHAKVLDFGIGTLLPGVRDADVATLTRTTEVLgTPTYCAPEQLRGEPVTPNSDLYAWGLIFL 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 37520484    231 ELLSGRR--PGEATPQQLTGKL------------AGPLASLVLKALCEDPLDRFGSVAA 275
Cdd:TIGR03903  181 ECLTGQRvvQGASVAEILYQQLspvdvslppwiaGHPLGQVLRKALNKDPRQRAASAPA 239
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
34-282 9.24e-81

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916  Cd Length: 260  Bit Score: 254.82  E-value: 9.24e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAErdDGQFDKRAAVKILQPQLHG-PGLRERFIGERQILASLDHPYITRLLDGGTtEQGLPYLV 112
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAEdEEFRERFLREARALARLSHPNIVRVYDVGE-DDGRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 113 MDYVEGQPINLYCNERK-LDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLpadpeATA 191
Cdd:cd14014  79 MEYVEGGSLADLLRERGpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL-----GDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 192 VFSQSMTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEAT----------------PQQLTGKLAGPLA 255
Cdd:cd14014 154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDspaavlakhlqeapppPSPLNPDVPPALD 233
                       250       260
                ....*....|....*....|....*..
gi 37520484 256 SLVLKALCEDPLDRFGSVAAFSLAIER 282
Cdd:cd14014 234 AIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-271 2.16e-55

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 188.12  E-value: 2.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484     34 YRIIRPVGQGGMGAVYLA-ERDDGQfdkRAAVKILQPQlHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTGK---LVAIKVIKKK-KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    113 MDYVEGQPI-NLYCNERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEATa 191
Cdd:smart00220  76 MEYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLT- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    192 vfsqsmTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRP--GEATPQQLTGKLAGP--------------LA 255
Cdd:smart00220 155 ------TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPfpGDDQLLELFKKIGKPkppfpppewdispeAK 228
                          250
                   ....*....|....*.
gi 37520484    256 SLVLKALCEDPLDRFG 271
Cdd:smart00220 229 DLIRKLLVKDPEKRLT 244
Pkinase pfam00069
Protein kinase domain;
34-271 3.59e-50

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 174.32  E-value: 3.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484    34 YRIIRPVGQGGMGAVYLA-ERDDGQFdkrAAVKILQPQLHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAkHRDTGKI---VAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNL-YLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   113 MDYVEGQPINLYCNERKLDVDERLRLFLK-VCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEATA 191
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKqILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSSLTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   192 VFSqsmtrllTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEATPQQLTGK--------------LAGPLASL 257
Cdd:pfam00069 157 FVG-------TPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEkiidqdfdsprpssISEEAKDL 229
                         250
                  ....*....|....
gi 37520484   258 VLKALCEDPLDRFG 271
Cdd:pfam00069 230 LKKLLKKDPSKRLT 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
34-293 4.63e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 172.23  E-value: 4.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAERDdgqfdKRAAVKILQPQLHGPG-LRERFIGERQILASLDHP-YITRLLDGGTTEQGLpYL 111
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR-----KLVALKVLAKKLESKSkEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL-YL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 112 VMDYVEGQPINLYCNER----KLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGN-PRLLDFGIAKLLPAD 186
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIgrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 187 PEATAVFSQSMTRLLTPGYASPEQIKG---EAITPASDEYSLAVVLCELLSGRRPGEATP-------------QQLTGKL 250
Cdd:COG0515 156 GSTSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKnssatsqtlkiilELPTPSL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 37520484 251 AGP------------LASLVLKALCEDPLDRFGSVAAFSLAIERHLTGQALPWPR 293
Cdd:COG0515 236 ASPlspsnpeliskaASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSD 290
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
41-269 1.51e-44

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


Pssm-ID: 270622  Cd Length: 215  Bit Score: 157.82  E-value: 1.51e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  41 GQGGMGAVYLAERDDGQfdKRAAVKILQPQLHGpGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLVMDYVEGqp 120
Cdd:cd00180   2 GKGSFGKVYKARDKETG--KKVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDVFETENFL-YLVMEYCEG-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 121 INLYC----NERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEatavFSQS 196
Cdd:cd00180  76 GSLKDllkeNKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDS----LLKT 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37520484 197 MTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELlsgrrpgeatpqqltgklaGPLASLVLKALCEDPLDR 269
Cdd:cd00180 152 TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------EELKDLIRRMLQYDPKKR 205
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
34-269 6.40e-39

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905  Cd Length: 252  Bit Score: 143.43  E-value: 6.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAE-RDDGQFdkrAAVKILQPQLHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARhKLTGEK---VAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKI-YLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 113 MDYVEGQpiNLY---CNERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADpea 189
Cdd:cd14003  78 MEYASGG--ELFdyiVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 190 tavfSQSMTRLLTPGYASPEQIKGEA-ITPASDEYSLAVVLCELLSGRRPGEATPQQLTGK------------LAGPLAS 256
Cdd:cd14003 153 ----SLLKTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRkilkgkypipshLSPDARD 228
                       250
                ....*....|...
gi 37520484 257 LVLKALCEDPLDR 269
Cdd:cd14003 229 LIRRMLVVDPSKR 241
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-275 9.27e-38

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


Pssm-ID: 270693  Cd Length: 250  Bit Score: 139.96  E-value: 9.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  40 VGQGGMGAVYLA-ERDDGQFdkrAAVKILQPQ-LHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLVMDYVE 117
Cdd:cd05123   1 LGKGSFGKVLLVrKKDTGKL---YAMKVLRKKeIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKL-YLVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 118 -GQPINLYCNERKLDvDERLRLFL-KVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLPADPEATAVFSQ 195
Cdd:cd05123  77 gGELFSHLSKEGRFP-EERARFYAaEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 196 smtrllTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEATPQQ------LTGKLAGP------LASLVLKALC 263
Cdd:cd05123 156 ------TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKeiyekiLKSPLKFPeyvspeAKSLISGLLQ 229
                       250
                ....*....|..
gi 37520484 264 EDPLDRFGSVAA 275
Cdd:cd05123 230 KDPTKRLGSGGA 241
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
40-269 4.80e-37

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


Pssm-ID: 270968  Cd Length: 272  Bit Score: 138.56  E-value: 4.80e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  40 VGQGGMGAVYLAERDDGqfdKRAAVKILQPQlHGPGLRERFIGERQILASLDHPYITRLLdGGTTEQGLPYLVMDYVEGQ 119
Cdd:cd14066   1 IGSGGFGTVYKGVLENG---TVVAVKRLNEM-NCAASKKEFLTELEMLGRLRHPNLVRLL-GYCLESDEKLLVYEYMPNG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 120 PIN--LYCNERK--LDVDERLRLFLKVCEAVHYAH---AHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLpadPEATAV 192
Cdd:cd14066  76 SLEdrLHCHKGSppLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLI---PPSESV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 193 FSQSMTRlLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEATPQQLTGKLagpLASLV---LKALCEDPLDR 269
Cdd:cd14066 153 SKTSAVK-GTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKD---LVEWVeskGKEELEDILDK 228
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
40-254 6.68e-37

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


Pssm-ID: 270901  Cd Length: 245  Bit Score: 137.28  E-value: 6.68e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  40 VGQGGMGAVYLAErddgQFDKRAAVKILQPQLHGPGLRERFIGERQILASLDHPYITRLLdGGTTEQGLPYLVMDYVEGQ 119
Cdd:cd13999   1 IGSGSFGEVYKGK----WRGTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFI-GACLSPPPLCIVTEYMPGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 120 piNLY----CNERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLpadpeatAVFSQ 195
Cdd:cd13999  76 --SLYdllhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIK-------NSTTE 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37520484 196 SMTRLL-TPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRP--GEATPQQLTGKLAGPL 254
Cdd:cd13999 147 KMTGVVgTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPfkELSPIQIAAAVVQKGL 208
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
34-242 4.95e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855  Cd Length: 258  Bit Score: 135.28  E-value: 4.95e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLAER-DDGqfdKRAAVKILQpqLHGPGLRER--FIGERQILASLDHPYITRLLDGGTTEQGLpY 110
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRkSDG---KLYVLKEID--LSNMSEKEReeALNEVKLLSKLKHPNIVKYYESFEENGKL-C 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 111 LVMDYVEG----QPINLYCNERKLdVDER--LRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLDFGIAKLLp 184
Cdd:cd08215  76 IVMEYADGgdlaQKIKKQKKKGQP-FPEEqiLDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 37520484 185 adpEATAVFSQSMTRllTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRPGEAT 242
Cdd:cd08215 154 ---ESTTDLAKTVVG--TPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEAN 206
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
34-238 8.30e-36

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687  Cd Length: 258  Bit Score: 134.53  E-value: 8.30e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  34 YRIIRPVGQGGMGAVYLA-ERDDGQfdkRAAVKILQPQLHGPGLRERFIGERQILASLDHPYITRLLDGGTTEQGLpYLV 112
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAvHKKTGE---EYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNL-YLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484 113 MDYVEGQpiNLY---CNERKLDVDERLRLFLKVCEAVHYAHAHRVIHRDLKPANILI---DPEGNPRLLDFGIAKLLPAD 186
Cdd:cd05117  78 MELCTGG--ELFdriVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 37520484 187 PEATavfsqsmTRLLTPGYASPEQIKGEAITPASDEYSLAVVLCELLSGRRP 238
Cdd:cd05117 156 EKLK-------TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPP 200
pknD PRK13184
serine/threonine-protein kinase; Reviewed
31-297 9.34e-35

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 139.14  E-value: 9.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484   31 LGAYRIIRPVGQGGMGAVYLAErdDGQFDKRAAVKILQPQLHG-PGLRERFIGERQILASLDHPYITRLLDggTTEQGLP 109
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAY--DPVCSRRVALKKIREDLSEnPLLKKRFLREAKIAADLIHPGIVPVYS--ICSDGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  110 -YLVMDYVEGQPINLY------CNERKLDVDER------LRLFLKVCEAVHYAHAHRVIHRDLKPANILIDPEGNPRLLD 176
Cdd:PRK13184  77 vYYTMPYIEGYTLKSLlksvwqKESLSKELAEKtsvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520484  177 FGIAK--------LLPADPEATAVFSQSMTR----LLTPGYASPEQIKGEAITPASDEYSLAVVLCELLS---------G 235
Cdd:PRK13184 157 WGAAIfkkleeedLLDIDVDERNICYSSMTIpgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTlsfpyrrkkG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37520484  236 RR---------PGEATPQQltgKLAGPLASLVLKALCEDPLDRFGSVAAFSLAIERHLTGQAlPWPRTGTL 297
Cdd:PRK13184 237 RKisyrdvilsPIEVAPYR---EIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP-EWTVKATL 303
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
34-238 2.85e-33

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692  Cd Length: 254  Bit Score: 127.3