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Conserved domains on  [gi|15673869|ref|NP_268044|]
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serine/threonine protein kinase [Lactococcus lactis subsp. lactis Il1403]

Protein Classification

serine/threonine protein kinase (domain architecture ID 11600214)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, similar to Bacillus subtilis PrkC, Streptomyces toyocaensis PK-1, and Streptococcus pneumoniae StkP.

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 ...
11-268 3.47e-126

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: 376.54  E-value: 3.47e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLgDRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLL-GRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 171 TMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIINLNPEVPQALENVVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250
                ....*....|....*...
gi 15673869 251 TAKDIKNRYTDVEEMMTD 268
Cdd:cd14014 240 LAKDPEERPQSAAELLAA 257
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
353-576 1.89e-53

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 225372  Cd Length: 303  Bit Score: 187.23  E-value: 1.89e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 353 ATLAWV-VSTPTNVKIPNVTNSTLSQAKSKIKDAKLKVGTVhKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVSTGNE 431
Cdd:COG2815  13 VLLATFfPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVR-ERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 432 dIIKMKDFVGEKIDEAMATlLKDYGIDESQVTQtSVPSDSYPAGTIIKQSPKKGSSFDTkgSEKITFEVSSGKQvevPDY 511
Cdd:COG2815  92 -YITVPDVVGLTIEEAVAK-LKAYGLNLSKITQ-EEVSDEVPAGTVISQSPSAGTEVKP--GETVKLTVSKGPE---TIT 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15673869 512 KPNGQYMTYSQYQAALKAAGFTNItlDPQATTNQQADGYVYSVYPNVGTSVDPTQEIVVTYSVYT 576
Cdd:COG2815 164 VPDLVGMTYDEASSNLKAAGLTVN--SKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGA 226
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-268 3.47e-126

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: 376.54  E-value: 3.47e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLgDRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLL-GRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 171 TMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIINLNPEVPQALENVVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250
                ....*....|....*...
gi 15673869 251 TAKDIKNRYTDVEEMMTD 268
Cdd:cd14014 240 LAKDPEERPQSAAELLAA 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-268 3.82e-75

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 243.98  E-value: 3.82e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869     12 YRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNFENDDIAiaRFQREAFAMAELSHPNIVGISDVGEFESQQYIVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTG-KLVAIKVIKKKKIKKDRE--RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869     92 FVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLtqTNT 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    172 MFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIINLNPEVPQALENVVIKAT 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*..
gi 15673869    252 AKDIKNRYTdVEEMMTD 268
Cdd:smart00220 236 VKDPEKRLT-AEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-326 1.22e-58

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 204.21  E-value: 1.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  12 YRIIKEIGRGGMANVYQGEDTflgdRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHP-NIVGISDVGEFESQQYIVM 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR----KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQN---APLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGT-VKVTDFGIAKALSETSL 166
Cdd:COG0515  78 EYVDGGSLEDLLKKIgrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 167 TQ-----TNTMFGSVHYLSPEQARGSN---ATVQSDIYAIGIILFELLTGQIPF---DGDSAVAIALKHFQESIPSII-- 233
Cdd:COG0515 158 TSsipalPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTPSLas 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 234 ----NLNPEVPQALENVVIKATAKDIKNRYTDVEEMMTDVATSTSL-DRRGEEKLVFNKDHDETKIMPANLINPYDTKPL 308
Cdd:COG0515 238 plspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLkESDLSDLLKPDDSAPLRLSLPPSLEALISSLNS 317
                       330
                ....*....|....*...
gi 15673869 309 IDKKEDNDSQTDEKAASS 326
Cdd:COG0515 318 LAISGSDLKLDDSNFSKE 335
Pkinase pfam00069
Protein kinase domain;
12-260 1.81e-56

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 193.97  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    12 YRIIKEIGRGGMANVYQGEDTfLGDRLVAIKVLRsNFENDDIAIARFQREAFAMAELSHPNIVGISDVgeFESQQ--YIV 89
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR-DTGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHPNIVRLYDA--FEDKDnlYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    90 MEFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLtqT 169
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSS--L 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869   170 NTMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIInlNPEVPQALENVVIK 249
Cdd:pfam00069 155 TSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPR--PSSISEEAKDLLKK 232
                         250
                  ....*....|.
gi 15673869   250 ATAKDIKNRYT 260
Cdd:pfam00069 233 LLKKDPSKRLT 243
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
353-576 1.89e-53

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225372  Cd Length: 303  Bit Score: 187.23  E-value: 1.89e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 353 ATLAWV-VSTPTNVKIPNVTNSTLSQAKSKIKDAKLKVGTVhKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVSTGNE 431
Cdd:COG2815  13 VLLATFfPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVR-ERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 432 dIIKMKDFVGEKIDEAMATlLKDYGIDESQVTQtSVPSDSYPAGTIIKQSPKKGSSFDTkgSEKITFEVSSGKQvevPDY 511
Cdd:COG2815  92 -YITVPDVVGLTIEEAVAK-LKAYGLNLSKITQ-EEVSDEVPAGTVISQSPSAGTEVKP--GETVKLTVSKGPE---TIT 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15673869 512 KPNGQYMTYSQYQAALKAAGFTNItlDPQATTNQQADGYVYSVYPNVGTSVDPTQEIVVTYSVYT 576
Cdd:COG2815 164 VPDLVGMTYDEASSNLKAAGLTVN--SKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGA 226
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
39-258 5.01e-45

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: 173.49  E-value: 5.01e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869     39 VAIKVLRSNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQ-YIVMEFVDGMTLKQYINQNAPLANDEAIEII 117
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLlFAVFEYVPGRTLREVLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    118 TEILSAMDMAHSHGIIHRDLKPQNVLVSSSGT---VKVTDFGIAKALS------ETSLTQTNTMFGSVHYLSPEQARGSN 188
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLPgvrdadVATLTRTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15673869    189 ATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQE---SIPSIINLNPevpqaLENVVIKATAKDIKNR 258
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPvdvSLPPWIAGHP-----LGQVLRKALNKDPRQR 233
pknD PRK13184
serine/threonine-protein kinase; Reviewed
11-269 4.90e-44

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 169.18  E-value: 4.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869   11 RYRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCS-RRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869   91 EFVDGMTLKQYINQ-------NAPLANDEAI----EIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAK 159
Cdd:PRK13184  82 PYIEGYTLKSLLKSvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  160 A-------LSETSLTQTNTMF----------GSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIAL 222
Cdd:PRK13184 162 FkkleeedLLDIDVDERNICYssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISY 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15673869  223 KHfqeSIPSIINLNP--EVPQALENVVIKATAKDIKNRYTDVEEMMTDV 269
Cdd:PRK13184 242 RD---VILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
366-427 1.03e-16

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 76.41  E-value: 1.03e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15673869 366 KIPNVTNSTLSQAKSKIKDAKLKVGTVHKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVS 427
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
365-428 2.11e-13

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 309063  Cd Length: 63  Bit Score: 67.26  E-value: 2.11e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15673869   365 VKIPNVTNSTLSQAKSKIKDAKLKVGTVhKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVST 428
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTV-EEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
361-428 1.37e-12

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 65.02  E-value: 1.37e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15673869    361 TPTNVKIPNVTNSTLSQAKSKIKDAKLKVgTVHKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVST 428
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKV-EVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-268 3.47e-126

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: 376.54  E-value: 3.47e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLgDRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLL-GRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLTQTN 170
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 171 TMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIINLNPEVPQALENVVIKA 250
Cdd:cd14014 160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRA 239
                       250
                ....*....|....*...
gi 15673869 251 TAKDIKNRYTDVEEMMTD 268
Cdd:cd14014 240 LAKDPEERPQSAAELLAA 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-268 3.82e-75

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 243.98  E-value: 3.82e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869     12 YRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNFENDDIAiaRFQREAFAMAELSHPNIVGISDVGEFESQQYIVME 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTG-KLVAIKVIKKKKIKKDRE--RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869     92 FVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLtqTNT 171
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    172 MFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIINLNPEVPQALENVVIKAT 251
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*..
gi 15673869    252 AKDIKNRYTdVEEMMTD 268
Cdd:smart00220 236 VKDPEKRLT-AEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-326 1.22e-58

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 204.21  E-value: 1.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  12 YRIIKEIGRGGMANVYQGEDTflgdRLVAIKVLRSNFENDDIAIARFQREAFAMAELSHP-NIVGISDVGEFESQQYIVM 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR----KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQN---APLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGT-VKVTDFGIAKALSETSL 166
Cdd:COG0515  78 EYVDGGSLEDLLKKIgrkGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 167 TQ-----TNTMFGSVHYLSPEQARGSN---ATVQSDIYAIGIILFELLTGQIPF---DGDSAVAIALKHFQESIPSII-- 233
Cdd:COG0515 158 TSsipalPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTPSLas 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 234 ----NLNPEVPQALENVVIKATAKDIKNRYTDVEEMMTDVATSTSL-DRRGEEKLVFNKDHDETKIMPANLINPYDTKPL 308
Cdd:COG0515 238 plspSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLkESDLSDLLKPDDSAPLRLSLPPSLEALISSLNS 317
                       330
                ....*....|....*...
gi 15673869 309 IDKKEDNDSQTDEKAASS 326
Cdd:COG0515 318 LAISGSDLKLDDSNFSKE 335
Pkinase pfam00069
Protein kinase domain;
12-260 1.81e-56

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 193.97  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    12 YRIIKEIGRGGMANVYQGEDTfLGDRLVAIKVLRsNFENDDIAIARFQREAFAMAELSHPNIVGISDVgeFESQQ--YIV 89
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR-DTGKIVAIKKIK-KEKIKKKKDKNILREIKILKKLNHPNIVRLYDA--FEDKDnlYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869    90 MEFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLtqT 169
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSS--L 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869   170 NTMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIInlNPEVPQALENVVIK 249
Cdd:pfam00069 155 TSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPR--PSSISEEAKDLLKK 232
                         250
                  ....*....|.
gi 15673869   250 ATAKDIKNRYT 260
Cdd:pfam00069 233 LLKKDPSKRLT 243
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-205 7.35e-55

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: 188.25  E-value: 7.35e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  18 IGRGGMANVYQGEDTFLGdRLVAIKVLrsNFENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVMEFVDGMT 97
Cdd:cd00180   1 LGKGSFGKVYKARDKETG-KKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  98 LKQYINQN-APLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKAL-SETSLTQTNTMFGS 175
Cdd:cd00180  78 LKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLdSDDSLLKTTGGTTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 15673869 176 VHYLSPEQARGSNATVQSDIYAIGIILFEL 205
Cdd:cd00180 158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PASTA COG2815
PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];
353-576 1.89e-53

PASTA domain, binds beta-lactams [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225372  Cd Length: 303  Bit Score: 187.23  E-value: 1.89e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 353 ATLAWV-VSTPTNVKIPNVTNSTLSQAKSKIKDAKLKVGTVhKQQSSTIAEGKVIKTDPTSGTTVRSNSSVDIYVSTGNE 431
Cdd:COG2815  13 VLLATFfPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVR-ERESDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 432 dIIKMKDFVGEKIDEAMATlLKDYGIDESQVTQtSVPSDSYPAGTIIKQSPKKGSSFDTkgSEKITFEVSSGKQvevPDY 511
Cdd:COG2815  92 -YITVPDVVGLTIEEAVAK-LKAYGLNLSKITQ-EEVSDEVPAGTVISQSPSAGTEVKP--GETVKLTVSKGPE---TIT 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15673869 512 KPNGQYMTYSQYQAALKAAGFTNItlDPQATTNQQADGYVYSVYPNVGTSVDPTQEIVVTYSVYT 576
Cdd:COG2815 164 VPDLVGMTYDEASSNLKAAGLTVN--SKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGA 226
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-258 3.20e-53

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: 184.66  E-value: 3.20e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  18 IGRGGMANVYQGedTFLGdRLVAIKVLRSNFENDDIaIARFQREAFAMAELSHPNIV---GIS-DVGEFesqqYIVMEFV 93
Cdd:cd13999   1 IGSGSFGEVYKG--KWRG-TDVAIKKLKVEDDNDEL-LKEFRREVSILSKLRHPNIVqfiGAClSPPPL----CIVTEYM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  94 DGMTLKQYI-NQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETSLTQTNTM 172
Cdd:cd13999  73 PGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 173 fGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDG----DSAVAIALKHFQESIPsiinlnPEVPQALENVVI 248
Cdd:cd13999 153 -GTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKElspiQIAAAVVQKGLRPPIP------PDCPPELSKLIK 225
                       250
                ....*....|
gi 15673869 249 KATAKDIKNR 258
Cdd:cd13999 226 RCWNEDPEKR 235
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
11-268 7.67e-51

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: 178.09  E-value: 7.67e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNFENDDIAIaRFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTG-EKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGiakaLSETSLTQT- 169
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG----LSNEFRGGSl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 170 -NTMFGSVHYLSPEQARGSN-ATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPsiinLNPEVPQALENVV 247
Cdd:cd14003 155 lKTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYP----IPSHLSPDARDLI 230
                       250       260
                ....*....|....*....|.
gi 15673869 248 IKATAKDIKNRYTdVEEMMTD 268
Cdd:cd14003 231 RRMLVVDPSKRIT-IEEILNH 250
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-260 1.48e-49

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: 174.96  E-value: 1.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTfLGDRLVAIKVLR-SNFENDDIAIArfQREAFAMAELSHPNIVGISDVGEFESQQYIV 89
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRK-SDGKLYVLKEIDlSNMSEKEREEA--LNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  90 MEFVDGMTLKQYINQ----NAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETS 165
Cdd:cd08215  78 MEYADGGDLAQKIKKqkkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869 166 lTQTNTMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAIALKHFQESIPSIinlNPEVPQALEN 245
Cdd:cd08215 158 -DLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPI---PSQYSSELRD 233
                       250
                ....*....|....*
gi 15673869 246 VVIKATAKDIKNRYT 260
Cdd:cd08215 234 LVNSMLQKDPEKRPS 248
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-212 6.72e-49

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: 172.77  E-value: 6.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  12 YRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNFENDDIAIarfQREAFAMAELSHPNIVGISDVGEFESQQYIVME 91
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTG-QIVAIKKINLESKEKKESI---LNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  92 FVDGMTLKQYINQNAPLANDEAIE-IITEILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGIAKALSETslTQTN 170
Cdd:cd05122  78 FCSGGSLKDLLKNTNKTLTEQQIAyVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDG--KTRN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15673869 171 TMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPF 212
Cdd:cd05122 156 TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY 197
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-220 8.67e-48

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: 169.96  E-value: 8.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLGDRlVAIKVL-RSNFENDDIAiaRFQREAFAMAELSHPNIVGISDVgeFESQQ--Y 87
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEE-YAVKIIdKKKLKSEDEE--MLRREIEILKRLDHPNIVKLYEV--FEDDKnlY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  88 IVMEFVDGMTLKQYINQNAPLANDEAIEIITEILSAMDMAHSHGIIHRDLKPQNVLVSS---SGTVKVTDFGIAKALSET 164
Cdd:cd05117  76 LVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIFEEG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15673869 165 SLTQtnTMFGSVHYLSPEQARGSNATVQSDIYAIGIILFELLTGQIPFDGDSAVAI 220
Cdd:cd05117 156 EKLK--TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQEL 209
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
11-260 2.49e-45

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783  Cd Length: 258  Bit Score: 163.08  E-value: 2.49e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  11 RYRIIKEIGRGGMANVYQGEDTFLGdRLVAIKVLRSNfENDDIAIARFQREAFAMAELSHPNIVGISDVGEFESQQYIVM 90
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLALNLDTG-ELMAVKEVELS-GDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15673869  91 EFVDGMTLKQYINQNAPLaNDEAIEIIT-EILSAMDMAHSHGIIHRDLKPQNVLVSSSGTVKVTDFGI