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Conserved domains on  [gi|21221774|ref|NP_627553|]
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Ser/Thr protein kinase [Streptomyces coelicolor A3(2)]

Protein Classification

STKc_PknB_like and PQQ_2 domain-containing protein (domain architecture ID 11602166)

STKc_PknB_like and PQQ_2 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 ...
21-273 1.57e-85

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: 273.69  E-value: 1.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARSTSGMR-VAVKVVHATYARDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATL 99
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRpVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTETGK 178
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 179 LIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEP-----DLTGVPDSLAPLVLRC 253
Cdd:cd14014 161 VLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppspLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 21221774 254 LAKEPEDRP-TPDELMRELRS 273
Cdd:cd14014 240 LAKDPEERPqSAAELLAALRA 260
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
403-670 5.56e-17

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


:

Pssm-ID: 315925  Cd Length: 233  Bit Score: 81.69  E-value: 5.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   403 GVVFALDPADGSTLWRHPVEETVRSEPPVVSGGLVQpeVGLLGPLEALDPATGEPEWQEDMPAydGLRTV----GDMLLL 478
Cdd:pfam13360   3 GTVSALDAATGAELWRVDLGTPLGGGVAVDGGTLFV--ATGGGQLVALDAATGKLLWRQTLSG--EVLGAplvaGGRVFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   479 TRADGMVTGVDSSSGRTRWAHRIPGQAvpyfTSFAGERHPAAYATSQSADGRRTHVTAVDPAGGDVRWDTELAGaltPVG 558
Cdd:pfam13360  79 VAADGSLAALDAETGKRLWSYQRSGPP----LALRSSGSPAVAGDTVVVGFASGKLVALDPKTGKVRWEAPLAA---PRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   559 TADGSVFlvvegatyGDVTAVVRytpatgatrrvtlpipveqasasagVRGDTVYLMGAGGSLVAVDMAAEKQAWRLEtg 638
Cdd:pfam13360 152 TNELERL--------VDITGTPV-------------------------VDGGRVCAVSYQGRLGAFDAATGRVLWSRD-- 196
                         250       260       270
                  ....*....|....*....|....*....|..
gi 21221774   639 VSRGSAPVSDGRHVYVTAPDGRLLGVDARKGK 670
Cdd:pfam13360 197 ISSINGPAVDGDLLYVVDDDGEVYALDRATGA 228
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-273 1.57e-85

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: 273.69  E-value: 1.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARSTSGMR-VAVKVVHATYARDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATL 99
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRpVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTETGK 178
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 179 LIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEP-----DLTGVPDSLAPLVLRC 253
Cdd:cd14014 161 VLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppspLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 21221774 254 LAKEPEDRP-TPDELMRELRS 273
Cdd:cd14014 240 LAKDPEERPqSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
22-269 1.74e-53

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 186.58  E-value: 1.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774     22 YRLESRLGSGGMGVVHLARST-SGMRVAVKVVHATyaRDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATLF 100
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKkTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    101 IPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDGP-KVIDFGISRPKDSELRTETgkL 179
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    180 IGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVV-----HDEPDLTGVPDSLAPLVLRCL 254
Cdd:smart00220 157 VGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*
gi 21221774    255 AKEPEDRPTPDELMR 269
Cdd:smart00220 236 VKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
22-269 3.07e-42

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 154.68  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    22 YRLESRLGSGGMGVVHLAR-STSGMRVAVKVVhATYARDPEFRGRFRQEVAAARRVS--------GAFTAPvvdadpeaG 92
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKI-KKEKIKKKKDKNILREIKILKKLNhpnivrlyDAFEDK--------D 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    93 RPWMATLFIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISR--PKD 169
Cdd:pfam00069  72 NLYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARqlNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   170 SELRTETgkliGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEPDlTGVPDSLAP- 248
Cdd:pfam00069 152 SSLTSFV----GTPWYMAPEVLRG-NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFD-SPRPSSISEe 225
                         250       260
                  ....*....|....*....|....
gi 21221774   249 ---LVLRCLAKEPEDRPTPDELMR 269
Cdd:pfam00069 226 akdLLKKLLKKDPSKRLTATEALQ 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-268 2.22e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 156.06  E-value: 2.22e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARSTsgMRVAVKVVHATYARDPEFRGRFRQEVAAARRVSGA-FTAPVVDADPEAGRPWMATL 99
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVKRNG---PMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG--PKVIDFGISRP-----KD 169
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrvVKLIDFGLAKLlpdpgST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 170 SELRTETGKLIGTPPYMAPEQFR--RPREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVV-------------- 233
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslasp 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21221774 234 HDEPDLTGVPDSLAPLVLRCLAKEPEDRPTPDELM 268
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDL 273
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
43-272 3.37e-21

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: 99.15  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774     43 SGMRVAVKVVHATYARDPEFRGRFRQEVAAARRVSGAFTAPVVDA-DPEAGRPWMATLFIPGPTLSEQVKRNGPMDEPQL 121
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    122 RRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG----PKVIDFGIS------RPKDSELRTETGKLIGTPPYMAPEQF 191
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrphAKVLDFGIGtllpgvRDADVATLTRTTEVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    192 RRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQvvHDEPDLTGVPDSLA--PL--VLR-CLAKEPEDRPTP-- 264
Cdd:TIGR03903  162 RG-EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ--QLSPVDVSLPPWIAghPLgqVLRkALNKDPRQRAASap 238
                          250
                   ....*....|
gi 21221774    265 --DELMRELR 272
Cdd:TIGR03903  239 alAERFRALE 248
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
106-309 4.61e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293  Cd Length: 478  Bit Score: 87.76  E-value: 4.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  106 LSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTETG-KLIGTP 183
Cdd:PTZ00267 156 IKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGiIKLGDFGFSKQYSDSVSLDVAsSFCGTP 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  184 PYMAPEQFRRPReVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHD--EPDLTGVPDSLAPLVLRCLAKEPEDR 261
Cdd:PTZ00267 236 YYLAPELWERKR-YSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGkyDPFPCPVSSGMKALLDPLLSKNPALR 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21221774  262 PTPDELMRE--LRSVAAAYD-----TQVFIPAPRTERAETPAEAGAEPAPRASVE 309
Cdd:PTZ00267 315 PTTQQLLHTefLKYVANLFQdivrhSETISPHDREEILRQLQESGERAPPPSSIR 369
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
403-670 5.56e-17

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 315925  Cd Length: 233  Bit Score: 81.69  E-value: 5.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   403 GVVFALDPADGSTLWRHPVEETVRSEPPVVSGGLVQpeVGLLGPLEALDPATGEPEWQEDMPAydGLRTV----GDMLLL 478
Cdd:pfam13360   3 GTVSALDAATGAELWRVDLGTPLGGGVAVDGGTLFV--ATGGGQLVALDAATGKLLWRQTLSG--EVLGAplvaGGRVFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   479 TRADGMVTGVDSSSGRTRWAHRIPGQAvpyfTSFAGERHPAAYATSQSADGRRTHVTAVDPAGGDVRWDTELAGaltPVG 558
Cdd:pfam13360  79 VAADGSLAALDAETGKRLWSYQRSGPP----LALRSSGSPAVAGDTVVVGFASGKLVALDPKTGKVRWEAPLAA---PRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   559 TADGSVFlvvegatyGDVTAVVRytpatgatrrvtlpipveqasasagVRGDTVYLMGAGGSLVAVDMAAEKQAWRLEtg 638
Cdd:pfam13360 152 TNELERL--------VDITGTPV-------------------------VDGGRVCAVSYQGRLGAFDAATGRVLWSRD-- 196
                         250       260       270
                  ....*....|....*....|....*....|..
gi 21221774   639 VSRGSAPVSDGRHVYVTAPDGRLLGVDARKGK 670
Cdd:pfam13360 197 ISSINGPAVDGDLLYVVDDDGEVYALDRATGA 228
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
400-718 3.90e-15

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224437  Cd Length: 370  Bit Score: 77.62  E-value: 3.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 400 ARPGVVFALDPADGSTLWRHPVEETVR--SEPPVVSGGLVQpeVG-LLGPLEALDPATGEPEWQ---EDMPAYDGLRTVG 473
Cdd:COG1520  75 TRDGNIFALNPDTGLVKWSYPLLGAVAqlSGPILGSDGKIY--VGsWDGKLYALDASTGTLVWSrnvGGSPYYASPPVVG 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 474 DMLLLTRA-DGMVTGVDSSSGRTRWAHRIPGQAVPYFTSFAGERHPAAYATSQSADGRrthVTAVDPAGGDVRWDTELAG 552
Cdd:COG1520 153 DGTVYVGTdDGHLYALNADTGTLKWTYETPAPLSLSIYGSPAIASGTVYVGSDGYDGI---LYALNAEDGTLKWSQKVSQ 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 553 ALtpvgtadgsvflvveGATYGDVTAVVRYTPAtgatrrvtlpipveqasasagVRGDTVYLMGAGGSLVAVDMAAEKQA 632
Cdd:COG1520 230 TI---------------GRTAISTTPAVDGGPV---------------------YVDGGVYAGSYGGKLLCLDADTGELI 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 633 WRLETGVSRGSAPVSDgrhVYVTAPDGRLLgVDARKGKLLGQTRPRLGAD---------SDTVPA--SLPAPLLAGGHVY 701
Cdd:COG1520 274 WSFPAGGSVQGSGLYT---TPVAGADGKVY-IGFTDNDGRGSGSLYALADvpggtllkwSYPVGGgySLSTVAGSDGTLY 349
                       330
                ....*....|....*...
gi 21221774 702 -AGAPDGTVFGVAGRDPG 718
Cdd:COG1520 350 fGGDDGRGLYAFRDGALL 367
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
379-710 5.26e-15

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511  Cd Length: 377  Bit Score: 77.28  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   379 VPAAQGGGMpqcsYAArrllcARPGVVFALDPADGSTLWRHPVEETVRSePPVVSGGLVQpeVGLL-GPLEALDPATGEP 457
Cdd:TIGR03300  60 QPAVAGGKV----YAA-----DADGTVAALDAETGKRLWRVDLDERLSG-GVGADGGLVF--VGTEkGEVIALDAEDGKE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   458 EWQEDM-------PAYDglrtvGDMLLLTRADGMVTGVDSSSGRTRWAHRIP-------GQAVPYF---TSFAGerhpaa 520
Cdd:TIGR03300 128 LWRAKLssevlspPLVA-----NGLVVVRTNDGRLTALDAATGERLWTYSRVtppltlrGSASPVIadgGVLVG------ 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   521 yatsqSADGRrthVTAVDPAGGDVRWDtelagalTPVGTADGSvflvvegatygdvTAVVRYTPATGAtrrvtlpiPVeq 600
Cdd:TIGR03300 197 -----FAGGK---LVALDLQTGQPLWE-------QRVALPKGR-------------TELERLVDVDGD--------PV-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   601 asasagVRGDTVYLMGAGGSLVAVDMAAEKQAWRLETGVSRGsaPVSDGRHVYVTAPDGRLLGVDARKGKLLGQTrprlg 680
Cdd:TIGR03300 239 ------VDGGQVYAVSYQGRVAALDLRSGRVLWKRDASSYQG--PAVDDNRLYVTDADGVVVALDRRSGSELWKN----- 305
                         330       340       350
                  ....*....|....*....|....*....|
gi 21221774   681 adSDTVPASLPAPLLAGGHVYAGAPDGTVF 710
Cdd:TIGR03300 306 --DELKYRQLTAPAVLGGYLVVGDFEGYLH 333
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
399-714 1.64e-13

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834  Cd Length: 358  Bit Score: 72.36  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 399 CARPGVVFALDPADGSTLWRHPVEETVRSEPPVVSGG--LVQPEVGllGPLEALDPATGEPEWQEDMPA---------YD 467
Cdd:cd10276  44 ADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNgkIFVGTES--GYLYALDAKDGSELWRTEVSDsqllspptyAD 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 468 GLRTVGDmllltrADGMVTGVDSSSGRTRWAH-------RIPGQAVP---YFTSFAGErhpaayatsqsADGrrtHVTAV 537
Cdd:cd10276 122 GKIYVGT------GDGRLYYCNAETGKVVWNRtstapelSLRGGAAPvgaYDVVFVGD-----------GNG---TVVAL 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 538 DPAGGDVRWDTELA---GALTPVGTADGSVFLVVegatYGDVTAVVRYTPATGATRRVT-LPIPVEQASASAGVRGD--- 610
Cdd:cd10276 182 NTGTGVDIWEFSVSeprGRTELPRMIDSSVTYVV----VGGYLYSTSYQGYLVALDFESgQFLWSRKASGGTSTSTDang 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 611 TVYLMGAGGSLVAVDMAAEKQAWRLETGVSRG-SAPV-SDGRHVYVT-APDGRLLGVDarkgKLLGQTRPRLGADSdtVP 687
Cdd:cd10276 258 RVYVGDGEGSLYCLDASTGDELWSQTVLLGRVlSSPAiYVGVYIYVTdNAEGYLYCLK----DNDGLTVARVEVDY--SQ 331
                       330       340
                ....*....|....*....|....*..
gi 21221774 688 ASLPAPLLAGGHVYAGAPDGTVFGVAG 714
Cdd:cd10276 332 YILQGPAVSDGWLYYGTDDGYLYALTR 358
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
401-707 1.29e-11

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857  Cd Length: 394  Bit Score: 66.88  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  401 RPGVVFALDPADGSTLWRHPVEETV----RSEPPVVSGGL--------VQPEVGLLGpleALDPATGEPEWQEDM----- 463
Cdd:PRK11138  77 RAGLVKALDADTGKEIWSVDLSEKDgwfsKNKSALLSGGVtvaggkvyIGSEKGQVY---ALNAEDGEVAWQTKVageal 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  464 --PAYDGlrtvgDMLLLTRADGMVTGVDSSSGRTRWAHRipgQAVPYFTsFAGERHPAAyatsqsadgrrthvtavdpAG 541
Cdd:PRK11138 154 srPVVSD-----GLVLVHTSNGMLQALNESDGAVKWTVN---LDVPSLT-LRGESAPAT-------------------AF 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  542 GdvrwdtelaGALtpVGTADGSVFLVVEGATYGDVTAVVrYTPaTGAT---RRV---TLPIPVeqasasagvrGDTVYLM 615
Cdd:PRK11138 206 G---------GAI--VGGDNGRVSAVLMEQGQLIWQQRI-SQP-TGATeidRLVdvdTTPVVV----------GGVVYAL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  616 GAGGSLVAVDMAAEKQAWRLETGVSRGSApvSDGRHVYVTAPDGRLLGVDARKGKLLGQTrprlgadSDTVPASLPAPLL 695
Cdd:PRK11138 263 AYNGNLVALDLRSGQIVWKREYGSVNDFA--VDGGRIYLVDQNDRVYALDTRGGVELWSQ-------SDLLHRLLTAPVL 333
                        330
                 ....*....|..
gi 21221774  696 AGGHVYAGAPDG 707
Cdd:PRK11138 334 YNGYLVVGDSEG 345
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
21-273 1.57e-85

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: 273.69  E-value: 1.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARSTSGMR-VAVKVVHATYARDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATL 99
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRpVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTETGK 178
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGrVKLTDFGIARALGDSGLTQTGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 179 LIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEP-----DLTGVPDSLAPLVLRC 253
Cdd:cd14014 161 VLGTPAYMAPEQARG-GPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppspLNPDVPPALDAIILRA 239
                       250       260
                ....*....|....*....|.
gi 21221774 254 LAKEPEDRP-TPDELMRELRS 273
Cdd:cd14014 240 LAKDPEERPqSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
22-269 1.74e-53

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 186.58  E-value: 1.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774     22 YRLESRLGSGGMGVVHLARST-SGMRVAVKVVHATyaRDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATLF 100
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKkTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    101 IPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDGP-KVIDFGISRPKDSELRTETgkL 179
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    180 IGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVV-----HDEPDLTGVPDSLAPLVLRCL 254
Cdd:smart00220 157 VGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*
gi 21221774    255 AKEPEDRPTPDELMR 269
Cdd:smart00220 236 VKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
22-269 3.07e-42

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 154.68  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    22 YRLESRLGSGGMGVVHLAR-STSGMRVAVKVVhATYARDPEFRGRFRQEVAAARRVS--------GAFTAPvvdadpeaG 92
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKhRDTGKIVAIKKI-KKEKIKKKKDKNILREIKILKKLNhpnivrlyDAFEDK--------D 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774    93 RPWMATLFIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISR--PKD 169
Cdd:pfam00069  72 NLYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGnLKITDFGLARqlNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774   170 SELRTETgkliGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEPDlTGVPDSLAP- 248
Cdd:pfam00069 152 SSLTSFV----GTPWYMAPEVLRG-NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFD-SPRPSSISEe 225
                         250       260
                  ....*....|....*....|....
gi 21221774   249 ---LVLRCLAKEPEDRPTPDELMR 269
Cdd:pfam00069 226 akdLLKKLLKKDPSKRLTATEALQ 249
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
28-268 6.83e-42

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: 152.81  E-value: 6.83e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  28 LGSGGMGVVHLAR-STSGMRVAVKVVHatYARDPEFRGRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATLFIPGPTL 106
Cdd:cd00180   1 LGKGSFGKVYKARdKETGKKVAVKVIP--KEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 107 SEQVKRN-GPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTETGKLIGTPP 184
Cdd:cd00180  79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGtVKLADFGLAKDLDSDDSLLKTTGGTTPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 185 YMAPEQFRRPREVGPAADVFTLGslmvhaatgrgpfdsdspyVVAYQVvhdepdltgvpDSLAPLVLRCLAKEPEDRPTP 264
Cdd:cd00180 159 YYAPPELLGGRYYGPKVDIWSLG-------------------VILYEL-----------EELKDLIRRMLQYDPKKRPSA 208

                ....
gi 21221774 265 DELM 268
Cdd:cd00180 209 KELL 212
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-268 2.22e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 156.06  E-value: 2.22e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARSTsgMRVAVKVVHATYARDPEFRGRFRQEVAAARRVSGA-FTAPVVDADPEAGRPWMATL 99
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVKRNG---PMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG--PKVIDFGISRP-----KD 169
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrvVKLIDFGLAKLlpdpgST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 170 SELRTETGKLIGTPPYMAPEQFR--RPREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVV-------------- 233
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslasp 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21221774 234 HDEPDLTGVPDSLAPLVLRCLAKEPEDRPTPDELM 268
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDL 273
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
21-269 9.59e-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: 144.97  E-value: 9.59e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARST-SGMRVAVKVVHATYARDPEFRgRFRQEVAAARRVsgafTAP-------VVDADpeaG 92
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKlTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLL----NHPniiklyeVIETE---N 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  93 RPWMATLFIPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDGP-KVIDFGISR--PKD 169
Cdd:cd14003  73 KIYLVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNlKIIDFGLSNefRGG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 170 SELRTetgkLIGTPPYMAPEQFRRPREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVVHDEPDLtgvPDSLAP- 248
Cdd:cd14003 153 SLLKT----FCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPI---PSHLSPd 225
                       250       260
                ....*....|....*....|....
gi 21221774 249 ---LVLRCLAKEPEDRPTPDELMR 269
Cdd:cd14003 226 ardLIRRMLVVDPSKRITIEEILN 249
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
21-269 1.50e-36

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: 139.26  E-value: 1.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  21 HYRLESRLGSGGMGVVHLARST-SGMRVAVKVVHATYARDPEfrgRFRQEVAAARRVSGAFTAPVVDADPEAGRPWMATL 99
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKkTGQIVAIKKINLESKEKKE---SILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 100 FIPGPTLSEQVK-RNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDGP-KVIDFGISrpKDSELRTETG 177
Cdd:cd05122  78 FCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEvKLIDFGLS--AQLSDGKTRN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 178 KLIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPF-DSDSPYVVAYQVVHDEPDL---TGVPDSLAPLVLRC 253
Cdd:cd05122 156 TFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPYsELPPMKALFLIATNGPPGLrnpKKWSKEFKDFLKKC 234
                       250
                ....*....|....*.
gi 21221774 254 LAKEPEDRPTPDELMR 269
Cdd:cd05122 235 LQKDPEKRPTAEQLLK 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
28-271 9.63e-36

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: 136.51  E-value: 9.63e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  28 LGSGGMGVVHLA--RSTSgmrVAVKVVHATYARDPEFRgRFRQEVAAARRVS--------GAFTAPvvdadpeaGRPWMA 97
Cdd:cd13999   1 IGSGSFGEVYKGkwRGTD---VAIKKLKVEDDNDELLK-EFRREVSILSKLRhpnivqfiGACLSP--------PPLCIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  98 TLFIPGPTLSEQV-KRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDG-PKVIDFGISRPKDSELRTE 175
Cdd:cd13999  69 TEYMPGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFtVKIADFGLSRIKNSTTEKM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 176 TGKlIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPFDSDSPYVVAYQVV--HDEPDL-TGVPDSLAPLVLR 252
Cdd:cd13999 149 TGV-VGTPRWMAPEVLRG-EPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVqkGLRPPIpPDCPPELSKLIKR 226
                       250
                ....*....|....*....
gi 21221774 253 CLAKEPEDRPTPDELMREL 271
Cdd:cd13999 227 CWNEDPEKRPSFSEIVKRL 245
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
28-269 2.68e-35

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: 135.73  E-value: 2.68e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  28 LGSGGMGVVHLARST-SGMRVAVKVVHATYARDPEFRgRFRQEVAAARRVS--------GAFTAPVvdadpeagrpwMAT 98
Cdd:cd06606   8 LGKGSFGSVYLALNLdTGELMAVKEVELSGDSEEELE-ALEREIRILSSLKhpnivrylGTERTEN-----------TLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774  99 LF---IPGPTLSEQVKRNGPMDEPQLRRLMAGLAEALRDIHRVGVVHRDLKPSNVLLAEDGP-KVIDFGISRPK-DSELR 173
Cdd:cd06606  76 IFleyVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVvKLADFGCAKRLaEIATG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21221774 174 TETGKLIGTPPYMAPEQFRRpREVGPAADVFTLGSLMVHAATGRGPF-DSDSPYVVAYQVVHDEpDLTGVPDSLAP---- 248
Cdd:cd06606 156 EG