|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
15-499 |
1.72e-144 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 420.74 E-value: 1.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQNDEAPT 94
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 95 ATAQPDTSRTAQAAATQESAAngnetngtgrtavlvgygpegetasrrrrpaapkpetsaefssETAAAQPDSPDTESGP 174
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAA-------------------------------------------AAAAAAPAAAAAPAAP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 175 SPqhaestaaetmsgnarpqlstTRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAvpvsqsrtmASQAESTA 254
Cdd:PRK11856 121 AA---------------------AAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA---------AAAAAPAA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 255 TPPAVPASGDGVSPPAREVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDHLRTTKsfagLTLTPLALVA 334
Cdd:PRK11856 171 AAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIG----VKLTVTDFLI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 335 KSALAAIAEFPGINTYWDEanQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLR 414
Cdd:PRK11856 247 KAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQ 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 415 GGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTASLLED 494
Cdd:PRK11856 325 GGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
....*
gi 2067492521 495 PLTLL 499
Cdd:PRK11856 405 PALLL 409
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
5-499 |
6.72e-106 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 326.39 E-value: 6.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 5 APQQSQGNVLEFRLPDLGEgLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPL 84
Cdd:PRK11855 111 AAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 85 IRVQNDEAPTATAQPDTSRTAQAAATQESAAngnetngtgrtavlvgygpegetasrrrrpaAPKPETSAefssetAAAQ 164
Cdd:PRK11855 190 VVIEVAAAAPAAAAAPAAAAPAAAAAAAPAP-------------------------------APAAAAAP------AAAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 165 PDSPDTESGpspqhaestaaetmsgnarpqlsttRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVpvsqSR 244
Cdd:PRK11855 233 PAAAAAPGK-------------------------APHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFV----KG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 245 TMASQAESTATPPAVPASGDGVSPPAR-------EVRT-PVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDHL 316
Cdd:PRK11855 284 AMSAAAAAAAAAAAAGGGGLGLLPWPKvdfskfgEIETkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 317 RTTKSFAGLTLTPLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREI 396
Cdd:PRK11855 364 KKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 397 GWLAETARSGGASPTDLRGGTFTITNVGVFG--VDTgvPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHR 474
Cdd:PRK11855 444 AELAKKARDGKLKPDDMQGGCFTISSLGGIGgtAFT--PIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHR 521
|
490 500
....*....|....*....|....*
gi 2067492521 475 MIDGELASRFLATTASLLEDPLTLL 499
Cdd:PRK11855 522 VIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
288-499 |
4.70e-84 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 258.63 E-value: 4.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 288 MLASARSIPQASTFVTVDCTASMELLDHLRTTKSFAGLTLTPLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLG 367
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 368 IAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGS 447
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2067492521 448 IRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTASLLEDPLTLL 499
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
15-499 |
3.78e-77 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 247.44 E-value: 3.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVqndeapt 94
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRI------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 95 ataqpdtsRTAQAAATQESAangnetngtgrtavlvgygpegetasrrrrPAAPKPETSAEFSSETAAAQPDSPDtesgp 174
Cdd:PRK05704 77 --------DEGAAAGAAAAA------------------------------AAAAAAAAAAPAQAQAAAAAEQSND----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 175 spqhaestaaetmsgnarpqlsttrpAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPvsqsrtmASQAESTA 254
Cdd:PRK05704 114 --------------------------ALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA-------AAAAAPAA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 255 TPPAVPASGDGVSPPAREVRTPVSGIRKRTA---------AAMLasarsipqaSTFVTVDCTASMELldhlRTTKSFA-- 323
Cdd:PRK05704 161 PAAAAPAAAPAPLGARPEERVPMTRLRKTIAerlleaqntTAML---------TTFNEVDMTPVMDL----RKQYKDAfe 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 324 ---GLTLTPLALVAKSALAAIAEFPGINTYWDeaNQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLA 400
Cdd:PRK05704 228 kkhGVKLGFMSFFVKAVVEALKRYPEVNASID--GDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 401 ETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGEL 480
Cdd:PRK05704 306 KKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKE 385
|
490
....*....|....*....
gi 2067492521 481 ASRFLATTASLLEDPLTLL 499
Cdd:PRK05704 386 AVGFLVTIKELLEDPERLL 404
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
5-499 |
4.81e-77 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 253.77 E-value: 4.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 5 APQQSQGNVLEFRLPDLGEGlaDAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGApL 84
Cdd:PRK11854 97 AAAPAAAAAKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGS-L 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 85 IRVQNDEAPTATAQPDTSRTAQAAATQESAANGNETN----GTGR---TAVLVGYGP-----------EGETASR----- 141
Cdd:PRK11854 174 IMVFEVAGEAPAAAPAAAEAAAPAAAPAAAAGVKDVNvpdiGGDEvevTEVMVKVGDkveaeqslitvEGDKASMevpap 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 142 -------------------------RRRPAAPKPETSAEFSSETAAAQPDSPDTESGPSPqhAESTAAETMSGNARPQls 196
Cdd:PRK11854 254 fagtvkeikvnvgdkvktgslimrfEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAA--KAEGKSEFAENDAYVH-- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 197 ttrpaATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVpvsqsRTMASQAESTATPPAVPASGDGVSP-----PAR 271
Cdd:PRK11854 330 -----ATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV-----KDAVKRAEAAPAAAAAGGGGPGLLPwpkvdFSK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 272 --EVRT-PVSGIRKRTAAAMLASARSIPQASTFVTVDCTAsmelLDHLRTT------KSFAGLTLTPLALVAKSALAAIA 342
Cdd:PRK11854 400 fgEIEEvELGRIQKISGANLHRNWVMIPHVTQFDKADITE----LEAFRKQqnaeaeKRKLGVKITPLVFIMKAVAAALE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 343 EFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLRGGTFTITN 422
Cdd:PRK11854 476 QMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISS 555
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067492521 423 VGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTASLLEDPLTLL 499
Cdd:PRK11854 556 IGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
15-499 |
2.65e-74 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 240.02 E-value: 2.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQndeapt 94
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 95 ataqpdtsrtaqaaatqESAANGNEtngtgrtavlvgygpegetasrrrrPAAPKPETSAEFSSETAAAQPDSPDTesgp 174
Cdd:TIGR01347 76 -----------------EGNDATAA-------------------------PPAKSGEEKEETPAASAAAAPTAAAN---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 175 spqhaestaaetmsgnarpqlsttRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVrgavpvsqsrTMASQAESTA 254
Cdd:TIGR01347 110 ------------------------RPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI----------IKKTEAPASA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 255 TPPAVPA-SGDGVSPPAREVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELldHLRTTKSFA---GLTLTPL 330
Cdd:TIGR01347 156 QPPAAAAaAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMEL--RKRYKEEFEkkhGVKLGFM 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 331 ALVAKSALAAIAEFPGINTYWDeaNQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASP 410
Cdd:TIGR01347 234 SFFVKAVVAALKRFPEVNAEID--GDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 411 TDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTAS 490
Cdd:TIGR01347 312 EDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKE 391
|
....*....
gi 2067492521 491 LLEDPLTLL 499
Cdd:TIGR01347 392 LLEDPRRLL 400
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
18-499 |
2.46e-66 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 219.94 E-value: 2.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 18 LPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQNDEAPTATA 97
Cdd:PTZ00144 49 VPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 98 qpdtsrtaqAAAtqesaangnetngtgrtavlvgygpegetasrrrrPAAPKPETSAEFSSETAAAQPDSPDTesgPSPQ 177
Cdd:PTZ00144 129 ---------PAA-----------------------------------AAAAKAEKTTPEKPKAAAPTPEPPAA---SKPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 178 HAESTaaetmsgnarpqlsttRPAATPAArrlarelgidlwfvagsgpdgavtvedvrgavpvsqsrtmasqaestATPP 257
Cdd:PTZ00144 162 PPAAA----------------KPPEPAPA-----------------------------------------------AKPP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 258 AVPASGDGvsppAREVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDHLRT--TKSFaGLTLTPLALVAK 335
Cdd:PTZ00144 179 PTPVARAD----PRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDdfQKKH-GVKLGFMSAFVK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 336 SALAAIAEFPGINTYWDeaNQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLRG 415
Cdd:PTZ00144 254 ASTIALKKMPIVNAYID--GDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 416 GTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTASLLEDP 495
Cdd:PTZ00144 332 GTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDP 411
|
....
gi 2067492521 496 LTLL 499
Cdd:PTZ00144 412 ARML 415
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-494 |
6.07e-65 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 220.65 E-value: 6.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 2 EDRAPQQSQGNVLEFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVG 81
Cdd:TIGR02927 115 PAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 82 APLIRVqnDEAPTATAQPdtsrtaqaaatqesaangnetngtgrtavlvgygPEGETASRRRRPAAPKPETSAEfssETA 161
Cdd:TIGR02927 195 TVLAII--GDANAAPAEP----------------------------------AEEEAPAPSEAGSEPAPDPAAR---APH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 162 AAQPDSPDTESGPSPQHAESTAAETMSGNArpqlsttrPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVS 241
Cdd:TIGR02927 236 AAPDPPAPAPAPAKTAAPAAAAPVSSGDSG--------PYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 242 QSRTMASQAESTATPPAVPASGDGVSPPA----REVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELldHLR 317
Cdd:TIGR02927 308 EEARAAAAAPAAAAAPAAPAAAAKPAEPDtaklRGTTQKMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAAL--RAR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 318 TTKSFA---GLTLTPLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTR 394
Cdd:TIGR02927 386 AKNDFLeknGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAK 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 395 EIGWLAETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDE-----LAIRWVTTLGI 469
Cdd:TIGR02927 466 AINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEdggesIAIRSVCYLPL 545
|
490 500
....*....|....*....|....*
gi 2067492521 470 SFDHRMIDGELASRFLATTASLLED 494
Cdd:TIGR02927 546 TYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
18-499 |
9.62e-65 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 216.20 E-value: 9.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 18 LPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPG-ETVLVGAPLirvqndeaptat 96
Cdd:TIGR01349 4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPI------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 97 aqpdtsrtaqaaatqesaangnetngtgrtAVLVGYGPEGETASrrrrpAAPKPETSAEFSSETAAAQPDSPDTESGPSP 176
Cdd:TIGR01349 72 ------------------------------AVLVEEKEDVADAF-----KNYKLESSASPAPKPSEIAPTAPPSAPKPSP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 177 QHAESTAAETMSGNARPQLSTTRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQsrTMASQAESTATP 256
Cdd:TIGR01349 117 APQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSP--ASANQQAAATTP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 257 PAVPASGDGvsPPAREVRTPVSGIRKRTAAAMLASARSIPqaSTFVTVDCTASmELLDhLRT--TKSFAGLT-LTPLALV 333
Cdd:TIGR01349 195 ATYPAAAPV--STGSYEDVPLSNIRKIIAKRLLESKQTIP--HYYVSIECNVD-KLLA-LRKelNAMASEVYkLSVNDFI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 334 AKSALAAIAEFPGINTYWDEanQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDL 413
Cdd:TIGR01349 269 IKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 414 RGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDE---LAIRWVTTLGISFDHRMIDGELASRFLATTAS 490
Cdd:TIGR01349 347 QGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKK 426
|
....*....
gi 2067492521 491 LLEDPLTLL 499
Cdd:TIGR01349 427 YLENPIEML 435
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-499 |
5.90e-64 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 217.05 E-value: 5.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 5 APQQSQ-GNVLEFRLPDLGeGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAP 83
Cdd:TIGR01348 107 APAAGQsSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 84 LIRVQNDEAptataqpdtsrtAQAAATQESAAngnetngtgrtavlvgygpegetasrrrRPAAPKPETSAEfssetAAA 163
Cdd:TIGR01348 186 ILTLSVAGS------------TPATAPAPASA----------------------------QPAAQSPAATQP-----EPA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 164 QPDSPDTESGPSPQHAEStaaetmsgnarpQLSTTRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQS 243
Cdd:TIGR01348 221 AAPAAAKAQAPAPQQAGT------------QNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 244 RTMASQAESTATPPAVPASGDGVSPPAREVRT-PVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDHLRTTKSF 322
Cdd:TIGR01348 289 RAQAAAASAAGGAPGALPWPNVDFSKFGEVEEvDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 323 AGLTLTPLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAET 402
Cdd:TIGR01348 369 EGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 403 ARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELAS 482
Cdd:TIGR01348 449 ARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVIDGADAA 528
|
490
....*....|....*..
gi 2067492521 483 RFLATTASLLEDPLTLL 499
Cdd:TIGR01348 529 RFTTYICESLADIRRLL 545
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
16-499 |
1.18e-63 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 212.66 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 16 FRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVqndeapta 95
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 96 taqpdtsrtaqaaATQESAANGNETNGTgrtavlvgygpegetasrrrrpaapkPETSAEFSSETaaaqpdSPDTESgps 175
Cdd:PLN02528 73 -------------MVEDSQHLRSDSLLL--------------------------PTDSSNIVSLA------ESDERG--- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 176 pqhaeSTAAETMSgnarpqlsttrpaaTPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQSRTMASQAEStAT 255
Cdd:PLN02528 105 -----SNLSGVLS--------------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSAEE-AT 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 256 PPAVPASGDGVSPPA----REVRTPVSGIRKRTAAAMLASArSIPQastFVTVD---CTASMELLDHLRTTKSFAGLTLT 328
Cdd:PLN02528 165 IAEQEEFSTSVSTPTeqsyEDKTIPLRGFQRAMVKTMTAAA-KVPH---FHYVEeinVDALVELKASFQENNTDPTVKHT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 329 PLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGA 408
Cdd:PLN02528 241 FLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 409 SPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPwVFRDELAIRWVTTLGISF--DHRMIDGELASRFLA 486
Cdd:PLN02528 321 NPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVP-RFVDDGNVYPASIMTVTIgaDHRVLDGATVARFCN 399
|
490
....*....|...
gi 2067492521 487 TTASLLEDPLTLL 499
Cdd:PLN02528 400 EWKSYVEKPELLM 412
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
202-495 |
6.31e-55 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 186.54 E-value: 6.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 202 ATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQSRTMASQAESTATPPAVPASGDGVSPPAREV--RTPVSG 279
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEgkREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 280 IRKRTAAAMLASARSIPQASTFVTVDCTASMEL----LDHLRTTKsfaGLTLTPLALVAKSALAAIAEFPGINTYWDEAN 355
Cdd:PRK11857 84 IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLrksvKDPVLKTE---GVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 356 QEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLV 435
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 436 NPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATTASLLEDP 495
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
15-499 |
3.44e-44 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 163.49 E-value: 3.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAqpGEtvlvGAPLIRVQNDEAPT 94
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVK--GD----GAKEIKVGEVIAIT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 95 ATAQPDTSRtaqaaatqesaangnetngtgrtavLVGYGPEGETAsrrrrPAAPKPETSAEFSSETAAAQPDSPdtesgP 174
Cdd:PLN02744 188 VEEEEDIGK-------------------------FKDYKPSSSAA-----PAAPKAKPSPPPPKEEEVEKPASS-----P 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 175 SPQhAESTAAETMSGNarpqlsttRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVpvsqsrtmASQAESTA 254
Cdd:PLN02744 233 EPK-ASKPSAPPSSGD--------RIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYL--------ASGGKGAT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 255 TPPAVPASGDGVSpparEVRTPVSGIRKRTAAAMLASARSIPQasTFVTVDCTAS--MELLDHLRTTK-SFAGLTLTPLA 331
Cdd:PLN02744 296 APPSTDSKAPALD----YTDIPNTQIRKVTASRLLQSKQTIPH--YYLTVDTRVDklMALRSQLNSLQeASGGKKISVND 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 332 LVAKSALAAIAEFPGINTYWdeANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPT 411
Cdd:PLN02744 370 LVIKAAALALRKVPQCNSSW--TDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 412 DLRGGTFTITNV-GVFGVDTGVPLVNPGEAAILCLGSIRKR--PWVFRDELAIRWVTTLGISFDHRMIDGELASRFLATT 488
Cdd:PLN02744 448 DYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAF 527
|
490
....*....|.
gi 2067492521 489 ASLLEDPLTLL 499
Cdd:PLN02744 528 KGYIENPESML 538
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
202-499 |
3.73e-43 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 156.22 E-value: 3.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 202 ATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRG------------AVPVSQSRTMA---------------------- 247
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVETykdtnvvrisplAKRIALEHNIAwqeiqgtghrgkimkkdvlall 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 248 --SQAESTATPPA----VPASGDGVSPPAREVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDH-LRTTK 320
Cdd:PRK14843 88 peNIENDSIKSPAqiekVEEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 321 SFAGLTLTPLALVAKSALAAIAEFPGINTYWDEANQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLA 400
Cdd:PRK14843 168 EATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 401 ETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGEL 480
Cdd:PRK14843 248 GRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMA 327
|
330
....*....|....*....
gi 2067492521 481 ASRFLATTASLLEDPLTLL 499
Cdd:PRK14843 328 GAKFMKDLKELIETPISML 346
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
11-502 |
4.42e-38 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 145.28 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 11 GNVLEFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQnd 90
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIIS-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 91 eaptataqpdtsrtaqaaatqesaangnetngtgrtavlvgygpegetasrrrrpaapkpeTSAEFSSETAAAQ--PDSP 168
Cdd:PLN02226 167 -------------------------------------------------------------KSEDAASQVTPSQkiPETT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 169 DTESGPSPQHAEstaaetmsgnaRPQLSTTRPAATPaarrlarelgidlwfvagsgpdgavtvedvrgavpvsqsrtmas 248
Cdd:PLN02226 186 DPKPSPPAEDKQ-----------KPKVESAPVAEKP-------------------------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 249 QAESTATPPAVPASGDGVSPPAREVRTPVSGIRKRTAAAMLASARSIPQASTFVTVDCTASMELLDHLRTT-KSFAGLTL 327
Cdd:PLN02226 211 KAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAfYEKHGVKL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 328 TPLALVAKSALAAIAEFPGINTYWDeaNQEIVTKHYVNLGIAVAADRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGG 407
Cdd:PLN02226 291 GLMSGFIKAAVSALQHQPVVNAVID--GDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 408 ASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIRKRPWVFRDELAIRWVTTLGISFDHRMIDGELASRFLAT 487
Cdd:PLN02226 369 ISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRR 448
|
490
....*....|....*
gi 2067492521 488 TASLLEDPLTLLSRI 502
Cdd:PLN02226 449 VKDVVEDPQRLLLDI 463
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
15-87 |
9.39e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 102.84 E-value: 9.39e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRV 87
Cdd:COG0508 4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
15-87 |
1.43e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 99.40 E-value: 1.43e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067492521 15 EFRLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRV 87
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
155-492 |
3.11e-24 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 106.90 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 155 EFSSETAAAQPDSPDTESGPSPQHAESTAAETMSGNARPQLSTTRPAATPAArrlarelgidlwfvagsgpdgavtvedv 234
Cdd:PRK12270 31 EFFADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAA---------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 235 rGAVPVSQSRTMASQAESTATPPAVPASGDGVSPpareVRTPVSGIRKRTAAAMLASaRSIPQASTFVTVdctaSMELL- 313
Cdd:PRK12270 83 -PPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED----EVTPLRGAAAAVAKNMDAS-LEVPTATSVRAV----PAKLLi 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 314 -------DHLRTTK----SFagltlTPL---ALVAksalaAIAEFPGINTYWDEAN--QEIVTKHYVNLGIAV-----AA 372
Cdd:PRK12270 153 dnrivinNHLKRTRggkvSF-----THLigyALVQ-----ALKAFPNMNRHYAEVDgkPTLVTPAHVNLGLAIdlpkkDG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 373 DRGLLVPNIKEAQSLSLRDLTREIGWLAETARSGGASPTDLRGGTFTITNVGVFGVDTGVPLVNPGEAAILCLGSIrKRP 452
Cdd:PRK12270 223 SRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYP 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2067492521 453 WVFR-------DELAIRWVTTLGISFDHRMIDGELASRFLATTASLL 492
Cdd:PRK12270 302 AEFQgaseerlAELGISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
15-87 |
1.56e-15 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 71.09 E-value: 1.56e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067492521 15 EFRLPDLGEGLADAElVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRV 87
Cdd:pfam00364 2 EIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
18-131 |
7.78e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 69.97 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 18 LPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQNDEAPTATA 97
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEI 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 2067492521 98 QpdtsrtAQAAATQESAANG----NETNGTGRTAVLVG 131
Cdd:PRK14875 87 D------AFIAPFARRFAPEgideEDAGPAPRKARIGG 118
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
202-235 |
1.83e-12 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 61.55 E-value: 1.83e-12
10 20 30
....*....|....*....|....*....|....
gi 2067492521 202 ATPAARRLARELGIDLWFVAGSGPDGAVTVEDVR 235
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
30-87 |
1.01e-10 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 57.43 E-value: 1.01e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2067492521 30 LVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRV 87
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
17-87 |
2.28e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 50.90 E-value: 2.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067492521 17 RLPDLGEGLADAELVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRV 87
Cdd:cd06663 3 LIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
35-88 |
1.26e-06 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 47.58 E-value: 1.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2067492521 35 VGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQ 88
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
37-75 |
1.70e-06 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 47.04 E-value: 1.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2067492521 37 VGDEVALNQTIAEVETAKAVVALPSPFAGRVVE----LLAQPG 75
Cdd:COG0509 47 VGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVEvneaLEDDPE 89
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
37-75 |
8.61e-06 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 44.45 E-value: 8.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2067492521 37 VGDEVALNQTIAEVETAKAVVALPSPFAGRVVE----LLAQPG 75
Cdd:cd06848 39 VGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEvneaLLDNPE 81
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
72-276 |
1.89e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.29 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 72 AQPGETVLVGAPLIRVQNDEAPTATAQPDTSRTAQAAATQESAANGNETNGTGRTAVLVGYGPEGETASRRRRPAAPKPE 151
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKA 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 152 TSAEFSSETAAAQPDSPDTESGPSP--QHAESTAAETMSGNARPQLSTTRPAATPAARRLARELGIDLWFVAGSGPDGAV 229
Cdd:PRK07764 674 GGAAPAAPPPAPAPAAPAAPAGAAPaqPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAG 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2067492521 230 TVEDVRGA-VPVSQSRTMASQAESTATPPAVPASGDGVSPPAREVRTP 276
Cdd:PRK07764 754 APAQPPPPpAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA 801
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
35-88 |
3.80e-05 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 46.37 E-value: 3.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2067492521 35 VGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQ 88
Cdd:PRK09282 538 VKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
57-299 |
1.06e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 57 VALPSPFAGRVVELLAQPGETVLVGAPLIRVqndeAPTATAQPDTSRTAQAAATQESAANGNETNGTGRTAVLVGyGPEG 136
Cdd:PRK07003 380 VPAPGARAAAAVGASAVPAVTAVTGAAGAAL----APKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVP-AKAN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 137 ETASRRRRPAAPKPETSAEFSSETAAAQPDSPDTESGPSPQHAESTAAETMSGN----------------ARPQLSTTRP 200
Cdd:PRK07003 455 ARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPdarapaaasredapaaAAPPAPEARP 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 201 AAtPAARRLARELGidlwfvagsgpdGAVTVEDV-RGA-VPVSQSRTMASQAesTATPPAVPASGDGVSPPAREVRTPVS 278
Cdd:PRK07003 535 PT-PAAAAPAARAG------------GAAAALDVlRNAgMRVSSDRGARAAA--AAKPAAAPAAAPKPAAPRVAVQVPTP 599
|
250 260
....*....|....*....|.
gi 2067492521 279 GIRKRTAAAMLASARSIPQAS 299
Cdd:PRK07003 600 RARAATGDAPPNGAARAEQAA 620
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
89-299 |
5.26e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 42.64 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 89 NDEAPTATAQPDTSRTAQAAATQESAANGNETNGTG---RTAVLVGYGPEGETASRRRRPAAPKPETSAEFSSETAAAqp 165
Cdd:pfam17823 59 NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGtdlSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAA-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 166 dsPDTESGPSPQHAESTAAETMSGNARPQLSTTRPAATPAARRLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQSRT 245
Cdd:pfam17823 137 --LPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGIST 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2067492521 246 MASqaeSTATPPA--VPASGDGVSPPAREVRTPVSGIRKRTAAAMLASARSIPQAS 299
Cdd:pfam17823 215 AAT---ATGHPAAgtALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAA 267
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
35-88 |
8.07e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 8.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2067492521 35 VGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQ 88
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
30-88 |
9.75e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 41.63 E-value: 9.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2067492521 30 LVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPGETVLVGAPLIRVQ 88
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
64-205 |
1.63e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 64 AGRVVELLAQPGETVLVGAPLIRVQNDEAPTATAQPDTSRTAQAAATQESAANGNETNGTGRTAVLVGYGPEGETASRRR 143
Cdd:PRK13108 288 SEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETS 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067492521 144 RPAAPKPETSA---------EFSSETAAAQPDSPDTESGPSPQHAESTAAETMSGNARP----QLSTTRPAATPA 205
Cdd:PRK13108 368 EADIEREQPGDlagqapaahQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPakpdELAVAGPGDDPA 442
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
26-98 |
1.66e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 26 ADAELVSWSVGVGDEVALNQTIAEVETAKAVVA----------LPSPFAGRVVELLAQPGETVLVGAPLIRVQNDEAPTA 95
Cdd:COG1566 167 AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAqaelnlarttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWV 246
|
...
gi 2067492521 96 TAQ 98
Cdd:COG1566 247 EAY 249
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
40-91 |
2.55e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.93 E-value: 2.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067492521 40 EVALNQTIAEVETAKAVVA----------LPSPFAGRVVELLAQPGETVLVGAPLIRVQNDE 91
Cdd:COG0845 105 KAALDQAQAALAAAQAALEqaranlayttIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLD 166
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
134-293 |
2.81e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 134 PEGETASRRRRPAAPKPETSAEFSSETAAAQPD-SPDTESGPSPQHAESTAAETMSGNARPQLST-----TRPAATPAAR 207
Cdd:PRK07764 365 PSASDDERGLLARLERLERRLGVAGGAGAPAAAaPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPqpapaPAPAPAPPSP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 208 RLARELGIDLWFVAGSGPDGAVTVEDVRGAVPVSQSRTMASQAESTATPPAVPASGDGVSPPAR---------EVRTPVS 278
Cdd:PRK07764 445 AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDaatlrerwpEILAAVP 524
|
170
....*....|....*
gi 2067492521 279 GIRKRTAAAMLASAR 293
Cdd:PRK07764 525 KRSRKTWAILLPEAT 539
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
30-146 |
2.92e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.90 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 30 LVSWSVGVGDEVALNQTIAEVETAKAVVALPSPFAGRVVELLAQPG-ETVLVGAPlIRVQNDEAPTATAQPDTSRTAQAA 108
Cdd:PRK11892 19 LAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTP-IAVLLEEGESASDAGAAPAAAAEA 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 2067492521 109 ATQESAANGNETNGTGRTAVLVGYGPEGETASRRRRPA 146
Cdd:PRK11892 98 AAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPA 135
|
|
| PRK01202 |
PRK01202 |
glycine cleavage system protein GcvH; |
37-78 |
4.64e-03 |
|
glycine cleavage system protein GcvH;
Pssm-ID: 234918 Cd Length: 127 Bit Score: 37.06 E-value: 4.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2067492521 37 VGDEVALNQTIAEVETAKAVVALPSPFAGRVVE----LLAQPgETV 78
Cdd:PRK01202 47 VGDEVKAGETFGVVESVKAASDIYAPVSGEVVEvneaLEDSP-ELV 91
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
88-292 |
5.32e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.47 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 88 QNDEAPTATAQPDTSRTAQAAATQESAANGNETNGTGRTAVLVGYGPEGETASRRRRPAAPKPET--SAEFSSETAAAQP 165
Cdd:PRK12323 368 SGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAlaAARQASARGPGGA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067492521 166 DSPDTESGPSPQHAESTAAETMSGNARPQLSTTRPAAtPAARRLARELGIDLW-----FVAGSGPDGAVTVedVRGAVPV 240
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAA-PAAAPAPADDDPPPWeelppEFASPAPAQPDAA--PAGWVAE 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2067492521 241 SQSRTMASQAESTATPPAVPASGDGVSPPAREVRTPVSGIRKRTAAAMLASA 292
Cdd:PRK12323 525 SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
|
|
| |
