|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-439 |
0e+00 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 626.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 2 ADLIELKVPDIGDFDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESsd 81
Cdd:PRK11855 117 GGVVEVKVPDIGEITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEV-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 82 AGAEENEKPAEKAAESKPAEKEKPAAAESKPAPTPTVANPEPertetlpyapdtGSAKKPSHASPSVRQFARELGVPLAA 161
Cdd:PRK11855 195 AAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAA------------AAPGKAPHASPAVRRLARELGVDLSQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 162 VVGSGQKGRITKEDVQNFVKQVMNAPAPKAAD-------GAGIPSVPVVNFEQFGEIESKELSRIKKISGKHLHACWLNI 234
Cdd:PRK11855 263 VKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAaaaagggGLGLLPWPKVDFSKFGEIETKPLSRIKKISAANLHRSWVTI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 235 PHVTQFDEADITELEEFRQENKEMAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIGVAVDTPNG 314
Cdd:PRK11855 343 PHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 315 LMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWN 394
Cdd:PRK11855 423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWD 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2535551012 395 GKEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:PRK11855 503 GKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
6-439 |
0e+00 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 567.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 6 ELKVPDIGDfDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIEssDAGAE 85
Cdd:PRK11854 208 DVNVPDIGG-DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE--VEGAA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 86 ENEKPAEKAAESKPAEKEKPAAAESKPAPTPTVANPEPERTEtlpYApdtgsakkpsHASPSVRQFARELGVPLAAVVGS 165
Cdd:PRK11854 285 PAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDA---YV----------HATPLVRRLAREFGVNLAKVKGT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 166 GQKGRITKEDVQNFVKQVM----NAPAPKAADGA--GIPSVPVVNFEQFGEIESKELSRIKKISGKHLHACWLNIPHVTQ 239
Cdd:PRK11854 352 GRKGRILKEDVQAYVKDAVkraeAAPAAAAAGGGgpGLLPWPKVDFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 240 FDEADITELEEFRQENKEMAAKK--GVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIGVAVDTPNGLMV 317
Cdd:PRK11854 432 FDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 318 PVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKE 397
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKE 591
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2535551012 398 FEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:PRK11854 592 FAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-439 |
0e+00 |
|
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: 535.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 2 ADLIELKVPDIGDFDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESSD 81
Cdd:TIGR01348 114 SGVQEVTVPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 82 AG--AEENEKPAEKAAESKPAEKEKPAAAeskPAPTPTvanpeperTETLPYAPDTGSAKKPSHASPSVRQFARELGVPL 159
Cdd:TIGR01348 194 STpaTAPAPASAQPAAQSPAATQPEPAAA---PAAAKA--------QAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 160 AAVVGSGQKGRITKEDVQNFVK-QVMNAPAPKAADGAGIPSV---PVVNFEQFGEIESKELSRIKKISGKHLHACWLNIP 235
Cdd:TIGR01348 263 SAVKGTGIKGRILREDVQRFVKePSVRAQAAAASAAGGAPGAlpwPNVDFSKFGEVEEVDMSRIRKISGANLTRNWTMIP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 236 HVTQFDEADITELEEFRQENKEMAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIGVAVDTPNGL 315
Cdd:TIGR01348 343 HVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 316 MVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNG 395
Cdd:TIGR01348 423 LVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNG 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2535551012 396 KEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:TIGR01348 503 KEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-433 |
6.64e-152 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 436.91 E-value: 6.64e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 5 IELKVPDIGDF-DSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIEssdAG 83
Cdd:PRK11856 3 FEFKMPDLGEGmTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE---EE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 84 AEENEKPAEKAAESKPAEKEKPAAAESKPAPTPTVANPEPErtetlpyapdtgsAKKPSHASPSVRQFARELGVPLAAVV 163
Cdd:PRK11856 80 GEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAP-------------AAAAAKASPAVRKLARELGVDLSTVK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 164 GSGQKGRITKEDVQNFVKQvmnaPAPKAADGAGIPSVPVVNFEQFGEIEskELSRIKKISGKHLHACWLNIPHVTQFDEA 243
Cdd:PRK11856 147 GSGPGGRITKEDVEAAAAA----AAPAAAAAAAAAAAPPAAAAEGEERV--PLSGMRKAIAKRMVESKREIPHFTLTDEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 244 DITELEEFRQENKEMAAKkgvsLTPLVFIMKAVVACLRQYPEFNASLSEDKqsLIYKKYYNIGVAVDTPNGLMVPVIRDV 323
Cdd:PRK11856 221 DVTALLALRKQLKAIGVK----LTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 324 DKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKEFEPRLM 403
Cdd:PRK11856 295 DKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKV 374
|
410 420 430
....*....|....*....|....*....|
gi 2535551012 404 LPLSISYDHRVIDGAAGARFTVMLNQMLSD 433
Cdd:PRK11856 375 MPLSLSFDHRVIDGADAARFLKALKELLEN 404
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
227-438 |
4.10e-102 |
|
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: 302.54 E-value: 4.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 227 LHACWLNIPHVTQFDEADITELEEFRQENKEMAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIG 306
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 307 VAVDTPNGLMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSR 386
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2535551012 387 HQMKPVWNGKEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVL 438
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-439 |
3.00e-92 |
|
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: 284.32 E-value: 3.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 5 IELKVPDIGDfdsvEIIEVLVAE-----GDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIEs 79
Cdd:TIGR01347 1 IEIKVPELAE----SITEGTVAEwhkkvGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 80 sdagaEENEKPAEKAAESKPaEKEKPAAAESKPAPTptvanpepertetlpyapdtgSAKKPSHASPSVRQFARELGVPL 159
Cdd:TIGR01347 76 -----EGNDATAAPPAKSGE-EKEETPAASAAAAPT---------------------AAANRPSLSPAARRLAKEHGIDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 160 AAVVGSGQKGRITKEDVQNFVKQVMNAPAPKAADGAGIPsvpvvnfEQFGEIESKE-LSRIKKISGKHLHACWLNIPHVT 238
Cdd:TIGR01347 129 SAVPGTGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAP-------AAATRPEERVkMTRLRQRIAERLKEAQNSTAMLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 239 QFDEADITELEEFRQENKEMAAKK-GVSLTPLVFIMKAVVACLRQYPEFNASLseDKQSLIYKKYYNIGVAVDTPNGLMV 317
Cdd:TIGR01347 202 TFNEVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEI--DGDDIVYKDYYDISVAVSTDRGLVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 318 PVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKE 397
Cdd:TIGR01347 280 PVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQ 359
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2535551012 398 FEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:TIGR01347 360 IEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
5-439 |
7.39e-92 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 283.65 E-value: 7.39e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 5 IELKVPDIGDfdSVE---IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALI-ESS 80
Cdd:PRK05704 3 VEIKVPTLPE--SVTeatIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIdEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 81 DAGAEENEKPAEKAAESKPAEKEKPAAAESKPAPtptvanpepertetlpyapdtgsakkpshASPSVRQFARELGVPLA 160
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-----------------------------LSPAARKLAAENGLDAS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 161 AVVGSGQKGRITKEDVQNFVKQVMNAPAPKAADGAGIPSVPvvnfeQFGEIESKE-LSRIKKISGKHLHACWLNIPHVTQ 239
Cdd:PRK05704 132 AVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAP-----LGARPEERVpMTRLRKTIAERLLEAQNTTAMLTT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 240 FDEADITELEEFRQENKEMAAKK-GVSLTPLVFIMKAVVACLRQYPEFNASLseDKQSLIYKKYYNIGVAVDTPNGLMVP 318
Cdd:PRK05704 207 FNEVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASI--DGDDIVYHNYYDIGIAVGTPRGLVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 319 VIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSlGGIGGQFF-TPIVNAPEVAILGVSRHQMKPVWNGKE 397
Cdd:PRK05704 285 VLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN-GGVFGSLMsTPIINPPQSAILGMHKIKERPVAVNGQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2535551012 398 FEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:PRK05704 364 IVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-431 |
7.37e-73 |
|
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: 239.53 E-value: 7.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 6 ELKVPDIGDfdSVE---IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIesSDA 82
Cdd:TIGR02927 128 EVKMPELGE--SVTegtVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII--GDA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 83 GAEENEKPAEKA---AESKPAEKEKPAAAESKPAPTPTVANPEPERTETLPYAPDTGSAKKPSHASPSVRQFARELGVPL 159
Cdd:TIGR02927 204 NAAPAEPAEEEApapSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 160 AAVVGSGQKGRITKEDV------QNFVKQVMNAPAPKAADGAGIPSVPVVNFEQFG-EIESKELSRIKKISGKHLHACWL 232
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVlaaakaAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKlRGTTQKMNRIRQITADKTIESLQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 233 NIPHVTQFDEADITELEEFRQENK-EMAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIGVAVDT 311
Cdd:TIGR02927 364 TSAQLTQVHEVDMTRVAALRARAKnDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 312 PNGLMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKP 391
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRP 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2535551012 392 V-----WNGKEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQML 431
Cdd:TIGR02927 524 RvikdeDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRL 568
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
24-439 |
7.57e-68 |
|
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: 222.36 E-value: 7.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 24 LVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDK-VSEGSVIALI--ESSD-AGAEENEKPAEKAAE-SK 98
Cdd:TIGR01349 20 LKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdVPVNKPIAVLveEKEDvADAFKNYKLESSASPaPK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 99 PAEKEkPAAAESKPAPTPTvanPEPERTETLPYAPDT-GSAKKPSHASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQ 177
Cdd:TIGR01349 100 PSEIA-PTAPPSAPKPSPA---PQKQSPEPSSPAPLSdKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 178 NFVKQVMnAPAPKAADGAGIPSVPVVNFEQFGEIESKELSRIKKISGKHLHACWLNIPHVTQFDEADITELEEFRQENKE 257
Cdd:TIGR01349 176 SFVPQSP-ASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 258 MAAKKgVSLTPLVFIMKAVVACLRQYPEFNASLSEdkQSLIYKKYYNIGVAVDTPNGLMVPVIRDVDKKGFLELAGELGE 337
Cdd:TIGR01349 255 MASEV-YKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 338 ISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKE---FEPRLMLPLSISYDHRV 414
Cdd:TIGR01349 332 LAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVASIMSVTLSCDHRV 411
|
410 420
....*....|....*....|....*
gi 2535551012 415 IDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:TIGR01349 412 IDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
18-423 |
7.44e-67 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 219.21 E-value: 7.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 18 VEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESSDAGAEENEKPAEKAAES 97
Cdd:PLN02528 13 CELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLLLPTDSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 98 KPAEkekpaAAESKpaptptvanpepertetlpyapDTGSAKKPSHASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQ 177
Cdd:PLN02528 93 NIVS-----LAESD----------------------ERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 178 NFVKQVMNAPAPKAADGAGIPSVPVVnfEQFGEIESKELSRIKKISGKHLH-------ACWLNIPHVTQFDEAD---ITE 247
Cdd:PLN02528 146 KYAAQKGVVKDSSSAEEATIAEQEEF--STSVSTPTEQSYEDKTIPLRGFQramvktmTAAAKVPHFHYVEEINvdaLVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 248 LEEFRQENKEMAakkGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKKYYNIGVAVDTPNGLMVPVIRDVDKKG 327
Cdd:PLN02528 224 LKASFQENNTDP---TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 328 FLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKEF-EPRLMLPL 406
Cdd:PLN02528 301 LLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNvYPASIMTV 380
|
410
....*....|....*..
gi 2535551012 407 SISYDHRVIDGAAGARF 423
Cdd:PLN02528 381 TIGADHRVLDGATVARF 397
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
3-439 |
7.33e-65 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 214.16 E-value: 7.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 3 DLIELKVPDIGD-FDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESSD 81
Cdd:PTZ00144 43 SIKVIKVPTMGDsISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 82 A-GAEENEKPAEKAAESKPAEKEKPAAAESKPAPTPTVANPEPERTETLPYAPdtgsakkPSHASPSVRQFARELGVPLa 160
Cdd:PTZ00144 123 ApPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAA-------KPPPTPVARADPRETRVPM- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 161 avvgsgqkgritkedvqnfvkqvmnapapkaadgagipsvpvvnfeqfgeieskelSRIKKISGKHLHACWLNIPHVTQF 240
Cdd:PTZ00144 195 --------------------------------------------------------SRMRQRIAERLKASQNTCAMLTTF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 241 DEADITELEEFRQENKEMAAKK-GVSLTPLVFIMKAVVACLRQYPEFNASLSEDKqsLIYKKYYNIGVAVDTPNGLMVPV 319
Cdd:PTZ00144 219 NECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 320 IRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKEFE 399
Cdd:PTZ00144 297 IRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIV 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2535551012 400 PRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:PTZ00144 377 IRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
27-423 |
1.65e-56 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 195.07 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 27 EGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDK-VSEGSVIALI--ESSDAGAEENEKPAEKAAESKPAEKE 103
Cdd:PLN02744 136 EGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIAITveEEEDIGKFKDYKPSSSAAPAAPKAKP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 104 KPAAAESKPAPTPTVAnPEPERTETlPYAPDTGSAkkpSHASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQNFVKQV 183
Cdd:PLN02744 216 SPPPPKEEEVEKPASS-PEPKASKP-SAPPSSGDR---IFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 184 MNAPAPKAADGAGIPSVPVVNFEQfgeieskelSRIKKISGKHLHACWLNIPHVTQFDEADITELEEFRQE---NKEMAA 260
Cdd:PLN02744 291 GKGATAPPSTDSKAPALDYTDIPN---------TQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQlnsLQEASG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 261 KKGVSLTPLVfiMKAVVACLRQYPEFNASLSEDkqsliYKKYY---NIGVAVDTPNGLMVPVIRDVDKKGFLELAGELGE 337
Cdd:PLN02744 362 GKKISVNDLV--IKAAALALRKVPQCNSSWTDD-----YIRQYhnvNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQ 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 338 ISVRAREGTLTAKDLQGGTFSISSLGG-IGGQFFTPIVNAPEVAIL--GVSRHQMKPVWNGKEFEPRLMLPLSISYDHRV 414
Cdd:PLN02744 435 LAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILavGSAEKRVIPGSGPDQYNFASFMSVTLSCDHRV 514
|
....*....
gi 2535551012 415 IDGAAGARF 423
Cdd:PLN02744 515 IDGAIGAEW 523
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
144-431 |
3.45e-56 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 188.08 E-value: 3.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 144 ASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQNFVKQVMNAPAPKAAdgAGIPSV--------PVVNFEQFgEIESKE 215
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEA--ASVSSAqqaaktaaPAAAPPKL-EGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 216 LSRIKKISGKHLHACWLNIPHVTQFDEADITELEEFRQENKEMAAK-KGVSLTPLVFIMKAVVACLRQYPEFNASLSEDK 294
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKtEGVKLTFLPFIAKAILIALKEFPIFAAKYDEAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 295 QSLIYKKYYNIGVAVDTPNGLMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIV 374
Cdd:PRK11857 161 SELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2535551012 375 NAPEVAILGVSRHQMKPVWNGKEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQML 431
Cdd:PRK11857 241 NYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-439 |
4.77e-49 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 173.40 E-value: 4.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 2 ADLIELKVPDIGD-FDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESS 80
Cdd:PLN02226 89 GDTVEAVVPHMGEsITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 81 dagaeenekpAEKAAESKPAEK--EKPAaaeskPAPTPTVANPEPERTETLPYApdtgsaKKPSHASPSvrqfarelgvp 158
Cdd:PLN02226 169 ----------EDAASQVTPSQKipETTD-----PKPSPPAEDKQKPKVESAPVA------EKPKAPSSP----------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 159 laavvgsgqkgritkedvqnfvkqvmnaPAPKAAdgAGIPSVPVVNFEQfgeieSKELSRIKKISGKHLHACWLNIPHVT 238
Cdd:PLN02226 217 ----------------------------PPPKQS--AKEPQLPPKERER-----RVPMTRLRKRVATRLKDSQNTFALLT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 239 QFDEADITELEEFRQENKE-MAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLseDKQSLIYKKYYNIGVAVDTPNGLMV 317
Cdd:PLN02226 262 TFNEVDMTNLMKLRSQYKDaFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVI--DGDDIIYRDYVDISIAVGTSKGLVV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 318 PVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSRHQMKPVWNGKE 397
Cdd:PLN02226 340 PVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGS 419
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2535551012 398 FEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSDIRKVLL 439
Cdd:PLN02226 420 VVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
145-433 |
4.61e-47 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 165.08 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 145 SPSVRQFARELGVPLAAVVGSGQKGRITKEDVQNFVKQvmNAPAPKAADGAGIPSVPVV--NFEQFGEIESKELSRIKKI 222
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPE--NIENDSIKSPAQIEKVEEVpdNVTPYGEIERIPMTPMRKV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 223 SGKHLHACWLNIPHVTQFDEADITELEEFRQENKE-MAAKKGVSLTPLVFIMKAVVACLRQYPEFNASLSEDKQSLIYKK 301
Cdd:PRK14843 130 IAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEpIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 302 YYNIGVAVDTPNGLMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAI 381
Cdd:PRK14843 210 YVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAI 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2535551012 382 LGVSRHQMKPVWNGKEFEPRLMLPLSISYDHRVIDGAAGARFTVMLNQMLSD 433
Cdd:PRK14843 290 LGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIET 341
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
5-77 |
2.98e-23 |
|
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: 92.82 E-value: 2.98e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535551012 5 IELKVPDIGD-FDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALI 77
Cdd:COG0508 3 IEIKMPDLGEsMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
5-77 |
1.11e-21 |
|
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: 88.23 E-value: 1.11e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535551012 5 IELKVPDIGD-FDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALI 77
Cdd:cd06849 1 TEIKMPDLGEsMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
6-77 |
3.55e-20 |
|
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: 84.19 E-value: 3.55e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2535551012 6 ELKVPDIGDFDSVEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALI 77
Cdd:pfam00364 2 EIKSPMIGESVREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
80-431 |
5.53e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 86.87 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 80 SDAGAEENEKPAEKAAESKPAEkEKPAAAESKPAPTPTVANPEPERTETLPYAPDTGSAKKPSHASPSVRQFARElgvPL 159
Cdd:PRK12270 34 ADYGPGSTAAPTAAAAAAAAAA-SAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAA---PA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 160 AAVVGSGQkgritkedvqnfvkQVMNAPApkaadgAGIpsvpVVNFEqfgeiESkelsrikkisgkhlhacwLNIPHVTQ 239
Cdd:PRK12270 110 AAAVEDEV--------------TPLRGAA------AAV----AKNMD-----AS------------------LEVPTATS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 240 FDEADITELEEFR-QENKEMAAKKG--VSLTPLvfIMKAVVACLRQYPEFNASLSED--KQSLIYKKYYNIGVAVDT--P 312
Cdd:PRK12270 143 VRAVPAKLLIDNRiVINNHLKRTRGgkVSFTHL--IGYALVQALKAFPNMNRHYAEVdgKPTLVTPAHVNLGLAIDLpkK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 313 NG---LMVPVIRDVDKKGFLELAGELGEISVRAREGTLTAKDLQGGTFSISSLGGIGGQFFTPIVNAPEVAILGVSrhQM 389
Cdd:PRK12270 221 DGsrqLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG--AM 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2535551012 390 K-PVwngkEFE---PRLMLPLSIS--------YDHRVIDGAAGARFTVMLNQML 431
Cdd:PRK12270 299 EyPA----EFQgasEERLAELGISkvmtltstYDHRIIQGAESGEFLRTIHQLL 348
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
143-177 |
4.91e-14 |
|
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: 65.79 E-value: 4.91e-14
10 20 30
....*....|....*....|....*....|....*
gi 2535551012 143 HASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQ 177
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
2.85e-12 |
|
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: 61.66 E-value: 2.85e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2535551012 20 IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALI 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
24-124 |
2.30e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 62.24 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 24 LVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVG-DKVSEGSVIALI--------ESSDAGAEENEKPAEKA 94
Cdd:PRK11892 23 LKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLleegesasDAGAAPAAAAEAAAAAP 102
|
90 100 110
....*....|....*....|....*....|
gi 2535551012 95 AESKPAEKEKPAAAESKPAPTPTVANPEPE 124
Cdd:PRK11892 103 AAAAAAAAKKAAPAPAAPAAPAAEVAADPD 132
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
23-78 |
5.69e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 52.48 E-value: 5.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2535551012 23 VLVAEGDSINADQEVITIESDKamMEIP--SSLSGTIKEMKVKVGDKVSEGSVIALIE 78
Cdd:PRK08225 15 IVVKVGDTVEEGQDVVILESMK--MEIPivAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
22-78 |
1.42e-08 |
|
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: 52.98 E-value: 1.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2535551012 22 EVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIE 78
Cdd:COG0511 80 KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-78 |
1.64e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 56.77 E-value: 1.64e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2535551012 20 IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIE 78
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
24-114 |
9.00e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 53.79 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 24 LVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIEssDAGAEENEKPAEKAAESKPAEKE 103
Cdd:PRK14875 23 LVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVA--DAEVSDAEIDAFIAPFARRFAPE 100
|
90
....*....|.
gi 2535551012 104 KPAAAESKPAP 114
Cdd:PRK14875 101 GIDEEDAGPAP 111
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-78 |
8.18e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 51.68 E-value: 8.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2535551012 20 IIEVLVAEGDSINADQEVITIEsdkAM-ME--IPSSLSGTIKEMKVKVGDKVSEGSVIALIE 78
Cdd:PRK12999 1087 VVTVLVKEGDEVKAGDPLAVIE---AMkMEttITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
18-71 |
1.75e-06 |
|
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: 45.51 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2535551012 18 VEIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEG 71
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-71 |
2.62e-06 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 50.08 E-value: 2.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2535551012 20 IIEVLVAEGDSINADQEVITIEsdkAM-ME--IPSSLSGTIKEMKVKVGDKVSEG 71
Cdd:COG1038 1087 VVKVLVKEGDEVKKGDPLLTIE---AMkMEttITAPRDGTVKEVLVKEGDQVEAG 1138
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
20-77 |
2.98e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 41.72 E-value: 2.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 20 IIEVLVAEGDSINADQEVITIESDKamMEIP--SSLSGTIKEMKVKVGDKVSEGSVIALI 77
Cdd:PRK05889 13 VLEVVVNEGDQIGKGDTLVLLESMK--MEIPvlAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
19-78 |
5.88e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 43.31 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 19 EIIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSviALIE 78
Cdd:PRK05641 94 KILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQ--PLIE 151
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
11-70 |
1.44e-04 |
|
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: 40.59 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 11 DIGDFDSVEIIEVlvaeGDSINADQEVITIESDKAMMEIPSSLSGTIkemkVKVGDKVSE 70
Cdd:cd06848 27 LLGDIVFVELPEV----GTEVKKGDPFGSVESVKAASDLYSPVSGEV----VEVNEALLD 78
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
20-80 |
1.77e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 43.94 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2535551012 20 IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIESS 80
Cdd:PRK14042 536 IIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVEVS 596
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
20-74 |
1.87e-04 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 43.77 E-value: 1.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2535551012 20 IIEVLVAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVI 74
Cdd:PRK14040 535 IFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| GCV_H |
pfam01597 |
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ... |
13-96 |
2.36e-04 |
|
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Pssm-ID: 396258 Cd Length: 122 Bit Score: 40.78 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 13 GDFDSVEIIEVlvaeGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVS-------EGSVIALIESSDAGAE 85
Cdd:pfam01597 31 GDIVFVELPEV----GTKVKKGESLAAIESVKAASPIYAPVSGEVVEVNEKLEDNPGlinkdpyEDGWIAKLKPSNLEEL 106
|
90
....*....|.
gi 2535551012 86 ENEKPAEKAAE 96
Cdd:pfam01597 107 ESLMTAEQYEK 117
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
13-59 |
3.06e-04 |
|
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: 40.49 E-value: 3.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2535551012 13 GDFDSVEIIEVlvaeGDSINADQEVITIESDKAMMEIPSSLSGTIKE 59
Cdd:COG0509 37 GDIVFVELPEV----GTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
48-79 |
4.71e-04 |
|
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: 38.17 E-value: 4.71e-04
10 20 30
....*....|....*....|....*....|..
gi 2535551012 48 EIPSSLSGTIKEMKVKVGDKVSEGSVIALIES 79
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEA 32
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
25-79 |
7.06e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 7.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2535551012 25 VAEGDSINADQEVITIESDKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIES 79
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
45-286 |
1.12e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 41.47 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 45 AMMEIPSSLSGTIKEMKVKVGDKVS-EGSVIALIESSDAGAEENEKPAEKAAESKPAEKEKPAAAESKPAPTPTVANPEP 123
Cdd:PRK14954 338 AVMQMTDFLMKTQGELKFQFEYQFRfELALLRLIELVRNDGGVAPSPAGSPDVKKKAPEPDLPQPDRHPGPAKPEAPGAR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 124 ERTETLPYAPDTGSAKKPSHASPSVRQFARELGVPLAAVVGSGQKGRITKEDVQNFVKQ-VMNAPA-PKAADGAGIPSV- 200
Cdd:PRK14954 418 PAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPGVDLGSWQGKFMNFTRNgSRKQPVqASSSDAAQTGVFe 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 201 PVVNFEQF----GEIESKELSRIKKISGKHLHACWLN--IPH-VTQFDEADITELEEFRQE----NKEMAAKKGVSLTPL 269
Cdd:PRK14954 498 GVAELEKLrmewNQFLEHLLKKGQKVLVTHLRSCELTscSPHgVVVMTCCRKFSYEELMQDaallSKEIESFYGIPLKLQ 577
|
250
....*....|....*..
gi 2535551012 270 VFIMKAVVACLRQYPEF 286
Cdd:PRK14954 578 IRYDAARDACTREKSIF 594
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
35-94 |
1.22e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.98 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2535551012 35 QEVITIESDKAMME--IPSSLSGTIKEMKVKVGDKVSEGSVIALIEssdAGAEENEKPAEKA 94
Cdd:PRK09282 509 KEIVVGGRPRASAPgaVTSPMPGTVVKVKVKEGDKVKAGDTVLVLE---AMKMENEIQAPVD 567
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
57-133 |
1.63e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 57 IKEMKVKVGDKVSEGSVIALIESSDAGAEENEKpaEKAAES-----KPAEK---------EKPAAAESKPAPTPTVANPE 122
Cdd:NF033838 371 IKQAKAKVESKKAEATRLEKIKTDRKKAEEEAK--RKAAEEdkvkeKPAEQpqpapapqpEKPAPKPEKPAEQPKAEKPA 448
|
90
....*....|.
gi 2535551012 123 PERTETlPYAP 133
Cdd:NF033838 449 DQQAEE-DYAR 458
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
82-199 |
2.55e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.08 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 82 AGAEENEKPAEKAAeSKPAEKEKPAAAESKPAPTPTVANPEPERTETLPYAPDTGSAKKPSHASPSVRQFARELGVPLAA 161
Cdd:PRK14951 367 AAAAEAAAPAEKKT-PARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445
|
90 100 110
....*....|....*....|....*....|....*...
gi 2535551012 162 VVGSGQKGRITKEDVQnfvKQVMNAPAPKAADGAGIPS 199
Cdd:PRK14951 446 ALAPAPPAQAAPETVA---IPVRVAPEPAVASAAPAPA 480
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
46-79 |
2.78e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 36.30 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|....
gi 2535551012 46 MMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIES 79
Cdd:PRK08225 1 MTKVYASMAGNVWKIVVKVGDTVEEGQDVVILES 34
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
55-141 |
3.10e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.90 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 55 GTIKEMKVKVGDKVSEGSVIALIESSDAGAE------------------ENEK----------PAEKAAESKPAEKEKPA 106
Cdd:PRK11892 17 GTLAKWLKKEGDKVKSGDVIAEIETDKATMEveavdegtlgkilvpegtEGVKvntpiavlleEGESASDAGAAPAAAAE 96
|
90 100 110
....*....|....*....|....*....|....*
gi 2535551012 107 AAESKPAPTPTVANPEPERTETLPYAPDTGSAKKP 141
Cdd:PRK11892 97 AAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| PRK06748 |
PRK06748 |
hypothetical protein; Validated |
16-78 |
3.39e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180678 [Multi-domain] Cd Length: 83 Bit Score: 36.38 E-value: 3.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2535551012 16 DSVEIIE-VLVAEGDSINADQEVITIES-DKAMMEIPSSLSGTIKEMKVKVGDKVSEGSVIALIE 78
Cdd:PRK06748 10 PCYGKVEkLFVRESSYVYEWEKLALIETiDKQKVEIKVGISGYIESLEVVEGQAIADQKLLITVR 74
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
89-202 |
6.72e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 38.93 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 89 KPAEKAAESKPAEKEKPAAAeskPAPTPTVANPEPERTETLPYAPDTGSAKKPShASPSVRQFARELGVPLAAVVGSGQK 168
Cdd:PRK14951 365 KPAAAAEAAAPAEKKTPARP---EAAAPAAAPVAQAAAAPAPAAAPAAAASAPA-APPAAAPPAPVAAPAAAAPAAAPAA 440
|
90 100 110
....*....|....*....|....*....|....
gi 2535551012 169 GritkedvqnfVKQVMNAPAPKAADGAGIPSVPV 202
Cdd:PRK14951 441 A----------PAAVALAPAPPAQAAPETVAIPV 464
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
90-193 |
7.23e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 38.68 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535551012 90 PAEKAAESKPAEKEKPAAAESKPAPTPT--VANPEPERTETlpyapdtgsAKKPShaspsvrqfarelgVPLAAVVGSGQ 167
Cdd:COG3266 305 PAAAAAAAAPAEAAAPQPTAAKPVVTETaaPAAPAPEAAAA---------AAAPA--------------APAVAKKLAAD 361
|
90 100
....*....|....*....|....*.
gi 2535551012 168 KGRITKEDVQNFVKQVMNAPAPKAAD 193
Cdd:COG3266 362 EQWLASQPASHYTLQLLGASSEAALE 387
|
|
| |
