|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
8-469 |
3.57e-140 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 408.80 E-value: 3.57e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAA----PAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQTVPAhpgaagagqagrqvpealqqPALQVIQAEAQEQLEPVRnsglhlsespriptievegglgss 247
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAA--------------------AAAPPAAAAEGEERVPLS------------------------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvtPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRkeginLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK11856 195 --------GMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK11856 262 SWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYF 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11856 342 TPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
8-469 |
9.91e-97 |
|
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: 297.42 E-value: 9.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPapgtpaapvrpaapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAA----------------APTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAagqtvpahpgaagagqagrqvpealQQPALQVIQAEAQEQLEPVRnsglhlsespRIPtievegglgss 247
Cdd:TIGR01347 145 IIKKTEAPASA-------------------------QPPAAAAAAAAPAAATRPEE----------RVK----------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:TIGR01347 179 ------MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:TIGR01347 253 EIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMS 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01347 333 TPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
265-469 |
3.23e-87 |
|
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: 265.95 E-value: 3.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 265 MRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVDK--IIVKRDINI 342
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 343 ALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFE 422
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 686543092 423 SIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
8-82 |
3.39e-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: 103.99 E-value: 3.39e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
8-81 |
4.10e-26 |
|
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: 100.94 E-value: 4.10e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
8-469 |
3.57e-140 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 408.80 E-value: 3.57e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAA----PAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQTVPAhpgaagagqagrqvpealqqPALQVIQAEAQEQLEPVRnsglhlsespriptievegglgss 247
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAA--------------------AAAPPAAAAEGEERVPLS------------------------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvtPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRkeginLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK11856 195 --------GMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-----LTVTDFLIKAVALALKKFPELNA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK11856 262 SWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYF 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11856 342 TPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLE 403
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
8-469 |
3.03e-105 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 319.47 E-value: 3.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAvaapa 87
Cdd:PRK05704 3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 gasagssapaaGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK05704 78 -----------EGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAAGQtvpahpgaagagqagrqvPEALQQPALQVIQAEAQEQLEPVrnsglhlsespriptievegglgss 247
Cdd:PRK05704 147 VLAALAAAAAAPAA------------------PAAAAPAAAPAPLGARPEERVPM------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidvTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:PRK05704 184 -------TRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:PRK05704 257 SIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMS 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK05704 337 TPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLE 398
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
8-469 |
7.13e-102 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 315.22 E-value: 7.13e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAEsLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAApslSAADAPMRSRY-SPAVQTLAAEHRIDLSAVPGTGLGGRITRK 166
Cdd:PRK11855 199 PAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAP---AAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 167 DVLAYLEngGAAAGQTVPAhpgaagagqagrqvpealqqpALQVIQAEAqeqlepvrnsGLHLSESPRIP-----TIEVE 241
Cdd:PRK11855 276 DVQAFVK--GAMSAAAAAA---------------------AAAAAAGGG----------GLGLLPWPKVDfskfgEIETK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 242 gglgssseyliDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKD 321
Cdd:PRK11855 323 -----------PLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQLKKEAE-KAGVKLTMLPFFIKAVVAALKE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 322 YPIMNSV--WAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNT 399
Cdd:PRK11855 391 FPVFNASldEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSL 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 400 GSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11855 471 GGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLA 540
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
8-469 |
9.91e-97 |
|
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: 297.42 E-value: 9.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPapgtpaapvrpaapslSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAA----------------APTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYLENGGAAagqtvpahpgaagagqagrqvpealQQPALQVIQAEAQEQLEPVRnsglhlsespRIPtievegglgss 247
Cdd:TIGR01347 145 IIKKTEAPASA-------------------------QPPAAAAAAAAPAAATRPEE----------RVK----------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 seylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNS 327
Cdd:TIGR01347 179 ------MTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 328 VWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILS 407
Cdd:TIGR01347 253 EIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMS 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 408 YPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01347 333 TPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLE 394
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
8-469 |
2.38e-89 |
|
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: 283.83 E-value: 2.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:TIGR02927 127 TEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAA--------GTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYS-----PAVQTLAAEHRIDLSAV 154
Cdd:TIGR02927 207 PAEPAEEEAPApseagsepAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSgpyvtPLVRKLAKDKGVDLSTV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 155 PGTGLGGRITRKDVLAylenggAAAGQTVPAhpgaagagqagrqvpEALQQPALQVIQAEAQEQLEPVRNSGLHLSespr 234
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLA------AAKAAEEAR---------------AAAAAPAAAAAPAAPAAAAKPAEPDTAKLR---- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 235 iptievegglGSSSEylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKA 314
Cdd:TIGR02927 342 ----------GTTQK----MNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQA 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 315 VVSAIKDYPIMNSVWAVD-KIIVKRDI-NIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGG 392
Cdd:TIGR02927 408 VTEALKAHPNVNASYNAEtKEVTYHDVeHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGG 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 393 TFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVI-----NDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDN 467
Cdd:TIGR02927 488 TFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKR 567
|
..
gi 686543092 468 LE 469
Cdd:TIGR02927 568 LE 569
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
265-469 |
3.23e-87 |
|
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: 265.95 E-value: 3.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 265 MRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKrKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVDK--IIVKRDINI 342
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAA-DEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 343 ALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFE 422
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 686543092 423 SIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLE 206
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
8-469 |
2.26e-80 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 261.86 E-value: 2.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 8 TDVVMPQLAESlvSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPA 87
Cdd:PRK11854 207 KDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 88 GASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPmrsRYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKD 167
Cdd:PRK11854 285 PAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYV---HATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 168 VLAYlenggaaagqtvpahpgaagagqagrqVPEALQQpalqviqAEAQEQLEPVRNSGLHLsesPRIPTIEVegglgsS 247
Cdd:PRK11854 362 VQAY---------------------------VKDAVKR-------AEAAPAAAAAGGGGPGL---LPWPKVDF------S 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 248 SEYLIDVTP---IRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRN-KLKDEFKRKEGINLTYLAFMMKAVVSAIKDYP 323
Cdd:PRK11854 399 KFGEIEEVElgrIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMP 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 324 IMNSVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGS 401
Cdd:PRK11854 479 RFNSSLSEDgqRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGG 558
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092 402 FGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PRK11854 559 LGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
13-469 |
1.21e-74 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 240.74 E-value: 1.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 13 PQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGeiiariavaapagasag 92
Cdd:PTZ00144 50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVG----------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 93 ssapaagtapqaaaaapapgtpaapvrpaapslsaadAPMrsryspavqtlaaeHRIDLSAVPGTGlggritrkdvlayl 172
Cdd:PTZ00144 113 -------------------------------------APL--------------SEIDTGGAPPAA-------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 173 engGAAAGQTVPAHPGAAGAGQAGRQVPEALQQPAlqviqAEAQEQLEPVRNSglhlSESPRIPTIEVEGGlgsSSEYLI 252
Cdd:PTZ00144 128 ---APAAAAAAKAEKTTPEKPKAAAPTPEPPAASK-----PTPPAAAKPPEPA----PAAKPPPTPVARAD---PRETRV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 253 DVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD 332
Cdd:PTZ00144 193 PMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 333 KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIIN 412
Cdd:PTZ00144 273 EIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIIN 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 686543092 413 YPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PTZ00144 353 PPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIE 409
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
10-469 |
1.62e-66 |
|
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: 220.05 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 10 VVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIARIAVAAPAG 88
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 89 ASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPS-------------LSAADAPMRSRYSPAVQTLAAEHRIDLSAVP 155
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPApqkqspepsspapLSDKESGDRIFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 156 GTGLGGRITRKDVLAYLEnggaaagqtvpahpgaagagqagrQVPEALQQPALQVIQAEAQEqLEPVrnsglhlsespri 235
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVP------------------------QSPASANQQAAATTPATYPA-AAPV------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 236 ptievegglgSSSEY-LIDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFkrKEGINLTYLAFMMKA 314
Cdd:TIGR01349 204 ----------STGSYeDVPLSNIRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMA--SEVYKLSVNDFIIKA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 315 VVSAIKDYPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTF 394
Cdd:TIGR01349 272 SALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTF 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092 395 TVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANIC---LSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01349 352 TISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEEKGFAVASIMsvtLSCDHRVIDGAVGAEFLKSFKKYLE 429
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
137-469 |
3.59e-62 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 204.64 E-value: 3.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 137 SPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLENGGAAAGQTVPAhpgaagagqagrQVPeALQQPALQVIQAEAQ 216
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAA------------SVS-SAQQAAKTAAPAAAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 217 EQLEPVRNSglhlsespriptievegglgssseylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDE 296
Cdd:PRK11857 72 PKLEGKREK----------------------------VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 297 FKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVW--AVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDE 374
Cdd:PRK11857 124 VLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYdeATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 375 LAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDG 454
Cdd:PRK11857 204 LAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDG 283
|
330
....*....|....*
gi 686543092 455 VICGRFLQRVKDNLE 469
Cdd:PRK11857 284 ATIGRFASRVKELLE 298
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-469 |
1.66e-61 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 207.69 E-value: 1.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 2 SDNTKLTDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:PLN02226 86 SESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 82 AvaapagasagssapaagtapqaaaaapapgtpaapvrpaapslSAADAPmrSRYSPAvqtlaaehridlSAVPGTGlgg 161
Cdd:PLN02226 166 S-------------------------------------------KSEDAA--SQVTPS------------QKIPETT--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 162 ritrkdvlaylenggaaagQTVPAHPGAAGAGQAGRQVPEAlQQPalqviqaEAQEQLEPVRNSglhlSESPRIPTIEve 241
Cdd:PLN02226 186 -------------------DPKPSPPAEDKQKPKVESAPVA-EKP-------KAPSSPPPPKQS----AKEPQLPPKE-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 242 gglgssSEYLIDVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIKD 321
Cdd:PLN02226 233 ------RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 322 YPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGS 401
Cdd:PLN02226 307 QPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 686543092 402 FGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PLN02226 387 YGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVE 454
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
12-477 |
3.88e-55 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 192.76 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 12 MPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIArIAVAA----- 85
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGaKEIKVGEVIA-ITVEEeedig 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 86 -----PAGASAGSSAPAAGTAPQAAAAAPAPGTPAAPVRPAAPSLSAADAPMRSRYSPAVQTLAAEHRIDLSAVPGTGLG 160
Cdd:PLN02744 196 kfkdyKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 161 GRITRKDVLAYLENGGAAAGQTVPAHPGAagagqagrqvpealqqPALQVIQaeaqeqlepvrnsglhlsesprIPTiev 240
Cdd:PLN02744 276 GRIVKADIEDYLASGGKGATAPPSTDSKA----------------PALDYTD----------------------IPN--- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 241 egglgssseylidvTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEGINLTYLAFMMKAVVSAIK 320
Cdd:PLN02744 315 --------------TQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 321 DYPIMNSVWAVDKIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTG 400
Cdd:PLN02744 381 KVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 401 S-FGSILSYPIINYPQAAILTFESIVKK--PVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLEgyTPDTKL 477
Cdd:PLN02744 461 GpFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIE--NPESML 538
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
32-469 |
1.58e-53 |
|
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: 188.55 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 32 GDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPAGASAGSSAPAAGTAPQAAAAAPAP 111
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPATAPAPASAQPAAQSPAATQPEP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 112 GTPAAPVRPAAPSLSAADAPMRSRY---SPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLENggaaagqtvpahpg 188
Cdd:TIGR01348 220 AAAPAAAKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKE-------------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 189 aagagqagrqvpealqqpalQVIQAEAQeqlePVRNSGLHLSESPrIPTIEVEGgLGSSSEylIDVTPIRNTIATRMRQS 268
Cdd:TIGR01348 286 --------------------PSVRAQAA----AASAAGGAPGALP-WPNVDFSK-FGEVEE--VDMSRIRKISGANLTRN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 269 VSEIPHAWTMIEVDVTNLVVLRNKLKDEfKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD--KIIVKRDINIALAV 346
Cdd:TIGR01348 338 WTMIPHVTHFDKADITEMEAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGgeQLILKKYVNIGVAV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 347 GTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVK 426
Cdd:TIGR01348 417 DTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGM 496
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 686543092 427 KPVVINDMIAVRSMANICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:TIGR01348 497 EPVWNGKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLA 539
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-469 |
1.55e-51 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 179.92 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 10 VVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIAVAAPAGA 89
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 90 SAGSSAPAAGTAPQAAAAAPAPGTPaapvrpaapSLSAADApmrsrySPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVL 169
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGS---------NLSGVLS------TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 170 AYLenggaaagqtvpahpgaagagqagrqvpealqqpalqvIQAEAQEQlepvrNSGLHLSESPRIPTIEVEGGLGSSSE 249
Cdd:PLN02528 146 KYA--------------------------------------AQKGVVKD-----SSSAEEATIAEQEEFSTSVSTPTEQS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 250 YLIDVTPIRN---TIATRMRQSVSeIPHAWTMIEVDVTNLVVLRNKLKDEfKRKEGINLTYLAFMMKAVVSAIKDYPIMN 326
Cdd:PLN02528 183 YEDKTIPLRGfqrAMVKTMTAAAK-VPHFHYVEEINVDALVELKASFQEN-NTDPTVKHTFLPFLIKSLSMALSKYPLLN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 327 SVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNNTGSFGS 404
Cdd:PLN02528 261 SCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGG 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686543092 405 ILSYPIINYPQAAILTFESIVKKPVVIND--MIAVRSMaNICLSLDHRILDGVICGRFLQRVKDNLE 469
Cdd:PLN02528 341 KFGSPVLNLPEVAIIALGRIQKVPRFVDDgnVYPASIM-TVTIGADHRVLDGATVARFCNEWKSYVE 406
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
135-469 |
1.43e-45 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 162.38 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 135 RYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVLAYLenggaaagqtvpAHPGAAGAGQAGRQVPEALQQPAlqviQAE 214
Cdd:PRK14843 50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL------------PENIENDSIKSPAQIEKVEEVPD----NVT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 215 AQEQLEpvrnsglhlsespRIPtievegglgssseylidVTPIRNTIATRMRQSVSEIPHAWTMIEVDVTNLVVLRNKLK 294
Cdd:PRK14843 114 PYGEIE-------------RIP-----------------MTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 295 DEFKRKEGINLTYLAFMMKAVVSAIKDYPIMNSVWAVD--KIIVKRDINIALAVGTEDSVMTPVIKKADQKNIAGLAREI 372
Cdd:PRK14843 164 EPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDgkTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 373 DELAQKTREGKLRLDDMQGGTFTVNNTGSFGSILSYPIINYPQAAILTFESIVKKPVVINDMIAVRSMANICLSLDHRIL 452
Cdd:PRK14843 244 KDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVV 323
|
330
....*....|....*..
gi 686543092 453 DGVICGRFLQRVKDNLE 469
Cdd:PRK14843 324 DGMAGAKFMKDLKELIE 340
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
8-82 |
3.39e-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: 103.99 E-value: 3.39e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
8-81 |
4.10e-26 |
|
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: 100.94 E-value: 4.10e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
8-81 |
3.61e-16 |
|
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: 73.02 E-value: 3.61e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686543092 8 TDVVMPQLAESlVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:pfam00364 1 TEIKSPMIGES-VREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
175-470 |
4.58e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 81.09 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 175 GGAAAGQTVPAHPGAAGAGQAGRQVPEALQQPALQVIQAEAQEQLEPVRNSGLHLSESPRIPTIEVEGGLGSsseyliDV 254
Cdd:PRK12270 44 PTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED------EV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 255 TPIR---NTIATRMRQSVsEIPHAWTMIEVDVTNLVVLRNKLKDEFKRKEG--INLTYL-AFmmkAVVSAIKDYPIMNSV 328
Cdd:PRK12270 118 TPLRgaaAAVAKNMDASL-EVPTATSVRAVPAKLLIDNRIVINNHLKRTRGgkVSFTHLiGY---ALVQALKAFPNMNRH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 329 WAVDK---IIVKR-DINIALAV------GTEdSVMTPVIKKADQKNIAGLAREIDELAQKTREGKLRLDDMQGGTFTVNN 398
Cdd:PRK12270 194 YAEVDgkpTLVTPaHVNLGLAIdlpkkdGSR-QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686543092 399 TGSFGSILSYP--------II-----NYP---QAAiltfesivkKPVVINDMiAVRSMANICLSLDHRILDGVICGRFLQ 462
Cdd:PRK12270 273 PGGIGTVHSVPrlmkgqgaIIgvgamEYPaefQGA---------SEERLAEL-GISKVMTLTSTYDHRIIQGAESGEFLR 342
|
....*...
gi 686543092 463 RVKDNLEG 470
Cdd:PRK12270 343 TIHQLLLG 350
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-82 |
1.21e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 72.28 E-value: 1.21e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARIA 82
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVA 77
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
135-169 |
3.29e-11 |
|
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: 57.70 E-value: 3.29e-11
10 20 30
....*....|....*....|....*....|....*
gi 686543092 135 RYSPAVQTLAAEHRIDLSAVPGTGLGGRITRKDVL 169
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
9-81 |
6.41e-10 |
|
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: 55.14 E-value: 6.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686543092 9 DVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
8-82 |
3.17e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 55.69 E-value: 3.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686543092 8 TDVVMPQLAESLVSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEG-QVISVGEIIARIA 82
Cdd:PRK11892 3 IEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLL 78
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-81 |
4.95e-07 |
|
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: 47.03 E-value: 4.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686543092 20 VSATIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:cd06850 6 MPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
23-81 |
1.83e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 44.06 E-value: 1.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 686543092 23 TIGKWLKQPGDRVEEYEPICELITDKVNAELPSTVEGTLVELLAEEGQVISVGEIIARI 81
Cdd:PRK09282 532 TVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| |
