|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
68-497 |
2.83e-167 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 478.83 E-value: 2.83e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 68 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSSDL 147
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 148 -----IQEEDVVETPAMAREEHTHQEIKGhkTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAkQTGAILPP 222
Cdd:PLN02528 81 rsdslLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 223 TLFQEIQTPPPVPPPAAAAARPASTAaalkappttpkpiftgKDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEVDLSRL 302
Cdd:PLN02528 158 SSAEEATIAEQEEFSTSVSTPTEQSY----------------EDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 303 VSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSV 382
Cdd:PLN02528 222 VELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 383 FQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGAGGQVVRAHIMNVS 462
Cdd:PLN02528 302 LEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVT 381
|
410 420 430
....*....|....*....|....*....|....*
gi 1951401369 463 WSADHRVIDGATMCRFSNLWREYLENPASMVLDLK 497
Cdd:PLN02528 382 IGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
282-492 |
8.73e-94 |
|
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: 283.28 E-value: 8.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 282 MTAAL-KIPHFGYCDEVDLSRLVSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKASHNIG 360
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 361 LAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 440
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1951401369 441 IQVLPRFgAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASM 492
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
66-496 |
3.48e-72 |
|
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: 234.63 E-value: 3.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSS 145
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 146 DLIQEE--DVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAILPPt 223
Cdd:TIGR01347 81 TAAPPAksGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 224 lfqeiqtpppvpppaaaaarpastaaalkAPPTTPKPIFTGKDVT-EPLKGFHKAM------VKTMTAALKIPHfgycdE 296
Cdd:TIGR01347 160 -----------------------------AAAAAAAPAAATRPEErVKMTRLRQRIaerlkeAQNSTAMLTTFN-----E 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 297 VDLSRLVSLRAELKSTTEAR-GVRLSYMPFFIKAASLSLLHFPVLNASVDEgcQNITYKASHNIGLAMDTNQGLLVPNVK 375
Cdd:TIGR01347 206 VDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 376 NVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFGAGGQVVR 455
Cdd:TIGR01347 284 NADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEI 362
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1951401369 456 AHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLDL 496
Cdd:TIGR01347 363 RPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
66-139 |
1.04e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 99.79 E-value: 1.04e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
66-139 |
2.27e-21 |
|
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: 87.81 E-value: 2.27e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
68-497 |
2.83e-167 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 478.83 E-value: 2.83e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 68 FKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSSDL 147
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 148 -----IQEEDVVETPAMAREEHTHQEIKGhkTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAkQTGAILPP 222
Cdd:PLN02528 81 rsdslLLPTDSSNIVSLAESDERGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAA-QKGVVKDS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 223 TLFQEIQTPPPVPPPAAAAARPASTAaalkappttpkpiftgKDVTEPLKGFHKAMVKTMTAALKIPHFGYCDEVDLSRL 302
Cdd:PLN02528 158 SSAEEATIAEQEEFSTSVSTPTEQSY----------------EDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 303 VSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSV 382
Cdd:PLN02528 222 VELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 383 FQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGAGGQVVRAHIMNVS 462
Cdd:PLN02528 302 LEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVT 381
|
410 420 430
....*....|....*....|....*....|....*
gi 1951401369 463 WSADHRVIDGATMCRFSNLWREYLENPASMVLDLK 497
Cdd:PLN02528 382 IGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
57-494 |
1.22e-154 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 451.20 E-value: 1.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 57 TAVVSRGPVVQFKLSDIGEgIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPL 136
Cdd:PRK11855 111 AAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 137 VDIETESSSDLIQEEDVVETPAMAREEH---------------THQEIKGHKTQ-ATPAVRRLAMENNIKLSEVVGTGKD 200
Cdd:PRK11855 190 VVIEVAAAAPAAAAAPAAAAPAAAAAAApapapaaaaapaaaaPAAAAAPGKAPhASPAVRRLARELGVDLSQVKGTGKK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 201 GRILKEDILNFL-AKQTGAILPPTlfqeiqtpppvpppaaaaARPASTAAALKAPPTtPKPIFT--GKDVTEPLKGFHKA 277
Cdd:PRK11855 270 GRITKEDVQAFVkGAMSAAAAAAA------------------AAAAAGGGGLGLLPW-PKVDFSkfGEIETKPLSRIKKI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 278 MVKTMTAAL-KIPHFGYCDEVDLSRLVSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKAS 356
Cdd:PRK11855 331 SAANLHRSWvTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKY 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 357 HNIGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIG 436
Cdd:PRK11855 411 FNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAIL 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1951401369 437 ALGKIQVLPrFGAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVL 494
Cdd:PRK11855 491 GVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
65-495 |
2.59e-122 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 363.73 E-value: 2.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 65 VVQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESS 144
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 145 SDLIQEEDVVET--------------PAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILN 210
Cdd:PRK11856 82 AEAAAAAEAAPEapapepapaaaaaaAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 211 FLAKQTGAILPPTlfqeiqtpppvpppaaaaarpastaaalkAPPTTPKPIFTGKDVTEPLKGFHKAMVKTMTAA-LKIP 289
Cdd:PRK11856 162 AAAAAAPAAAAAA-----------------------------AAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 290 HFGYCDEVDLSRLVSLRAELKstteARGVRLSYMPFFIKAASLSLLHFPVLNASVDEgcQNITYKASHNIGLAMDTNQGL 369
Cdd:PRK11856 213 HFTLTDEVDVTALLALRKQLK----AIGVKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 370 LVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGa 449
Cdd:PRK11856 287 IVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV- 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1951401369 450 GGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLD 495
Cdd:PRK11856 366 DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
282-492 |
8.73e-94 |
|
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: 283.28 E-value: 8.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 282 MTAAL-KIPHFGYCDEVDLSRLVSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKASHNIG 360
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 361 LAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGK 440
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1951401369 441 IQVLPRFgAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASM 492
Cdd:pfam00198 161 IRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
58-494 |
1.48e-73 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 244.53 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 58 AVVSRGPVVQFKLSDIGEGimEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLV 137
Cdd:PRK11854 199 APAAAAGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 138 DIETESS---SDLIQEEDVVETPAMAREEHTHQEIK------------GHKTQATPAVRRLAMENNIKLSEVVGTGKDGR 202
Cdd:PRK11854 277 RFEVEGAapaAAPAKQEAAAPAPAAAKAEAPAAAPAakaegksefaenDAYVHATPLVRRLAREFGVNLAKVKGTGRKGR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 203 ILKEDILNFL---------AKQTGA-------ILP-----PTLFQEIQTPppvpppaaaaarpastaaalkaPPTTPKPI 261
Cdd:PRK11854 357 ILKEDVQAYVkdavkraeaAPAAAAaggggpgLLPwpkvdFSKFGEIEEV----------------------ELGRIQKI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 262 fTGKDVteplkgfHKAMVKtmtaalkIPHFGYCDEVDLSRLVSLRAELKSTTEAR--GVRLSYMPFFIKAASLSLLHFPV 339
Cdd:PRK11854 415 -SGANL-------HRNWVM-------IPHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 340 LNASVDEGCQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSI 419
Cdd:PRK11854 480 FNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGL 559
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1951401369 420 GGTYAKPVILPPEVAIGALGKIQVLPRFGaGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVL 494
Cdd:PRK11854 560 GTTHFTPIVNAPEVAILGVSKSAMEPVWN-GKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
66-496 |
3.48e-72 |
|
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: 234.63 E-value: 3.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSS 145
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 146 DLIQEE--DVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAILPPt 223
Cdd:TIGR01347 81 TAAPPAksGEEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 224 lfqeiqtpppvpppaaaaarpastaaalkAPPTTPKPIFTGKDVT-EPLKGFHKAM------VKTMTAALKIPHfgycdE 296
Cdd:TIGR01347 160 -----------------------------AAAAAAAPAAATRPEErVKMTRLRQRIaerlkeAQNSTAMLTTFN-----E 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 297 VDLSRLVSLRAELKSTTEAR-GVRLSYMPFFIKAASLSLLHFPVLNASVDEgcQNITYKASHNIGLAMDTNQGLLVPNVK 375
Cdd:TIGR01347 206 VDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDG--DDIVYKDYYDISVAVSTDRGLVVPVVR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 376 NVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPrFGAGGQVVR 455
Cdd:TIGR01347 284 NADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEI 362
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1951401369 456 AHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLDL 496
Cdd:TIGR01347 363 RPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
63-494 |
1.26e-69 |
|
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: 232.07 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 63 GPVVQFKLSDIGeGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETE 142
Cdd:TIGR01348 114 SGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 143 SSSDLIQEEDVVETPAMAREEHTHQE--------------IKGHKTQ-------ATPAVRRLAMENNIKLSEVVGTGKDG 201
Cdd:TIGR01348 193 GSTPATAPAPASAQPAAQSPAATQPEpaaapaaakaqapaPQQAGTQnpakvdhAAPAVRRLAREFGVDLSAVKGTGIKG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 202 RILKEDILNFLAKQTGailpptlfqeiqtpppvpppAAAAARPASTAAALKAPPtTPKPIFT--GKDVTEPLKGFHKAMV 279
Cdd:TIGR01348 273 RILREDVQRFVKEPSV--------------------RAQAAAASAAGGAPGALP-WPNVDFSkfGEVEEVDMSRIRKISG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 280 KTMTAA-LKIPHFGYCDEVDLSRLVSLRAELKSTTEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEGCQNITYKASHN 358
Cdd:TIGR01348 332 ANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVN 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 359 IGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGAL 438
Cdd:TIGR01348 412 IGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGV 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1951401369 439 GKIQVLPRFGaGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVL 494
Cdd:TIGR01348 492 SKSGMEPVWN-GKEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
69-496 |
1.51e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 225.10 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 69 KLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESS--SD 146
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAagAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 147 LIQEEDVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAILPPtlfq 226
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAP---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 227 eiqtpppvpppaaaaarpastaaalKAPPTTPKPIFTG-------------KDVTEPLKgfhkaMVKTMTAALKIphFgy 293
Cdd:PRK05704 162 -------------------------AAAAPAAAPAPLGarpeervpmtrlrKTIAERLL-----EAQNTTAMLTT--F-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 294 cDEVDLSRLVSLRAELKSTTEAR-GVRLSYMPFFIKAASLSLLHFPVLNASVDeGcQNITYKASHNIGLAMDTNQGLLVP 372
Cdd:PRK05704 208 -NEVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASID-G-DDIVYHNYYDIGIAVGTPRGLVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 373 NVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--KIQVLPr 446
Cdd:PRK05704 285 VLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERP- 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1951401369 447 FGAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLDL 496
Cdd:PRK05704 358 VAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
173-489 |
5.84e-65 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 212.35 E-value: 5.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 173 KTQATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAKQTGAilpPTLFQEIQTPPPVPPPAAaaarpastaaalk 252
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 253 APPTTPKPIFTGKdvTEPLKGFHKAMVKTMTAALK-IPHFGYCDEVDLSRLVSLRAELK-STTEARGVRLSYMPFFIKAA 330
Cdd:PRK11857 65 AAPAAAPPKLEGK--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 331 SLSLLHFPVLNASVDEGCQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGT 410
Cdd:PRK11857 143 LIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1951401369 411 FTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFgAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENP 489
Cdd:PRK11857 223 FTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
61-487 |
2.43e-60 |
|
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: 207.94 E-value: 2.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 61 SRGPVVQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIE 140
Cdd:TIGR02927 122 GSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 141 TESSSDLIQEEDVVETPAMAREEHTHQEIKGHKTQA-------------------------------TPAVRRLAMENNI 189
Cdd:TIGR02927 202 DANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAApdppapapapaktaapaaaapvssgdsgpyvTPLVRKLAKDKGV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 190 KLSEVVGTGKDGRILKEDILNFLAKQTGAILPPTlfqeiqtpppvpppAAAAARPASTAAALKAPPTTPKPIFTGKdvTE 269
Cdd:TIGR02927 282 DLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAA--------------APAAAAAPAAPAAAAKPAEPDTAKLRGT--TQ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 270 PLKGFHKAMVKTMTAALKI-PHFGYCDEVDLSRLVSLRAELKSTTEAR-GVRLSYMPFFIKAASLSLLHFPVLNASVDEG 347
Cdd:TIGR02927 346 KMNRIRQITADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 348 CQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPV 427
Cdd:TIGR02927 426 TKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPI 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 428 ILPPEVAIGALGKIQVLPRF---GAGGQVVRAHIM-NVSWSADHRVIDGATMCRFSNLWREYLE 487
Cdd:TIGR02927 506 LNPPQAAILGTGAIVKRPRVikdEDGGESIAIRSVcYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
78-494 |
2.11e-59 |
|
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: 201.95 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 78 MEV-TVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGV-------------------------------IKRLYYD 125
Cdd:TIGR01349 11 MTTgNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYlakilvpegtkdvpvnkpiavlveekedvadAFKNYKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 126 VDATALVGKPLVDIETESSSD-LIQEEDVVETPAMAREEHTHQEIKGHKTQATPAVRRLAMENNIKLSEVVGTGKDGRIL 204
Cdd:TIGR01349 91 ESSASPAPKPSEIAPTAPPSApKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 205 KEDILNFLAKQTgAILPPTLFQEIQTPppvpppaaaaarpastaaalkAPPTTPKPifTGKDVTEPLKGFHKAMVKTMTA 284
Cdd:TIGR01349 171 KKDIESFVPQSP-ASANQQAAATTPAT---------------------YPAAAPVS--TGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 285 ALK-IPHFGYCDEVDLSRLVSLRAELKSTTEARgVRLSYMPFFIKAASLSLLHFPVLNASVDEgcQNITYKASHNIGLAM 363
Cdd:TIGR01349 227 SKQtIPHYYVSIECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTD--NFIRRYKNVDISVAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 364 DTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALG--KI 441
Cdd:TIGR01349 304 ATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavED 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1951401369 442 QVLPRFGAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVL 494
Cdd:TIGR01349 384 VAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
46-496 |
2.02e-56 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 193.36 E-value: 2.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 46 NLQMFSCRTLHTAVVSRGPVVQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYD 125
Cdd:PTZ00144 25 SLRKLQPACSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 126 VDATALVGKPLVDIETesssDLIQEEDVVETPAMAREEHTHQEIKGHKTQATPAvrrlamennIKLSEVVGTGKDgrilk 205
Cdd:PTZ00144 105 EGDTVEVGAPLSEIDT----GGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEP---------PAASKPTPPAAA----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 206 edilnflAKQTGAILPPTLFQEIQTPPpvpppaaaaarpastaaalkaPPTTPKPIFT-GKDVTEPLKGFHK--AMVKTM 282
Cdd:PTZ00144 167 -------KPPEPAPAAKPPPTPVARAD---------------------PRETRVPMSRmRQRIAERLKASQNtcAMLTTF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 283 TaalkiphfgycdEVDLSRLVSLRAELKSTTEAR-GVRLSYMPFFIKAASLSLLHFPVLNASVDEGCqnITYKASHNIGL 361
Cdd:PTZ00144 219 N------------ECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 362 AMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKI 441
Cdd:PTZ00144 285 AVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAI 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1951401369 442 QVLPrFGAGGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLDL 496
Cdd:PTZ00144 365 KKRP-VVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
79-494 |
5.34e-47 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 171.19 E-value: 5.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 79 EVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATAL-VGKPL-VDIETE-----------SSS 145
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIkVGEVIaITVEEEedigkfkdykpSSS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 146 DLIQEEDVVETPAMAREEHTHQ-----EIKGHKTQ----------ATPAVRRLAMENNIKLSEVVGTGKDGRILKEDILN 210
Cdd:PLN02744 206 AAPAAPKAKPSPPPPKEEEVEKpasspEPKASKPSappssgdrifASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 211 FLAKQ-TGAilpptlfqeiqtpppvpppaaaaarpastaaalKAPPTTPKPIfTGKDVTE-PLKGFHKAMVKTMTAALK- 287
Cdd:PLN02744 286 YLASGgKGA---------------------------------TAPPSTDSKA-PALDYTDiPNTQIRKVTASRLLQSKQt 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 288 IPHFGYCDEVDLSRLVSLRAELKSTTEA-RGVRLSYMPFFIKAASLSLLHFPVLNAS-VDEgcqNITYKASHNIGLAMDT 365
Cdd:PLN02744 332 IPHYYLTVDTRVDKLMALRSQLNSLQEAsGGKKISVNDLVIKAAALALRKVPQCNSSwTDD---YIRQYHNVNINVAVQT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 366 NQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGS-IGGTYAKPVILPPEVAIGALGKIQ-- 442
Cdd:PLN02744 409 ENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAEkr 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1951401369 443 VLPRFGAGgQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVL 494
Cdd:PLN02744 489 VIPGSGPD-QYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
63-496 |
1.48e-34 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 135.27 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 63 GPVVQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIET- 141
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKs 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 142 -ESSSDLIQEEDVVETPAmAREEHTHQEIKGHKTQATPAVRRlamenniklsevvgtgkdgrilkedilnflakqtgail 220
Cdd:PLN02226 169 eDAASQVTPSQKIPETTD-PKPSPPAEDKQKPKVESAPVAEK-------------------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 221 pPtlfqeiqtpppvpppaaaaarpastaaalKAPPTTPKPIFTGKDVTEPLKGFHKA-----MVKTMTAALKIPHFGYC- 294
Cdd:PLN02226 210 -P-----------------------------KAPSSPPPPKQSAKEPQLPPKERERRvpmtrLRKRVATRLKDSQNTFAl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 295 ----DEVDLSRLVSLRAELKST-TEARGVRLSYMPFFIKAASLSLLHFPVLNASVDEgcQNITYKASHNIGLAMDTNQGL 369
Cdd:PLN02226 260 lttfNEVDMTNLMKLRSQYKDAfYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDG--DDIIYRDYVDISIAVGTSKGL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 370 LVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFgA 449
Cdd:PLN02226 338 VVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-V 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1951401369 450 GGQVVRAHIMNVSWSADHRVIDGATMCRFSNLWREYLENPASMVLDL 496
Cdd:PLN02226 417 GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
177-494 |
5.69e-34 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 131.18 E-value: 5.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 177 TPAVRRLAMENNIKLSEVVGTGKDGRILKEDILNFLAK--QTGAILPPTLFQEIQTPPPvpppaaaaarpastaaalKAP 254
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPEniENDSIKSPAQIEKVEEVPD------------------NVT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 255 PTtpkpiftGKDVTEPLKGFHKAMVKTMTAA-LKIPHFGYCDEVDLSRLVSLRAE-LKSTTEARGVRLSYMPFFIKAASL 332
Cdd:PRK14843 114 PY-------GEIERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 333 SLLHFPVLNASVDEGCQNITYKASHNIGLAMDTNQGLLVPNVKNVQLLSVFQIAQELNRLQTLGAAGQLGTSELSGGTFT 412
Cdd:PRK14843 187 TLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 413 LSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGAGGQVVRAhIMNVSWSADHRVIDGATMCRFSNLWREYLENPASM 492
Cdd:PRK14843 267 ISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRP-IMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISM 345
|
..
gi 1951401369 493 VL 494
Cdd:PRK14843 346 LI 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
66-139 |
1.04e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 99.79 E-value: 1.04e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
66-139 |
2.27e-21 |
|
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: 87.81 E-value: 2.27e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 66 VQFKLSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
66-139 |
2.15e-19 |
|
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: 82.26 E-value: 2.15e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1951401369 66 VQFKLSDIGEGIMEVtVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
176-209 |
5.55e-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: 5.55e-14
10 20 30
....*....|....*....|....*....|....
gi 1951401369 176 ATPAVRRLAMENNIKLSEVVGTGKDGRILKEDIL 209
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
252-478 |
1.02e-11 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 67.61 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 252 KAPPTTPKPIFTGKDVTEPLKGFHKAMVKTMTAALKIPhfgycdevdlsRLVSLRA---------------ELKSTteaR 316
Cdd:PRK12270 101 AAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP-----------TATSVRAvpakllidnrivinnHLKRT---R 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 317 GVRLSY-------MpffIKAaslsLLHFPVLNASVDE--GCQNITYKASHNIGLAMDT-----NQGLLVPNVKNVQLLSV 382
Cdd:PRK12270 167 GGKVSFthligyaL---VQA----LKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLpkkdgSRQLVVPAIKGAETMDF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 383 FQIAQELNRLQTLGAAGQLGTSELSGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGKIQVLPRFGAGGQVVRAH----- 457
Cdd:PRK12270 240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgisk 319
|
250 260
....*....|....*....|.
gi 1951401369 458 IMNVSWSADHRVIDGATMCRF 478
Cdd:PRK12270 320 VMTLTSTYDHRIIQGAESGEF 340
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
67-160 |
3.86e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 65.41 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 67 QFKLSDIGEGimEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSSD 146
Cdd:PRK11854 4 EIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAA 81
|
90
....*....|....
gi 1951401369 147 LIQEEDVVETPAMA 160
Cdd:PRK11854 82 DAAPAQAEEKKEAA 95
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
70-139 |
1.77e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 51.29 E-value: 1.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 70 LSDIGEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
74-221 |
6.70e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 54.56 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 74 GEGIMEVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDIETESSSDliQEEDV 153
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD--AEIDA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951401369 154 VetpamareehthqeikghktqATPAVRRLAMEnNIKLSEVVGTGKDGRILKEDIlNFLAKQTGAILP 221
Cdd:PRK14875 89 F---------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
81-139 |
1.53e-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: 39.71 E-value: 1.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1951401369 81 TVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYYDVDATALVGKPLVDI 139
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
79-180 |
1.80e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.67 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951401369 79 EVTVKEWYVKEGDKVSQFDSICEVQSDKASVTITSRYDGVIKRLYydVDATA---LVGKPLVDI--ETESSSDLI----- 148
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKIL--VPEGTegvKVNTPIAVLleEGESASDAGaapaa 93
|
90 100 110
....*....|....*....|....*....|..
gi 1951401369 149 QEEDVVETPAMAREEHTHQEIKGHKTQATPAV 180
Cdd:PRK11892 94 AAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAA 125
|
|
| |
