|
Name |
Accession |
Description |
Interval |
E-value |
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
3-818 |
0e+00 |
|
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE.
Pssm-ID: 439499 [Multi-domain] Cd Length: 816 Bit Score: 1759.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 3 VLSIVVFLALLGVVFYHRVNLTLSSLILVAYTAVMGAIGLWSFWLLLPLAIVLLPLNLSSVRRSLLSAPALRAFRKVMPP 82
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 83 MSTTEKEAIDAGTTWWEGDLFRGAPDWNKLHSYPKPRLTEEEQAFIDGPVEEACRMANDFQITHELADLPPELWAYLKEH 162
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 163 RFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTEEQKNHYLPGLARGDEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 243 PEAGSDAGAIPDVGTVCMGEWQGKQVLGMRLTWNKRYITLAPVATVLGLAFKLHDPNRLLSDNESPGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 323 EIGNRHFPLNVPFQNGPTRGTDVFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGSLKSIALATGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 403 FKISIGKMEGIEEPLARIAGNTYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMLGESNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 483 LARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVLDEMAAAQNND----LNAFDKSLFGHLGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 559 TNGRTSATPTKDATRRYYQQLNRLSANLALLSDVSMGVLGGSLKRRERISARLGDILSQMYLASAVLKRFDDEGRQKEDL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 639 PLVHWGVQDSLHKAEQALDDLLRNFPNRFIAGALRFVVFPFGRVHTAPSDRLDHQLAKILQVPSATRSRLGRGQYLTPSE 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 719 HNPIGLLEAALADVMAAEPIHERLCKAAGKNLPFTRLDRLAERALEEGKISADEAKILVKAEESRLRSINVDDFAPDALa 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDEL- 799
|
810 820
....*....|....*....|
gi 515495739 799 aakPEKPAAQSKRQQQTEAA 818
Cdd:NF038187 800 ---AAKPAKRPAKQKQDEAA 816
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
42-812 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1559.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 42 LWSFWLLLPLAIVLLPLNLSSVRRSLLSAPALRAFRKVMPPMSTTEKEAIDAGTTWWEGDLFRGAPDWNKLHSYPKPRLT 121
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 122 EEEQAFIDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITV 201
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 202 GVPNSLGPGELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWQGKQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 282 LAPVATVLGLAFKLHDPNRLLSDNESPGITCALIPTSTPGVEIGNRHFPLNVPFQNGPTRGTDVFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 362 GWRMLVECLSVGRGITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVMDAAASLITYALVQG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 442 EKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMLGESNFLARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 522 DEMAAAQNND---LNAFDKSLFGHLGHVGSNKVRSFWLGLTNGRTSATPTKDATRRYYQQLNRLSANLALLSDVSMGVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 599 GSLKRRERISARLGDILSQMYLASAVLKRFDDEGRQKEDLPLVHWGVQDSLHKAEQALDDLLRNFPNRFIAGALRFVVFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 679 FGRVHTAPSDRLDHQLAKILQVPSATRSRLGRGQYLTPSEHNPIGLLEAALADVMAAEPIHERLCKAAGKN-LPFTRLDR 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 515495739 758 LAERALEEGKISADEAKILVKAEESRLRSINVDDFAPDALAAAKPEKPAAQSKRQ 812
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVE 775
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
59-797 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1190.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 59 NLSSVRRSLLSAPALRAFRKVMPPMSTTEKEAIDAGTTWWEGDLFRGAPDWNKLHSYPKPRLTEEEQAFIDGPVEEACRM 138
Cdd:PRK13026 17 AVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQAFIDNEVETLLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 139 ANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITVGVPNSLGPGELLQHYGT 218
Cdd:PRK13026 97 LDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHYGT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 219 EEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWQGKQVLGMRLTWNKRYITLAPVATVLGLAFKLHDP 298
Cdd:PRK13026 177 QEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPVATVLGLAFKLRDP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 299 NRLLSDNESPGITCALIPTSTPGVEIGNRHFPLNVPFQNGPTRGTDVFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITL 378
Cdd:PRK13026 257 DGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRMLVECLSAGRGISL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 379 PSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHR 458
Cdd:PRK13026 337 PALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPSVVTAIAKYHMTEL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 459 GQQSIVDAMDIAGGKGIMLGESNFLARAYQGAPIAITVEGANILTRTMMIFGQGAIRCHPYVLDEMAAAQNND----LNA 534
Cdd:PRK13026 417 ARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEMEAAAMEDehegLEA 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 535 FDKSLFGHLGHVGSNKVRSFWLGLTNGRTSATPTKDATRRYYQQLNRLSANLALLSDVSMGVLGGSLKRRERISARLGDI 614
Cdd:PRK13026 497 FDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDLKRKEMLSARLGDV 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 615 LSQMYLASAVLKRFDDEGRQKEDLPLVHWGVQDSLHKAEQALDDLLRNFPNRFIAGALRFVVFPFGRVHTAPSDRLDHQL 694
Cdd:PRK13026 577 LSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGNHFRAPSDKLARQL 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 695 AKILQVPSATRSRLGRGQYLTPSEHNPIGLLEAALADVMAAEPIHERLCKA--AGKNLPFTRLDRLAERALEEGKISADE 772
Cdd:PRK13026 657 AELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAqrEGKLPRKVPLLELFAKALEKGVITADE 736
|
730 740
....*....|....*....|....*
gi 515495739 773 AKILVKAEESRLRSINVDDFAPDAL 797
Cdd:PRK13026 737 AEKLLAADKLRLDAIQVDDFTPDFM 761
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
514-792 |
1.23e-164 |
|
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally uncharacterized and is predominantly found in various prokaryotic acyl-coenzyme A dehydrogenases and seems to be essential for its function.
Pssm-ID: 430522 [Multi-domain] Cd Length: 284 Bit Score: 478.14 E-value: 1.23e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 514 IRCHPYVLDEMAAAQNND----LNAFDKSLFGHLGHVGSNKVRSFWLGLTNGRTSATPTKDATRRYYQQLNRLSANLALL 589
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 590 SDVSMGVLGGSLKRRERISARLGDILSQMYLASAVLKRFDDEGRQKEDLPLVHWGVQDSLHKAEQALDDLLRNFPNRFIA 669
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 670 GALRFVVFPFGRVHTAPSDRLDHQLAKILQVPSATRSRLGRGQYLTPSEHNPIGLLEAALADVMAAEPIHERLCKAAGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 515495739 749 NLPFTRLDRLAERALEEGKISADEAKILVKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
119-508 |
1.44e-88 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 285.20 E-value: 1.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 119 RLTEEEQAFIDgPVEEAC--RMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGI 196
Cdd:COG1960 4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 197 LAITVGVPNslGPGELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGtvcmgEWQGKqvlGMRLTWN 276
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTA-----VRDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 277 KRYITLAPVATVLGLAFKLHDpnrllsDNESPGITCALIPTSTPGVEIGNRHFPLNV-PFQNGPTRGTDVFVPIDYIIGG 355
Cdd:COG1960 153 KTFITNAPVADVILVLARTDP------AAGHRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVMDAAASLIT 435
Cdd:COG1960 227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515495739 436 YALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMlgESNFLARAYQGAPIAITVEGANILTRTMMI 508
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT--REYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
152-500 |
1.49e-35 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 138.94 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKNHYLPGLAR 231
Cdd:cd01158 32 PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKKYLPPLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 232 GDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWqgkqvlgmRLTWNKRYITLAPVATVLgLAFKLHDPnrllsDNESPGIT 311
Cdd:cd01158 111 GEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDP-----SKGYRGIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 312 CALIPTSTPGVEIGNRHFPL--------NVPFQngptrgtDVFVPIDYIIGGPkmaGQGWRMLVECLSVGRgITLPSNST 383
Cdd:cd01158 177 AFIVERDTPGLSVGKKEDKLgirgssttELIFE-------DVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 384 GslksIALA----TGAYAHIRRQFKISIGKMEGIEEPLARIAgntyVMDAAASLITYA----LVQGEKPAVLSAIVKYHC 455
Cdd:cd01158 246 G----IAQAaldaAVDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaarlKDNGEPFIKEAAMAKLFA 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515495739 456 THRGQQSIVDAMDIAGGKGIMlgeSNFLA-RAYQGAPIAITVEGAN 500
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
207-500 |
1.82e-33 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 131.64 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 207 LGPGELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIpdvGTVCM---GEWqgkqvlgmRLTWNKRYITLA 283
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGI---RTTARkdgDGY--------VLNGRKIFISNG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 284 PVATVLGLAFKLHDpnrllSDNESPGITCALIPTSTPGVEIGNrhfPLNVPFQNG-PTRG---TDVFVPIDYIIGGPkma 359
Cdd:cd00567 111 GDADLFIVLARTDE-----EGPGHRGISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 360 GQGWRMLVECLSVGRgITLPSNSTGSLKSiAL-ATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYvmdaAASLITYAL 438
Cdd:cd00567 180 GGGFELAMKGLNVGR-LLLAAVALGAARA-ALdEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELE----AARLLLYRA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515495739 439 VQG-----EKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGimLGESNFLARAYQGAPIAITVEGAN 500
Cdd:cd00567 254 AWLldqgpDEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA 318
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-513 |
4.97e-32 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 129.51 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 101 DLFRGAPDWNKLHSYP---KPRLTEEEQAFIdGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLE 177
Cdd:cd01161 5 NMFLGDIVTKQVFPYPsvlTEEQTEELNMLV-GPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 178 FSPYAQAMVLQKLaGVSGILAITVGVPNSLG-PGELLqhYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPdvg 256
Cdd:cd01161 84 LNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 257 tvCMGEWQ--GKQVLgmrLTWNKRYIT---LAPVATVLGlAFKLHDPNRLLSDnespGITCALIPTSTPGVEIGNRHFPL 331
Cdd:cd01161 158 --TTAVLSedGKHYV---LNGSKIWITnggIADIFTVFA-KTEVKDATGSVKD----KITAFIVERSFGGVTNGPPEKKM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 332 NVPFQNGPT-RGTDVFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKM 410
Cdd:cd01161 228 GIKGSNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 411 EGIEEPLARIAGNTYVMDAAASLITYALVQGEKP--AVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMlgESNFLARAYQ 488
Cdd:cd01161 304 GLIQEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFM--REYGVERVLR 381
|
410 420
....*....|....*....|....*
gi 515495739 489 GAPIAITVEGANILTRtMMIFGQGA 513
Cdd:cd01161 382 DLRIFRIFEGTNEILR-LFIALTGL 405
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
120-478 |
6.65e-24 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 104.75 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 120 LTEEEQAFIDGpVEEAC------RMANDFqithELADLPPELWAYLKEHRFFAMIIKkEYGGLEFSPYAQAMVLQKLAGV 193
Cdd:cd01151 13 LTEEERAIRDT-AREFCqeelapRVLEAY----REEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 194 SGILAITVGVPNSLGPGELlQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGaipdvGTVCMGEWQGKqvlGMRL 273
Cdd:cd01151 87 DSGYRSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 274 TWNKRYITLAPVATVLGLAFKLHDPNrllsdnespGITCALIPTSTPGVE---IGNRhFPLNVPfQNGPTRGTDVFVPID 350
Cdd:cd01151 158 NGSKTWITNSPIADVFVVWARNDETG---------KIRGFILERGMKGLSapkIQGK-FSLRAS-ITGEIVMDNVFVPEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 351 YIIGGPKmagqGWRMLVECLSVGR-GItlpsnstgSLKSIALATGA------YAHIRRQFKISIGKMEGIEEPLARIAGN 423
Cdd:cd01151 227 NLLPGAE----GLRGPFKCLNNARyGI--------AWGALGAAEDCyhtarqYVLDRKQFGRPLAAFQLVQKKLADMLTE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 515495739 424 TYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMLG 478
Cdd:cd01151 295 IALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDE 349
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-474 |
4.47e-23 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 102.10 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKNHYLPGLAR 231
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 232 GDEIPCFALTSPEAGSDAgaipdVGTVCMGEWQGKQVLgmrLTWNKRYITLAPVATVLgLAFKLHDPnrllsDNESPGIT 311
Cdd:cd01156 114 GEHIGALAMSEPNAGSDV-----VSMKLRAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDP-----SAGAHGIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 312 CALIPTSTPGVEIGNRHFPLNVpfqngptRGT--------DVFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPSNST 383
Cdd:cd01156 180 AFIVEKGMPGFSRAQKLDKLGM-------RGSntcelvfeDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAGGPI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 384 GSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNTYVMDAAAslityALVQGEKPAVLSAIVKYHCTHR 458
Cdd:cd01156 249 GIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAK-----ACDRGNMDPKDAAGVILYAAEK 323
|
330
....*....|....*.
gi 515495739 459 GQQSIVDAMDIAGGKG 474
Cdd:cd01156 324 ATQVALDAIQILGGNG 339
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
121-233 |
1.28e-21 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 90.60 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 121 TEEEQAFIDG----------PVEEACRMANDFqitheladlPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKL 190
Cdd:pfam02771 1 TEEQEALRDTvrefaeeeiaPHAAEWDEEGEF---------PRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 515495739 191 AGVSGILAITVGVPNSLGpGELLQHYGTEEQKNHYLPGLARGD 233
Cdd:pfam02771 72 ARADASVALALSVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
152-500 |
1.03e-17 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 86.01 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAgVSGILAITVGVPNSLGpGELLQHYGTEEQKNHYLPGLAR 231
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 232 GDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWQgkqvlgmrLTWNKRYITLAPVATVLGLAFKLHDPNRllsdnESPGIT 311
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVARTGGEAR-----GAGGIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 312 CALIPTSTPGVEIGNRHFPLNVPFQNGPTRG-TDVFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGSLKSIA 390
Cdd:cd01160 177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 391 LATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIA 470
Cdd:cd01160 253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350
....*....|....*....|....*....|
gi 515495739 471 GGKGIMLGESnfLARAYQGAPIAITVEGAN 500
Cdd:cd01160 333 GGWGYMREYP--IARAYRDARVQPIYGGTT 360
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
120-474 |
8.12e-17 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 83.26 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 120 LTEEEQAFIDgpveeacrMANDFQiTHELA----------DLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQK 189
Cdd:cd01162 1 LNEEQRAIQE--------VARAFA-AKEMAphaadwdqkkHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 190 LAGVSGILAITVGVPNSLGpgELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWQgkqvl 269
Cdd:cd01162 72 LSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYV----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 270 gmrLTWNKRYITLAPVATVLGLAFKlhdpnrllSDNESP-GITCALIPTSTPGVEIGNRHFPLNVPFQngPTRGT---DV 345
Cdd:cd01162 145 ---LNGSKAFISGAGDSDVYVVMAR--------TGGEGPkGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAVifeDC 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 346 FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTY 425
Cdd:cd01162 212 RVPVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELV 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515495739 426 vmdaAASLITY----ALVQGEKPAV-LSAIVKYHCTHRGQQSIVDAMDIAGGKG 474
Cdd:cd01162 288 ----ASRLMVRraasALDRGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
131-487 |
3.71e-14 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 75.27 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 131 PVEEACRMANDFQITHELADLPPELWAylKEHRFFAMIIK-----------KEYGGLEFSPYAQAMVLQKLAGVSGILAI 199
Cdd:PLN02526 31 PEEQALRKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGCPGLSITASAIATAEVARVDASCST 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 200 TVGVPNSLGPGELLQhYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTVCMGEWQgkqvlgmrLTWNKRY 279
Cdd:PLN02526 109 FILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWI--------LNGQKRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 280 I---TLAPVATVLGLAFKLHDPNRLLSDNESPGITCALIPTstpgvEIGNRHfplnvpFQNGPTRGTDVFVPIDYIIGGP 356
Cdd:PLN02526 180 IgnsTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIEN-----KIGLRM------VQNGDIVLKDVFVPDEDRLPGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 357 kmagQGWRMLVECLSVGRGITlpsnstgSLKSIALATGAY--AHI----RRQFKISIGKMEGIEEPLARIAGNTYVMdaa 430
Cdd:PLN02526 249 ----NSFQDTNKVLAVSRVMV-------AWQPIGISMGVYdmCHRylkeRKQFGAPLAAFQINQEKLVRMLGNIQAM--- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515495739 431 aSLITYALVQ----GEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMlgeSNFL-ARAY 487
Cdd:PLN02526 315 -FLVGWRLCKlyesGKMTPGHASLGKAWITKKARETVALGRELLGGNGIL---ADFLvAKAF 372
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
119-474 |
3.51e-13 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 72.07 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 119 RLTEEEQAFIDGPVEEACRMA--NDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAgvsgi 196
Cdd:PRK12341 4 SLTEEQELLLASIRELITRNFpeEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 197 laiTVGVP-NSLGPGELL---QHYGTEEQ-KNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTvcmgEWQGKQVLGM 271
Cdd:PRK12341 79 ---KCGAPaFLITNGQCIhsmRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYT----RKNGKVYLNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 272 RLTWnkryITLAPVAT-VLGLAfklHDPNrllSDNESPGITCALIPTSTPGVEIGNRHfplNVPFQNGPTRGT---DVFV 347
Cdd:PRK12341 152 QKTF----ITGAKEYPyMLVLA---RDPQ---PKDPKKAFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEVyldNVEV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 348 PIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVM 427
Cdd:PRK12341 219 EESDLVG---EEGMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENM 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 515495739 428 DAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKG 474
Cdd:PRK12341 295 RNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
155-474 |
7.31e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 71.45 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 155 LWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKNHYLPGLARGDE 234
Cdd:PLN02519 64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 235 IPCFALTSPEAGSDAgaipdVGTVCMGEWQGKqvlGMRLTWNKRYITLAPVATVLGLAFKlhdpnrllSDNE--SPGITC 312
Cdd:PLN02519 143 VGALAMSEPNSGSDV-----VSMKCKAERVDG---GYVLNGNKMWCTNGPVAQTLVVYAK--------TDVAagSKGITA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 313 ALIPTSTPGVEIGNRHFPLNVpfqngptRGTDV--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTG 384
Cdd:PLN02519 207 FIIEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 385 SLKSIALATGAYAHIRRQFKISIGKMEGIEEPLAriagNTYVMDAAASLITYALVQGEKPAVLS----AIVKYHCTHRGQ 460
Cdd:PLN02519 276 LMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLA----DMYTSLQSSRSYVYSVARDCDNGKVDrkdcAGVILCAAERAT 351
|
330
....*....|....
gi 515495739 461 QSIVDAMDIAGGKG 474
Cdd:PLN02519 352 QVALQAIQCLGGNG 365
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
171-481 |
1.27e-11 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 67.37 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 171 KEYGGLEFSPYAQAMVLQKLA-----GVSGILAItvgvpNSLGPgeLLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEA 245
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMAaagapVPFNQIGI-----DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 246 GSDAGAIPDVGTVCMGEWQgkqvlgmrLTWNKRYITLAPVATVLGLAFKlhdpnrllSDNESP---GITCALIPTSTPGV 322
Cdd:cd01152 129 GSDLAGLRTRAVRDGDDWV--------VNGQKIWTSGAHYADWAWLLVR--------TDPEAPkhrGISILLVDMDSPGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 323 EI-------GNRHFplNVPFQngptrgTDVFVPIDYIIGGPkmaGQGWRMLVECLSVGRGITLPSNSTG----SLKSIAL 391
Cdd:cd01152 193 TVrpirsinGGEFF--NEVFL------DDVRVPDANRVGEV---NDGWKVAMTTLNFERVSIGGSAATFfellLARLLLL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 392 ATGAYAHIRRQFkisigkmegIEEPLARIAGNTYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAG 471
Cdd:cd01152 262 TRDGRPLIDDPL---------VRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLG 332
|
330
....*....|
gi 515495739 472 GKGIMLGESN 481
Cdd:cd01152 333 TAALLRDPAP 342
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
237-325 |
4.92e-11 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 59.99 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 237 CFALTSPEAGSDAGAIpdvgTVCMGEWQGkqvLGMRLTWNKRYITLAPVATVLGLAFKLHDPNRllsdneSPGITCALIP 316
Cdd:pfam02770 1 AFALTEPGAGSDVASL----KTTAADGDG---GGWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
....*....
gi 515495739 317 TSTPGVEIG 325
Cdd:pfam02770 68 KDAPGVSVR 76
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
360-500 |
1.59e-10 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 59.96 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 360 GQGWRMLVECLSVGRgITLPSNSTGSLKSIALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNTYVMDAAASLITYALV 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515495739 440 QGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGIMLGESnfLARAYQGAPIAITVEGAN 500
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
119-475 |
1.36e-09 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 61.00 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 119 RLTEEEQAFIDGPVEeacRMAND-----FQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSPYAQAMVLQKLAGV 193
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 194 SGILAITVGVPNslGPGELLQHyGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAIPDVGTvcmgEWQGKqvlgMRL 273
Cdd:PRK03354 81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYT----RRNGK----VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 274 TWNKRYITLA---PVATVLGlafklhdpnRLLSDNESPGITCALIPTSTPGVEIGnrhfPL-----------NVPFQNGP 339
Cdd:PRK03354 150 NGSKCFITSSaytPYIVVMA---------RDGASPDKPVYTEWFVDMSKPGIKVT----KLeklglrmdsccEITFDDVE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 340 TRGTDVFvpidyiiggpKMAGQGWRMLVECLSVGRGITLPSNSTGSLKSIALATgAYAHIRRQFKISIGKMEGIEEPLAR 419
Cdd:PRK03354 217 LDEKDMF----------GREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAA-RYANQRVQFGEAIGRFQLIQEKFAH 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 515495739 420 IAGNTYVMDAAASLITYALVQGEKPAVLSAIVKYHCTHRGQQSIVDAMDIAGGKGI 475
Cdd:PRK03354 286 MAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-500 |
4.59e-05 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 46.61 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 166 AMIIKKEYGGLEFsPYAQAMVLQKL--AGVSGILAITVGVPNSlgpgELLQHYGTEEQKNHYLPGLARGDEIPCFALTSP 243
Cdd:cd01153 52 ALGVPEEYGGQGL-PITVYSALAEIfsRGDAPLMYASGTQGAA----ATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 244 EAGSDAG-----AIPDVGtvcmGEWqgkqvlgmRLTWNKRYIT--------------LA----PVATVLGLAFKLHdPNR 300
Cdd:cd01153 127 DAGSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLV-PKF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 301 LLsDNESPGITCALIP-------TSTPGVEIGNRHFPLnvpfqngptrgtdvfvpidyiIGGPKMA-------GQGWRML 366
Cdd:cd01153 194 LD-DGERNGVTVARIEekmglhgSPTCELVFDNAKGEL---------------------IGEEGMGlaqmfamMNGARLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 367 VECLSVGRGitlpsnSTGSLKSIalatgAYAHIRRQFK---ISIGKMEGIEEPLARIAGNT---YVMDAAASLITYALVQ 440
Cdd:cd01153 252 VGTQGTGLA------EAAYLNAL-----AYAKERKQGGdliKAAPAVTIIHHPDVRRSLMTqkaYAEGSRALDLYTATVQ 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515495739 441 --GEKPAV--------------LSAIVKYHCTHRGQQSIVDAMDIAGGKGIMlgESNFLARAYQGAPIAITVEGAN 500
Cdd:cd01153 321 dlAERKATegedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYT--REYPIEQYYRDARITTIYEGTT 394
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
185-502 |
6.48e-05 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 46.21 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 185 MVLQKLAGVSGILAITVG-VPnslgpgeLLQHYGTEEQKnHYLPGLA-RGDEIPCFA---LTSPEAGSDAGAIPDVGTVC 259
Cdd:cd01154 101 LLSDAAAGLLCPLTMTDAaVY-------ALRKYGPEELK-QYLPGLLsDRYKTGLLGgtwMTEKQGGSDLGANETTAERS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 260 MGE-WqgkqvlgmRLTWNKRYIT--LAPVATVLGLAfklhdpnrLLSDNESPGITCALIPTSTP-----GVEI------- 324
Cdd:cd01154 173 GGGvY--------RLNGHKWFASapLADAALVLARP--------EGAPAGARGLSLFLVPRLLEdgtrnGYRIrrlkdkl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 325 GNRHFPL-NVPFQNGptrgtdvfvpIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTGSL----KSIALAtGAYAHI 399
Cdd:cd01154 237 GTRSVATgEVEFDDA----------EAYLIGDE---GKGIYYILEMLNISR----LDNAVAALgimrRALSEA-YHYARH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 400 RRQFKISIgkmegIEEPL-----ARIAgntyVMDAAASLITYALV------QGEKPA------VLSAIVKYHCTHRGQQS 462
Cdd:cd01154 299 RRAFGKPL-----IDHPLmrrdlAEME----VDVEAATALTFRAArafdraAADKPVeahmarLATPVAKLIACKRAAPV 369
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 515495739 463 IVDAMDIAGGKGIMlgESNFLARAYQGAPIAITVEG-ANIL 502
Cdd:cd01154 370 TSEAMEVFGGNGYL--EEWPVARLHREAQVTPIWEGtGNIQ 408
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-252 |
2.33e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 44.86 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 133 EEACRMANDFQITheladLPP---ELWAYLKEHRFFAMIIKKEYGGLEFsPYAQAMVLQKL-AGVSGILAITVGVpnSLG 208
Cdd:PTZ00456 84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGQAL-PLSVGFITRELmATANWGFSMYPGL--SIG 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 515495739 209 PGELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPEAGSDAGAI 252
Cdd:PTZ00456 156 AANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQV 199
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
211-355 |
4.87e-04 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 43.15 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 211 ELLQHYGTEEQKNHYLPGLARGDEIPCFALTSPE-AGSDAGAIPdvgtvCMGEWQGKQVLgmrLTWNKRYITLA--P--- 284
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE-----CSIERDGDDYV---INGRKWWSSGAgdPrck 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515495739 285 VATVLGlafklhdpnRLLSDNESPGI--TCALIPTSTPGVEI----------GNRHFPLNVPFQNgptrgtdVFVPIDYI 352
Cdd:cd01155 174 IAIVMG---------RTDPDGAPRHRqqSMILVPMDTPGVTIirplsvfgydDAPHGHAEITFDN-------VRVPASNL 237
|
...
gi 515495739 353 IGG 355
Cdd:cd01155 238 ILG 240
|
|
| |
