|
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 ... |
3-814 |
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: 1781.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 3 ILSILATVVLLGVLFYHRVSLLLSSLILLAWTAALGVAGLWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPP 82
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 83 MSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEH 162
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 163 RFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTS 242
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 243 PEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGV 322
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 323 EIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQ 402
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 403 FKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNF 482
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 483 LARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGL 558
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 559 TRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADL 638
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 639 PLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTP 718
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 719 HNPVGLLEEALLDVMAADPIHQKICKQLGKNLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELA 798
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
810
....*....|....*.
gi 493863265 799 TQPVKLPEKHRKPEAA 814
Cdd:NF038187 801 AKPAKRPAKQKQDEAA 816
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
42-814 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1587.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 42 LWNIWVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLT 121
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 122 AEEQAFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITV 201
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 202 GVPNSLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYIT 281
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 282 LAPIATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQ 361
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 362 GWRMLVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLG 441
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 442 EKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNFLARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVL 521
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 522 EEMAAAQNND---VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLG 598
Cdd:PRK09463 481 KEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 599 GSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFP 678
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 679 TGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGKN-LPFTRLDE 757
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGkLPFLRLDE 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863265 758 LAKQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEELATQPVKLPEKHRKPEAA 814
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVEAA 777
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
46-803 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1190.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 46 WVLVPLAIILLPFNLTPMRKSMISAPVFKGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGNPDWKKLHNYPQPRLTAEEQ 125
Cdd:PRK13026 4 LIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 126 AFIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPN 205
Cdd:PRK13026 84 AFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 206 SLGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPI 285
Cdd:PRK13026 164 SLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 286 ATVLGLAFKLSDPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGQDIFVPIDYIIGGPKMAGQGWRM 365
Cdd:PRK13026 244 ATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 366 LVECLSVGRGITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPA 445
Cdd:PRK13026 324 LVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 446 VLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGNFLARGYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMA 525
Cdd:PRK13026 404 VVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEME 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 526 AAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSL 601
Cdd:PRK13026 484 AAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 602 KRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVAGALRVVIFPTGR 681
Cdd:PRK13026 564 KRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGN 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 682 HHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQL--GKNLPFTRLDELA 759
Cdd:PRK13026 644 HFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLELF 723
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 493863265 760 KQALAGGIIDNSEAAILVKAEESRLRSINVDDFEPEEL---ATQPVK 803
Cdd:PRK13026 724 AKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPDFMekkTLQSRK 770
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
514-792 |
1.77e-160 |
|
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: 467.35 E-value: 1.77e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 514 IRCHPYVLEEMAAAQNND----VDAFDKLLFKHIGHVGSNKVRSFWLGLTRGLTSATPTGDATKRYYQHLNRLSANLALL 589
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 590 SDVSMAVLGGSLKRRERISARLGDVLSQIFLASAVLKRYDDEGRQEADLPLVHWGVQDAMYQAEQAIDDLLANFPNRFVA 669
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 670 GALRVVIFPTGRHHLAPSDKLDHKVAKILQVPSATRSRIGRGQYLAPTPHNPVGLLEEALLDVMAADPIHQKICKQLGK- 748
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 493863265 749 NLPFTRLDELAKQALAGGIIDNSEAAILVKAEESRLRSINVDDF 792
Cdd:pfam09317 241 KLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
119-508 |
1.69e-86 |
|
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: 279.42 E-value: 1.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDgPVEEAC--RMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGI 196
Cdd:COG1960 4 ELTEEQRALRD-EVREFAeeEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 197 LAITVGVPNslGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVvcmgeWQGQqvlGMRLTWN 276
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV-----RDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 277 KRYITLAPIATVLGLAFKLsDPEKllggeEELGITCALIPTSTPGVEIGRRHFPLNV-PFQNGPTRGQDIFVPIDYIIGG 355
Cdd:COG1960 153 KTFITNAPVADVILVLART-DPAA-----GHRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 356 PkmaGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLIT 435
Cdd:COG1960 227 E---GKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863265 436 YGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAPIAITVEGANILTRSMMI 508
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYP--LERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
145-500 |
1.77e-36 |
|
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: 141.64 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 145 THEMadlPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKDH 224
Cdd:cd01158 28 KGEF---PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 225 YLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIATVLgLAFKLSDPEKllgG 304
Cdd:cd01158 104 YLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPSK---G 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 305 EEelGITCALIPTSTPGVEIGRRHFPLNVpfQNGPT---RGQDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgItlpsn 381
Cdd:cd01158 172 YR--GITAFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-I----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 382 stgGLKSVAMGIG--------AYAHIRRQFKISIGKMEGIEEPLARIAgnayVMDAAASLITYG-IML---GEKPAVLSA 449
Cdd:cd01158 239 ---GIAAQALGIAqaaldaavDYAKERKQFGKPIADFQGIQFKLADMA----TEIEAARLLTYKaARLkdnGEPFIKEAA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493863265 450 IVKYHCTHRAQQSIIDAMDIAGGKGIMlgeGNFLA-RGYQGAPIAITVEGAN 500
Cdd:cd01158 312 MAKLFASEVAMRVTTDAVQIFGGYGYT---KDYPVeRYYRDAKITEIYEGTS 360
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-513 |
1.85e-34 |
|
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: 136.44 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 101 DLFQGNPDWKKLhnYPQPRLTAEEQA----FIDGPVEEACRMANDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGL 176
Cdd:cd01161 5 NMFLGDIVTKQV--FPYPSVLTEEQTeelnMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 177 EFSAYAQARVLQKLaGVSGILAITVGVPNSLG-PGELLqhYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDT 255
Cdd:cd01161 83 GLNNTQYARLAEIV-GMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 256 GVVcmgEWQGQQVLgmrLTWNKRYITLAPIATVLGLAFKLsdPEKLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPF 335
Cdd:cd01161 160 AVL---SEDGKHYV---LNGSKIWITNGGIADIFTVFAKT--EVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 336 QNGPT-RGQDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIE 414
Cdd:cd01161 232 SNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 415 EPLARIAGNAYVMDAAASLITyGIM---LGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAP 491
Cdd:cd01161 308 EKLANMAILQYATESMAYMTS-GNMdrgLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERVLRDLR 384
|
410 420
....*....|....*....|..
gi 493863265 492 IAITVEGANILTRsMMIFGQGA 513
Cdd:cd01161 385 IFRIFEGTNEILR-LFIALTGL 405
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
207-511 |
3.58e-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: 130.87 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 207 LGPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWqgqqvlgmRLTWNKRYITLAPIA 286
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 287 TVLGLAFKLSDPekllgGEEELGITCALIPTSTPGVEIGRrhfPLNVPFQNG-PTRG---QDIFVPIDYIIGGPkmaGQG 362
Cdd:cd00567 114 DLFIVLARTDEE-----GPGHRGISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGEE---GGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 363 WRMLVECLSVGRgITLPSNSTGGLKSvAMGIGA-YAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDA----AASLITYG 437
Cdd:cd00567 183 FELAMKGLNVGR-LLLAAVALGAARA-ALDEAVeYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLllyrAAWLLDQG 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863265 438 ImlgEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGimLGEGNFLARGYQGAPIAITVEGANilTRSMMIFGQ 511
Cdd:cd00567 261 P---DEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA--EIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-474 |
5.04e-24 |
|
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: 104.80 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKDHYLPRLAR 231
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 232 GQEIPCFALTSPEAGSDagaipdtgVVCM---GEWQGQQVLgmrLTWNKRYITLAPIATVLgLAFKLSDPEKllggeEEL 308
Cdd:cd01156 114 GEHIGALAMSEPNAGSD--------VVSMklrAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDPSA-----GAH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 309 GITCALIPTSTPGVEIGRRHFPLNVpfqngptRG--------QDIFVPIDYIIGGpkmAGQGWRMLVECLSVGRGItLPS 380
Cdd:cd01156 177 GITAFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGG---ENKGVYVLMSGLDYERLV-LAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 381 NSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHC 455
Cdd:cd01156 246 GPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVAKACDR-----GNMDPKDAAGVILYA 320
|
330
....*....|....*....
gi 493863265 456 THRAQQSIIDAMDIAGGKG 474
Cdd:cd01156 321 AEKATQVALDAIQILGGNG 339
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
120-478 |
3.33e-22 |
|
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: 99.74 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFIDGpVEEAC--RMANDFAITHEMADLPPELWAYLKEHRFFAMIIKkEYGGLEFSAYAQARVLQKLAGVSGIL 197
Cdd:cd01151 13 LTEEERAIRDT-AREFCqeELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREVERVDSGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 198 AITVGVPNSLGPGELlQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGaipdtGVVCMGEWQGQqvlGMRLTWNK 277
Cdd:cd01151 91 RSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYKLNGSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 278 RYITLAPIATVLGLAFKLSDPEKLLGgeeelgitcALIPTSTPGVEIGRRH--FPLNVPfQNGPTRGQDIFVPIDYIIGG 355
Cdd:cd01151 162 TWITNSPIADVFVVWARNDETGKIRG---------FILERGMKGLSAPKIQgkFSLRAS-ITGEIVMDNVFVPEENLLPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 356 PKmagqGWRMLVECLSVGR-GItlpsnSTGGLkSVAMGIGA----YAHIRRQFKISIGKMEGIEEPLARIAGNayvmdaa 430
Cdd:cd01151 232 AE----GLRGPFKCLNNARyGI-----AWGAL-GAAEDCYHtarqYVLDRKQFGRPLAAFQLVQKKLADMLTE------- 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863265 431 aslITYGIMLGEKPAVLS----------AIVKYHCTHRAQQSIIDAMDIAGGKGIMLG 478
Cdd:cd01151 295 ---IALGLLACLRVGRLKdqgkatpeqiSLLKRNNCGKALEIARTAREMLGGNGISDE 349
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
121-232 |
1.17e-20 |
|
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: 87.90 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 121 TAEEQAFIDGPVEEACRMANDFAITHEMAD-LPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAI 199
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGeFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 493863265 200 TVGVPNSLGpGELLQHYGTEEQKDHYLPRLARG 232
Cdd:pfam02771 81 ALSVHSSLG-APPILRFGTEEQKERYLPKLASG 112
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
120-474 |
9.94e-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: 82.88 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFIDgpveeacrMANDFAiTHEMA----------DLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQK 189
Cdd:cd01162 1 LNEEQRAIQE--------VARAFA-AKEMAphaadwdqkkHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 190 LAGVSGILAITVGVPNSLGpgELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvl 269
Cdd:cd01162 72 LSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYV----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 270 gmrLTWNKRYITLAPIATVLGLAFKLsdpekllGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQngPTRG---QDIF 346
Cdd:cd01162 145 ---LNGSKAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQ--PTRAvifEDCR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 347 VPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLAriagnayv 426
Cdd:cd01162 213 VPVENRLGG---EGQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLA-------- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863265 427 mDAAASLITYGIML---------GEKPAV-LSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:cd01162 281 -DMATELVASRLMVrraasaldrGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
152-476 |
4.01e-14 |
|
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: 74.84 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 152 PPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAgVSGILAITVGVPNSLGpGELLQHYGTEEQKDHYLPRLAR 231
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 232 GQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQgqqvlgmrLTWNKRYITLAPIATVLGLAFKlSDPEKLLGGeeelGIT 311
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYV--------LNGSKTFITNGMLADVVIVVAR-TGGEARGAG----GIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 312 CALIPTSTPGVEIGRRHFPLNVPFQNGPTRG-QDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVA 390
Cdd:cd01160 177 LFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLG---EENKGFYYLMQNLPQER-LLIAAGALAAAEFML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 391 MGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIA 470
Cdd:cd01160 253 EETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
....*.
gi 493863265 471 GGKGIM 476
Cdd:cd01160 333 GGWGYM 338
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
155-474 |
3.90e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 72.22 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 155 LWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGVSGILAITVGVPNSLGPGELLQHyGTEEQKDHYLPRLARGQE 234
Cdd:PLN02519 64 LWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 235 IPCFALTSPEAGSDagaipdtgVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLgLAFKLSDPEkllGGEEelGITCAL 314
Cdd:PLN02519 143 VGALAMSEPNSGSD--------VVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL-VVYAKTDVA---AGSK--GITAFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 315 IPTSTPGVEIGRRHFPLNVpfqngptRGQDI--------FVPIDYIIGGpkmAGQGWRMLVECLSVGRgITLPSNSTGGL 386
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLGM-------RGSDTcelvfencFVPEENVLGQ---EGKGVYVMMSGLDLER-LVLAAGPLGLM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 387 KSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARI-----AGNAYVMDAAASLITygimlGEKPAVLSAIVKYHCTHRAQQ 461
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDN-----GKVDRKDCAGVILCAAERATQ 352
|
330
....*....|...
gi 493863265 462 SIIDAMDIAGGKG 474
Cdd:PLN02519 353 VALQAIQCLGGNG 365
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
237-335 |
5.47e-12 |
|
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: 62.68 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 237 CFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlGMRLTWNKRYITLAPIATVLGLAFKLSDPEKllggeeELGITCALIP 316
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*....
gi 493863265 317 TSTPGVEIGRRHFPLNVPF 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLGVRG 86
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
120-427 |
6.52e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 68.34 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 120 LTAEEQAFidgpveeacRMANDFAITHEMADLPPELWAylKEHRFFAMIIK-----------KEYG--GLEFSAYAQArv 186
Cdd:PLN02526 29 LTPEEQAL---------RKRVRECMEKEVAPIMTEYWE--KAEFPFHIIPKlgslgiaggtiKGYGcpGLSITASAIA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 187 LQKLAGVSGILAITVGVPNSLGPGELLQhYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEW--Q 264
Cdd:PLN02526 96 TAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWilN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 265 GQqvlgmrltwnKRYITLAPIATVLGLAFKLSDPEKLLG---GEEELGITCALIPTstpgvEIGRRHfplnvpFQNGPTR 341
Cdd:PLN02526 175 GQ----------KRWIGNSTFADVLVIFARNTTTNQINGfivKKGAPGLKATKIEN-----KIGLRM------VQNGDIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 342 GQDIFVPIDYIIGGPkmagQGWRMLVECLSVGRgITLPSNSTGglksVAMGIGAYAHI----RRQFKISIGKMEGIEEPL 417
Cdd:PLN02526 234 LKDVFVPDEDRLPGV----NSFQDTNKVLAVSR-VMVAWQPIG----ISMGVYDMCHRylkeRKQFGAPLAAFQINQEKL 304
|
330
....*....|
gi 493863265 418 ARIAGNAYVM 427
Cdd:PLN02526 305 VRMLGNIQAM 314
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
169-474 |
9.03e-12 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD 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. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 67.61 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 169 IKKEYGGLEFSAYAQARVLQKLA-GVSGILAITVGvpNSLGPGELLQHyGTEEQKDHYLPRLARGQEIPCFALTSPEAGS 247
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 248 DAGAIPDTGVVCMGEW--QGQQVL---GMRLTWnkrYITLAPiatvlglafklSDPE-KLLGGEeelGITCALIPTSTPG 321
Cdd:cd01157 128 DVAGIKTKAEKKGDEYiiNGQKMWitnGGKANW---YFLLAR-----------SDPDpKCPASK---AFTGFIVEADTPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 322 VEIGRRHfpLNVPFQNGPTRG---QDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTG--GLKSVAMGIGA- 395
Cdd:cd01157 191 IQPGRKE--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGavGLAQRALDEATk 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493863265 396 YAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:cd01157 262 YALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
171-375 |
6.22e-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: 65.06 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 171 KEYGGLEFSAYAQARVLQKLA-----GVSGILAItvgvpNSLGPgeLLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEA 245
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMAaagapVPFNQIGI-----DLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 246 GSDAGAIPDTGVVCMGEWQ--GQQVlgmrltWNkryiTLAPIATVLGLAFKlSDPEkllgGEEELGITCALIPTSTPGVE 323
Cdd:cd01152 129 GSDLAGLRTRAVRDGDDWVvnGQKI------WT----SGAHYADWAWLLVR-TDPE----APKHRGISILLVDMDSPGVT 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863265 324 I-------GRRHFplNVPFQNgptrgqDIFVPIDYIIGGPkmaGQGWRMLVECLSVGRG 375
Cdd:cd01152 194 VrpirsinGGEFF--NEVFLD------DVRVPDANRVGEV---NDGWKVAMTTLNFERV 241
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
119-474 |
1.68e-10 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 63.59 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDGPVEEACRMA--NDFAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAgvsgi 196
Cdd:PRK12341 4 SLTEEQELLLASIRELITRNFpeEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 197 laiTVGVP-NSLGPGELL---QHYGTEEQK----DHYLprlARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqv 268
Cdd:PRK12341 79 ---KCGAPaFLITNGQCIhsmRRFGSAEQLrktaESTL---ETGDPAYALALTEPGAGSDNNSATTTYTRKNGK------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 269 lgMRLTWNKRYITLA---PIATVLGLAFKLSDPEKllggeeelGITCALIPTSTPGVEIGRRHfplNVPFQNGPTRG--- 342
Cdd:PRK12341 147 --VYLNGQKTFITGAkeyPYMLVLARDPQPKDPKK--------AFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEvyl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 343 QDIFVPIDYIIGgpkMAGQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAG 422
Cdd:PRK12341 214 DNVEVEESDLVG---EEGMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAI 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493863265 423 NAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKG 474
Cdd:PRK12341 290 KIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
119-475 |
2.71e-09 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 59.85 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 119 RLTAEEQAFIDGPVEeacRMAND-----FAITHEMADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYAQARVLQKLAGV 193
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnweayFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 194 SGILAITVGVPNslGPGELLQHyGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEwqgqqvlgMRL 273
Cdd:PRK03354 81 GAPTYVLYQLPG--GFNTFLRE-GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGK--------VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 274 TWNKRYIT-LAPIATVLGLAFKLSDPEKLLGGEeelgitcALIPTSTPGVEIG-------RRHFPLNVPFQNGPTRGQDI 345
Cdd:PRK03354 150 NGSKCFITsSAYTPYIVVMARDGASPDKPVYTE-------WFVDMSKPGIKVTkleklglRMDSCCEITFDDVELDEKDM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 346 FvpidyiiggpKMAGQGWRMLVECLSVGRGITLPSNStgGLKSVAMGIGA-YAHIRRQFKISIGKMEGIEEPLARIAGNA 424
Cdd:PRK03354 223 F----------GREGNGFNRVKEEFDHERFLVALTNY--GTAMCAFEDAArYANQRVQFGEAIGRFQLIQEKFAHMAIKL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 493863265 425 YVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGI 475
Cdd:PRK03354 291 NSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
360-500 |
7.40e-09 |
|
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: 55.34 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 360 GQGWRMLVECLSVGRgITLPSNSTGGLKSVAMGIGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIM 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493863265 440 LGEKPAVLSAIVKYHCTHRAQQSIIDAMDIAGGKGIMLGEGnfLARGYQGAPIAITVEGAN 500
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTS 138
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-328 |
9.91e-07 |
|
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: 52.01 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 166 AMIIKKEYGGLEF-----SAYAQARvlqkLAGVSGILAITVGVPNSlgpgELLQHYGTEEQKDHYLPRLARGQEIPCFAL 240
Cdd:cd01153 52 ALGVPEEYGGQGLpitvySALAEIF----SRGDAPLMYASGTQGAA----ATLLAHGTEAQREKWIPRLAEGEWTGTMCL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 241 TSPEAGSDAG-----AIPDTGvvcmGEWqgqqvlgmRLTWNKRYIT--------------LA----PIATVLGLAFKLSd 297
Cdd:cd01153 124 TEPDAGSDLGalrtkAVYQAD----GSW--------RINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLV- 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863265 298 PEKLLGG----------EEELGI----TCALIPTSTPGVEIGRRH 328
Cdd:cd01153 191 PKFLDDGerngvtvariEEKMGLhgspTCELVFDNAKGELIGEEG 235
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
133-259 |
3.32e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 47.56 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 133 EEACRMANDFAIThemadLPP---ELWAYLKEHRFFAMIIKKEYGG--LEFSAYAQARVLQKLAGVSgiLAITVGVpnSL 207
Cdd:PTZ00456 84 SEGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGGqaLPLSVGFITRELMATANWG--FSMYPGL--SI 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 493863265 208 GPGELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVC 259
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPS 206
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
211-333 |
1.14e-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: 45.46 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 211 ELLQHYGTEEQKDHYLPRLARGQEIPCFALTSPE-AGSDAgaipdTGVVCMGEWQGQQVLgmrLTWNKRYITLA-----P 284
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDA-----TNIECSIERDGDDYV---INGRKWWSSGAgdprcK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493863265 285 IATVLGlafkLSDPEKLLGGEEELGItcaLIPTSTPGVEIGRrhfPLNV 333
Cdd:cd01155 174 IAIVMG----RTDPDGAPRHRQQSMI---LVPMDTPGVTIIR---PLSV 212
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
188-502 |
9.02e-03 |
|
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: 39.28 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 188 QKLAGVSGILAITVG-VPnslgpgeLLQHYGTEEQKDHYLPRLARGQEIPCFA---LTSPEAGSDAGAIPDTGVVCMGE- 262
Cdd:cd01154 104 DAAAGLLCPLTMTDAaVY-------ALRKYGPEELKQYLPGLLSDRYKTGLLGgtwMTEKQGGSDLGANETTAERSGGGv 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 263 WqgqqvlgmRLTWNKrYITLAPIATVlglAFKLSDPEKLLGGEEelGITCALIPTSTP-----GVEI-------GRRHFP 330
Cdd:cd01154 177 Y--------RLNGHK-WFASAPLADA---ALVLARPEGAPAGAR--GLSLFLVPRLLEdgtrnGYRIrrlkdklGTRSVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 331 L-NVPFQNGptrgqdifvpIDYIIGGPkmaGQGWRMLVECLSVGRgitlPSNSTGglksvAMGI--------GAYAHIRR 401
Cdd:cd01154 243 TgEVEFDDA----------EAYLIGDE---GKGIYYILEMLNISR----LDNAVA-----ALGImrralseaYHYARHRR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863265 402 QFKISIgkmegIEEPLAR--IAGNAYVMDAAASLITYGIMLGEKPA-----------VLSAIVKYHCTHRAQQSIIDAMD 468
Cdd:cd01154 301 AFGKPL-----IDHPLMRrdLAEMEVDVEAATALTFRAARAFDRAAadkpveahmarLATPVAKLIACKRAAPVTSEAME 375
|
330 340 350
....*....|....*....|....*....|....*
gi 493863265 469 IAGGKGIMlgEGNFLARGYQGAPIAITVEG-ANIL 502
Cdd:cd01154 376 VFGGNGYL--EEWPVARLHREAQVTPIWEGtGNIQ 408
|
|
|