|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-1014 |
0e+00 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 1524.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 2 DVSRRKFFKICAGGMAGTTAAALGFAPKMALAQARNFKLLRAKEIRNTCTYCSVGCGLLMYSLGDGAKNAKEAIYHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 82 PDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSDKWQRISWDEAFNRIARLMKADRDANFIEKNEQGVTVNRWLST 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 162 GMLCASAASNETGMLTQKFVRSLGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 242 RWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTNASLLVRDDFAFEEG 321
Cdd:TIGR01553 241 KWAIRAKKKG-AKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 322 LFSGYDAEKRQYDKSSWNYQFDENGYAKRDETLTHPRCVWNLLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTSAAD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 402 RTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSTSLPGYLTLPSDKQTDLQSY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 482 LSANTPKATLPEQVNYWSNYPKFFVSLMKSFYGEAAQKENDWGFEWLPKWDQAYDVI-KYFNMMDNGNVTGYICQGFNPV 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDSWlTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 561 ASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFWQNHGesndVDPSAIQTEVFRLPSTCFAEEDGSIANSGRWLQWHWKGQ 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 641 DAPGEARNDGEILAGIYHRLRELYRTEGGKGAEPLLKMSWRYKQPDHPESEEVAKENNGYALADLYDQNgtLLAKKGQLL 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDFKVGD--VEYKKGQQI 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 721 NSFALLRDDGSTASSCWIYTGSWTEQGNQMANRDNADPSGLGNTLGWAWAWPLNRRVLYNRASADINGKPWDAKRMLIQW 800
Cdd:TIGR01553 714 ATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALVEW 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 801 NGS--KWVGnDIPDFN-TAPPGSNTGPFIMQQEGLGRLFALDKLAEGPFPEHYEPIETPLGTNPLHPKVVSSPVVRLYEE 877
Cdd:TIGR01553 794 NAAekKWVG-DIPDYPpTAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYKT 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 878 DAIRLGKKDKFPYVGTTYRLTEHFHTWTKHALLNSIAQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRL 957
Cdd:TIGR01553 873 DEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRI 952
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205134601 958 RTLNVNGQQVETVGIPLHWGFEGVARKGYIANTLTPNVGDSNSQTPEYKAFLVNIEK 1014
Cdd:TIGR01553 953 KPLAIQGQQVHMIGIPIHWGWSFLKNGGDATNILTPSVGDPNTGTPETKAFLVNIEK 1009
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
47-873 |
0e+00 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 1035.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 47 RNTCTYCSVGCGLLMYSLGdgaknakEAIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSDKWQRISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQN-------GVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 127 DEAFNRIARLMKADRDANFIEKNEQGVTVNRWLSTGMLCASAASNETGMLTQKFVRSLGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 207 TFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 287 VLLYLIennkinaeyvkhytnasllvrddfafeeglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnllkq 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 367 hvsRYTPEVVENICGTPKADFLKVCDVLASTSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 447 GHSNIQGLTDLGLLSTSLPGYLTlpsdkqtdlqsylsantpkatlpeqvnywsnypkffvslmksfygeaaqkendwgfe 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 527 wlpkwdqaydvikyfnmmdngnvtgyicqGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFWQNHGesndVDPSA 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 607 IQTEVFRLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHRLRELYRTEGGKGAEPLLKmsWRYKQPD 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 687 HPESEEVAKENNGYALADLY-DQNGTLLAKKGQLLNSFALLRDDGSTASSCWIYTGSWTEQGNqMANRDNADPSGLGNTL 765
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYtGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYP 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 766 GWAWAWPLNRRVLYNRASADINGKPWDAKRMLIQWNGSK-WVGNDIPDF-NTAPPGSNTGPFIMQQEGLGRLFALDKlaE 843
Cdd:cd02752 544 GWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGLGwWWKGDVPDGpWPAAKEHGCGPFIMAPEGQARLFVWNF--D 621
|
810 820 830
....*....|....*....|....*....|
gi 1205134601 844 GPFPEHYEPIETPLGTNplHPKVVSSPVVR 873
Cdd:cd02752 622 GPFPEHYEPLESPRPDL--HSKVAKNPTYK 649
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
15-1012 |
0e+00 |
|
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type found in the Actinomycetota, as in the genera Streptomyces, Nocardiopsis, Gordonia, and Saccharomonospora. Many are selenoproteins.
Pssm-ID: 469399 [Multi-domain] Cd Length: 1066 Bit Score: 928.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 15 GMAGTTAAALGFAPKMALAQarnfkllraKEIRNTCTYCSVGCGLLMYslgdgAKNAKeaIYHIEGDPDHPVSRGALCPK 94
Cdd:NF041513 21 GAAARSARTRALRPRTATAD---------RVVRSVCPYCAVGCGQKVY-----VKDEK--VVQIEGDPDSPISRGRLCPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 95 GAGLLDYVHSENRLRYPQYRAPGSDKWQRISWDEAFNRIARLMKADRDANFIEKNEQGVTVNRWLSTGMLCASAASNETG 174
Cdd:NF041513 85 GSASLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEEN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 175 MLTQKFVRSLGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdAT 254
Cdd:NF041513 165 YLIKKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAKARG-AT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 255 LIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTNASLLVRDDFAFEE---GLFSGYDAEKR 331
Cdd:NF041513 244 VIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFRDTEdldGLFSGFDPETG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 332 QYDKSSWNYQFDEN----------------------------------GYAKRDETLTHPRCVWNLLKQHVSRYTPEVVE 377
Cdd:NF041513 324 SYDPASWQYEGVEVaaaagqrdqlydsrggahesargeehgsggapvaGAPRRDETLQDPRCVFQILKRHFARYTPEMVE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 378 NICGTPKADFLKVCDVLASTSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDL 457
Cdd:NF041513 404 EICGIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 458 GLLSTSLPGYLTLP-SDKQTDLQSYLSANTPkatlpeQVNYWSNYPKFFVSLMKSFYGEAAQKENDWGFEWLPKWDQA-- 534
Cdd:NF041513 484 PTLFNLLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDhs 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 535 -YDVIkyFNMMDnGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFWQNHGE--SNDVDPSAIQTEV 611
Cdd:NF041513 558 tYQTV--MAMLD-GKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEieTGELRTEDIGTEV 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 612 FRLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDgeiLAGIYH---RLRELYRTEGGKGAEPLLKMSWRY---KQP 685
Cdd:NF041513 635 FFFPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSD---LWFFYHlgrRIREKLAGSTDPRDRPLLDLTWDYpteGPH 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 686 DHPESEEVAKENNGYALAdlydqngtllakkGQLLNSFALLRDDGSTASSCWIYTGSWTEQGNQMANRDnadPSGLGNTL 765
Cdd:NF041513 712 GEPDAEAVLAEINGYDLS-------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWV 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 766 G--WAWAWPLNRRVLYNRASADINGKPWDAKRMLIQWN--GSKWVGNDIPDFN-TAPPG-------------SNTGPFIM 827
Cdd:NF041513 776 AaeWGWAWPANRRILYNRASADPEGRPWSERKKYVWWDaeAGRWTGYDVPDFPvDKPPDyrpppgatgpaalSGDDPFIM 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 828 QQEGLGRLFALDKLAEGPFPEHYEPIETPLGtNPLHPKvVSSPVVRLYEEDAIRLGKK------DKFPYVGTTYRLTEHf 901
Cdd:NF041513 856 QADGKGWLFAPAGLVDGPLPTHYEPQESPVR-NPLYGQ-QRNPARKVYPREDNRYHPSggepgaEVYPYVFTTYRLTEH- 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 902 HT------WTKHAllnSIAQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTLNVNGQQVETVGIPLH 975
Cdd:NF041513 933 HTaggmsrWLPYL---AELQPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYH 1009
|
1050 1060 1070
....*....|....*....|....*....|....*..
gi 1205134601 976 WGFEGVARkGYIANTLTPNVGDSNSQTPEYKAFLVNI 1012
Cdd:NF041513 1010 WGPNGLVT-GDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
44-1015 |
4.61e-150 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 461.66 E-value: 4.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 44 KEIRNTCTYCSVGCGLLMYSLGDGaknakeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGsdKWQR 123
Cdd:COG3383 5 KKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 124 ISWDEAFNRIARLMKADRDANFIEkneqgvtvnrwlSTGMLCASAASNETGMLTQKFVRS-LGMLAVDNQARVUHGPTVA 202
Cdd:COG3383 76 VSWDEALDLVAERLREIQAEHGPD------------AVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 203 SLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDIT 282
Cdd:COG3383 144 GLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNG-AKLIVVDPRRTETARLADLHLQIKPGTDLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 283 FLSGVLLYLIENNKINAEYVKHYTNasllvrddfafeeglfsGYDAekrqydksswnyqfdengyakrdetlthprcvwn 362
Cdd:COG3383 223 LLNGLLHVIIEEGLVDEDFIAERTE-----------------GFEE---------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 363 lLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTSAAdrttTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGV 442
Cdd:COG3383 252 -LKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRA----MILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 443 NALRGHSNIQGLTDLGLLSTSLPGYLtlpsdkqtdlqsylsantpKATLPEqvnywsnypkffvslmksfygEAAQKEND 522
Cdd:COG3383 327 FPLTGQNNVQGGRDMGALPNVLPGYR-------------------DVTDPE---------------------HRAKVADA 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 523 WGFEWLPKWdQAYDVIKYFNMMDNGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFwqnhgesNDV 602
Cdd:COG3383 367 WGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY-------ADV 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 603 dpsaiqtevfRLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHRLrelyrteggkGAEpllkmsWRY 682
Cdd:COG3383 439 ----------VLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRL----------GYG------FDY 492
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 683 kqpDHPES--EEVAKENNGYALAdlydqngtllakkgqllnSFALLRDDGStasscwiytgswteqgnqmanrdnadpsg 760
Cdd:COG3383 493 ---DSPEEvfDEIARLTPDYSGI------------------SYERLEALGG----------------------------- 522
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 761 lgntlgwaWAWPLNrrvlynraSADINGKPwdakRMLIQwngskwvgndipDFNTAppgsntgpfimqqEGLGRLFALdk 840
Cdd:COG3383 523 --------VQWPCP--------SEDHPGTP----RLFTG------------RFPTP-------------DGKARFVPV-- 555
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 841 laegpfpEHYEPIETPlgtnplhpkvvsspvvrlyeedairlgkKDKFPYVGTTYRLTEHFHTWTKH---ALLNSIAqPE 917
Cdd:COG3383 556 -------EYRPPAELP----------------------------DEEYPLVLTTGRLLDQWHTGTRTrrsPRLNKHA-PE 599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 918 QFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTlnvnGqqveTVGIPLHWGFEGvarkgyiANTLTPNVGD 997
Cdd:COG3383 600 PFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP----G----TVFMPFHWGEGA-------ANALTNDALD 664
|
970
....*....|....*...
gi 1205134601 998 SNSQTPEYKAFLVNIEKA 1015
Cdd:COG3383 665 PVSKQPEYKACAVRVEKV 682
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
28-1015 |
1.00e-127 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 403.07 E-value: 1.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 28 PKMALAQARNFKLLRAKEIRNTCTYCSVGCGLLMYSLGDGaknakeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENR 107
Cdd:COG0243 6 FKAAGAGAAALEAAGTKTVKTTCPGCGVGCGLGVKVEDGR-------VVRVRGDPDHPVNRGRLCAKGAALDERLYSPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 108 LRYPQYR--APGSDKWQRISWDEAFNRIARLMKADRDanfiEKNEQGVtvnrWLSTGMLCASAASNETGMLTQKFVRSLG 185
Cdd:COG0243 79 LTYPMKRvgPRGSGKFERISWDEALDLIAEKLKAIID----EYGPEAV----AFYTSGGSAGRLSNEAAYLAQRFARALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 186 MLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNDATLIVVDPRFTRT 265
Cdd:COG0243 151 TNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTET 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 266 ASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTNasllvrddfafeeglfsGYDAekrqydksswnyqfden 345
Cdd:COG0243 231 AAIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTV-----------------GFDE----------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 346 gyakrdetlthprcvwnlLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTsaadRTTTFLYALGWTQHTVGAQNIRTM 425
Cdd:COG0243 277 ------------------LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQQHSNGTQTVRAI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 426 AMIQLLLGNMGMAGGGVNALRGHsniqgltdlgllstslpgyltlpsdkqtdlqsylsantpkatlpeqvnywsnypkff 505
Cdd:COG0243 335 ANLALLTGNIGKPGGGPFSLTGE--------------------------------------------------------- 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 506 vslmksfygeaaqkendwgfewlpkwdqaydvikyfnMMDNG---NVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVI 582
Cdd:COG0243 358 -------------------------------------AILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVI 400
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 583 DPLVTETSTFwqnhgesNDVdpsaiqtevfRLPSTCFAEEDGSIANSG-RWLQWHWKGQDAPGEARNDGEILAGIYHRLr 661
Cdd:COG0243 401 DTFLTETARY-------ADI----------VLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRL- 462
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 662 elyrteggkGAEPLLkmswrykqPDHPESEEVAKEnngyaladlydqngtLLAKKGQLLNSFALLRDDGstasscwiytg 741
Cdd:COG0243 463 ---------GFEEAF--------PWGRTEEDYLRE---------------LLEATRGRGITFEELREKG----------- 499
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 742 swteqgnqmanrdnadpsglgntlgwAWAWPLNRRVLYnrasadingkpwdakrmliqwngskwvGNDIPdFNTAppgSn 821
Cdd:COG0243 500 --------------------------PVQLPVPPEPAF---------------------------RNDGP-FPTP---S- 521
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 822 tgpfimqqeglGRL-FALDKLAEGPFPEHYEPIEtplGTNPLhpkvvsspvvrlyeedairlgkKDKFPYVGTTYRLTEH 900
Cdd:COG0243 522 -----------GKAeFYSETLALPPLPRYAPPYE---GAEPL----------------------DAEYPLRLITGRSRDQ 565
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 901 FHTWT-KHALLNSIaQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTlnvngqqvETVGIPLHWGFE 979
Cdd:COG0243 566 WHSTTyNNPRLREI-GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GVVFAPHGWWYE 636
|
970 980 990
....*....|....*....|....*....|....*.
gi 1205134601 980 GVARKGYIANTLTPNVGDSNSQTPEYKAFLVNIEKA 1015
Cdd:COG0243 637 PADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1012 |
1.18e-122 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 389.52 E-value: 1.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYslgdgAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRApgSDKWQRISWDE 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIRE--GDKFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 129 AFNRIARLMKADRDAnfiekneQGVTvnrwlSTGMLCASAASNETGMLTQKFVRS-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKEIKEK-------YGPD-----SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 208 FGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNG-AKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 288 LLYLIENNKINAEYVKHYTNasllvrddfAFEEglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnlLKQH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAFIEKRTE---------GFEE-------------------------------------------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 368 VSRYTPEVVENICGTPKADFLKvcdvLASTSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 448 HSNIQGLTDLGLLSTSLPGYltlpsdkqtdlqsylsantpkatlpEQVNYWSNYPKFfvslmksfygeaaqkENDWGFEW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGY-------------------------QPVSDEEVREKF---------------AKAWGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 528 LPKwDQAYDVIKYFNMMDNGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFwqnhgesndvdpsai 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 608 qTEVFrLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHRLrelyrteggkGAEpllkmsWRYkqpDH 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANAL----------GLD------WNY---NH 486
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 688 PesEEVAKEnngyaladlydqngtllakkgqllnsfallrddgsTASSCWIYTGswteqgnqmANRDNADpsGLGNTLgw 767
Cdd:TIGR01591 487 P--QEIMDE-----------------------------------IRELTPLFAG---------LTYERLD--ELGSLQ-- 516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 768 awaWPLNRRVLYNRASADINGkpwdakrmliqwngskwvgndipdfntappgsntgpfIMQQEGLGRLFALDKLAegpfp 847
Cdd:TIGR01591 517 ---WPCNDSDASPTSYLYKDK-------------------------------------FATPDGKAKFIPLEWVA----- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 848 ehyePIETPlgtnplhpkvvsspvvrlyeedairlgkKDKFPYVGTTYRLTEHFHT--WTKH--ALLNSIaqPEQFVEIS 923
Cdd:TIGR01591 552 ----PIEEP----------------------------DDEYPLILTTGRVLTHYNVgeMTRRvaGLRRLS--PEPYVEIN 597
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 924 EGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRlrtlnvngQQVETVGIPLHWGFEGVarkgyiaNTLTPNVGDSNSQTP 1003
Cdd:TIGR01591 598 TEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDR--------VNKGAIYITMHFWDGAV-------NNLTTDDLDPISGTP 662
|
....*....
gi 1205134601 1004 EYKAFLVNI 1012
Cdd:TIGR01591 663 EYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-660 |
3.49e-117 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 369.62 E-value: 3.49e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYSlgdgaKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGsdKWQRISWDE 128
Cdd:cd02753 3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 129 AFNRIARLMKADRDANFIEkneqgvtvnrwlSTGMLCASAASNETGMLTQKFVRS-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:cd02753 74 ALSLVASRLKEIKDKYGPD------------AIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSPTVAGLAET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 208 FGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKnNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGV 287
Cdd:cd02753 142 LGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAK-RNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 288 LLYLIENNKINAEYVKHYTNasllvrddfafeeglfsGYDAekrqydksswnyqfdengyakrdetlthprcvwnlLKQH 367
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTE-----------------GFEE-----------------------------------LKEI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 368 VSRYTPEVVENICGTPKADFLKVcdvlASTSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02753 249 VEKYTPEYAERITGVPAEDIREA----ARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 448 HSNIQGLTDLGLLSTSLPGYltlpsdkqtdlqsylsantpkatlpeqvnywsnypkffvslmksfygeaaqkendwgfew 527
Cdd:cd02753 325 QNNVQGACDMGALPNVLPGY------------------------------------------------------------ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 528 lpkwdqaydvikyfnmmdngnVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFwqnhgesNDVdpsai 607
Cdd:cd02753 345 ---------------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL-------ADV----- 391
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1205134601 608 qteVfrLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHRL 660
Cdd:cd02753 392 ---V--LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRL 439
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-660 |
1.57e-86 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 283.06 E-value: 1.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 47 RNTCTYCSVGCGLLMYSlgdgaKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSDKWQRISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 127 DEAFNRIARLMKADRDAnfiekneqgvtvNRWLSTGMLCASAASNETGMLTQKFVRSLGMLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREK------------YGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 207 TFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRG-AKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 287 vllyliennkinaeyvkhytnasllvrddfafeeglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnllkq 366
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 367 hvsrytpEVVENICGTPKADFLKVCDVLASTsaadRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 220 -------EWAAEITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 447 ghsniqgltdlgllstslpgyltlpsdkqtdlqsylsantpkatlpeqvnywsnypkffvslmksfygeaaqkendwgfe 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 527 wlpkwdqaydvikyfnmmdngnvtgyicqGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTFwqnhgesNDVdpsa 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-------ADV---- 326
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1205134601 607 iqtevfRLPSTCFAEEDGSIANSGRWLQWHWKGQDAPGEARNDGEILAGIYHRL 660
Cdd:cd00368 327 ------VLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-660 |
3.50e-84 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 282.96 E-value: 3.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 47 RNTCTYCSVGCGLLMYSLGDGAKNAKeaiyhieGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSdKWQRISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 127 DEAFNRIARLMKADRDanfiEKNEQGVTVnrwLSTGMLCasaasNETGMLTQKFVRS-LGMLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFKAIQA----EYGPDSVAF---YGSGQLL-----TEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 206 PTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAK-NNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 285 SGVLLYLIENNKINAEYVKHYTNasllvrddfafeeglfsGYDAekrqydksswnyqfdengyakrdetlthprcvwnlL 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTE-----------------GFEE-----------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 365 KQHVSRYTPEVVENICGTPKADFLKVCDVLASTsaadRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 445 LRGHSNIQGLTDLGLLSTSLPGYLTLPSDKqtdlqsylsantpkatlpeqvnywsnypkffvslmksfygEAAQKENDWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 525 FEWLPKWDQA-YDVIKYFNMMDNGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDP-LVTETSTFwqnhgesNDV 602
Cdd:cd02754 365 VPEGTIPPKPgLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEY-------ADL 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205134601 603 dpsaiqtevfRLPSTCFAEEDGSIANSGRWLQwHWKGQ-DAPGEARNDGEILAGIYHRL 660
Cdd:cd02754 438 ----------VLPAASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRL 485
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
886-1014 |
8.14e-57 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 191.67 E-value: 8.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 886 DKFPYVGTTYRLTEHFHTW--TKHALLNSIAQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRtlnvn 963
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 964 gqqVETVGIPLHWGFEGVaRKGYIANTLTPNVGDSNSQTPEYKAFLVNIEK 1014
Cdd:cd02792 76 ---PHEVGIPYHWGGMGL-VIGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-661 |
2.32e-51 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 190.60 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 107 RLRYPQYRAPGSDKWQRISWDEAFNRIARLMKAdrdanfIEKNEQGvtvnrWLSTGmlcasAASNETGMLTQKFVRSLGM 186
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRA------LDPDRAA-----FYTSG-----RASNEAAYLYQLFARAYGT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDP------ 260
Cdd:cd02767 128 NNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRG-GKIIVINPlrepgl 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 261 -RF----------TRTASVADIYAPIRSGTDITFLSGVLLYLIEN-----NKINAEYVKHYTNasllvrddfafeeglfs 324
Cdd:cd02767 207 eRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTS----------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 325 GYDAEKRQYDKSSWnyqfdengyakrdetlthprcvwnllkqhvsrytpEVVENICGTPKADFLKVCDVLASTSAAdrtt 404
Cdd:cd02767 270 GFEEYVAALRALSW-----------------------------------DEIERASGLSREEIEAFAAMYAKSERV---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 405 TFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlstslpgyltlpsdkqtdlqsylsa 484
Cdd:cd02767 311 VFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 485 nTPKatlPEQVNywsnypkffvslmksfygeAAQKENDWGFEwLPKWDqAYDVIKYFNMMDNGNVTGYICQGFNPVASFP 564
Cdd:cd02767 366 -TEK---PFPEF-------------------LDALEEVFGFT-PPRDP-GLDTVEAIEAALEGKVKAFISLGGNFAEAMP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 565 DKNKVVRSLSKLKYMVVIDpLVTETSTFWqnHGESN-----------DVDPSAIQTEVFRLPSTCFAEEDGSIANSGRWL 633
Cdd:cd02767 421 DPAATEEALRRLDLTVHVA-TKLNRSHLV--HGEEAlilpclgrteiDMQAGGAQAVTVEDSMSMTHTSRGRLKPASRVL 497
|
570 580 590
....*....|....*....|....*....|...
gi 1205134601 634 Q-----WHWKGQDAPGEARNDGEILAGIYHRLR 661
Cdd:cd02767 498 LseeaiVAGIAGARLGEAKPEWEILVEDYDRIR 530
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-701 |
1.14e-46 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 179.62 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 107 RLRYPQYRAPGSDKWQRISWDEAFNRIARLMkadrdaNFIEKNEqgvtVNRWLStgmlcaSAASNETGMLTQKFVRSLGM 186
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIAAKL------NSLDPKQ----VAFYTS------GRTSNEAAYLYQLFARSLGS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDP------ 260
Cdd:TIGR01701 163 NNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRG-AKIIAINPlrergl 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 261 -RFTRTAS-----------VADIYAPIRSGTDITFLSGVLLYLIENNK------INAEYVKHYTNasllvrddfafeegl 322
Cdd:TIGR01701 242 eRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDaqpgslIDHEFIANHTN--------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 323 fsGYDAEKRQYDKSSWNyqfdengyakrdetlthprcvwnllkqhvsrytpeVVENICGTPKADFLKVCDVLAstsaADR 402
Cdd:TIGR01701 307 --GFDELRRHVLQLNWN-----------------------------------DIERSSGLSQEEILEFAKLLA----NSR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 403 TTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlstslpgyltlpsdkqtdlqsyl 482
Cdd:TIGR01701 346 RVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGI----------------------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 483 santpkatlpeqvnyWSNYPKFFVslmksfygeaAQKENDWGFEwLPKWdQAYDVIKYFNMMDNGNVTGYICQGFNPVAS 562
Cdd:TIGR01701 403 ---------------TEKPEEEFL----------ARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNFLEA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 563 FPDKNKVVRSLSKLKYMVVIDplvTETSTFWQNHGESNDVDPSAIQTEVFRLPSTCFAEedgSIANSGRwLQWHWKGQDA 642
Cdd:TIGR01701 456 MPDTAAIERALRQLDLRVHVA---TKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAV---SVESSMR-MVHFSRGILK 528
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205134601 643 P--GEARNDGEILAGIYHRLrelyrteggkgaEPLLKMSWRYKQPDHPE-SEEVAKENNGYA 701
Cdd:TIGR01701 529 PrgAELRSEWAIIAEIAKAL------------LPETPVAWEILVDTYDQiRDAIAATNPGYD 578
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
886-1014 |
4.54e-44 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 155.36 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 886 DKFPYVGTTYRLTEHFHTW--TKHALLNSIAQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRtlnvn 963
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 964 gqqVETVGIPLHWGFEGvarKGYIANTLTPNVGDSNSQTPEYKAFLVNIEK 1014
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-454 |
6.40e-44 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 167.04 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 47 RNTCTY-CSVGCGLLMYSLGDGAKNakeaiyhIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRA-PGSDKWQRI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 125 SWDEAFNRIARLMKAdrdanfiekneqgvTVNRWLSTGMLCASAASNeTGMLTQKFVRSL-GMLAVDNQAR-VUHGPTVA 202
Cdd:cd02766 74 SWDEALDTIAAKLKE--------------IKAEYGPESILPYSYAGT-MGLLQRAARGRFfHALGASELRGtICSGAGIE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 203 SLAPTFGRgAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDIT 282
Cdd:cd02766 139 AQKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRG-AKVVVIDPYRTATAARADLHIQIRPGTDGA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 283 FLSGVLLYLIENNKINAEYVKHYTnasllvrddFAFEEglfsgydaekrqydksswnyqfdengyakrdetlthprcvwn 362
Cdd:cd02766 217 LALGVAKVLFREGLYDRDFLARHT---------EGFEE------------------------------------------ 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 363 lLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTSaadRTTTFLyALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGV 442
Cdd:cd02766 246 -LKAHLETYTPEWAAEITGVSAEEIEELARLYGEAK---PPSIRL-GYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
410
....*....|..
gi 1205134601 443 NALRGHSNIQGL 454
Cdd:cd02766 321 FYSNSGPPVKAL 332
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
3.91e-43 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 163.62 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 48 NTCTYCSVGCGLLMYslgdgAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGR--VVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 126 WDEAFNRIARLMKADRDanfiEKNEQGVTVNRWLSTGMlcasaasnetgMLTQKFVRSLGMLAVDNQARVUHGP-TVASL 204
Cdd:cd02755 76 WDEALQYIASKLKEIKE----QHGPESVLFGGHGGCYS-----------PFFKHFAAAFGSPNIFSHESTCLASkNLAWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 205 APTFGRGAMTNhwVDIKNANVVVVMGGNAAEA-HPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITF 283
Cdd:cd02755 141 LVIDSFGGEVN--PDFENARYIILFGRNLAEAiIVVDARRLMKALENG-AKVVVVDPRFSELASKADEWIPIKPGTDLAF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 284 LSGVLLYLIENNKINAEYVKHYTNasllvrddfAFEEglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnl 363
Cdd:cd02755 218 VLALIHVLISENLYDAAFVEKYTN---------GFEL------------------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 364 LKQHVSRYTPEVVENICGTPKADFLKVC-DVLASTSAADrtttflYALGWtqHTVGAQN----IRTMAMIQLLLGNMGMA 438
Cdd:cd02755 246 LKAHVKPYTPEWAAQITDIPADTIRRIArEFAAAAPHAV------VDPGW--RGTFYSNsfqtRRAIAIINALLGNIDKR 317
|
..
gi 1205134601 439 GG 440
Cdd:cd02755 318 GG 319
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
2.28e-40 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 155.93 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYslgdgAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRA--PGSDKWQRISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 127 DEAFNRIARLMKADRDanfiEKNEQGVTVnrWLSTGMLCASAASnetgMLTQKFVRSLGMLAVDNQARVUHGPT-VASLA 205
Cdd:cd02759 76 DEALDEIAEKLAEIKA----EYGPESIAT--AVGTGRGTMWQDS----LFWIRFVRLFGSPNLFLSGESCYWPRdMAHAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 206 PTFGRGAMTNHwvDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLS 285
Cdd:cd02759 146 TTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 286 GVLLYLIENNKINAEYVKHYTNasllvrddfAFEEglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnlLK 365
Cdd:cd02759 224 GMLNVIINEGLYDKDFVENWCY---------GFEE-------------------------------------------LA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 366 QHVSRYTPEVVENICGTPKADFLKVCDVLASTSAAdrtttflyALGWT---QHTV-GAQNIRTMAMIQLLLGNMGMAGGG 441
Cdd:cd02759 252 ERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPA--------CIQWGlaiDQQKnGTQTSRAIAILRAITGNLDVPGGN 323
|
...
gi 1205134601 442 VNA 444
Cdd:cd02759 324 LLI 326
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-590 |
2.94e-38 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 151.01 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYSlgDGAKNAKeaiyhIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSdkWQRISWDE 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 129 AFNRIARLMKADRDAN------FIEKNEQ-----GVTVNRWLSTGMLCASAASNETGMLTQKFVRSLGMlavdnqarvuh 197
Cdd:cd02762 74 AFDEIAERLRAIRARHggdavgVYGGNPQahthaGGAYSPALLKALGTSNYFSAATADQKPGHFWSGLM----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 198 gptvaslaptFGRGaMTNHWVDIKNANVVVVMGGNAAEAHpvGFRWAM-EAKNNNDA------TLIVVDPRFTRTASVAD 270
Cdd:cd02762 143 ----------FGHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTApDRVLRLKAakdrggSLVVIDPRRTETAKLAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 271 IYAPIRSGTDITFLSGvLLYLIennkinaeyvkhytnasllvrddfaFEEGLfsgydaekrqydksswnyqFDENGYAKR 350
Cdd:cd02762 210 EHLFVRPGTDAWLLAA-MLAVL-------------------------LAEGL-------------------TDRRFLAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 351 DETLTHprcvwnlLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTSAADrtttfLYA-LGWTQHTVGAQNIRTMAMIQ 429
Cdd:cd02762 245 CDGLDE-------VRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAA-----VYGrLGVQTQLFGTLCSWLVKLLN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 430 LLLGNMGMAGGgvnalrghsniqgltdlGLLSTSLpgyltLPSDKQTDLQS--YLSANTPKATLPEqvnYWSNYPkffVS 507
Cdd:cd02762 313 LLTGNLDRPGG-----------------AMFTTPA-----LDLVGQTSGRTigRGEWRSRVSGLPE---IAGELP---VN 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 508 LMksfygeAAQKENDwgfewlpkwdqaydvikyfnmmDNGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVT 587
Cdd:cd02762 365 VL------AEEILTD----------------------GPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMT 416
|
...
gi 1205134601 588 ETS 590
Cdd:cd02762 417 ETT 419
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-453 |
3.90e-37 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 148.01 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 51 TYCSVGCG---LLMYSLGDGAKNAKEAiyHIEGDPDHPVsrgaLCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRIS 125
Cdd:cd02765 2 TACPPNCGgrcPLKCHVRDGKIVKVEP--NEWPDKTYKR----GCTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 126 WDEAFNRIARLMKAdrdanfiEKNEQGVTVNRWLStgmlcasAASNETGMLTQKFVRSLGMLAVDNQARVUHGPTVA-SL 204
Cdd:cd02765 76 WDEALDTIADKLTE-------AKREYGGKSILWMS-------SSGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGfNR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 205 APTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITFL 284
Cdd:cd02765 142 VTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENG-AKIVVIDPVYSTTAAKADQWVPIRPGTDPALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 285 SGVLLYLIENNKINAEYVKHYTNASLLVRDDfafeEGLF---SGYDAEKRQYDKSSWNYqfDENGYAKRDETLTHP---- 357
Cdd:cd02765 221 LGMINYILEHNWYDEAFLKSNTSAPFLVRED----NGTLlrqADVTATPAEDGYVVWDT--NSDSPEPVAATNINPaleg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 358 ---------RCVWNLLKQHVSRYTPEVVENICGTPKADFLKVCDVLASTSAAdrtttFLYALGWTQHTV-GAQNIRTMAM 427
Cdd:cd02765 295 eytingvkvHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPS-----GIWGFGGVDRYYhSHVFGRTAAI 369
|
410 420 430
....*....|....*....|....*....|
gi 1205134601 428 IQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 370 LAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
46-440 |
3.91e-33 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 135.26 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 46 IRNTCTYCSVGCGLLMYSLGDGAKNakeaiyhIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRA------PGSD 119
Cdd:cd02757 2 VPSTCQGCTAWCGLQAYVEDGRVTK-------VEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrDVDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 120 KWQRISWDEAFNRIA-RLMKAdrdanfIEKNEQgvtvnrwlSTGMLCASAASNETGMLTQKFVRSLGMLAVDNQARVUhg 198
Cdd:cd02757 75 KFVPISWDEALDTIAdKIRAL------RKENEP--------HKIMLHRGRYGHNNSILYGRFTKMIGSPNNISHSSVC-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 199 ptvaSLAPTFGRGAMTNHW----VDIKNANVVVVMGGNAAEA-HPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYA 273
Cdd:cd02757 139 ----AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 274 PIRSGTDITFLSGVLLYLIENNKINAEYVKHYTNasllVRDDFAFEEGLFSGYDAEKRQYDKSSWnyqfdengyakrdet 353
Cdd:cd02757 215 PIKPGEDGALALAIAHVILTEGLWDKDFVGDFVD----GKNYFKAGETVDEESFKEKSTEGLVKW--------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 354 lthprcvWNLlkqHVSRYTPEVVENICGTPKADFLKVCDVLAstSAADRTTTFLYAlGWTQHTVGAQNIRTMAMIQLLLG 433
Cdd:cd02757 276 -------WNL---ELKDYTPEWAAKISGIPAETIERVAREFA--TAAPAAAAFTWR-GATMQNRGSYNSMACHALNGLVG 342
|
....*..
gi 1205134601 434 NMGMAGG 440
Cdd:cd02757 343 SIDSKGG 349
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-459 |
2.17e-28 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 122.85 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 102 VHSENRLRYPQYRAPGSDKWQRISWDEAFNRIARLMKADRDANFIEKNEQGVTvnrwlstgmlcasaaSNETGMLTQKFV 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRT---------------SNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 182 RSLGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPVGFRwAMEAKNNNDATLIVVDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 261 ------RFT-----------RTASVADIYAPIRSGTDITFLSGVLLYLIENNkinaEYVKHYTNASLLvrdDFAFEEGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 324 SGYDAEKRQYDKSSWnyqfdengyakrdetlthprcvwnllkqhvsrytpEVVENICGTPKADFLKVCDVLAstsAADRT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEW-----------------------------------KDIERISGLSQTQIAELADAYA---AAERT 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1205134601 404 TtFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGL 459
Cdd:PRK09939 362 I-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI 416
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
1.59e-27 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 119.35 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 79 EGDPDHPVSRGalCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRISWDEAFNRIARLMKadrdaNFIEK--NEqGVT 154
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIASELK-----RIIEKygNE-AIY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 155 VNrwLSTGMLCASAASNetgmltQKFVRSLGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGN 232
Cdd:cd02770 105 VN--YGTGTYGGVPAGR------GAIARLLNLTGgyLNYYGTYSWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 233 AAEAHPVGFR---WAMEAKNNNdATLIVVDPRFTRTASV-ADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTna 308
Cdd:cd02770 177 PAETRMGGGGstyYYLQAKKAG-AKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYC-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 309 sllVRDDfafEEGLFSGYDAEkrqydKSSWNYQFDEnGYakrDETlthPRcvwnllkqhvsryTPEVVENICGTPKADFL 388
Cdd:cd02770 254 ---VGFD---AEHLPEGAPPN-----ESYKDYVLGT-GY---DGT---PK-------------TPEWASEITGVPAETIR 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 389 KvcdvLASTSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 303 R----LAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
1.95e-27 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 119.75 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLmyslgdgAK--NAKEAIYHIEGDPDHPVS---------------------------RGALCPKGAGLL 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 100 DYVHSENRLRYPQYRA--PGSDKWQRISWDEAFNRIA---RL--------MKADRDAN-FIEKN--EQGVTVNrwlstgM 163
Cdd:cd02758 76 QYLYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVVeggDLfgeghvegLKAIRDLDtPIDPDhpDLGPKAN------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 164 LCASAASNE--TGMLTQKFVRSLGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANVVVVMGGNAAEAHPvG 240
Cdd:cd02758 150 LLYTFGRDEgrTPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 241 FRWA----MEAKNNNDATLIVVDPRFTRTASVAD---IYAPIRSGTDITFLSGVLLYLIENNKINAEYVKH--------- 304
Cdd:cd02758 229 FKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIpskeaakaa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 305 ----YTNASLLVRDDFAfeeglfsgydaekrqydKSSwnyqfdengyakrdetlthprcvWNLLKQHVSRYTPEVVENIC 380
Cdd:cd02758 309 gepsWTNATHLVITVRV-----------------KSA-----------------------LQLLKEEAFSYSLEEYAEIC 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205134601 381 GTPKADFLKvcdvLAS--TSAADRTTTFlyALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02758 349 GVPEAKIIE----LAKefTSHGRAAAVV--HHGGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-447 |
7.50e-26 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 114.74 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 2 DVSRRKFFKICA-GGMA-GTTAAALGFAPKMALAQARNFKLLRAKEIRNTCTY-CSVGCGLLMYSLgDGAknakeaIYHI 78
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAmASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVV-DGE------IKYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 79 E----GDPDHP-VSRGALCPKGAGLLDYVHSENRLRYPQYR--APGSDKWQRISWDEAFNRIA----RLMKadrdanfiE 147
Cdd:PRK14990 86 EtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYDIIAtnmqRLIK--------E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 148 KNEQGVTVNRWLST--GMLCASAASNETgmLTQKFVRSLGMLaVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANV 225
Cdd:PRK14990 158 YGNESIYLNYGTGTlgGTMTRSWPPGNT--LVARLMNCCGGY-LNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 226 VVVMGGNAAEAHPVG---FRWAMEAKNNNDATLIVVDPRFTRT-ASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEY 301
Cdd:PRK14990 235 VVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 302 VKHYTNAsllvrddfafeeglfsgydaekrqYDKSSWNYQFDENGYAKrdetlthpRCVWNLLKQHVSRyTPEVVENICG 381
Cdd:PRK14990 315 LDKYCVG------------------------YDEKTLPASAPKNGHYK--------AYILGEGPDGVAK-TPEWASQITG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205134601 382 TPKADFLKVCDVLASTSAAdrtttfLYALGW--TQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK14990 362 VPADKIIKLAREIGSTKPA------FISQGWgpQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-592 |
4.63e-25 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 112.07 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 1 MDVSRRKFFKicaGGMAGTTAAALGFAPKMALAqARNFKLLR--AKEIRNTCTYCSVGCGLLMYSLGDgaKNAkeaiyHI 78
Cdd:PRK15488 1 MSLSRRDFLK---GAGAGCAACALGSLLPGALA-ANEIAQLKgkTKLTPSICEMCSTRCPIEARVVNG--KNV-----FI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 79 EGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRISWDEAFNRIARLMkadrdaNFIEKNEQGVTVn 156
Cdd:PRK15488 70 QGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKL------NAIKQQHGPESV- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 157 rwlstgmlCASAASNETGMLTQKFVRSLGMLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANVVVVMGGNAAEA 236
Cdd:PRK15488 143 --------AFSSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLYEG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 237 HPVGF-RWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTnasllvrdd 315
Cdd:PRK15488 211 INMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYT--------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 316 fafeeglfSGYDAekrqydksswnyqfdengyakrdetlthprcvwnlLKQHVSRYTPEVVENICGTPKADFLKVCDVLA 395
Cdd:PRK15488 282 --------SGFEE-----------------------------------LAASVKEYTPEWAEAISDVPADDIRRIARELA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 396 STSAA------DRTTTflyalgwTQHTVgaQNIRTMAMIQLLLGNMGMAGG--------GVNALRGHSNIQGLTDlglls 461
Cdd:PRK15488 319 AAAPHaivdfgHRATF-------TPEEF--DMRRAIFAANVLLGNIERKGGlyfgknasVYNKLAGEKVAPTLAK----- 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 462 tslPGYLTLPsdkqtdlqsylsanTPKATLPEQVNywsnyPKFFvslMKSFYGEAAQKENDWGFEWLPkwdqaYDvIKyf 541
Cdd:PRK15488 385 ---PGVKGMP--------------KPTAKRIDLVG-----EQFK---YIAAGGGVVQSIIDATLTQKP-----YQ-IK-- 431
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 542 nmmdngnvtGYICQGFNPVASFPDKNKVVRSLSKLKYMVVIDPLVTETSTF 592
Cdd:PRK15488 432 ---------GWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAY 473
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
897-1006 |
6.06e-24 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 97.01 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 897 LTEHFHTW--TKHALLNSIaQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRtlnvngqqVETVGIPL 974
Cdd:cd02775 1 LRDHFHSGtrTRNPWLREL-APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVP--------PGVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 1205134601 975 HWGFEGVarKGYIANTLTPNVGDSNSQTPEYK 1006
Cdd:cd02775 72 GWGHRGG--RGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
5.18e-23 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 105.30 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYsLGDGAknakeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDGK------VRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 127 DEAFNRIARLMKADRdanfiEKNEQGVTvnrwLSTGmlcasaaSNETGMLTQKFVRSLGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02763 76 EEAFSIATKRLKAAR-----ATDPKKFA----FFTG-------RDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 207 TFGRGAMTNHWVDIKNANvVVVMGGNAAEAHPVGFRWAMEAKNNNDATLIVVDPRFTRTASVADIYAPIRSGTDITFLSG 286
Cdd:cd02763 140 SIGGSFWEFGGPDLEHTK-YFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 287 VLLYLIENNKINAEYVKHYTNASLLVrddfafeeglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnllkq 366
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 367 hvsRYTPEVVENICGTPKADFLKVCDVLASTSAADRTT---------------------TFLYALGWTQHTVGAQNIRTM 425
Cdd:cd02763 245 ---DYTPEWVEKITGIPADTIRRIAKELGVTARDQPIElpiawtdvwgrkhekitgrpvSFHAMRGIAAHSNGFQTIRAL 321
|
410
....*....|....*
gi 1205134601 426 AMIQLLLGNMGMAGG 440
Cdd:cd02763 322 FVLMMLLGTIDRPGG 336
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-447 |
7.42e-23 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 105.37 E-value: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 1 MDVSRRKFFKICAggmAGTTAAALGFA-PKMALAQARNfkllRAKEIR---NTCTYCSVGCGLLMyslgdGAKNAKeaIY 76
Cdd:PRK13532 1 MKLSRRDFMKANA---AAAAAAAAGLSlPAVANAVVGS----AQTAIKwdkAPCRFCGTGCGVLV-----GTKDGR--VV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 77 HIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYP-------QYRAPGsdKWQRISWDEAFNRIARLMKAdrdanfiEKN 149
Cdd:PRK13532 67 ATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFKK-------ALK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 150 EQGVTvnrwlSTGMLCASAASNETGMLTQKFVRSlGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVV 227
Cdd:PRK13532 138 EKGPT-----AVGMFGSGQWTIWEGYAASKLMKA-GFRSnnIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 228 VMGGNAAEAHPVgfRWA--MEAKNNNDATLIVVDPRFT-RTASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKH 304
Cdd:PRK13532 212 LWGSNMAEMHPI--LWSrvTDRRLSNPDVKVAVLSTFEhRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 305 YTNASLLV-------RDDFAFEEglfsgyDAEKRQYDKSSWNYQFDEngYAKrdetlthprcvwnllkqHVSRYTPEVVE 377
Cdd:PRK13532 290 HTNFRKGAtdigyglRPTHPLEK------AAKNPGTAGKSEPISFEE--FKK-----------------FVAPYTLEKTA 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205134601 378 NICGTPKADFLKVCDVLASTsaaDRTTTFLYALGWTQHTVG--AQNIrtMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK13532 345 KMSGVPKEQLEQLAKLYADP---NRKVVSFWTMGFNQHTRGvwANNL--VYNIHLLTGKISTPGNGPFSLTG 411
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
886-1015 |
5.36e-22 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 92.25 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 886 DKFPYVGTTYRLTEHFHTWT---KHALLNSIAqPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTrrlrtlnv 962
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVT-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1205134601 963 NGQQVETVGIPLHWGFEGVARKGyiANTLTPNVGDSNSQTPEYKAFLVNIEKA 1015
Cdd:cd02791 72 DRVRPGEVFVPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-653 |
4.28e-20 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 93.23 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 107 RLRYPQYRApGSDKWQRISWDEAFNRIARLMKADRDanfiEKNEQGVTVNRWlstgmlCASAASNETGMLTQKFVRSLGM 186
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIK----KYGPDAIAINGG------SGGLTDVESLYALKKLLNRLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 187 LAV---DNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANVVVVMGGNAAEAHPV-GFRWAMEAKNNNdATLIVVDPRF 262
Cdd:pfam00384 70 KNGnteDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIlNARIRKAALKGK-AKVIVIGPRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 263 TRTASVADIyaPIRSGTDITFLSGVLLYLIENNKinaeyvkhytnasllvrddfafeeglfsgydaekrqYDKSSwnyqf 342
Cdd:pfam00384 149 DLTYADEHL--GIKPGTDLALALAGAHVFIKELK------------------------------------KDKDF----- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 343 dengyakrdetlthprcvwnllkqhvsrytpevvenicgTPKAdflkvcdvlastsaadrttTFLYALGWTQHTVGAQNI 422
Cdd:pfam00384 186 ---------------------------------------APKP-------------------IIIVGAGVLQRQDGEAIF 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 423 RTMAMIQLLLGNMGMAGGGVNALR---GHSNIQGLTDLGLLSTslpgyltlpsdkqtdlqsylsantpkatlpeqvnyws 499
Cdd:pfam00384 208 RAIANLADLTGNIGRPGGGWNGLNilqGAASPVGALDLGLVPG------------------------------------- 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 500 nypkffvslmksfygeaaqkendwgfewlpkwdqaYDVIKYFNMMDNGNVTGYICQGFNPVASFPDKNKVVRSLSKLKYM 579
Cdd:pfam00384 251 -----------------------------------IKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLF 295
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205134601 580 VVIDPlvtetstFWQNHGESN-DVdpsaiqtevfRLPSTCFAEEDGSIANS-GRWLQWHwKGQDAPGEARNDGEIL 653
Cdd:pfam00384 296 VVYDG-------HHGDKTAKYaDV----------ILPAAAYTEKNGTYVNTeGRVQSTK-QAVPPPGEAREDWKIL 353
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
82-447 |
1.31e-19 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 93.15 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 82 PDH-PvsRGalCPKGAGLLDYVHSENRLRYPQYRAP--GSDKWQRISWDEAFNRIarlmkADRDANFIEKN--EQGVTVN 156
Cdd:cd02750 44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELI-----ADAIIDTIKKYgpDRVIGFS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 157 RWLSTGMLCASAASnetgmltqKFVRSLGMLAVDNQARVUHGPTVASLapTFGRGAMTNHWVDIKNANVVVVMGGNAAEA 236
Cdd:cd02750 115 PIPAMSMVSYAAGS--------RFASLIGGVSLSFYDWYGDLPPGSPQ--TWGEQTDVPESADWYNADYIIMWGSNVPVT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 237 HPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLLYLIENNKINAEYVKHYTNASLLVrddf 316
Cdd:cd02750 185 RTPDAHFLTEARYNG-AKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLV---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 317 afeeglfsgydaekrqydksswnyqfdengyakrdetlthprcvwnllkqhvsrYTPEVVENICGTPKADFLKvcdvLAS 396
Cdd:cd02750 260 ------------------------------------------------------YTPAWQEAITGVPRETVIR----LAR 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 397 TSAADRTTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02750 282 EFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
1.36e-19 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 94.22 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 92 CPKGAGLLDYVHSENRLRYPQYR------------APGSDKWQRISWDEAFNRIARLMKADRDA---NFIEKNEQGvtvn 156
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLVASELKRIREKygnEAIFGGSYG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 157 rWLSTGMLCASaasnetgmltqkfvRSLgmlavdnQARV--UHGPTVASLAP---------------TFGRGAMTNHWVD 219
Cdd:cd02751 108 -WASAGRLHHA--------------QSL-------LHRFlnLIGGYLGSYGTystgaaqvilphvvgSDEVYEQGTSWDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 220 I-KNANVVVVMGGNAAE--------AHPVGFRWAMEAKNNNdATLIVVDPRFTRTASV-ADIYAPIRSGTDITFLSGVLL 289
Cdd:cd02751 166 IaEHSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAKDAG-VRFICIDPRYTDTAAVlAAEWIPIRPGTDVALMLAMAH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 290 YLIENNKINAEYVKHYTnasllvrddfafeeglfSGYDAEKRQYDKSSwnyqfdeNGYAKrdetlthprcvwnllkqhvs 369
Cdd:cd02751 245 TLITEDLHDQAFLARYT-----------------VGFDEFKDYLLGES-------DGVPK-------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 370 ryTPEVVENICGTPkADFLKvcdVLASTSAADRtTTFLYALGWTQHTVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHS 449
Cdd:cd02751 281 --TPEWAAEITGVP-AETIR---ALAREIASKR-TMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYS 353
|
410
....*....|....*.
gi 1205134601 450 NIQGLTDLGLLSTSLP 465
Cdd:cd02751 354 NGGGPPRGGAGGPGLP 369
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
886-1014 |
2.33e-19 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 84.60 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 886 DKFPYVGTTYRLTEHFHTWT---KHALLNSIAqPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRtlnv 962
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTmtrRAEGLDAIA-PEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVP---- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1205134601 963 NGQqvetVGIPLHWgFEGVarkgyiANTLTPNVGDSNSQTPEYKAFLVNIEK 1014
Cdd:cd02790 76 EGV----VFMPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
44-104 |
1.51e-18 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 79.99 E-value: 1.51e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 44 KEIRNTCTYCSVGCGLLMYSlgdgaKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHS 104
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEV-----KDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
893-1009 |
1.30e-17 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 79.24 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 893 TTYRLTEHFHTWTKHALLNSIAQPEQ-FVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTlnvnGqqveTVG 971
Cdd:pfam01568 4 ITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP----G----VVF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1205134601 972 IPLHWGFEgvaRKGYIANTLTPNVGDSNSQTPEYKAFL 1009
Cdd:pfam01568 76 MPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
44-104 |
1.84e-17 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 76.95 E-value: 1.84e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 44 KEIRNTCTYCSVGCGLLMYSlgdgaknAKEAIYHIEGDPDHPVSRGALCPKGAGLLDYVHS 104
Cdd:pfam04879 2 KVVKTICPYCGVGCGLEVHV-------KDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
49-239 |
8.06e-16 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 81.28 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMyslgdGAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRapGSDKWQRISWDE 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 129 AFNRIARLMKADRDAnfiekneqgvtvnrwlsTGMLCASAASNETGMLTQKFVR-SLGMLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK-----------------VGGIGSPRASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190
....*....|....*....|....*....|..
gi 1205134601 208 FGRGAMTNHwvDIKNANVVVVMGGNAAEAHPV 239
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPR 162
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-390 |
2.49e-14 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 77.70 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 50 CTYCSVGCGLLMYSLGDGAknakeaIYHIEGDPD----HPvSRGALCPKGAGLLDYVHSENRLRYPQYRA---------P 116
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHP-ARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 117 GsdkWQRISWDEAFNRIARLMKADRDANFIekNEQGVtVNRWLSTGmlcasaASNETGMLTQKFVRSLGMLAVDNQARVU 196
Cdd:cd02760 77 G---FVPISWDEALDLVAAKLRRVREKGLL--DEKGL-PRLAATFG------HGGTPAMYMGTFPAFLAAWGPIDFSFGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 197 HGPTVASLAPTFGRGAMTNHWV---DIKNANVVVVMGGNA-AEAHPVGFRWAMEAKNNNdATLIVVDPRFTRTASVADIY 272
Cdd:cd02760 145 GQGVKCVHSEHLYGEFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVRG-YKRVQVEPHLSVTGACSAEW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 273 APIRSGTDITF---LSGVLLYLIENNKINAEYVKHYTNASLLVRDDfafeeGLFSGYDAEKRQ--YD-KSSWNYQFDENG 346
Cdd:cd02760 224 VPIRPKTDPAFmfaMIHVMVHEQGLGKLDVPFLRDRTSSPYLVGPD-----GLYLRDAATGKPlvWDeRSGRAVPFDTRG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205134601 347 YAK----------------RDETLTHP----RCVWNLLKQHVSRYTPEVVENICGTPKADFLKV 390
Cdd:cd02760 299 AVPavagdfavdgavsvdaDDETAIHQgvegTTAFTMLVEHMRKYTPEWAESICDVPAATIRRI 362
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
43-362 |
1.16e-12 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 72.13 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 43 AKEIRNTCTYCSVGCGLLMYSLGDGAKNAKE----AI-------------------------------YHIEGDPDH--P 85
Cdd:cd02756 10 AERYNVTCHFCIVGCGYHVYVWPVGEEGGPSpgqnAIgydlvdqvpplnlqwypktmhyvvvtqdgreVYIVIVPDKecP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 86 VSRGALCPKGAGLLDYVHS------ENRLRYPQYRApgSDKWQRISWDEAFNRIARLMKADRDAnfiEKNEQGVTVNRW- 158
Cdd:cd02756 90 VNSGNYSTRGGTNAERIWSpdnrvgETRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGILDK---DGNDDAVFASRFd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 159 -----------LSTGMLCASAasnetgmLTQKFVRslgmlaVDNqaRVUHGPTVASLAPTfGRGAMTNHWVDIKNANVVV 227
Cdd:cd02756 165 hggggggfennWGVGKFFFMA-------LQTPFVR------IHN--RPAYNSEVHATREM-GVGELNNSYEDARLADTIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 228 VMGGNAAEAHPVGF-----------------RWAMEAKNNNDATLIVVDPRFTRTASVADIYA--------PIRSGTDIT 282
Cdd:cd02756 229 LWGNNPYETQTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgkdrvlhlQVNPGTDTA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 283 FLSGVLLYLIENNkinaeyvkhytnasllvrDDFAFEEGLFSGYDAEKRQYdKSSWNYQFDENGYAKRDETLTHPRCVWN 362
Cdd:cd02756 309 LANAIARYIYESL------------------DEVLAEAEQITGVPRAQIEK-AADWIAKPKEGGYRKRVMFEYEKGIIWG 369
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
34-279 |
1.14e-11 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 68.33 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 34 QARNFKLlraKEIRNTCTYCSVGCGLLMyslgdGAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQY 113
Cdd:COG1034 209 KARPWEL---KKTPSICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 114 RAPGsdKWQRISWDEAFNRIARLMKADRDAnfieKNEQGVTvnrwlstgMLCAsaasnetgmltqkfvrslgmlavdnqa 193
Cdd:COG1034 279 RKDG--ELVEASWEEALAAAAEGLKALKKA----ENSVGAA--------LLGA--------------------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 194 rvuhGPTVASLAPTFGRGAmtnhwvdiknANVVVVMGGNAAEAHPVGFRWAMeaknNNDATLIVVDPRFTRTASVADIYA 273
Cdd:COG1034 318 ----LPDAAAILEAAEAGK----------LKALVLLGADPYDLDPAAALAAL----AKADFVVVLDHFGSATAERADVVL 379
|
250
....*....|.
gi 1205134601 274 PI-----RSGT 279
Cdd:COG1034 380 PAaafaeKSGT 390
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-239 |
1.46e-11 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 67.31 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 50 CTYCSVGCGLLMyslgdGAKNAKeaIYHIEGDPDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRapGSDKWQRISWDEA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 130 FNRIARLMKAdrdanfIEKNEQGVTVNrwlstgmlcaSAASNETGMLTQKFVRSLGMLAVDNQARvuhGPTVASLAPTFG 209
Cdd:cd02768 75 LKTVAEGLKA------VKGDKIGGIAG----------PRADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLRG 135
|
170 180 190
....*....|....*....|....*....|
gi 1205134601 210 RGAMTNHWVDIKNANVVVVMGGNAAEAHPV 239
Cdd:cd02768 136 NYLFNTSIAEIEEADAVLLIGSNLRKEAPL 165
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
5-293 |
4.65e-11 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 66.36 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 5 RRKFFKICAGGMAGTTAAALGFAPKMA---LAQARNFKLLRAKEIRNTCTYCSVGCGLLMySLGDGaKNAKeaiyhIEGD 81
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRYPVEKIvpyVIWPENIVPGETVYYATSLVPAGEGQGVLV-KTVDG-RPIK-----IEGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 82 PDHPVSRGALCPKGAGLLDYVHSENRLRYPQYRAPGSdKWQRISWDEAFNRIARLMKADRDAnfiekneQGVTV--NRWL 159
Cdd:cd02764 74 PDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDG-AYVASDWADFDAKVAEQLKAVKDG-------GKLAVlsGNVN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 160 STGMLCASAASNETGMLTQKFVRSLGmlavDNQarvuhgPTVASLAPTFGRGAMTNHwvDIKNANVVVVMGGNAAE--AH 237
Cdd:cd02764 146 SPTTEALIGDFLKKYPGAKHVVYDPL----SAE------DVNEAWQASFGKDVVPGY--DFDKAEVIVSIDADFLGswIS 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205134601 238 PVGFRWAMEAKNNNDAT-----LIVVDPRFTRTASVADIYAPIRSGTDITFLSGVLLYLIE 293
Cdd:cd02764 214 AIRHRHDFAAKRRLGAEepmsrLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIK 274
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-285 |
1.31e-10 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 64.66 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 49 TCTYCSVGCGLLMYSLGDGAKNAkeaiyhiegdpdhpvSRGAlCPKGAGLLdyvhSENRLRYPQYRAPGSDkwqrISWDE 128
Cdd:cd02761 3 VCPFCGLLCDDIEVEVEDNKITK---------------VRNA-CRIGAAKF----ARYERRITTPRIDGKP----VSLEE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 129 AFNRIARLMKADRDANFiekneqgvtvnrwlstGMLCASaaSNETgmltQKFVRSLGMLA---VDNQARVUHGPTVASLA 205
Cdd:cd02761 59 AIEKAAEILKEAKRPLF----------------YGLGTT--VCEA----QRAGIELAEKLgaiIDHAASVCHGPNLLALQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 206 PtfgRGAMTNHWVDIKN-ANVVVVMGGNAAEAHP------VGFRWAMEA-KNNNDATLIVVDPRFTRTASVADIYAPIRS 277
Cdd:cd02761 117 D---SGWPTTTLGEVKNrADVIVYWGTNPMHAHPrhmsrySVFPRGFFReGGREDRTLIVVDPRKSDTAKLADIHLQIDP 193
|
....*...
gi 1205134601 278 GTDITFLS 285
Cdd:cd02761 194 GSDYELLA 201
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
888-1014 |
7.79e-10 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 57.70 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 888 FPYVGTTYRLTEHFHTwtKHALLNSIAQ--PEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTLNVNGQ 965
Cdd:cd02781 3 PLILTTGARSYYYFHS--EHRQLPSLRElhPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205134601 966 QvetvGiplHWGFEGVARKGYI-------ANTLTPN-VGDSNSQTPEYKAFLVNIEK 1014
Cdd:cd02781 81 H----G---WWYPEREAGEPALggvwesnANALTSDdWNDPVSGSSPLRSMLCKIYK 130
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
889-1014 |
1.96e-08 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 53.43 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 889 PYVGTTYRLTEHFHTWTKH-ALLNSIAqPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTlnvngqqv 967
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANnPLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1205134601 968 ETVGIPLHWG-----FEGVARKGYIANTLTPNVGDSNSQTPEYKAFLVNIEK 1014
Cdd:cd02778 72 DTVFMPHGFGhwapaLSRAYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
887-958 |
1.37e-07 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 51.21 E-value: 1.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205134601 887 KFPYVGTTYRLTEHFH-TWTKHALLNSIaQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLR 958
Cdd:cd02785 1 KYPLACIQRHSRFRVHsQFSNVPWLLEL-QPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
907-993 |
4.17e-07 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 49.59 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 907 HALLNSI---------AQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRTlnvnGQQVETVGIPLHWg 977
Cdd:cd02786 11 HNFLNSTfanlpelraKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPP----GVVVAEGGWWREH- 85
|
90
....*....|....*.
gi 1205134601 978 fegvARKGYIANTLTP 993
Cdd:cd02786 86 ----SPDGRGVNALTS 97
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
1-440 |
8.82e-07 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 53.08 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 1 MDVSRRKFFKicaGGMA--GTTAAALGFAPKMA-----LAQARNFKLLRAK--------EIR----------------NT 49
Cdd:PRK14991 1 MDKTRRQLLK---GGLAagGLAAFAAGYSDTAKraakgLLNGTSGKPTRDRihgnsltpEYRvdaqgqlqpnpqqrvaNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 50 -CTYCSVGCGLLMYslgdgAKNAKEAIYHIEGDPDHPVS--------------------------RGALCPKGAGLLDYV 102
Cdd:PRK14991 78 qCLGCWTQCGVRVR-----VDNATNKILRIAGNPYHPLStdhhidmstpvkeafeslsgesglegRSTACARGNAMLEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 103 HSENRLRYPQYR-AP-GSDKWQRISWDEAFNRIAR---L--------MKADRDANFI---EKNEQGVTVNRWLSTGmlca 166
Cdd:PRK14991 153 DSPYRVLQPLKRvGKrGSGKWQRISFEQLVEEVVEggdLfgeghvdgLRAIRDLDTPidaKNPEYGPKANQLLVTN---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 167 saASNEtGM--LTQKFVR-SLGMLAVDNQARVUhgptvaSLAPTFGRGAMTN------HWV-DIKNANVVVVMGGNAAEA 236
Cdd:PRK14991 229 --ASDE-GRdaFIKRFAFnSFGTRNFGNHGSYC------GLAYRAGSGALMGdldknpHVKpDWDNVEFALFIGTSPAQS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 237 -HPvgF----RWAMEAKNNNDATLIVVDPRFTRTASVA----DIYAPIRSGTDITFLSGVLLYLIENNKINAEYV----- 302
Cdd:PRK14991 300 gNP--FkrqaRQLANARTRGNFEYVVVAPALPLSSSLAagdnNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLaqpgv 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 303 --------KHYTNASLLVRDD--------FAFEEGLFSGYDAEKRQYDKSSwnYQFDENGYAKRDETLTHPRCVW----- 361
Cdd:PRK14991 378 aamqaageASWTNATHLVIADpghprygqFLRASDLGLPFEGEARGDGEDT--LVVDAADGELVPATQAQPARLFveqyv 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 362 --------------NLLKQHVSRYTPEVVENICGTPKADFLKvcdvLASTSAADRTTTFLYALGWTQHTVGAQNIRTMAM 427
Cdd:PRK14991 456 tladgqrvrvksslQLLKEAARKLSLAEYSEQCGVPEAQIIA----LAEEFTSHGRKAAVISHGGTMSGNGFYNAWAIMM 531
|
570
....*....|...
gi 1205134601 428 IQLLLGNMGMAGG 440
Cdd:PRK14991 532 LNALIGNLNLKGG 544
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
102-238 |
9.30e-06 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 49.27 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 102 VHSENRLRYPQYRAPGsdKWQRISWDEAFNRIARLMKAdrdanFIEKNEQGvtvnrwlSTGMLCASAASNETGMLTQKFV 181
Cdd:cd02772 49 LNSEDRLTKPMIKKDG--QWQEVDWETALEYVAEGLSA-----IIKKHGAD-------QIGALASPHSTLEELYLLQKLA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205134601 182 RSLGMLAVDNQARVUHGPTVASLAPTFGrgaMTNHWVDIKNANVVVVMGGNAAEAHP 238
Cdd:cd02772 115 RGLGSDNIDHRLRQSDFRDDAKASGAPW---LGMPIAEISELDRVLVIGSNLRKEHP 168
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
917-993 |
1.15e-04 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 43.13 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205134601 917 EQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTRRLR--TLNVNGQQVETVGIPlhwGFEGVARKGYIANTLTP 993
Cdd:cd02776 30 GPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPrgTVFMYHAQERHVNVP---GSKLTGKRGGIHNSVTR 105
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
888-982 |
1.54e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 43.05 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 888 FPYVGTTYRLTEHFHTWTKHALLNSIaQPEQFVEISEGLAKSKGIANGDWVKVSSRRGFIRAVAVVTrrlrtlnvNGQQV 967
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEI-KPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVT--------EGVRP 71
|
90
....*....|....*...
gi 1205134601 968 ETVGIPL---HWGFEGVA 982
Cdd:cd02780 72 GVVAIEHgygHWAYGAVA 89
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
927-1014 |
2.41e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 41.80 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205134601 927 AKSKGIANGDWVKVSSRRGFIRAVAVVTRRLRtlnvngQQVetVGIPlH--W----GFEGVARKGYIaNTLTPNVGDS-N 999
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIM------PGV--VALP-EgaWydpdDNGGLDKGGNP-NVLTSDIPTSkL 112
|
90
....*....|....*
gi 1205134601 1000 SQTPEYKAFLVNIEK 1014
Cdd:cd02777 113 AQGNPANTCLVEIEK 127
|
|
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