|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-1015 |
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: 1504.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 2 QVSRRQFFKICAGGMAGTTAAALGFAPGVALAETRQYKLLRTRETRNTCTYCSVGCGLLMYSLGDGAKNAKASIFHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 82 PDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLIKEDRDANFIEKNADGVTVNRWLST 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 162 GMLCASASSNETGYLTQKFTRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 242 RWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTNASLIVREDYHFEDG 321
Cdd:TIGR01553 241 KWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 322 LFSGYDAEKRKYDKTSWNYELDEKGFAKRDTTLQHPRCVWNLLKEHVSRYTPEVVENICGTPKADFLKVCELIAETSAKD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 402 KTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYMNLPSEKQTDLQTY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 482 LTASTPKPLLEGQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYD-VLQYFEMMHQGKVNGYLCQGFNPV 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDsWLTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 561 ASFPNKNKVVESLSKLKFLVTIDPLNTETSTFWQNHGesndVDPSKIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGA 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 641 DAPGIAMNDGEILAGIFLRLRKMYAAEGGANPEPVLNMTWNYSTPENPAPEEVAMESNGKALADVIDPatgTVLAKKGDQ 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDFKVG---DVEYKKGQQ 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 721 LSTFAHLRDDGTTSSGCWIFAGSWTPKGNQMANRDNADPSGLGNTLGWAWAWPLNRRILYNRASADPQGNPWDPKRQLLK 800
Cdd:TIGR01553 713 IATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALVE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 801 WDGAKWGGV-DIPDY-STAPPGSDVGPFIMQPEGMGRLFAIDKMAEGPFPEHYEPFETPLGTNPLHPNVVSNPAARIFKG 878
Cdd:TIGR01553 793 WNAAEKKWVgDIPDYpPTAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYKT 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 879 DFDALGKKDKFPYVGTTYRLTEHFHYWTKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRI 958
Cdd:TIGR01553 873 DEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRI 952
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1236119465 959 RTLNVHGQQVDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1015
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 ... |
47-874 |
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: 989.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 47 RNTCTYCSVGCGLLMYSLGDgaknakaSIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNG-------VWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 127 EEAFDRIAKLIKEDRDANFIEKNADGVTVNRWLSTGMLCASASSNETGYLTQKFTRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 207 TFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 287 VLLYLMtnekynreyteaytnaslivredyhfedglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnllke 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 367 hvsRYTPEVVENICGTPKADFLKVCELIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 447 GHSNIQGLTDLGLLSQSLPGYMNlpsekqtdlqtyltastpkpllegqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 527 wlpkwdkgydvlqyfemmhqgkvngylcqGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFWQNHGesndVDPSK 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 607 IQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIFLRLRKMYAAEGGANPEPVLNmtWNYSTPE 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 687 NPAPEEVAMESNGKALADVIDPATGTVLAKKGDQLSTFAHLRDDGTTSSGCWIFAGSWTPKGNqMANRDNADPSGLGNTL 766
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYTGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYP 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 767 GWAWAWPLNRRILYNRASADPQGNPWDPKRQLLKWDGAKWG-GVDIPDY-STAPPGSDVGPFIMQPEGMGRLFAIDKmaE 844
Cdd:cd02752 544 GWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGLGWWwKGDVPDGpWPAAKEHGCGPFIMAPEGQARLFVWNF--D 621
|
810 820 830
....*....|....*....|....*....|
gi 1236119465 845 GPFPEHYEPFETPLGTNplHPNVVSNPAAR 874
Cdd:cd02752 622 GPFPEHYEPLESPRPDL--HSKVAKNPTYK 649
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
15-1013 |
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: 911.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 15 GMAGTTAAALGFAPGVALAEtrqykllrtRETRNTCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPK 94
Cdd:NF041513 21 GAAARSARTRALRPRTATAD---------RVVRSVCPYCAVGCGQKVY-----VKDEK--VVQIEGDPDSPISRGRLCPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 95 GAGLVDFIHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLIKEDRDANFIEKNADGVTVNRWLSTGMLCASASSNETG 174
Cdd:NF041513 85 GSASLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEEN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 175 YLTQKFTRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAK 254
Cdd:NF041513 165 YLIKKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAK-ARGAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 255 LIVIDPRFTRTASVADFYTPIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTNASLIVREDYHFE---DGLFSGYDAEKR 331
Cdd:NF041513 244 VIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFRDTedlDGLFSGFDPETG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 332 KYDKTSWNYELDE----------------------------------KGFAKRDTTLQHPRCVWNLLKEHVSRYTPEVVE 377
Cdd:NF041513 324 SYDPASWQYEGVEvaaaagqrdqlydsrggahesargeehgsggapvAGAPRRDETLQDPRCVFQILKRHFARYTPEMVE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 378 NICGTPKADFLKVCELIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGLTDL 457
Cdd:NF041513 404 EICGIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 458 GLLSQSLPGYMNLP-SEKQTDLQTYLTASTPkpllegQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYD 536
Cdd:NF041513 484 PTLFNLLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDHS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 537 VLQYFEMMHQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFWQNHGE--SNDVDPSKIQTEVFRL 614
Cdd:NF041513 558 TYQTVMAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEieTGELRTEDIGTEVFFF 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 615 PSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIFLRLRKMYAAEGGANPEPVLNMTWNYSTP---ENPAPE 691
Cdd:NF041513 638 PAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLDLTWDYPTEgphGEPDAE 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 692 EVAMESNGKALAdvidpatgtvlakkGDQLSTFAHLRDDGTTSSGCWIFAGSWTPKGNQMANRDnadPSGLGNTLG--WA 769
Cdd:NF041513 718 AVLAEINGYDLS--------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWVAaeWG 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 770 WAWPLNRRILYNRASADPQGNPWDPKRQLLKWD--GAKWGGVDIPDY--STAP---PGSDVG---------PFIMQPEGM 833
Cdd:NF041513 781 WAWPANRRILYNRASADPEGRPWSERKKYVWWDaeAGRWTGYDVPDFpvDKPPdyrPPPGATgpaalsgddPFIMQADGK 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 834 GRLFAIDKMAEGPFPEHYEPFETPLGtNPLHPnVVSNPAARIFKGDFDALGKK------DKFPYVGTTYRLTEHF----- 902
Cdd:NF041513 861 GWLFAPAGLVDGPLPTHYEPQESPVR-NPLYG-QQRNPARKVYPREDNRYHPSggepgaEVYPYVFTTYRLTEHHtaggm 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 903 HYWTKHAllnAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTLNVHGQQVDTIGIPIHWGYEGV 982
Cdd:NF041513 939 SRWLPYL---AELQPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGPNGL 1015
|
1050 1060 1070
....*....|....*....|....*....|.
gi 1236119465 983 AkKGFIANTLTPFVGDANTQTPEFKAFLVNV 1013
Cdd:NF041513 1016 V-TGDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-1016 |
2.21e-156 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 478.22 E-value: 2.21e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 43 TRETRNTCTYCSVGCGLLMYSLGDGaknakasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdKWQ 122
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 123 QISWEEAFDRIAKLIKEDRDanfiEKNADGVtvnrwlstGMLCASASSNETGYLTQKFTRA-LGMLAVDNQARVUHGPTV 201
Cdd:COG3383 75 EVSWDEALDLVAERLREIQA----EHGPDAV--------AFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 202 ASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDI 281
Cdd:COG3383 143 AGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 282 TFLSGVLLYLMTNEKYNREYTEAYTNaslivredyhfedglfsGYDAekrkydktswnyeldekgfakrdttlqhprcvw 361
Cdd:COG3383 222 ALLNGLLHVIIEEGLVDEDFIAERTE-----------------GFEE--------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 362 nlLKEHVSRYTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGG 441
Cdd:COG3383 252 --LKASVAKYTPERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 442 VNALRGHSNIQGLTDLGLLSQSLPGYMNLPSEKqtdlqtyltastpkpllegqvnywgnypkffvsmmkaffgDKATAEN 521
Cdd:COG3383 326 PFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPE----------------------------------------HRAKVAD 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 522 SWGFDWLPKWdKGYDVLQYFEMMHQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFwqnhgesND 601
Cdd:COG3383 366 AWGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY-------AD 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 602 VdpskiqtevfRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIflrLRKMyaaegGANpepvlnmtWN 681
Cdd:COG3383 438 V----------VLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAEL---ARRL-----GYG--------FD 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 682 YSTpenpaPEEVAMEsngkaladvidpatgtvlakkgdqlstfahlrddgttssgcwifagswtpkgnqmanrdnadpsg 761
Cdd:COG3383 492 YDS-----PEEVFDE----------------------------------------------------------------- 501
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 762 lgntlgWAWAWPLNRRILYNRasadpqgnpwdpkrqLLKWDGAKWggvdiPDYSTAPPGSDvgpfimqpegmgRLFAidk 841
Cdd:COG3383 502 ------IARLTPDYSGISYER---------------LEALGGVQW-----PCPSEDHPGTP------------RLFT--- 540
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 842 maegpfpehyEPFETPLGTNPLHPNVVSNPAARIfkgdfdalgkKDKFPYVGTTYRLTEHFH--YWTKH-ALLNAIAqPE 918
Cdd:COG3383 541 ----------GRFPTPDGKARFVPVEYRPPAELP----------DEEYPLVLTTGRLLDQWHtgTRTRRsPRLNKHA-PE 599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 919 QFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlnvhgqqvDTIGIPIHWGYEGvakkgfiANTLTPFVGD 998
Cdd:COG3383 600 PFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTNDALD 664
|
970
....*....|....*...
gi 1236119465 999 ANTQTPEFKAFLVNVEKV 1016
Cdd:COG3383 665 PVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1013 |
3.97e-128 |
|
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: 404.16 E-value: 3.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRApgSDKWQQISWEE 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIRE--GDKFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 129 AFDRIAKLIKEDRDANfieknadGVTvnrwlSTGMLCASASSNETGYLTQKFTRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKEIKEKY-------GPD-----SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 208 FGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 288 LLYLMTNEKYNREYTEAYTNAslivredyhFEDglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnlLKEH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAFIEKRTEG---------FEE-------------------------------------------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 368 VSRYTPEVVENICGTPKADFLKvcelIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 448 HSNIQGLTDLGLLSQSLPGYMNLPSEkqtdlqtyltastpkpllegqvnywgnypkffvSMMKAFfgdkataENSWGFDW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGYQPVSDE---------------------------------EVREKF-------AKAWGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 528 LPKwDKGYDVLQYFEMMHQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFwqnhgesndvdpski 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 608 qTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILagiflrlrKMYAAEGGANpepvlnmtWNYSTPen 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII--------QELANALGLD--------WNYNHP-- 487
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 688 papeevamesngkalADVIDpatgtvlakkgdqlsTFAHLrddgttssgCWIFAGswtpkgnqmANRDNADpsGLGNTLg 767
Cdd:TIGR01591 488 ---------------QEIMD---------------EIREL---------TPLFAG---------LTYERLD--ELGSLQ- 516
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 768 wawaWPLNrrilynraSADPQGNPwdpkrqLLKWDGakwggvdipdystappgsdvgpfIMQPEGMGRLFAIDKMAegpf 847
Cdd:TIGR01591 517 ----WPCN--------DSDASPTS------YLYKDK-----------------------FATPDGKAKFIPLEWVA---- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 848 pehyePFETPlgtnplhpnvvsnpaarifkgdfdalgkKDKFPYVGTTYRLTEHFHY--WTKHALLNAIAQPEQFVEIGE 925
Cdd:TIGR01591 552 -----PIEEP----------------------------DDEYPLILTTGRVLTHYNVgeMTRRVAGLRRLSPEPYVEINT 598
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 926 KLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRtlnvhgqqVDTIGIPIHWGYEGVakkgfiaNTLTPFVGDANTQTPE 1005
Cdd:TIGR01591 599 EDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVN--------KGAIYITMHFWDGAV-------NNLTTDDLDPISGTPE 663
|
....*...
gi 1236119465 1006 FKAFLVNV 1013
Cdd:TIGR01591 664 YKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
16-1016 |
5.96e-123 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 390.36 E-value: 5.96e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 16 MAGTTAAALGFAPGVALAETrqykllrTRETRNTCTYCSVGCGLLMYSLGDGAKnakasifHIEGDPDHPVNRGALCPKG 95
Cdd:COG0243 1 MSLRDFKAAGAGAAALEAAG-------TKTVKTTCPGCGVGCGLGVKVEDGRVV-------RVRGDPDHPVNRGRLCAKG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 96 AGLVDFIHSESRLKFPEYR--APGSDKWQQISWEEAFDRIAKLIKEDRDanfiEKNADGVtvnrWLSTGMLCASASSNET 173
Cdd:COG0243 67 AALDERLYSPDRLTYPMKRvgPRGSGKFERISWDEALDLIAEKLKAIID----EYGPEAV----AFYTSGGSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 174 GYLTQKFTRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKIHNGA 253
Cdd:COG0243 139 AYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 254 KLIVIDPRFTRTASVADFYTPIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTNaslivredyhfedglfsGYDAekrky 333
Cdd:COG0243 219 KIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTV-----------------GFDE----- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 334 dktswnyeldekgfakrdttlqhprcvwnlLKEHVSRYTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWT 413
Cdd:COG0243 277 ------------------------------LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 414 QHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSniqgltdlgllsqslpgymnlpsekqtdlqtyltastpkpLLEG 493
Cdd:COG0243 323 QHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGEA----------------------------------------ILDG 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 494 QvnywgNYPkffvsmMKAFFgdkataenswgfdwlpkwdkgydvlqyfemmhqgkvngylCQGFNPVASFPNKNKVVESL 573
Cdd:COG0243 363 K-----PYP------IKALW----------------------------------------VYGGNPAVSAPDTNRVREAL 391
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 574 SKLKFLVTIDPLNTETSTFwqnhgesNDVdpskiqtevfRLPSTCFAEENGSIVNSG-RWLQWHWKGADAPGIAMNDGEI 652
Cdd:COG0243 392 RKLDFVVVIDTFLTETARY-------ADI----------VLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEI 454
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 653 LAGIFLRLrkmyaaegGANPEpvlnMTWNYStpenpaPEEVamesngkaLADVIDPATGTVLakkgdqlsTFAHLRDDGt 732
Cdd:COG0243 455 FAELAKRL--------GFEEA----FPWGRT------EEDY--------LRELLEATRGRGI--------TFEELREKG- 499
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 733 tssgcwifagswtpkgnqmanrdnadpsglgntlgwAWAWPLnrrilynrasadPQGNPWdpkrqllkwdgAKWGGVDIP 812
Cdd:COG0243 500 ------------------------------------PVQLPV------------PPEPAF-----------RNDGPFPTP 520
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 813 DystappgsdvgpfimqpegmGRL-FAIDKMAEGPFPEHYEPFEtplgtnplhpnvvsnpaarifkgdfDALGKKDKFPY 891
Cdd:COG0243 521 S--------------------GKAeFYSETLALPPLPRYAPPYE-------------------------GAEPLDAEYPL 555
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 892 VGTTYRLTEHFHYWT-KHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlnvhgqqvDT 970
Cdd:COG0243 556 RLITGRSRDQWHSTTyNNPRLREI-GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GV 626
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1236119465 971 IGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKAFLVNVEKV 1016
Cdd:COG0243 627 VFAPHGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-686 |
4.89e-121 |
|
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: 380.02 E-value: 4.89e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdKWQQISWEE 128
Cdd:cd02753 3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 129 AFDRIAKLIKEDRDANFIEknadgvtvnrwlSTGMLCASASSNETGYLTQKFTRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:cd02753 74 ALSLVASRLKEIKDKYGPD------------AIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSPTVAGLAET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 208 FGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKIhNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSGV 287
Cdd:cd02753 142 LGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 288 LLYLMTNEKYNREYTEAYTNaslivredyhfedglfsGYDAekrkydktswnyeldekgfakrdttlqhprcvwnlLKEH 367
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTE-----------------GFEE-----------------------------------LKEI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 368 VSRYTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRG 447
Cdd:cd02753 249 VEKYTPEYAERITGVPAEDIREAARMYATA----KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 448 HSNIQGLTDLGLLSQSLPGYmnlpsekqtdlqtyltastpkpllegqvnywgnypkffvsmmkaffgdkataenswgfdw 527
Cdd:cd02753 325 QNNVQGACDMGALPNVLPGY------------------------------------------------------------ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 528 lpkwdkgydvlqyfemmhqgkVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFwqnhgesNDVdpski 607
Cdd:cd02753 345 ---------------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL-------ADV----- 391
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1236119465 608 qteVfrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIFLRLrkmyaaegGANpepvlnmtWNYSTPE 686
Cdd:cd02753 392 ---V--LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRL--------GYP--------GFYSHPE 449
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-660 |
2.43e-90 |
|
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: 299.91 E-value: 2.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 47 RNTCTYCSVGCGLLMYSLGDGAKNAKasifhieGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSdKWQQISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 127 EEAFDRIAKLIKEDRDanfiEKNADGVTVnrwLSTGMLCasassNETGYLTQKFTRA-LGMLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFKAIQA----EYGPDSVAF---YGSGQLL-----TEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 206 PTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAK-IHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 285 SGVLLYLMTNEKYNREYTEAYTNaslivredyhfedglfsGYDAekrkydktswnyeldekgfakrdttlqhprcvwnlL 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTE-----------------GFEE-----------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 365 KEHVSRYTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 445 LRGHSNIQGLTDLGLLSQSLPGYMNLPSEKqtdlqtyltastpkpllegqvnywgnypkffvsmmkaffgDKATAENSWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 525 FDWLPKWDK-GYDVLQYFEMMHQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDP-LNTETSTFwqnhgesNDV 602
Cdd:cd02754 365 VPEGTIPPKpGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEY-------ADL 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1236119465 603 dpskiqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGIAMNDGEILAGIFLRL 660
Cdd:cd02754 438 ----------VLPAASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRL 485
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-660 |
2.84e-85 |
|
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: 279.60 E-value: 2.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 47 RNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSDKWQQISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 127 EEAFDRIAKLIKEDRDAnfieknadgvtvNRWLSTGMLCASASSNETGYLTQKFTRALGMLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREK------------YGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 207 TFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 287 vllylmtnekynreyteaytnaslivredyhfedglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnllke 366
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 367 hvsrytpEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 220 -------EWAAEITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 447 ghsniqgltdlgllsqslpgymnlpsekqtdlqtyltastpkpllegqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 527 wlpkwdkgydvlqyfemmhqgkvngylcqGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETSTFwqnhgesNDVdpsk 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-------ADV---- 326
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1236119465 607 iqtevfRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIFLRL 660
Cdd:cd00368 327 ------VLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
887-1015 |
2.56e-54 |
|
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: 184.35 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRtlnvh 964
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1236119465 965 gqqVDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1015
Cdd:cd02792 76 ---PHEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-583 |
6.56e-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: 189.44 E-value: 6.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 107 RLKFPEYRAPGSDKWQQISWEEAFDRIAKLIK--EDRDANFieknadgvtvnrWLStgmlcaSASSNETGYLTQKFTRAL 184
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRalDPDRAAF------------YTS------GRASNEAAYLYQLFARAY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 185 GMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP---- 260
Cdd:cd02767 126 GTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlrep 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 261 ---RF----------TRTASVADFYTPIRSGTDITFLSGVLLYLMTNEKY-----NREYTEAYTNaslivredyhfedgl 322
Cdd:cd02767 205 gleRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEpgnvlDHDFIAEHTS--------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 323 fsGYDAEKRKYDKTSWnyeldekgfakrdttlqhprcvwnllkehvsrytpEVVENICGTPKADFLKVceliAETSAKDK 402
Cdd:cd02767 270 --GFEEYVAALRALSW-----------------------------------DEIERASGLSREEIEAF----AAMYAKSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 403 TASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgymnlpsekqtdlqtyl 482
Cdd:cd02767 309 RVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI----------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 483 tasTPKPLLEgqvnywgnypkFFVSMmkaffgdkataENSWGFDwLPKWdKGYDVLQYFEMMHQGKVNGYLCQGFNPVAS 562
Cdd:cd02767 366 ---TEKPFPE-----------FLDAL-----------EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAEA 418
|
490 500
....*....|....*....|.
gi 1236119465 563 FPNKNKVVESLSKLKFLVTID 583
Cdd:cd02767 419 MPDPAATEEALRRLDLTVHVA 439
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
4.14e-46 |
|
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: 172.48 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 48 NTCTYCSVGCGLLMYslgdgAKNAKAsiFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGRV--VKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 126 WEEAFDRIAKLIKEDRDanfiEKNADGVTVNRWLSTGMlcasassnetgYLTQKFTRALGMLAVDNQARVUHGP-TVASL 204
Cdd:cd02755 76 WDEALQYIASKLKEIKE----QHGPESVLFGGHGGCYS-----------PFFKHFAAAFGSPNIFSHESTCLASkNLAWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 205 APTFGRGAMTNhwVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFL 284
Cdd:cd02755 141 LVIDSFGGEVN--PDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 285 SGVLLYLMTNEKYNREYTEAYTNAslivredyhFEdglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnLL 364
Cdd:cd02755 219 LALIHVLISENLYDAAFVEKYTNG---------FE-------------------------------------------LL 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236119465 365 KEHVSRYTPEVVENICGTPKADFLKVCELIAeTSAKDKTASFLYALGWTQHSIGAQniRTMAMVQLLLGNMGMAGG 440
Cdd:cd02755 247 KAHVKPYTPEWAAQITDIPADTIRRIAREFA-AAAPHAVVDPGWRGTFYSNSFQTR--RAIAIINALLGNIDKRGG 319
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-454 |
1.12e-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: 169.35 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 47 RNTCTY-CSVGCGLLMYSLGDGAKNakasifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA-PGSDKWQQI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 125 SWEEAFDRIAKLIKEDRDANFIE-----KNADGVTVNRWLSTGMlcasassnetgyltqkFTRALGMLAVDNQarVUHGP 199
Cdd:cd02766 74 SWDEALDTIAAKLKEIKAEYGPEsilpySYAGTMGLLQRAARGR----------------FFHALGASELRGT--ICSGA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 200 TVASLAPTFGRgAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGT 279
Cdd:cd02766 136 GIEAQKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 280 DITFLSGVLLYLMTNEKYNREYTEAYTNaslivredyhfedglfsGYDAekrkydktswnyeldekgfakrdttlqhprc 359
Cdd:cd02766 214 DGALALGVAKVLFREGLYDRDFLARHTE-----------------GFEE------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 360 vwnlLKEHVSRYTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAG 439
Cdd:cd02766 246 ----LKAHLETYTPEWAAEITGVSAEEIEELARLYGEA----KPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPG 317
|
410
....*....|....*
gi 1236119465 440 GGVNALRGHSNIQGL 454
Cdd:cd02766 318 GGAFYSNSGPPVKAL 332
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-589 |
1.60e-44 |
|
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: 173.07 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 107 RLKFPEYRAPGSDKWQQISWEEAFDRIAKLIkedrdaNFIE-KNADGVTVNRwlstgmlcasaSSNETGYLTQKFTRALG 185
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIAAKL------NSLDpKQVAFYTSGR-----------TSNEAAYLYQLFARSLG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 186 MLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP----- 260
Cdd:TIGR01701 162 SNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAK-KRGAKIIAINPlrerg 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 261 --RFTRTAS-----------VADFYTPIRSGTDITFLSGVLLYLMTNEKY------NREYTEAYTNaslivredyhfedg 321
Cdd:TIGR01701 241 leRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDAqpgsliDHEFIANHTN-------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 322 lfsgydaekrkydktswnyeldekGFAK-RDTTLQHPrcvWNllkehvsrytpeVVENICGTPKADFLKVCELIAETSAk 400
Cdd:TIGR01701 307 ------------------------GFDElRRHVLQLN---WN------------DIERSSGLSQEEILEFAKLLANSRR- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 401 dktASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGltdlgllsqslpgymnlpsekqtdlqt 480
Cdd:TIGR01701 347 ---VVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQG--------------------------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 481 yltastpkpllEGQVNYWGNYPKFFvsmmkaffgdKATAENSWGFDwLPKWdKGYDVLQYFEMMHQGKVNGYLCQGFNPV 560
Cdd:TIGR01701 397 -----------DRTMGITEKPEEEF----------LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNFL 453
|
490 500
....*....|....*....|....*....
gi 1236119465 561 ASFPNKNKVVESLSKLKFLVTIDPLNTET 589
Cdd:TIGR01701 454 EAMPDTAAIERALRQLDLRVHVATKLNRS 482
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
2.63e-42 |
|
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: 161.70 E-value: 2.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA--PGSDKWQQISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 127 EEAFDRIAKLIKEDRDanfiEKNADGVTVnrWLSTGMLCASASSNETGYLTQKFTRALGMLAVDnqarVUHGPT-VASLA 205
Cdd:cd02759 76 DEALDEIAEKLAEIKA----EYGPESIAT--AVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGE----SCYWPRdMAHAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 206 PTFGRGAMTNHwvDIKNANLIVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLS 285
Cdd:cd02759 146 TTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 286 GVLLYLMTNEKYNREYTEAYTNAslivredyhFEDglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnlLK 365
Cdd:cd02759 224 GMLNVIINEGLYDKDFVENWCYG---------FEE-------------------------------------------LA 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1236119465 366 EHVSRYTPEVVENICGTPKADFLKVCELIaetsAKDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNA 444
Cdd:cd02759 252 ERVQEYTPEKVAEITGVPAEKIRKAARLY----ATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLI 326
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
887-1015 |
2.78e-41 |
|
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: 147.27 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRtlnvh 964
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1236119465 965 gqqVDTIGIPIHWGYEGvakKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1015
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-453 |
1.38e-40 |
|
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: 158.41 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 51 TYCSVGCG---LLMYSLGDGaknakaSIFHIEGD--PDHPVNRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQ 123
Cdd:cd02765 2 TACPPNCGgrcPLKCHVRDG------KIVKVEPNewPDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 124 ISWEEAFDRIAKLIKEDRDaNFIEKNADGVTVNRWLSTGMLCASASSNETGYLTqkFTRALGMLAVDNQARVuhgptvas 203
Cdd:cd02765 74 ITWDEALDTIADKLTEAKR-EYGGKSILWMSSSGDGAILSYLRLALLGGGLQDA--LTYGIDTGVGQGFNRV-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 204 LAPTFGRGamTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITF 283
Cdd:cd02765 143 TGGGFMPP--TNEITDWVNAKTIIIWGSNILETQFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 284 LSGVLLYLMTNEKYNREYTEAYTNASLIVREDyhfeDGLF---SGYDAEKRKYDKTSWNYELDEKGFAkrDTTLQHP--- 357
Cdd:cd02765 220 ALGMINYILEHNWYDEAFLKSNTSAPFLVRED----NGTLlrqADVTATPAEDGYVVWDTNSDSPEPV--AATNINPale 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 358 ----------RCVWNLLKEHVSRYTPEVVENICGTPKADFlkvcELIAETSAKDKtASFLYALGWTQH-SIGAQNIRTMA 426
Cdd:cd02765 294 geytingvkvHTVLTALREQAASYPPKAAAEICGLEEAII----ETLAEWYATGK-PSGIWGFGGVDRyYHSHVFGRTAA 368
|
410 420 430
....*....|....*....|....*....|.
gi 1236119465 427 MVQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 369 ILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-590 |
2.24e-35 |
|
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: 142.54 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYSlgDGAKNAKasifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGSdkWQQISWEE 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 129 AFDRIAKLIKEDRDANfieknaDGVTVNRWLSTGMLCASASSNETGYLtqkfTRALGMLAVDNQARVUHGPTVASLAPTF 208
Cdd:cd02762 74 AFDEIAERLRAIRARH------GGDAVGVYGGNPQAHTHAGGAYSPAL----LKALGTSNYFSAATADQKPGHFWSGLMF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 209 GRGaMTNHWVDIKNANLIVVMGGNAAEAHpvGFRWAM-------EAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDI 281
Cdd:cd02762 144 GHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTApdrvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 282 TFLSGvLLYLMtnekynreyteaytnaslivredyhFEDGLFsgydaekrkydktswnyelDEKGFAKRDTTLQHprcvw 361
Cdd:cd02762 221 WLLAA-MLAVL-------------------------LAEGLT-------------------DRRFLAEHCDGLDE----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 362 nlLKEHVSRYTPEVVENICGTPkADFLKvcELIAETSAKDKTAsfLYA-LGWTQHSIGAQNIRTMAMVQLLLGNMGMAGG 440
Cdd:cd02762 251 --VRAALAEFTPEAYAPRCGVP-AETIR--RLAREFAAAPSAA--VYGrLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 441 gvnalrghsniqgltdlGLLSQSLpgymnLPSEKQTDLQTYLTASTPKPllegqvnywgnypkffVSMMKAFFGD---KA 517
Cdd:cd02762 324 -----------------AMFTTPA-----LDLVGQTSGRTIGRGEWRSR----------------VSGLPEIAGElpvNV 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1236119465 518 TAEnswgfdwlpkwdkgydvlqyfEMM--HQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKFLVTIDPLNTETS 590
Cdd:cd02762 366 LAE---------------------EILtdGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETT 419
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
49-440 |
3.88e-32 |
|
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: 132.18 E-value: 3.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYslgdgAKNAKASifHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRA------PGSDKWQ 122
Cdd:cd02757 5 TCQGCTAWCGLQAY-----VEDGRVT--KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrDVDPKFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 123 QISWEEAFD----RIAKLIKEDRDANFIeknadgVTVNRWlstgmlcasasSNETGYLTQKFTRALGMLAVDNQARVUhg 198
Cdd:cd02757 78 PISWDEALDtiadKIRALRKENEPHKIM------LHRGRY-----------GHNNSILYGRFTKMIGSPNNISHSSVC-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 199 ptvaSLAPTFGRGAMTNHW----VDIKNANLIVVMGGNAAEA-HPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYT 273
Cdd:cd02757 139 ----AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 274 PIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTNASLIVREDYHFEDGLFSgydaEKRKYDKTSWnyeldekgfakrdtt 353
Cdd:cd02757 215 PIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGETVDEESFK----EKSTEGLVKW--------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 354 lqhprcvWNllkEHVSRYTPEVVENICGTPKADFLKVCELIAetSAKDKTASFLYAlGWTQHSIGAQNIRTMAMVQLLLG 433
Cdd:cd02757 276 -------WN---LELKDYTPEWAAKISGIPAETIERVAREFA--TAAPAAAAFTWR-GATMQNRGSYNSMACHALNGLVG 342
|
....*..
gi 1236119465 434 NMGMAGG 440
Cdd:cd02757 343 SIDSKGG 349
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-582 |
1.20e-30 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 129.78 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 102 IHSESRLKFPEYRAPGSDKWQQISWEEAFDRIAKLIKEDRDANFIEKNADGVTvnrwlstgmlcasasSNETGYLTQKFT 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRT---------------SNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 182 RALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRwAMEAKIHNGAKLIVIDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 261 ------RFT-----------RTASVADFYTPIRSGTDITFLSGVLLYLMTNEkynrEYTEAYTNASLIvreDYHFEDGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 324 SGYDAEKRKYDKTSWnyeldekgfakrdttlqhprcvwnllkehvsrytpEVVENICGTPKAdflKVCELIAETSAKDKT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEW-----------------------------------KDIERISGLSQT---QIAELADAYAAAERT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 404 AsFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgymnlpsekqtdlqtylt 483
Cdd:PRK09939 362 I-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI------------------------ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 484 asTPKPLLEgqvnywgnypkfFVSMMKAFFGdkataenswgfdWLPKWDKGYDVLQYFEMMHQGKVNGYLCQGFNPVASF 563
Cdd:PRK09939 417 --TEKPSAE------------FLARLGERYG------------FTPPHAPGHAAIASMQAICTGQARALICMGGNFALAM 470
|
490
....*....|....*....
gi 1236119465 564 PNKNKVVESLSKLKFLVTI 582
Cdd:PRK09939 471 PDREASAVPLTQLDLAVHV 489
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
1.19e-28 |
|
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: 122.82 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 79 EGDPDHPVNRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIA---KLIKEDRDANFIEKNADGV 153
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIAselKRIIEKYGNEAIYVNYGTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 154 TVNRWLSTGMLCASASSNETGYLTQKFTralgmlavdnqarVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNA 233
Cdd:cd02770 111 TYGGVPAGRGAIARLLNLTGGYLNYYGT-------------YSWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 234 AEAHPVGFR---WAMEAKiHNGAKLIVIDPRFTRTASV-ADFYTPIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTnas 309
Cdd:cd02770 178 AETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYC--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 310 livredYHF-EDGLFSGYDAEKrkydktswNYeldeKGFakrdttlqhprcVWNLLKEHVSRyTPEVVENICGTPKADFL 388
Cdd:cd02770 254 ------VGFdAEHLPEGAPPNE--------SY----KDY------------VLGTGYDGTPK-TPEWASEITGVPAETIR 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236119465 389 KVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 303 RLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-447 |
7.26e-26 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 114.74 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 2 QVSRRQFFKICA-GGMA-GTTAAALGFAPGVALAETRQYKLLRTRETRNTCTY-CSVGCGLLMYSLgDGAknakasIFHI 78
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAmASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVV-DGE------IKYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 79 EGDPDHPVNRGAL-----CPKGAGLVDFIHSESRLKFPEYR--APGSDKWQQISWEEAFDRIA----KLIKEDRDA---- 143
Cdd:PRK14990 86 ETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYDIIAtnmqRLIKEYGNEsiyl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 144 NFIEKNADGVTVNRWLSTGMLCASASSNETGYLTQKFTRALGMLAvdnqarvuhgptvASLAPTFGRGAMTNHWVDIKNA 223
Cdd:PRK14990 166 NYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA-------------EGLNYTYGGWADGNSPSDIENS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 224 NLIVVMGGNAAEAHPVG---FRWAMEAKIHNGAKLIVIDPRFTRT-ASVADFYTPIRSGTDITFLSGvLLYLMTNEkynr 299
Cdd:PRK14990 233 KLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNG-LAYVMITE---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 300 eyteaytnaSLIvreDYHFEDGLFSGYD-------AEKRKYDKTswnYELDE--KGFAKrdttlqhprcvwnllkehvsr 370
Cdd:PRK14990 308 ---------NLV---DQPFLDKYCVGYDektlpasAPKNGHYKA---YILGEgpDGVAK--------------------- 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236119465 371 yTPEVVENICGTPKADFLKVCELIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRG 447
Cdd:PRK14990 352 -TPEWASQITGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-440 |
1.00e-25 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 114.38 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 1 MQVSRRQFFKicaGGMAGTTAAALG-FAPGvALAETRQYKLL-RTRETRNTCTYCSVGCGLLMYSLGDgaKNakasIFhI 78
Cdd:PRK15488 1 MSLSRRDFLK---GAGAGCAACALGsLLPG-ALAANEIAQLKgKTKLTPSICEMCSTRCPIEARVVNG--KN----VF-I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 79 EGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIAKLIKEDRDanfiEKNADGVTVn 156
Cdd:PRK15488 70 QGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKLNAIKQ----QHGPESVAF- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 157 rwlstgmlcaSASSNETGYLTQKFTRALGMLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANLIVVMGGNAAEA 236
Cdd:PRK15488 145 ----------SSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLYEG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 237 HPVGF-RWAMEAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSGVLLYLMTNEKYNREYTEAYTnaslivred 315
Cdd:PRK15488 211 INMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYT--------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 316 yhfedglfSGYDAekrkydktswnyeldekgfakrdttlqhprcvwnlLKEHVSRYTPEVVENICGTPKADFLKVCELIA 395
Cdd:PRK15488 282 --------SGFEE-----------------------------------LAASVKEYTPEWAEAISDVPADDIRRIARELA 318
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1236119465 396 EtSAKDKTASFLYALGWTQHSIgaQNIRTMAMVQLLLGNMGMAGG 440
Cdd:PRK15488 319 A-AAPHAIVDFGHRATFTPEEF--DMRRAIFAANVLLGNIERKGG 360
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-447 |
5.26e-25 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 112.30 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 1 MQVSRRQFFKICAggmAGTTAAALGFA-PGVALAETRQyKLLRTRETRNTCTYCSVGCGLLMyslgdGAKNAKasIFHIE 79
Cdd:PRK13532 1 MKLSRRDFMKANA---AAAAAAAAGLSlPAVANAVVGS-AQTAIKWDKAPCRFCGTGCGVLV-----GTKDGR--VVATQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKFP-------EYRAPGsdKWQQISWEEAFDRIAKLIKedrdANFIEKNADG 152
Cdd:PRK13532 70 GDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFK----KALKEKGPTA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 153 VtvnrwlstGMLcasASSNET---GYLTQKFTRAlGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIV 227
Cdd:PRK13532 144 V--------GMF---GSGQWTiweGYAASKLMKA-GFRSnnIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 228 VMGGNAAEAHPVgfRWA--MEAKI-HNGAKLIVIDPRFTRTASVADfyTPI--RSGTDITFLSGVLLYLMTNEKYNREYT 302
Cdd:PRK13532 212 LWGSNMAEMHPI--LWSrvTDRRLsNPDVKVAVLSTFEHRSFELAD--NGIifTPQTDLAILNYIANYIIQNNAVNWDFV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 303 EAYTNASLIV-------REDyhfeDGLFSgyDAEKRKYDKTSWNYELDEkgfakrdttlqhprcvwnlLKEHVSRYTPEV 375
Cdd:PRK13532 288 NKHTNFRKGAtdigyglRPT----HPLEK--AAKNPGTAGKSEPISFEE-------------------FKKFVAPYTLEK 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236119465 376 VENICGTPKADFLKVCELIAETsaKDKTASFlYALGWTQHSIG--AQNIrtMAMVQLLLGNMGMAGGGVNALRG 447
Cdd:PRK13532 343 TAKMSGVPKEQLEQLAKLYADP--NRKVVSF-WTMGFNQHTRGvwANNL--VYNIHLLTGKISTPGNGPFSLTG 411
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
1.26e-24 |
|
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: 110.51 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLmyslgdgAK--NAKASIFHIEGDPDHPVN---------------------------RGALCPKGAGLV 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 100 DFIHSESRLKFPEYRA--PGSDKWQQISWEEAFDRIA--------------KLIKeDRDANFIEKNAD-GVTVNrwlstg 162
Cdd:cd02758 76 QYLYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVVeggdlfgeghveglKAIR-DLDTPIDPDHPDlGPKAN------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 163 MLCASASSNETG-YLTQKFTR-ALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANLIVVMGGNAAEAHPv 239
Cdd:cd02758 149 QLLYTFGRDEGRtPFIKRFANqAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 240 GFRWA----MEAKIHNGAKLIVIDPRFTRTASVAD---FYTPIRSGTDITFLSGVLLYLMTNEKYNREY-----TEA--- 304
Cdd:cd02758 228 PFKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYlsipsKEAaka 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 305 -----YTNASLIVREdyhfedglfsgydaekrkydktswnyeldekgfAKRDTTLQhprcvwnLLKEHVSRYTPEVVENI 379
Cdd:cd02758 308 agepsWTNATHLVIT---------------------------------VRVKSALQ-------LLKEEAFSYSLEEYAEI 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236119465 380 CGTPKAdflKVCELIAETSAKDKTASFLYAlGWTQHSIGAQNIRTMAMVQLLLGNMGMAGG 440
Cdd:cd02758 348 CGVPEA---KIIELAKEFTSHGRAAAVVHH-GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
3.41e-24 |
|
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: 109.15 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYsLGDGaknakaSIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDG------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 127 EEAFDRIAKLIKEDRDANfIEKNAdgvtvnrwLSTGmlcasasSNETGYLTQKFTRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02763 76 EEAFSIATKRLKAARATD-PKKFA--------FFTG-------RDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 207 TFGRGAMTNHWVDIKNANLIvVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSG 286
Cdd:cd02763 140 SIGGSFWEFGGPDLEHTKYF-MMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 287 VLLYLMTNEKYNREYTEAYTNASLIVredyhfedglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnllke 366
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 367 hvsRYTPEVVENICGTPKADFLKVCELIAETS---------------------AKDKTASFLYALGWTQHSIGAQNIRTM 425
Cdd:cd02763 245 ---DYTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrkhekITGRPVSFHAMRGIAAHSNGFQTIRAL 321
|
410
....*....|....*
gi 1236119465 426 AMVQLLLGNMGMAGG 440
Cdd:cd02763 322 FVLMMLLGTIDRPGG 336
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
6.30e-24 |
|
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: 107.70 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 92 CPKGAGLVDFIHSESRLKFPEYR------------APGSDKWQQISWEEAFDRIAKLIKEDRDA---NFIEKNADGvtvn 156
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLVASELKRIREKygnEAIFGGSYG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 157 rWLSTGMLCASASS-----NETG-YLTQKFTRALGmlavdnQARVuhgptvasLAP----TFGRGAMTNHWVDI-KNANL 225
Cdd:cd02751 108 -WASAGRLHHAQSLlhrflNLIGgYLGSYGTYSTG------AAQV--------ILPhvvgSDEVYEQGTSWDDIaEHSDL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 226 IVVMGGNAAE--------AHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASV-ADFYTPIRSGTDITFLSGVLLYLMTNEK 296
Cdd:cd02751 173 VVLFGANPLKtrqgggggPDHGSYYYLKQAK-DAGVRFICIDPRYTDTAAVlAAEWIPIRPGTDVALMLAMAHTLITEDL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 297 YNREYTEAYTnaslivredyhfedglfSGYDAEKrkydktswNYELDEK-GFAKrdttlqhprcvwnllkehvsryTPEV 375
Cdd:cd02751 252 HDQAFLARYT-----------------VGFDEFK--------DYLLGESdGVPK----------------------TPEW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 376 VENICGTPKADFLKVCELIAetsakDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRGHSNIQGLT 455
Cdd:cd02751 285 AAEITGVPAETIRALAREIA-----SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPP 359
|
410
....*....|
gi 1236119465 456 DLGLLSQSLP 465
Cdd:cd02751 360 RGGAGGPGLP 369
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
898-1007 |
6.50e-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: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 898 LTEHFH--YWTKHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRtlnvhgqqVDTIGIPI 975
Cdd:cd02775 1 LRDHFHsgTRTRNPWLREL-APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVP--------PGVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 1236119465 976 HWGYEGvaKKGFIANTLTPFVGDANTQTPEFK 1007
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-653 |
2.53e-23 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 102.86 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 107 RLKFPEYRApGSDKWQQISWEEAFDRIAKLIKEDRDanfiEKNADGVTVNRWlstgmlCASASSNETGYLTQKFTRALGM 186
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIK----KYGPDAIAINGG------SGGLTDVESLYALKKLLNRLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 187 LAV---DNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGfrWAME--AKIHNGAKLIVIDPR 261
Cdd:pfam00384 70 KNGnteDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIL--NARIrkAALKGKAKVIVIGPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 262 FTRTasVADFYTPIRSGTDITFLSGVLLYLMTNEKYNreyteaytnaslivredyhfedglfsgydaekrkydktswnye 341
Cdd:pfam00384 148 LDLT--YADEHLGIKPGTDLALALAGAHVFIKELKKD------------------------------------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 342 ldeKGFAKRdttlqhprcvwnllkehvsrytpevvenicgtpkadflkvceliaetsakdktASFLYALGWTQHSIGAQN 421
Cdd:pfam00384 183 ---KDFAPK-----------------------------------------------------PIIIVGAGVLQRQDGEAI 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 422 IRTMAMVQLLLGNMGMAGGGVNALR---GHSNIQGLTDLGLlsqslpgymnlpsekqtdlqtyltastpkpllegqvnyw 498
Cdd:pfam00384 207 FRAIANLADLTGNIGRPGGGWNGLNilqGAASPVGALDLGL--------------------------------------- 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 499 gnypkffvsmmkaffgdkataenswgfdwlpkwDKGYDVLQYFEMMHQGKVNGYLCQGFNPVASFPNKNKVVESLSKLKF 578
Cdd:pfam00384 248 ---------------------------------VPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDL 294
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236119465 579 LVTIDPlntetstFWQNHGESN-DVdpskiqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGIAMNDGEIL 653
Cdd:pfam00384 295 FVVYDG-------HHGDKTAKYaDV----------ILPAAAYTEKNGTYVNTEGRVQ-STKQAvPPPGEAREDWKIL 353
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
82-447 |
1.27e-20 |
|
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: 96.23 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 82 PDH-PvnRGalCPKGAGLVDFIHSESRLKFPEYRAP--GSDKWQQISWEEAFDRIAKLIKE-------DRDANFIEKNAd 151
Cdd:cd02750 44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELIADAIIDtikkygpDRVIGFSPIPA- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 152 gvtvnrwlsTGMLCASASSnetgyltqKFTRALGMLAVDNQARVUHGPTVASLapTFGRGAMTNHWVDIKNANLIVVMGG 231
Cdd:cd02750 119 ---------MSMVSYAAGS--------RFASLIGGVSLSFYDWYGDLPPGSPQ--TWGEQTDVPESADWYNADYIIMWGS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 232 NAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYTPIRSGTDiTFLSGVLLYLMTNEK-YNREYTEAYTNASL 310
Cdd:cd02750 180 NVPVTRTPDAHFLTEAR-YNGAKVVVVSPDYSPSAKHADLWVPIKPGTD-AALALAMAHVIIKEKlYDEDYLKEYTDLPF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 311 IVredyhfedglfsgydaekrkydktswnyeldekgfakrdttlqhprcvwnllkehvsrYTPEVVENICGTPKADFLKV 390
Cdd:cd02750 258 LV----------------------------------------------------------YTPAWQEAITGVPRETVIRL 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1236119465 391 celiAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMVQLLLGNMGMAGGGVNALRG 447
Cdd:cd02750 280 ----AREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
887-1015 |
6.48e-20 |
|
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: 86.14 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIrtlnv 963
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTmtrRAEGLDAIA-PEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRV----- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1236119465 964 hgqQVDTIGIPIHWgYEGVakkgfiANTLTPFVGDANTQTPEFKAFLVNVEK 1015
Cdd:cd02790 75 ---PEGVVFMPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
887-1016 |
7.65e-20 |
|
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: 86.09 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTLNV 963
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1236119465 964 HgqqvdtigIPIHWGYEGVAKKGfiANTLTPFVGDANTQTPEFKAFLVNVEKV 1016
Cdd:cd02791 80 F--------VPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
894-1010 |
1.98e-18 |
|
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: 81.55 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 894 TTYRLTEHFHYWTKHALLNAIAQPEQ-FVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlnvhgqqvDTIG 972
Cdd:pfam01568 4 ITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--------GVVF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1236119465 973 IPIHWGYEgvaKKGFIANTLTPFVGDANTQTPEFKAFL 1010
Cdd:pfam01568 76 MPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-104 |
3.36e-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: 79.22 E-value: 3.36e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236119465 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 104
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEV-----KDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
43-104 |
2.84e-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: 76.56 E-value: 2.84e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236119465 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 104
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHV-----KDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-264 |
1.46e-15 |
|
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: 80.02 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 50 CTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRapGSDKWQQISWEEA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 130 FDRIAKLIKEdrdanfIEKNADGVTVNrwlstgmlcaSASSNETGYLTQKFTRALGMLAVDNQARvuhGPTVASLAPTFG 209
Cdd:cd02768 75 LKTVAEGLKA------VKGDKIGGIAG----------PRADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLRG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 210 RGAMTNHWVDIKNANLIVVMGGNAAEAHPVgfrwaMEAKI-----HNGAKLIVIDPRFTR 264
Cdd:cd02768 136 NYLFNTSIAEIEEADAVLLIGSNLRKEAPL-----LNARLrkavkKKGAKIAVIGPKDTD 190
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-403 |
8.99e-15 |
|
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: 78.86 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 50 CTYCSVGCGLLMYSLGDGAknakasIFHIEGDPD----HPVnRGALCPKGAGLVDFIHSESRLKFPEYRA---------P 116
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 117 GsdkWQQISWEEAFDRIAKLIKEDRDANFIEKNA---DGVTVNRWLSTGMLCASASSNETGYLTQKFTRALGMLAVDNQA 193
Cdd:cd02760 77 G---FVPISWDEALDLVAAKLRRVREKGLLDEKGlprLAATFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQGVKCVHS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 194 RVUHGptvaslaptfgrGAMTNHWV---DIKNANLIVVMGGNA-AEAHPVGFRWAMEAKIHnGAKLIVIDPRFTRTASVA 269
Cdd:cd02760 154 EHLYG------------EFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVR-GYKRVQVEPHLSVTGACS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 270 DFYTPIRSGTDITF---LSGVLLYLMTNEKYNREYTEAYTNASLIVRedyhfEDGLFSgYDAEKRK---YD-KTSWNYEL 342
Cdd:cd02760 221 AEWVPIRPKTDPAFmfaMIHVMVHEQGLGKLDVPFLRDRTSSPYLVG-----PDGLYL-RDAATGKplvWDeRSGRAVPF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 343 DEKGFAK----------------RDTTLQHP----RCVWNLLKEHVSRYTPEVVENICGTPKADFLKVCELIAETSAKDK 402
Cdd:cd02760 295 DTRGAVPavagdfavdgavsvdaDDETAIHQgvegTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLENASIGS 374
|
.
gi 1236119465 403 T 403
Cdd:cd02760 375 T 375
|
|
| 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 |
1.12e-14 |
|
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: 77.81 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRapGSDKWQQISWEE 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 129 AFDRIAKLIKEDRDAnfieknADGVTVNRwlstgmlcasaSSNETGYLTQKFTR-ALGMLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK------VGGIGSPR-----------ASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190
....*....|....*....|....*....|..
gi 1236119465 208 FGRGAMTNHwvDIKNANLIVVMGGNAAEAHPV 239
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPR 162
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
49-668 |
1.43e-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: 71.74 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMY---------------SLG----------DGAKNAKASI----------FHIEGDPDH--PVNRGAL 91
Cdd:cd02756 16 TCHFCIVGCGYHVYvwpvgeeggpspgqnAIGydlvdqvpplNLQWYPKTMHyvvvtqdgreVYIVIVPDKecPVNSGNY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 92 CPKGAGLVDFIHS------ESRLKFPEYRApgSDKWQQISWEEAFDRIAKLIKEDRDAnfiEKNADGVTVNRWLSTGmlc 165
Cdd:cd02756 96 STRGGTNAERIWSpdnrvgETRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGILDK---DGNDDAVFASRFDHGG--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 166 aSASSNETGYLTQKF---TRALGMLAVDNqaRVUHGPTVASLAPTfGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGF- 241
Cdd:cd02756 168 -GGGGFENNWGVGKFffmALQTPFVRIHN--RPAYNSEVHATREM-GVGELNNSYEDARLADTIVLWGNNPYETQTVYFl 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 242 ----------------RWAMEAKIHNGAKLIVIDPRFTRTASVAD--------FYTPIRSGTDITFLSGVLLYlmtneky 297
Cdd:cd02756 244 nhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARY------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 298 nreyteaytnaslivredyhfedglfsgydaekrkydktswnyeldekgfakrdttlqhprcVWNLLKEHVSRytpevVE 377
Cdd:cd02756 317 --------------------------------------------------------------IYESLDEVLAE-----AE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 378 NICGTPKADFLKVCELIAETSA--KDKTASFLYALG--WtqhsiGAQNIRTM-AMVQL--LLGNMGMAGGGVNALRGHSn 450
Cdd:cd02756 330 QITGVPRAQIEKAADWIAKPKEggYRKRVMFEYEKGiiW-----GNDNYRPIySLVNLaiITGNIGRPGTGCVRQGGHQ- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 451 iQGLTdlgllsqsLPGYmnlPSEKQTDLQTYlTASTPKPLLEGQVNY---WGNYPkfFVSMMKAFFGDKATAENSWgfdw 527
Cdd:cd02756 404 -EGYV--------RPPP---PPPPWYPQYQY-APYIDQLLISGKGKVlwvIGCDP--YKTTPNAQRLRETINHRSK---- 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 528 lpkwdkgydvlqyfemmhqgKVNGYLCQGFNPVasfPNKNKVVESLSKLK------FLVTIDPLNTET---------STF 592
Cdd:cd02756 465 --------------------LVTDAVEAALYAG---TYDREAMVCLIGDAiqpgglFIVVQDIYPTKLaedahvilpAAA 521
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236119465 593 WqnhGESNDVdpskiqtevfrlpstcfaeengSIVNSGRWLQWHWKGADAPGIAMNDGEILAGIFLRLRKMYAAEG 668
Cdd:cd02756 522 N---GEMNET----------------------SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIYELYQEEG 572
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
104-260 |
1.18e-10 |
|
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: 64.68 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 104 SESRLKFPEYRAPGsdKWQQISWEEAFDRIAKLIKEDRDanfiEKNADgvtvnrwlSTGMLCASASSNETGYLTQKFTRA 183
Cdd:cd02772 51 SEDRLTKPMIKKDG--QWQEVDWETALEYVAEGLSAIIK----KHGAD--------QIGALASPHSTLEELYLLQKLARG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1236119465 184 LGMLAVDNQARVUHGPTVASLAPTFGrgaMTNHWVDIKNANLIVVMGGNAAEAHP-VGFRWAMEAKihNGAKLIVIDP 260
Cdd:cd02772 117 LGSDNIDHRLRQSDFRDDAKASGAPW---LGMPIAEISELDRVLVIGSNLRKEHPlLAQRLRQAVK--KGAKLSAINP 189
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
5-288 |
1.04e-09 |
|
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: 62.12 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 5 RRQFFKICAGGMAGTTAAALG-----FAPGVALAETRQykLLRTRETRNTCTYCSVGCGLLMySLGDGAKnakasiFHIE 79
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRypvekIVPYVIWPENIV--PGETVYYATSLVPAGEGQGVLV-KTVDGRP------IKIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKFPeYRAPGSDKWQQISWEEAfdriAKLIKEDRDANfieKNADGVTVnrwl 159
Cdd:cd02764 72 GNPDHPASLGGTSARAQASVLSLYDPDRAQGP-LRRGIDGAYVASDWADF----DAKVAEQLKAV---KDGGKLAV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 160 stgmlcasASSNETGYLTQKFTRALgmLAVDNQARVU-HGPTVASLAPTFGRGAMTNHWV---DIKNANLIVVMGGNAAE 235
Cdd:cd02764 140 --------LSGNVNSPTTEALIGDF--LKKYPGAKHVvYDPLSAEDVNEAWQASFGKDVVpgyDFDKAEVIVSIDADFLG 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 236 AHPVGFRWA---MEAKIH----NGAKLIVIDPRFTRTASVADFYTPIRSGTDITFLSGVL 288
Cdd:cd02764 210 SWISAIRHRhdfAAKRRLgaeePMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLA 269
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-279 |
4.31e-09 |
|
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: 59.85 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 41 LRTRETrnTCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKFPEYRAPGsdK 120
Cdd:COG1034 215 LKKTPS--ICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG--E 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 121 WQQISWEEAFDRIAKLIKEDRDAnfieKNADGVTvnrwlstgMLCAsassnetgyltqkftralgmlavdnqarvuhGPT 200
Cdd:COG1034 284 LVEASWEEALAAAAEGLKALKKA----ENSVGAA--------LLGA-------------------------------LPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 201 VASLAPTFGRGAmtnhwvdiknANLIVVMGGNAAEAHPVgfrwAMEAKIHNGAKLIVIDPRFTRTASVADFYTPI----- 275
Cdd:COG1034 321 AAAILEAAEAGK----------LKALVLLGADPYDLDPA----AALAALAKADFVVVLDHFGSATAERADVVLPAaafae 386
|
....
gi 1236119465 276 RSGT 279
Cdd:COG1034 387 KSGT 390
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-465 |
6.25e-09 |
|
The MopB_DMSOR-BSOR-TMAOR 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. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 59.97 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 79 EGDPDhPvnrgalCPKGAGLVDFIHSESRLKFPEYR-------------APGSDKWQQISWEEAFDRIAKLIKEDRDanf 145
Cdd:cd02769 25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRK--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 146 iEKNADGV--TVNRWLSTGMLCASASS-----NETG-YLTQKFTRALGMLAVDNqarvuhgPTVasLAPTFGRGAMTNHW 217
Cdd:cd02769 95 -TYGNEAIfgGSYGWSSAGRFHHAQSLlhrflNLAGgYVGSVGDYSTGAAQVIL-------PHV--VGSMEVYTEQQTSW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 218 VDI-KNANLIVVMGGNA----------AEAHPVgfRWAMEAKIHNGAKLIVIDPRFTRTASVADF-YTPIRSGTDITFLS 285
Cdd:cd02769 165 PVIaEHTELVVAFGADPlknaqiawggIPDHQA--YSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALML 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 286 GVLLYLMTNEKYNREYTEAYTnaslivredyhfedglfSGYDAEKRkydktswnYELDEK-GFAKrdttlqhprcvwnll 364
Cdd:cd02769 243 ALAHTLVTEGLHDKAFLARYT-----------------VGFDKFLP--------YLLGESdGVPK--------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 365 kehvsryTPEVVENICGTPkADFLKvcELiAETSAKDKTasfLYALGWT----QHsiGAQNIrTMAMVqL--LLGNMGMA 438
Cdd:cd02769 283 -------TPEWAAAICGIP-AETIR--EL-ARRFASKRT---MIMAGWSlqraHH--GEQPH-WMAVT-LaaMLGQIGLP 344
|
410 420
....*....|....*....|....*..
gi 1236119465 439 GGGVNALRGHSNIQGLTDLGLLSQSLP 465
Cdd:cd02769 345 GGGFGFGYHYSNGGGPPRGAAPPPALP 371
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
889-984 |
9.15e-09 |
|
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: 54.99 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 889 FPYVGTTYRLTEHFHYWTKHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTkrirtlnvHGQQV 968
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEI-KPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVT--------EGVRP 71
|
90
....*....|....*....
gi 1236119465 969 DTIGIPI---HWGYEGVAK 984
Cdd:cd02780 72 GVVAIEHgygHWAYGAVAS 90
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-285 |
2.05e-08 |
|
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: 57.73 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 49 TCTYCSVGCGLLMYSLGDGAKNAKASIfhiegdpdhpvnrgalCPKG-AGLVDFIHSesrlkfpeYRAPGSDKwQQISWE 127
Cdd:cd02761 3 VCPFCGLLCDDIEVEVEDNKITKVRNA----------------CRIGaAKFARYERR--------ITTPRIDG-KPVSLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 128 EAFDRIAKLIKEDRdanfieknadgvtvnRWLSTGMlcaSASSNETgyltqkfTRALGMLA------VDNQARVUHGPTV 201
Cdd:cd02761 58 EAIEKAAEILKEAK---------------RPLFYGL---GTTVCEA-------QRAGIELAeklgaiIDHAASVCHGPNL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 202 ASLAPtfgRGAMTNHWVDIKN-ANLIVVMGGNAAEAHPVGFR---WAMEAKIHNGA----KLIVIDPRFTRTASVADFYT 273
Cdd:cd02761 113 LALQD---SGWPTTTLGEVKNrADVIVYWGTNPMHAHPRHMSrysVFPRGFFREGGredrTLIVVDPRKSDTAKLADIHL 189
|
250
....*....|..
gi 1236119465 274 PIRSGTDITFLS 285
Cdd:cd02761 190 QIDPGSDYELLA 201
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
909-1015 |
1.50e-07 |
|
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: 51.12 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 909 ALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlnvhgqqvDTIGIPIHWGYegVAKKGFI 988
Cdd:cd02778 21 PLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--------DTVFMPHGFGH--WAPALSR 89
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90 100 110
....*....|....*....|....*....|....
gi 1236119465 989 A-------NTLTPFVGDANTQTPEFKAFLVNVEK 1015
Cdd:cd02778 90 AygggvndNNLLPGSTEPVSGGAGLQEFTVTVRK 123
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| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
888-959 |
2.75e-07 |
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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: 50.44 E-value: 2.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236119465 888 KFPYVGTTY--RLTEHFHYWTKHALLnaIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02785 1 KYPLACIQRhsRFRVHSQFSNVPWLL--ELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
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| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
889-1015 |
9.57e-07 |
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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: 48.84 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236119465 889 FPYVGTTYRLTEHFHywTKHALLNAIAQ--PEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTLNVHGQ 966
Cdd:cd02781 3 PLILTTGARSYYYFH--SEHRQLPSLRElhPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAE 80
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236119465 967 QvdtiGipiHWGYEGVAKKGFI-------ANTLT------PFVGDANtqtpeFKAFLVNVEK 1015
Cdd:cd02781 81 H----G---WWYPEREAGEPALggvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
928-959 |
1.34e-04 |
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The MopB_DMSOR-BSOR-TMAOR 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.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 42.62 E-value: 1.34e-04
10 20 30
....*....|....*....|....*....|..
gi 1236119465 928 ANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02793 42 AAARGIADGDIVRVFNDRGACLAGAVVTDGIM 73
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| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
928-959 |
1.62e-04 |
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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: 42.57 E-value: 1.62e-04
10 20 30
....*....|....*....|....*....|..
gi 1236119465 928 ANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIM 74
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