|
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: 1482.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 2 QVSRRQFFKICAGGMAGTTAAALGFAPGVALAETRQYKLLRTRETRNTCTYCSVGCGLLMYSLGDGAKNAKASIFHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 82 PDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYQAQNAEGVTVNRWLTT 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 162 GMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 242 RWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTNASLIVREDFGFDDG 321
Cdd:TIGR01553 241 KWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 322 LFTGYDADKRQYDKTSWHYELDENGFAKHDTTLQHPRCVWNLLKQHVSRYTPDMVENICGTPKADFLKVCEYIAETSAKD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 402 KTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYLTLPSEKQTDLQTY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 482 LAANTPKPLLKDQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGYD-VLQYFEMMKQGKVNGYICQGFNPV 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDsWLTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 561 ASFPNKNKVVASLSKLKYLVTIDPLNTETSTFWQNHGesndVDPAKIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGA 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 641 DAPGIAMTDGEILAGIFLRLRKMYSEQGGANPEQVLNMTWNYTKPYEPASEEVAMESNGKALADLIDPatgAVVVKKGQQ 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDFKVG---DVEYKKGQQ 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 721 LSSFAQLRDDGTTSSGCWIFAGSWTPEGNMMARRDNADPSGLGNTLGWAWAWPLNRRILYNRASADPQGNPWDPKRQLLK 800
Cdd:TIGR01553 713 IATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALVE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 801 WEGGKWAgW--DIPDYSAAA-PGSDVGPFIMQPEGMGRLFAIDKMAEGPFPEHYEPFETPLGTNPLHPNVISNPAARIFK 877
Cdd:TIGR01553 793 WNAAEKK-WvgDIPDYPPTApPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYK 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 878 DDADALGKADKFPYVGTTYRLTEHFHYWTKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKR 957
Cdd:TIGR01553 872 TDEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKR 951
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 499298135 958 IRTLKADGKDIDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:TIGR01553 952 IKPLAIQGQQVHMIGIPIHWGWSFLKNGGDATNILTPSVGDPNTGTPETKAFLVNIEK 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: 979.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 47 RNTCTYCSVGCGLLMYSLGDgaknakaSIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSDKWQQISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNG-------VWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 127 EEAFDRIAKLMKEDRDANYQAQNAEGVTVNRWLTTGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 207 TFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 287 VMLYLLtnekynreyteaytnaslivredfgfddglftgydadkrqydktswhyeldengfakhdttlqhprcvwnllkq 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 367 hvsRYTPDMVENICGTPKADFLKVCEYIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 447 GHSNIQGLTDLGLLSQSLPGYLTlpsekqtdlqtylaantpkpllkdqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 527 wlpkwdkgydvlqyfemmkqgkvngyicqGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFWQNHGesndVDPAK 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 607 IQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIFLRLRKMYSEQGGANPEQVLNmtWNYTKPY 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 687 EPASEEVAMESNGKALADLIDPATGAVVVKKGQQLSSFAQLRDDGTTSSGCWIFAGSWTPEGNmMARRDNADPSGLGNTL 766
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYTGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYP 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 767 GWAWAWPLNRRILYNRASADPQGNPWDPKRQLLKWEG-GKWAGWDIPDYSA-AAPGSDVGPFIMQPEGMGRLFAIDKmaE 844
Cdd:cd02752 544 GWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGlGWWWKGDVPDGPWpAAKEHGCGPFIMAPEGQARLFVWNF--D 621
|
810 820 830
....*....|....*....|....*....|
gi 499298135 845 GPFPEHYEPFETPLGTNplHPNVISNPAAR 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: 921.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 15 GMAGTTAAALGFAPGVALAEtrqykllrtRETRNTCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVSRGALCPK 94
Cdd:NF041513 21 GAAARSARTRALRPRTATAD---------RVVRSVCPYCAVGCGQKVY-----VKDEK--VVQIEGDPDSPISRGRLCPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 95 GAGLVDFIHSESRLKFPQYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANYQAQNAEGVTVNRWLTTGMLCASASSNETG 174
Cdd:NF041513 85 GSASLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEEN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 175 YLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAK 254
Cdd:NF041513 165 YLIKKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAK-ARGAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 255 LIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTNASLIVREDFGfD----DGLFTGYDADK 330
Cdd:NF041513 244 VIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFR-DtedlDGLFSGFDPET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 331 RQYDKTSWHYELDEN----------------------------------GFAKHDTTLQHPRCVWNLLKQHVSRYTPDMV 376
Cdd:NF041513 323 GSYDPASWQYEGVEVaaaagqrdqlydsrggahesargeehgsggapvaGAPRRDETLQDPRCVFQILKRHFARYTPEMV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 377 ENICGTPKADFLKVCEYIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTD 456
Cdd:NF041513 403 EEICGIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 457 LGLLSQSLPGYLTLP-SEKQTDLQTYLAANTPkpllkdQVNYWGNYPKFFVSMMKAFFGDKATAENSWGFDWLPKWDKGY 535
Cdd:NF041513 483 IPTLFNLLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDH 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 536 DVLQYFEMMKQGKVNGYICQGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFWQNHGE--SNDVDPAKIQTEVFR 613
Cdd:NF041513 557 STYQTVMAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEieTGELRTEDIGTEVFF 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 614 LPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIFLRLRKMYSEQGGANPEQVLNMTWNY-TKPY--EPAS 690
Cdd:NF041513 637 FPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLDLTWDYpTEGPhgEPDA 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 691 EEVAMESNGKALAdlidpatgavvvkkGQQLSSFAQLRDDGTTSSGCWIFAGSWTPEGNMMARRDnadPSGLGNTLG--W 768
Cdd:NF041513 717 EAVLAEINGYDLS--------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWVAaeW 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 769 AWAWPLNRRILYNRASADPQGNPWDPKRQLLKW--EGGKWAGWDIPDYSAAAP----------------GSDvgPFIMQP 830
Cdd:NF041513 780 GWAWPANRRILYNRASADPEGRPWSERKKYVWWdaEAGRWTGYDVPDFPVDKPpdyrpppgatgpaalsGDD--PFIMQA 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 831 EGMGRLFAIDKMAEGPFPEHYEPFETPLGtNPLHPnVISNPAARIFKDDADALGK------ADKFPYVGTTYRLTEHF-- 902
Cdd:NF041513 858 DGKGWLFAPAGLVDGPLPTHYEPQESPVR-NPLYG-QQRNPARKVYPREDNRYHPsggepgAEVYPYVFTTYRLTEHHta 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 903 ---HYWTKHAllnAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTLKADGKDIDTIGIPIHWGY 979
Cdd:NF041513 936 ggmSRWLPYL---AELQPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGP 1012
|
1050 1060 1070
....*....|....*....|....*....|....
gi 499298135 980 EGVAkKGFIANTLTPFVGDANTQTPEFKSFLVNV 1013
Cdd:NF041513 1013 NGLV-TGDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-1016 |
2.51e-151 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 465.13 E-value: 2.51e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 43 TRETRNTCTYCSVGCGLLMYSLGDGaknakasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGsdKWQ 122
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 123 QISWEEAFDRIAKLMKEDRDANyqaqNAEGVtvnrwlttGMLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTV 201
Cdd:COG3383 75 EVSWDEALDLVAERLREIQAEH----GPDAV--------AFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 202 ASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDI 281
Cdd:COG3383 143 AGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 282 AFLSGVMLYLLTNEKYNREYTEAYTNaslivredfGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvw 361
Cdd:COG3383 222 ALLNGLLHVIIEEGLVDEDFIAERTE---------GFEE----------------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 362 nlLKQHVSRYTPDMVENICGTPKADFLKVCEYIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGG 441
Cdd:COG3383 252 --LKASVAKYTPERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 442 VNALRGHSNIQGLTDLGLLSQSLPGYLTLPSEKqtdlqtylaantpkpllkdqvnywgnypkffvsmmkaffgDKATAEN 521
Cdd:COG3383 326 PFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPE----------------------------------------HRAKVAD 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 522 SWGFDWLPKWdKGYDVLQYFEMMKQGKVNGYICQGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFwqnhgesND 601
Cdd:COG3383 366 AWGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY-------AD 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 602 VdpakiqtevfRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIflrLRKMyseqgGANpeqvlnmtWN 681
Cdd:COG3383 438 V----------VLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAEL---ARRL-----GYG--------FD 491
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 682 YTKPyepasEEVAMEsngkaLADLIDPATGAvvvkkgqqlsSFAQLRDDGttssgcwifagswtpegnmmarrdnadpsg 761
Cdd:COG3383 492 YDSP-----EEVFDE-----IARLTPDYSGI----------SYERLEALG------------------------------ 521
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 762 lgntlgwAWAWPLNrrilynraSADPQGNPwdpkrqllkweggkwagwdipdysaaapgsdvgpfimqpegmgRLFAidk 841
Cdd:COG3383 522 -------GVQWPCP--------SEDHPGTP-------------------------------------------RLFT--- 540
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 842 maegpfpehyEPFETPLGTNPLHPNVISNPAARIfkddadalgkADKFPYVGTTYRLTEHFH--YWTKH-ALLNAIAqPE 918
Cdd:COG3383 541 ----------GRFPTPDGKARFVPVEYRPPAELP----------DEEYPLVLTTGRLLDQWHtgTRTRRsPRLNKHA-PE 599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 919 QFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdiDTIGIPIHWGYEGvakkgfiANTLTPFVGD 998
Cdd:COG3383 600 PFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTNDALD 664
|
970
....*....|....*...
gi 499298135 999 ANTQTPEFKSFLVNVEKV 1016
Cdd:COG3383 665 PVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1007 |
5.34e-127 |
|
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: 401.07 E-value: 5.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRApgSDKWQQISWEE 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIRE--GDKFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 129 AFDRIAKLMKEDRDaNYQAQnaegvtvnrwlTTGMLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKEIKE-KYGPD-----------SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 208 FGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 288 MLYLLTNEKYNREYTEAYTNaslivredfGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnlLKQH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAFIEKRTE---------GFEE-------------------------------------------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 368 VSRYTPDMVENICGTPKADFLKvceyIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 448 HSNIQGLTDLGLLSQSLPGYLTlpsekqtdlqtylaantpkplLKDQVNywgnypkffvsmMKAFfgdkataENSWGFDW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGYQP---------------------VSDEEV------------REKF-------AKAWGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 528 LPKwDKGYDVLQYFEMMKQGKVNGYICQGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFwqnhgesndvdpaki 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 608 qTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILagiflrlrKMYSEQGGANpeqvlnmtWNYTKPYE 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII--------QELANALGLD--------WNYNHPQE 489
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 688 PASEevamesngkaladlidpatgavvvkkgqqlssFAQLrddgttssgCWIFAGswtpegnmMARRDNADPSGLgntlg 767
Cdd:TIGR01591 490 IMDE--------------------------------IREL---------TPLFAG--------LTYERLDELGSL----- 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 768 wawAWPLNrrilynraSADPQGNPwdpkrqLLKWEGgkwagwdipdysaaapgsdvgpfIMQPEGMGRLFAIDKMAegpf 847
Cdd:TIGR01591 516 ---QWPCN--------DSDASPTS------YLYKDK-----------------------FATPDGKAKFIPLEWVA---- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 848 pehyePFETPlgtnplhpnvisnpaarifkddadalgkADKFPYVGTTYRLTEHFHY--WTKHALLNAIAQPEQFVEIGE 925
Cdd:TIGR01591 552 -----PIEEP----------------------------DDEYPLILTTGRVLTHYNVgeMTRRVAGLRRLSPEPYVEINT 598
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 926 KLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdiDTIGIPIHWGYEGVakkgfiaNTLTPFVGDANTQTPE 1005
Cdd:TIGR01591 599 EDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNK--------GAIYITMHFWDGAV-------NNLTTDDLDPISGTPE 663
|
..
gi 499298135 1006 FK 1007
Cdd:TIGR01591 664 YK 665
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
16-1016 |
2.01e-122 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 389.20 E-value: 2.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 16 MAGTTAAALGFAPGVALAETrqykllrTRETRNTCTYCSVGCGLLMYSLGDGAKnakasifHIEGDPDHPVSRGALCPKG 95
Cdd:COG0243 1 MSLRDFKAAGAGAAALEAAG-------TKTVKTTCPGCGVGCGLGVKVEDGRVV-------RVRGDPDHPVNRGRLCAKG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 96 AGLVDFIHSESRLKFPQYR--APGSDKWQQISWEEAFDRIAKLMKEDRDAnyqaQNAEGVtvnrWLTTGMLCASASSNET 173
Cdd:COG0243 67 AALDERLYSPDRLTYPMKRvgPRGSGKFERISWDEALDLIAEKLKAIIDE----YGPEAV----AFYTSGGSAGRLSNEA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 174 GYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGA 253
Cdd:COG0243 139 AYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 254 KLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTNaslivredfGFDDglftgydadkrqy 333
Cdd:COG0243 219 KIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTV---------GFDE------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 334 dktswhyeldengfakhdttlqhprcvwnlLKQHVSRYTPDMVENICGTPKADFLKVCEYIAETsakdKTASFLYALGWT 413
Cdd:COG0243 277 ------------------------------LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 414 QHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGhsniqgltdlgllsqslpgyltlpsekqtdlqtylaantpkpllkd 493
Cdd:COG0243 323 QHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG---------------------------------------------- 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 494 qvnywgnypkffvsmmkaffgdkataenswgfdwlpkwdkgydvlqyfEMMKQGK---VNGYICQGFNPVASFPNKNKVV 570
Cdd:COG0243 357 ------------------------------------------------EAILDGKpypIKALWVYGGNPAVSAPDTNRVR 388
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 571 ASLSKLKYLVTIDPLNTETSTFwqnhgesNDVdpakiqtevfRLPSTCFAEENGSIVNSG-RWLQWHWKGADAPGIAMTD 649
Cdd:COG0243 389 EALRKLDFVVVIDTFLTETARY-------ADI----------VLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSD 451
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 650 GEILAGIFLRLrkmyseqgGANPEqvlnMTWNYTKpyepasEEVamesngkaLADLIDPATGAVVvkkgqqlsSFAQLRD 729
Cdd:COG0243 452 WEIFAELAKRL--------GFEEA----FPWGRTE------EDY--------LRELLEATRGRGI--------TFEELRE 497
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 730 DGttssgcwifagswtpegnmmarrdnadpsglgntlgwAWAWPLnrrilynrasadPQGNPWdPKRQLLKWEGGKWAgw 809
Cdd:COG0243 498 KG-------------------------------------PVQLPV------------PPEPAF-RNDGPFPTPSGKAE-- 525
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 810 dipdysaaapgsdvgpfimqpegmgrlFAIDKMAEGPFPEHYEPFEtplgtnplhpnvisnpaarifkddaDALGKADKF 889
Cdd:COG0243 526 ---------------------------FYSETLALPPLPRYAPPYE-------------------------GAEPLDAEY 553
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 890 PYVGTTYRLTEHFHYWT-KHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdi 968
Cdd:COG0243 554 PLRLITGRSRDQWHSTTyNNPRLREI-GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP-------- 624
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 499298135 969 DTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKSFLVNVEKV 1016
Cdd:COG0243 625 GVVFAPHGWWYEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-677 |
1.44e-118 |
|
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: 373.47 E-value: 1.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGsdKWQQISWEE 128
Cdd:cd02753 3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 129 AFDRIAKLMKEDRDAnYQAQNAEGvtvnrwlttgmLCASASSNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:cd02753 74 ALSLVASRLKEIKDK-YGPDAIAF-----------FGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSPTVAGLAET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 208 FGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIhNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGV 287
Cdd:cd02753 142 LGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 288 MLYLLTNEKYNREYTEAYTNaslivredfGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnlLKQH 367
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTE---------GFEE-------------------------------------------LKEI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 368 VSRYTPDMVENICGTPKADFLKvceyIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02753 249 VEKYTPEYAERITGVPAEDIRE----AARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 448 HSNIQGLTDLGLLSQSLPGYLtlpsekqtdlqtylaantpkpllkdqvnywgnypkffvsmmKAFFgdkataenswgfdw 527
Cdd:cd02753 325 QNNVQGACDMGALPNVLPGYV-----------------------------------------KALY-------------- 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 528 lpkwdkgydvlqyfemmkqgkvngyiCQGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFwqnhgesNDVdpaki 607
Cdd:cd02753 350 --------------------------IMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL-------ADV----- 391
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 608 qteVfrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIflrLRKMYSEQGGANPEQVLN 677
Cdd:cd02753 392 ---V--LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQEL---ANRLGYPGFYSHPEEIFD 453
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-660 |
1.54e-85 |
|
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: 286.81 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 47 RNTCTYCSVGCGLLMYSLGDGAKNAKasifhieGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSdKWQQISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 127 EEAFDRIAKLMKedrdanyQAQNAEGVTVNRWLTTGMLCasassNETGYLTQKFSRA-LGMLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFK-------AIQAEYGPDSVAFYGSGQLL-----TEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 206 PTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAK-IHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 285 SGVMLYLLTNEKYNREYTEAYTNaslivredfGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnlL 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTE---------GFEE-------------------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 365 KQHVSRYTPDMVENICGTPKADFLKVCEYIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 445 LRGHSNIQGLTDLGLLSQSLPGYLTLPSEKqtdlqtylaantpkpllkdqvnywgnypkffvsmmkaffgDKATAENSWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 525 FDWLPKWDK-GYDVLQYFEMMKQGKVNGYICQGFNPVASFPNKNKVVASLSKLKYLVTIDP-LNTETSTFwqnhgesNDV 602
Cdd:cd02754 365 VPEGTIPPKpGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTETAEY-------ADL 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 499298135 603 dpakiqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGIAMTDGEILAGIFLRL 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 |
1.33e-82 |
|
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: 272.66 E-value: 1.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 47 RNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSDKWQQISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 127 EEAFDRIAKLMKEDRDANyqaqNAEGVtvnrwlttGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREKY----GPDAI--------AFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 207 TFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 287 vmlylltnekynreyteaytnaslivredfgfddglftgydadkrqydktswhyeldengfakhdttlqhprcvwnllkq 366
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 367 hvsrytpDMVENICGTPKADFLKVceyiAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 220 -------EWAAEITGVPAETIRAL----AREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 447 ghsniqgltdlgllsqslpgyltlpsekqtdlqtylaantpkpllkdqvnywgnypkffvsmmkaffgdkataenswgfd 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 527 wlpkwdkgydvlqyfemmkqgkvngyicqGFNPVASFPNKNKVVASLSKLKYLVTIDPLNTETSTFwqnhgesNDVdpak 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-------ADV---- 326
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 499298135 607 iqtevfRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIFLRL 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 |
2.47e-53 |
|
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: 181.65 E-value: 2.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkad 964
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499298135 965 gkdiDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02792 77 ----HEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-583 |
8.32e-52 |
|
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: 192.14 E-value: 8.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 107 RLKFPQYRAPGSDKWQQISWEEAFDRIAKLMKedrdaNYQAQNAEgvtvnrWLTTGMlcasaSSNETGYLTQKFSRALGM 186
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLR-----ALDPDRAA------FYTSGR-----ASNEAAYLYQLFARAYGT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP------ 260
Cdd:cd02767 128 NNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlrepgl 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 261 -RF----------TRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKY-----NREYTEAYTNaslivredfGFDDglft 324
Cdd:cd02767 207 eRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEpgnvlDHDFIAEHTS---------GFEE---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 325 gYDADKRQydkTSWhyeldengfakhdttlqhprcvwnllkqhvsrytpDMVENICGTPKADFLKVceyiAETSAKDKTA 404
Cdd:cd02767 274 -YVAALRA---LSW-----------------------------------DEIERASGLSREEIEAF----AAMYAKSERV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 405 SFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgyltlpsekqtdlqtylaa 484
Cdd:cd02767 311 VFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 485 nTPKPLlkdqvnywgnyPKFFVSMmkaffgdkataENSWGFDwLPKWdKGYDVLQYFEMMKQGKVNGYICQGFNPVASFP 564
Cdd:cd02767 366 -TEKPF-----------PEFLDAL-----------EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAEAMP 420
|
490
....*....|....*....
gi 499298135 565 NKNKVVASLSKLKYLVTID 583
Cdd:cd02767 421 DPAATEEALRRLDLTVHVA 439
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
7.38e-49 |
|
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: 180.57 E-value: 7.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 48 NTCTYCSVGCGLLMYslgdgAKNAKAsiFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGRV--VKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 126 WEEAFDRIAKLMKEDRdanyQAQNAEGVTVNRWLTTGMlcasassnetgYLTQKFSRALGMLAVDNQARVUHGP-TVASL 204
Cdd:cd02755 76 WDEALQYIASKLKEIK----EQHGPESVLFGGHGGCYS-----------PFFKHFAAAFGSPNIFSHESTCLASkNLAWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 205 APTFGRGAMTNhwVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFL 284
Cdd:cd02755 141 LVIDSFGGEVN--PDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 285 SGVMLYLLTNEKYNREYTEAYTNaslivredfGFDdglftgydadkrqydktswhyeldengfakhdttlqhprcvwnLL 364
Cdd:cd02755 219 LALIHVLISENLYDAAFVEKYTN---------GFE-------------------------------------------LL 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499298135 365 KQHVSRYTPDMVENICGTPKADFLKVCEYIAeTSAKDKTASFLYALGWTQHSIGAQniRTMAMIQLLLGNMGMAGG 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 |
2.44e-47 |
|
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: 177.06 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 47 RNTCTY-CSVGCGLLMYSLGDGAKNakasifhIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRA-PGSDKWQQI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 125 SWEEAFDRIAKLMKEDRDAnyqaQNAEGVTVNRWL-TTGMLcasassneTGYLTQKFSRALGMLAVDNQarVUHGPTVAS 203
Cdd:cd02766 74 SWDEALDTIAAKLKEIKAE----YGPESILPYSYAgTMGLL--------QRAARGRFFHALGASELRGT--ICSGAGIEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 204 LAPTFGRgAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAF 283
Cdd:cd02766 140 QKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGTDGAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 284 LSGVMLYLLTNEKYNREYTEAYTnaslivredFGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnl 363
Cdd:cd02766 218 ALGVAKVLFREGLYDRDFLARHT---------EGFEE------------------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 364 LKQHVSRYTPDMVENICGTPKADFLKVCEYIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVN 443
Cdd:cd02766 246 LKAHLETYTPEWAAEITGVSAEEIEELARLYGEA----KPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGAF 321
|
410
....*....|.
gi 499298135 444 ALRGHSNIQGL 454
Cdd:cd02766 322 YSNSGPPVKAL 332
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-611 |
2.10e-46 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 178.85 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 107 RLKFPQYRAPGSDKWQQISWEEAFDRIAKLMKE---DRDANYqaqnaegvtvnrwlTTGMlcasaSSNETGYLTQKFSRA 183
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSldpKQVAFY--------------TSGR-----TSNEAAYLYQLFARS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 184 LGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDP--- 260
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAK-KRGAKIIAINPlre 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 261 ----RFTRTAS-----------VADFYAPIRSGTDIAFLSGVMLYLLTNEKY------NREYTEAYTNaslivredfgfd 319
Cdd:TIGR01701 239 rgleRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDAqpgsliDHEFIANHTN------------ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 320 dglftgydadkrqydktswhyeldenGFAKhdttlqhprcvwnlLKQHVSRYTPDMVENICGTPKADFLKVceyiAETSA 399
Cdd:TIGR01701 307 --------------------------GFDE--------------LRRHVLQLNWNDIERSSGLSQEEILEF----AKLLA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 400 KDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgyltlpsekqtdlq 479
Cdd:TIGR01701 343 NSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGI-------------------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 480 tylaantpkpllkdqvnyWGNYPKFFvsmmkaffgdKATAENSWGFDwLPKWdKGYDVLQYFEMMKQGKVNGYICQGFNP 559
Cdd:TIGR01701 403 ------------------TEKPEEEF----------LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNF 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499298135 560 VASFPNKNKVVASLSKLKYLVTIDPLNTETSTFwqnHGESNDVDPAKIQTEV 611
Cdd:TIGR01701 453 LEAMPDTAAIERALRQLDLRVHVATKLNRSHVL---AKEEALILPVLGRYEQ 501
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
1.94e-44 |
|
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: 168.25 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYslgdgAKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRA--PGSDKWQQISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 127 EEAFDRIAKLMKEDRdANYqaqNAEGVTVnrWLTTGMLCASASSNETGYLTQKFSRALGMLAVDnqarVUHGPT-VASLA 205
Cdd:cd02759 76 DEALDEIAEKLAEIK-AEY---GPESIAT--AVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGE----SCYWPRdMAHAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 206 PTFGRGAMTNHwvDIKNANLVVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLS 285
Cdd:cd02759 146 TTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 286 GvMLYLLTNEK-YNREYTEAYTNaslivredfGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnlL 364
Cdd:cd02759 224 G-MLNVIINEGlYDKDFVENWCY---------GFEE-------------------------------------------L 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 365 KQHVSRYTPDMVENICGTPKADFLKvceyIAETSAKDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02759 251 AERVQEYTPEKVAEITGVPAEKIRK----AARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLI 326
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-453 |
1.13e-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: 158.80 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 51 TYCSVGCG---LLMYSLGDGaknakaSIFHIEGD--PDHPVSRGalCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQ 123
Cdd:cd02765 2 TACPPNCGgrcPLKCHVRDG------KIVKVEPNewPDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 124 ISWEEAFDRIAKLMKEDRDaNYQAQNAEGVTVNRWLTTGMLCASASSNETGYLTQKF----SRALGMlavdnqarvuhgp 199
Cdd:cd02765 74 ITWDEALDTIADKLTEAKR-EYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYgidtGVGQGF------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 200 tvaSLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGT 279
Cdd:cd02765 140 ---NRVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIRPGT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 280 DIAFLSGVMLYLLTNEKYNREYTEAYTNASLIVREDFG--FDDGLFTG---------YDADKRQY---DKTSWHYELdEN 345
Cdd:cd02765 216 DPALALGMINYILEHNWYDEAFLKSNTSAPFLVREDNGtlLRQADVTAtpaedgyvvWDTNSDSPepvAATNINPAL-EG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 346 GFAKHDTTLqHPrcVWNLLKQHVSRYTPDMVENICGTPKADFlkvcEYIAETSAKDKtASFLYALGWTQH-SIGAQNIRT 424
Cdd:cd02765 295 EYTINGVKV-HT--VLTALREQAASYPPKAAAEICGLEEAII----ETLAEWYATGK-PSGIWGFGGVDRyYHSHVFGRT 366
|
410 420 430
....*....|....*....|....*....|...
gi 499298135 425 MAMIQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 367 AAILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
887-1015 |
1.62e-40 |
|
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: 144.96 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 887 DKFPYVGTTYRLTEHFHYW--TKHALLNAIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRtlkad 964
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499298135 965 gkdIDTIGIPIHWGYEGvakKGFIANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
4.50e-36 |
|
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: 144.46 E-value: 4.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYSlgDGAKNAKasifhIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSdkWQQISWEE 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 129 AFDRIAKLMKEDRDA-----------NYQAQNAEGVTVNRWLTTGMLCASASSNETG-YLTQKFSrALGMlavdnqarvu 196
Cdd:cd02762 74 AFDEIAERLRAIRARhggdavgvyggNPQAHTHAGGAYSPALLKALGTSNYFSAATAdQKPGHFW-SGLM---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 197 hgptvaslaptFGRGaMTNHWVDIKNANLVVVMGGNAAEAHpvGFRWAM-------EAKIHNGAKLIVIDPRFTRTASVA 269
Cdd:cd02762 143 -----------FGHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTApdrvlrlKAAKDRGGSLVVIDPRRTETAKLA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 270 DFYAPIRSGTDIAFLSGvMLYLLtnekynreyteaytnaslivredfgFDDGLFtgydadkrqydktswhyelDENGFAK 349
Cdd:cd02762 209 DEHLFVRPGTDAWLLAA-MLAVL-------------------------LAEGLT-------------------DRRFLAE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 350 HDTTLQHprcvwnlLKQHVSRYTPDMVENICGTPKADFLKVCEYIAetSAkdKTASFLYALGWTQHSIGAQNIRTMAMIQ 429
Cdd:cd02762 244 HCDGLDE-------VRAALAEFTPEAYAPRCGVPAETIRRLAREFA--AA--PSAAVYGRLGVQTQLFGTLCSWLVKLLN 312
|
410
....*....|.
gi 499298135 430 LLLGNMGMAGG 440
Cdd:cd02762 313 LLTGNLDRPGG 323
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
49-440 |
2.50e-31 |
|
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: 129.87 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYslgdgAKNAKASifHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRA------PGSDKWQ 122
Cdd:cd02757 5 TCQGCTAWCGLQAY-----VEDGRVT--KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrDVDPKFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 123 QISWEEAFDRIAKLMKEDRDANYQaqnaegvtvnrwlTTGMLCASASSNETGYLTQKFSRALGMLAVDNQARVUhgptva 202
Cdd:cd02757 78 PISWDEALDTIADKIRALRKENEP-------------HKIMLHRGRYGHNNSILYGRFTKMIGSPNNISHSSVC------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 203 SLAPTFGRGAMTNHW----VDIKNANLVVVMGGNAAEA-HPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRS 277
Cdd:cd02757 139 AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 278 GTDIAFLSGVMLYLLTNEKYNREYTEAYTNasliVREDFGfddglfTGYDADKRQYDKTSWHyeldenGFAKhdttlqhp 357
Cdd:cd02757 219 GEDGALALAIAHVILTEGLWDKDFVGDFVD----GKNYFK------AGETVDEESFKEKSTE------GLVK-------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 358 rcvWnlLKQHVSRYTPDMVENICGTPKADFLKVCEYIAetSAKDKTASFLYAlGWTQHSIGAQNIRTMAMIQLLLGNMGM 437
Cdd:cd02757 275 ---W--WNLELKDYTPEWAAKISGIPAETIERVAREFA--TAAPAAAAFTWR-GATMQNRGSYNSMACHALNGLVGSIDS 346
|
...
gi 499298135 438 AGG 440
Cdd:cd02757 347 KGG 349
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
4.23e-31 |
|
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: 130.14 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 79 EGDPDHPVSRGalCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQISWEEAFDRIAKLMKEDRDaNYqaqNAEGVTVN 156
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIASELKRIIE-KY---GNEAIYVN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 157 rwlttgmlCASASSNETGYLTQKFSRALGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAA 234
Cdd:cd02770 107 --------YGTGTYGGVPAGRGAIARLLNLTGgyLNYYGTYSWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 235 EAHPVGFR---WAMEAKiHNGAKLIVIDPRFTRTASV-ADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTnasl 310
Cdd:cd02770 179 ETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYC---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 311 ivredFGFD-DGLFTGYDADKRQYDktswhYEL--DENGFAKhdttlqhprcvwnllkqhvsryTPDMVENICGTPKADF 387
Cdd:cd02770 254 -----VGFDaEHLPEGAPPNESYKD-----YVLgtGYDGTPK----------------------TPEWASEITGVPAETI 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499298135 388 LKVCEYIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 302 RRLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-582 |
8.15e-30 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 127.47 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 102 IHSESRLKFPQYRAPGSDKWQQISWEEAFDRIAKLMKEDRDANyqaqNAEGVTVNRwlttgmlcasaSSNETGYLTQKFS 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPN----QVEFYTSGR-----------TSNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 182 RALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGFRwAMEAKIHNGAKLIVIDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 261 ------RFT-----------RTASVADFYAPIRSGTDIAFLSGVMLYLLTNEkynrEYTEAYTNASLIvreDFGFDDGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 324 TGYDADKRQYDKTSWHyeldengfakhdttlqhprcvwnllkqhvsrytpdMVENICGTPKAdflKVCEYIAETSAKDKT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEWK-----------------------------------DIERISGLSQT---QIAELADAYAAAERT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 404 AsFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgyltlpsekqtdlqtyla 483
Cdd:PRK09939 362 I-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI------------------------ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 484 anTPKPLLKdqvnywgnypkfFVSMMKAFFGdkataenswgfdWLPKWDKGYDVLQYFEMMKQGKVNGYICQGFNPVASF 563
Cdd:PRK09939 417 --TEKPSAE------------FLARLGERYG------------FTPPHAPGHAAIASMQAICTGQARALICMGGNFALAM 470
|
490
....*....|....*....
gi 499298135 564 PNKNKVVASLSKLKYLVTI 582
Cdd:PRK09939 471 PDREASAVPLTQLDLAVHV 489
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-440 |
7.49e-28 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 120.93 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 1 MQVSRRQFFKicaGGMAGTTAAALG-FAPGvALAETRQYKLL-RTRETRNTCTYCSVGCGLLMYSLGDgaKNakasIFhI 78
Cdd:PRK15488 1 MSLSRRDFLK---GAGAGCAACALGsLLPG-ALAANEIAQLKgKTKLTPSICEMCSTRCPIEARVVNG--KN----VF-I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 79 EGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQISWEEAFDRIAKLMKEDRdanyQAQNAEGVTVn 156
Cdd:PRK15488 70 QGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKLNAIK----QQHGPESVAF- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 157 rwlttgmlcaSASSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANLVVVMGGNAAEA 236
Cdd:PRK15488 145 ----------SSKSGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLYEG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 237 HPVGF-RWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTNaslivred 315
Cdd:PRK15488 211 INMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTS-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 316 fGFDDglftgydadkrqydktswhyeldengfakhdttlqhprcvwnlLKQHVSRYTPDMVENICGTPKADFLKVCEYIA 395
Cdd:PRK15488 283 -GFEE-------------------------------------------LAASVKEYTPEWAEAISDVPADDIRRIARELA 318
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 499298135 396 EtSAKDKTASFLYALGWTQHSIgaQNIRTMAMIQLLLGNMGMAGG 440
Cdd:PRK15488 319 A-AAPHAIVDFGHRATFTPEEF--DMRRAIFAANVLLGNIERKGG 360
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-447 |
1.63e-27 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 120.13 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 2 QVSRRQFFKICA-GGMA-GTTAAALGFAPGVALAETRQYKLLRTRETRNTCTY-CSVGCGLLMYSLgDGAknakasIFHI 78
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAmASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVV-DGE------IKYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 79 E----GDPDHP-VSRGALCPKGAGLVDFIHSESRLKFPQYR--APGSDKWQQISWEEAFDRIA----KLMKEDRDA---- 143
Cdd:PRK14990 86 EtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYDIIAtnmqRLIKEYGNEsiyl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 144 NYQAQNAEGVTVNRWLTTGMLCASASSNETGYLTQKFSRALGMLAvdnqarvuhgptvASLAPTFGRGAMTNHWVDIKNA 223
Cdd:PRK14990 166 NYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA-------------EGLNYTYGGWADGNSPSDIENS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 224 NLVVVMGGNAAEAHPVG---FRWAMEAKIHNGAKLIVIDPRFTRT-ASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNR 299
Cdd:PRK14990 233 KLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 300 EYTEAYTnaslivredFGFDDGLFTGYDADKRQYDKtswhYELDE--NGFAKhdttlqhprcvwnllkqhvsryTPDMVE 377
Cdd:PRK14990 313 PFLDKYC---------VGYDEKTLPASAPKNGHYKA----YILGEgpDGVAK----------------------TPEWAS 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 378 NICGTPKADFLKVCEYIAETsakdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK14990 358 QITGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-447 |
3.00e-24 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 109.60 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 1 MQVSRRQFFKICAggmAGTTAAALGFA-PGVALAETRQyKLLRTRETRNTCTYCSVGCGLLMyslgdGAKNAKasIFHIE 79
Cdd:PRK13532 1 MKLSRRDFMKANA---AAAAAAAAGLSlPAVANAVVGS-AQTAIKWDKAPCRFCGTGCGVLV-----GTKDGR--VVATQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 80 GDPDHPVSRGALCPKGAGLVDFIHSESRLKFP-------QYRAPGsdKWQQISWEEAFDRIAKLMKedrdANYQAQNAEG 152
Cdd:PRK13532 70 GDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFK----KALKEKGPTA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 153 VtvnrwlttGMLcasASSNET---GYLTQKFSRAlGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVV 227
Cdd:PRK13532 144 V--------GMF---GSGQWTiweGYAASKLMKA-GFRSnnIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 228 VMGGNAAEAHPVgfRWA--MEAKI-HNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEA 304
Cdd:PRK13532 212 LWGSNMAEMHPI--LWSrvTDRRLsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 305 YTNASLIVrEDFGF----DDGLFTgyDADKRQYDKTSWHYELDEngFAKhdttlqhprcvwnllkqHVSRYTPDMVENIC 380
Cdd:PRK13532 290 HTNFRKGA-TDIGYglrpTHPLEK--AAKNPGTAGKSEPISFEE--FKK-----------------FVAPYTLEKTAKMS 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499298135 381 GTPKADFLKVCEYIAETsaKDKTASFlYALGWTQHSIG--AQNIrtMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK13532 348 GVPKEQLEQLAKLYADP--NRKVVSF-WTMGFNQHTRGvwANNL--VYNIHLLTGKISTPGNGPFSLTG 411
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
3.57e-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: 109.35 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLmyslgdgAK--NAKASIFHIEGDPDHPVS---------------------------RGALCPKGAGLV 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 100 DFIHSESRLKFPQYRA--PGSDKWQQISWEEAFDRIA---KLMKE----------DRDANYQAQNAE-GVTVNrwlttgM 163
Cdd:cd02758 76 QYLYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVVeggDLFGEghveglkairDLDTPIDPDHPDlGPKAN------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 164 LCASASSNETG-YLTQKFSR-ALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANLVVVMGGNAAEAHPvG 240
Cdd:cd02758 150 LLYTFGRDEGRtPFIKRFANqAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 241 FRWA----MEAKIHNGAKLIVIDPRFTRTASVAD---FYAPIRSGTDIAFLSGVMLYLLTNEKYNREY-----TEA---- 304
Cdd:cd02758 229 FKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYlsipsKEAakaa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 305 ----YTNASLIVREdfgfddglftgydadkrqydktswhyeldengfAKHDTTLQhprcvwnLLKQHVSRYTPDMVENIC 380
Cdd:cd02758 309 gepsWTNATHLVIT---------------------------------VRVKSALQ-------LLKEEAFSYSLEEYAEIC 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499298135 381 GTPKADflkvceyIAETsAKD-----KTASFLYAlGWTQHSIGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02758 349 GVPEAK-------IIEL-AKEftshgRAAAVVHH-GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
4.27e-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: 108.77 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYsLGDGaknakaSIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDG------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 127 EEAFDRIAKLMKEDRdanyqAQNAEGVTvnrwLTTGmlcasasSNETGYLTQKFSRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02763 76 EEAFSIATKRLKAAR-----ATDPKKFA----FFTG-------RDQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 207 TFGRGAMTNHWVDIKNANLvVVMGGNAAEAHPVGFRWAMEAKIHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSG 286
Cdd:cd02763 140 SIGGSFWEFGGPDLEHTKY-FMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 287 VMLYLLTNEKYNREYTEAYTNASLIVredfgfddglftgydadkrqydktswhyeldengfakhdttlqhprcvwnllkq 366
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 367 hvsRYTPDMVENICGTPKADFLKVCEYIAETS---------------------AKDKTASFLYALGWTQHSIGAQNIRTM 425
Cdd:cd02763 245 ---DYTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrkhekITGRPVSFHAMRGIAAHSNGFQTIRAL 321
|
410
....*....|....*
gi 499298135 426 AMIQLLLGNMGMAGG 440
Cdd:cd02763 322 FVLMMLLGTIDRPGG 336
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
898-1007 |
1.22e-23 |
|
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: 96.23 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 898 LTEHFH--YWTKHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdiDTIGIPI 975
Cdd:cd02775 1 LRDHFHsgTRTRNPWLREL-APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPP--------GVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 499298135 976 HWGYEGvaKKGFIANTLTPFVGDANTQTPEFK 1007
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-298 |
3.01e-23 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 102.48 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 107 RLKFPQYRApGSDKWQQISWEEAFDRIAKLMKEDRDANYQAQNAEGVTVNRWLttgmlcasasSNETGYLTQKFSRALGM 186
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLT----------DVESLYALKKLLNRLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 187 LAV---DNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHPVGfrWAME--AKIHNGAKLIVIDPR 261
Cdd:pfam00384 70 KNGnteDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIL--NARIrkAALKGKAKVIVIGPR 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 499298135 262 FTRTasVADFYAPIRSGTDIAFLSGVMLYLLTNEKYN 298
Cdd:pfam00384 148 LDLT--YADEHLGIKPGTDLALALAGAHVFIKELKKD 182
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
3.26e-23 |
|
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: 105.39 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 92 CPKGAGLVDFIHSESRLKFPQYR------------APGSDKWQQISWEEAFDRIAKLMKEDRDAnYQAQNAEGvTVNRWL 159
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLVASELKRIREK-YGNEAIFG-GSYGWA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 160 TTGMLCASASSnetgyltqkFSRALGMlavdnqarvuHGPTVASLAP---------------TFGRGAMTNHWVDI-KNA 223
Cdd:cd02751 110 SAGRLHHAQSL---------LHRFLNL----------IGGYLGSYGTystgaaqvilphvvgSDEVYEQGTSWDDIaEHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 224 NLVVVMGGNAAE--------AHPVGFRWAMEAKiHNGAKLIVIDPRFTRTASV-ADFYAPIRSGTDIAFLSGVMLYLLTN 294
Cdd:cd02751 171 DLVVLFGANPLKtrqgggggPDHGSYYYLKQAK-DAGVRFICIDPRYTDTAAVlAAEWIPIRPGTDVALMLAMAHTLITE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 295 EKYNREYTEAYTnaslivredfgfddglfTGYDADKRqydktswHYELDENGFAKhdttlqhprcvwnllkqhvsryTPD 374
Cdd:cd02751 250 DLHDQAFLARYT-----------------VGFDEFKD-------YLLGESDGVPK----------------------TPE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 375 MVENICGTPKADFLKVCEYIAetsakDKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGL 454
Cdd:cd02751 284 WAAEITGVPAETIRALAREIA-----SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGP 358
|
410
....*....|.
gi 499298135 455 TDLGLLSQSLP 465
Cdd:cd02751 359 PRGGAGGPGLP 369
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
82-447 |
2.18e-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: 95.46 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 82 PDH-PvsRGalCPKGAGLVDFIHSESRLKFPQYRAP--GSDKWQQISWEEAFDRIAKLMKeDRDANYQAQNAEGVTvnRW 158
Cdd:cd02750 44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELIADAII-DTIKKYGPDRVIGFS--PI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 159 LTTGMLCASASSnetgyltqKFSRALGMLAVDNQARVUHGPTVASLapTFGRGAMTNHWVDIKNANLVVVMGGNAAEAHP 238
Cdd:cd02750 117 PAMSMVSYAAGS--------RFASLIGGVSLSFYDWYGDLPPGSPQ--TWGEQTDVPESADWYNADYIIMWGSNVPVTRT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 239 VGFRWAMEAKiHNGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSGVMLYLLTNEKYNREYTEAYTNASLIVredfgf 318
Cdd:cd02750 187 PDAHFLTEAR-YNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLV------ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 319 ddglftgydadkrqydktswhyeldengfakhdttlqhprcvwnllkqhvsrYTPDMVENICGTPKADFLKVCEYIAETs 398
Cdd:cd02750 260 ----------------------------------------------------YTPAWQEAITGVPRETVIRLAREFATN- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 499298135 399 akdKTASFLYALGWTQHSIGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02750 287 ---GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
887-1016 |
5.66e-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: 86.47 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlka 963
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRP--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499298135 964 dGkdidTIGIPIHWGYEGVAKKGfiANTLTPFVGDANTQTPEFKSFLVNVEKV 1016
Cdd:cd02791 77 -G----EVFVPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
887-1015 |
2.36e-19 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 84.60 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 887 DKFPYVGTTYRLTEHFHYWT---KHALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlka 963
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTmtrRAEGLDAIA-PEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPE--- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499298135 964 dgkdiDTIGIPIHWgYEGVakkgfiANTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02790 77 -----GVVFMPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
894-1010 |
1.06e-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: 82.32 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 894 TTYRLTEHFHYWTKHALLNAIAQPEQ-FVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdiDTIG 972
Cdd:pfam01568 4 ITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--------GVVF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 499298135 973 IPIHWGYEgvaKKGFIANTLTPFVGDANTQTPEFKSFL 1010
Cdd:pfam01568 76 MPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-104 |
1.37e-17 |
|
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: 77.29 E-value: 1.37e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499298135 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHS 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 |
1.24e-16 |
|
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: 74.64 E-value: 1.24e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499298135 43 TRETRNTCTYCSVGCGLLMYSlgdgaKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHS 104
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHV-----KDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-398 |
1.45e-16 |
|
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: 84.64 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 50 CTYCSVGCGLLMYSLGDGAknakasIFHIEGDPD----HPvSRGALCPKGAGLVDFIHSESRLKFPQYRA---------P 116
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHP-ARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 117 GsdkWQQISWEEAFDRI-AKL--MKEDRDANYQAQNAEGVTVNRWLTTGMLCASASSNETGYLTQKFSRALGMLAVDNQA 193
Cdd:cd02760 77 G---FVPISWDEALDLVaAKLrrVREKGLLDEKGLPRLAATFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQGVKCVHS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 194 RVUHGptvaslaptfgrGAMTNHWV---DIKNANLVVVMGGNA-AEAHPVGFRWAMEAKIHnGAKLIVIDPRFTRTASVA 269
Cdd:cd02760 154 EHLYG------------EFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVR-GYKRVQVEPHLSVTGACS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 270 DFYAPIRSGTDIAF---LSGVMLYLLTNEKYNREYTEAYTNASLIVRedfgfDDGLFTGYDADKRQ--YD-KTSWHYELD 343
Cdd:cd02760 221 AEWVPIRPKTDPAFmfaMIHVMVHEQGLGKLDVPFLRDRTSSPYLVG-----PDGLYLRDAATGKPlvWDeRSGRAVPFD 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499298135 344 ENGFAK----------------HDTTLQHP----RCVWNLLKQHVSRYTPDMVENICGTPKADFLKVC-EYIAETS 398
Cdd:cd02760 296 TRGAVPavagdfavdgavsvdaDDETAIHQgvegTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIArEFLENAS 371
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
49-239 |
8.12e-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: 75.12 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRapGSDKWQQISWEE 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 129 AFDRIAKLMKEDRDAnyqaqnAEGVTVNRwlttgmlcasaSSNETGYLTQKFSR-ALGMLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK------VGGIGSPR-----------ASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190
....*....|....*....|....*....|..
gi 499298135 208 FGRGAMTNHwvDIKNANLVVVMGGNAAEAHPV 239
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPR 162
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-287 |
1.01e-13 |
|
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: 74.24 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 50 CTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRapGSDKWQQISWEEA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 130 FDRIAKlmkedrdaNYQAQNAEGVTVnrwlttgmlCASA-SSNETGYLTQKFSRALGMLAVDNQARvuhGPTVASLAPTF 208
Cdd:cd02768 75 LKTVAE--------GLKAVKGDKIGG---------IAGPrADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 209 GRGAMTNHWVDIKNANLVVVMGGNAAEAHPVgfrwaMEAKI-----HNGAKLIVIDPRFTRTASVADFYApIRSGTDIAF 283
Cdd:cd02768 135 GNYLFNTSIAEIEEADAVLLIGSNLRKEAPL-----LNARLrkavkKKGAKIAVIGPKDTDLIADLTYPV-SPLGASLAT 208
|
....
gi 499298135 284 LSGV 287
Cdd:cd02768 209 LLDI 212
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
49-721 |
5.53e-11 |
|
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: 66.74 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMY---------------SLG----------DGAKNAKASI----------FHIEGDPDH--PVSRGAL 91
Cdd:cd02756 16 TCHFCIVGCGYHVYvwpvgeeggpspgqnAIGydlvdqvpplNLQWYPKTMHyvvvtqdgreVYIVIVPDKecPVNSGNY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 92 CPKGAGLVDFIHS------ESRLKFPQYRApgSDKWQQISWEEAFDRIAKLMKE--DRDANYQA--------QNAEGVTV 155
Cdd:cd02756 96 STRGGTNAERIWSpdnrvgETRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGilDKDGNDDAvfasrfdhGGGGGGFE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 156 NRWLTtGMLCASAssnetgyLTQKFSRalgmlaVDNqaRVUHGPTVASLAPTfGRGAMTNHWVDIKNANLVVVMGGNAAE 235
Cdd:cd02756 174 NNWGV-GKFFFMA-------LQTPFVR------IHN--RPAYNSEVHATREM-GVGELNNSYEDARLADTIVLWGNNPYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 236 AHPVGF-----------------RWAMEAKIHNGAKLIVIDPRFTRTASVADFYA--------PIRSGTDIAFLSGVMLY 290
Cdd:cd02756 237 TQTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgkdrvlhlQVNPGTDTALANAIARY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 291 LLtnEKYNREYTEAytnaslivredfgfddglftgydadkrqydktswhyeldengfakhdttlqhprcvwnllkqhvsr 370
Cdd:cd02756 317 IY--ESLDEVLAEA------------------------------------------------------------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 371 ytpdmvENICGTPKADFLKVCEYIAETSA--KDKTASFLYALG--WtqhsiGAQNIRTMAMI---QLLLGNMGMAGGGVN 443
Cdd:cd02756 329 ------EQITGVPRAQIEKAADWIAKPKEggYRKRVMFEYEKGiiW-----GNDNYRPIYSLvnlAIITGNIGRPGTGCV 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 444 ALRGHSniQGLTdlgllsqsLPGYltlPSEKQTDLQTYlAANTPKPLLKDQVNY---WGNYPkfFVSMMKAFFGDKATAE 520
Cdd:cd02756 398 RQGGHQ--EGYV--------RPPP---PPPPWYPQYQY-APYIDQLLISGKGKVlwvIGCDP--YKTTPNAQRLRETINH 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 521 NSWgfdwlpkwdkgydvlqyfemmkqgKVNGYICQGFNPVASfPNKNKVVASLSKLK----YLVTIDPLNTET------- 589
Cdd:cd02756 462 RSK------------------------LVTDAVEAALYAGTY-DREAMVCLIGDAIQpgglFIVVQDIYPTKLaedahvi 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 590 --STFWqnhGESNDVdpakiqtevfrlpstcfaeengSIVNSGRWLQWHWKGADAPGIAMTDGEILAGIFLRLRKMYSEQ 667
Cdd:cd02756 517 lpAAAN---GEMNET----------------------SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIYELYQEE 571
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499298135 668 GGAN--PEQVLNMTW-----NYTKPYEPASEEVAMES----NGKALADLIDPATGAVVVKKGQQL 721
Cdd:cd02756 572 GKGGsaQYQFFGFIWkteedNFMDGSQEFADGGEFSEdyyvLGQERYEGVTYNRLKAVGVNGIQL 636
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
104-260 |
1.09e-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: 65.07 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 104 SESRLKFPQYRAPGsdKWQQISWEEAFDRIAKLMKEDRDANYQAQnaegvtvnrwltTGMLCASASSNETGYLTQKFSRA 183
Cdd:cd02772 51 SEDRLTKPMIKKDG--QWQEVDWETALEYVAEGLSAIIKKHGADQ------------IGALASPHSTLEELYLLQKLARG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499298135 184 LGMLAVDNQARVUHGPTVASLAPTFGrgaMTNHWVDIKNANLVVVMGGNAAEAHP-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 ... |
5-286 |
2.28e-10 |
|
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: 64.43 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 5 RRQFFKICAGGMAGTTAAALG-----FAPGVALAETRQykLLRTRETRNTCTYCSVGCGLLMySLGDGAKnakasiFHIE 79
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRypvekIVPYVIWPENIV--PGETVYYATSLVPAGEGQGVLV-KTVDGRP------IKIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 80 GDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGSdKWQQISWEEAFDRIAKLMKEDRDanyqaqnAEGVTVnrwl 159
Cdd:cd02764 72 GNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDG-AYVASDWADFDAKVAEQLKAVKD-------GGKLAV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 160 ttgmlcasASSNETGYLTQKFSRALgmLAVDNQARVU-HGPTVASLAPTFGRGAMTNHWV---DIKNANLVVVMGGNAAE 235
Cdd:cd02764 140 --------LSGNVNSPTTEALIGDF--LKKYPGAKHVvYDPLSAEDVNEAWQASFGKDVVpgyDFDKAEVIVSIDADFLG 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499298135 236 AHPVGFRWA---MEAKIH----NGAKLIVIDPRFTRTASVADFYAPIRSGTDIAFLSG 286
Cdd:cd02764 210 SWISAIRHRhdfAAKRRLgaeePMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALG 267
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-306 |
2.18e-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: 61.51 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 79 EGDPDhPvsrgalCPKGAGLVDFIHSESRLKFPQYR-------------APGSDKWQQISWEEAFDRIAKLMKEDRDAnY 145
Cdd:cd02769 25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKT-Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 146 QAQNAEGVTVNrWLTTGMLCASASS-----NETG-YLTQKFSRALGMLAVDNqarvuhgPTVasLAPTFGRGAMTNHWVD 219
Cdd:cd02769 97 GNEAIFGGSYG-WSSAGRFHHAQSLlhrflNLAGgYVGSVGDYSTGAAQVIL-------PHV--VGSMEVYTEQQTSWPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 220 I-KNANLVVVMGGNA----------AEAHPVgfRWAMEAKIHNGAKLIVIDPRFTRTASVADF-YAPIRSGTDIAFLSGV 287
Cdd:cd02769 167 IaEHTELVVAFGADPlknaqiawggIPDHQA--YSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLAL 244
|
250
....*....|....*....
gi 499298135 288 MLYLLTNEKYNREYTEAYT 306
Cdd:cd02769 245 AHTLVTEGLHDKAFLARYT 263
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
889-984 |
8.89e-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: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 889 FPYVGTTYRLTEHFHYWTKHALLNAIaQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdi 968
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEI-KPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRP-------- 71
|
90
....*....|....*....
gi 499298135 969 DTIGIPI---HWGYEGVAK 984
Cdd:cd02780 72 GVVAIEHgygHWAYGAVAS 90
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-288 |
1.27e-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: 58.50 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 49 TCTYCSVGCGLLMYSLGDGAKNAkasifhiegdpdhpvSRGAlCPKGAGLvdFIHSESRLKFPQYRApgsdkwQQISWEE 128
Cdd:cd02761 3 VCPFCGLLCDDIEVEVEDNKITK---------------VRNA-CRIGAAK--FARYERRITTPRIDG------KPVSLEE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 129 AFDRIAKLMKEDRdanyqaqnaegvtvnRWLTTGMLCASASSNETGYLTQKFSRALgmlaVDNQARVUHGPTVASLAPtf 208
Cdd:cd02761 59 AIEKAAEILKEAK---------------RPLFYGLGTTVCEAQRAGIELAEKLGAI----IDHAASVCHGPNLLALQD-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 209 gRGAMTNHWVDIKN-ANLVVVMGGNAAEAHPVGFR---WAMEAKIHNGA----KLIVIDPRFTRTASVADFYAPIRSGTD 280
Cdd:cd02761 118 -SGWPTTTLGEVKNrADVIVYWGTNPMHAHPRHMSrysVFPRGFFREGGredrTLIVVDPRKSDTAKLADIHLQIDPGSD 196
|
....*...
gi 499298135 281 IAFLSGVM 288
Cdd:cd02761 197 YELLAALR 204
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-279 |
2.31e-08 |
|
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: 57.54 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 41 LRTRETrnTCTYCSVGCGLLMyslgdGAKNAKasIFHIEGDPDHPVSRGALCPKGAGLVDFIHSESRLKFPQYRAPGsdK 120
Cdd:COG1034 215 LKKTPS--ICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG--E 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 121 WQQISWEEAFDRIAKLMKEDRDanyqAQNAEGVTvnrwlttgMLCAsassnetgyltqkfsralgmlavdnqarvuhGPT 200
Cdd:COG1034 284 LVEASWEEALAAAAEGLKALKK----AENSVGAA--------LLGA-------------------------------LPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 201 VASLAPTFGRGAmtnhwvdiknANLVVVMGGNAAEAHPVgfrwAMEAKIHNGAKLIVIDPRFTRTASVADFYAPI----- 275
Cdd:COG1034 321 AAAILEAAEAGK----------LKALVLLGADPYDLDPA----AALAALAKADFVVVLDHFGSATAERADVVLPAaafae 386
|
....
gi 499298135 276 RSGT 279
Cdd:COG1034 387 KSGT 390
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
909-1015 |
1.02e-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: 51.51 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 909 ALLNAIAqPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIRTlkadgkdiDTIGIPIHWGYegVAKKGFI 988
Cdd:cd02778 21 PLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--------DTVFMPHGFGH--WAPALSR 89
|
90 100 110
....*....|....*....|....*....|....
gi 499298135 989 A-------NTLTPFVGDANTQTPEFKSFLVNVEK 1015
Cdd:cd02778 90 AygggvndNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
888-959 |
2.65e-07 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 50.44 E-value: 2.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499298135 888 KFPYVGTTY--RLTEHFHYWTKHALLnaIAQPEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02785 1 KYPLACIQRhsRFRVHSQFSNVPWLL--ELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
889-1015 |
5.98e-06 |
|
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: 46.53 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499298135 889 FPYVGTTYRLTEHFHywTKHALLNAIAQ--PEQFVEIGEKLANKLGIAHGDTVKVSSNRGYIKAKAVVTkrirtlkaDGK 966
Cdd:cd02781 3 PLILTTGARSYYYFH--SEHRQLPSLRElhPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLT--------PGI 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499298135 967 DIDTIGIPIHWGY--EGVAKKGFI------ANTLT------PFVGDANtqtpeFKSFLVNVEK 1015
Cdd:cd02781 73 RPGVVRAEHGWWYpeREAGEPALGgvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
928-959 |
1.34e-04 |
|
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 499298135 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 |
1.59e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 42.57 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|..
gi 499298135 928 ANKLGIAHGDTVKVSSNRGYIKAKAVVTKRIR 959
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIM 74
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