|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-1017 |
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: 1448.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 2 QVSRRQFFKLCAGGMAGTTIATLGFMPETALADTRSYKLLRATETRNTCPYCSVGCGILMYSLGDGAKNAKADIFHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 82 PDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSNEYKRISWDEAFERIAAHMKRDRDANFVEKNADGVTVNRWLTT 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 162 GFLAASASSNEAGWLTHKFTRSLGLLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 242 RWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAALLVNPDFKFDDG 321
Cdd:TIGR01553 241 KWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 322 LFSGYNADKHSYDKSTWTYQLDDKGMAKRDDSLSDPRCVINLMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETGAHD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 402 KTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDIGLLSTSLPGYLNMPSEKEPTLESY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 482 LSKYTSKPLADGQMNYWQNYPKFFVSLMKAMWGDKATADNQWGYDWLPKWDKSYD-VLQYFELMHQGKINGYFCQGFNPI 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDsWLTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 561 LAFPDKNKVVASLSKLKYLVIMDPLATDTSTFWKNHGeqndVKTAEIQTEVFRLPTTCFAEEDGAVVNSGRWLQWHWKGA 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 641 DAPGEAITDAEILAGIFTRLKAQYAKDGGKNAEAIMSLSWAYGDPHEPKPEELAKELNGKALADIPDPknpgQFLAKKGE 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDFKVG----DVEYKKGQ 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 721 QLSGFALLQADGSTASGCWIFAGSWTQAGNQMARRDNSDPSGLGNTLGWAWAWPANRRVLYNRASCKPDGTPWDKKRTLI 800
Cdd:TIGR01553 712 QIATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALV 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 801 KWNGEKWTGI-DVPDFKADEPPGSAMGPFIMQAEGLGRLFALDKMAEGPFPEHYEPFETPLGTNPLHPKVVSNPAARVFP 879
Cdd:TIGR01553 792 EWNAAEKKWVgDIPDYPPTAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYK 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 880 ADREQMGKHDAFPYAATTYRLTEHFHGWTKHARLNAIAQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKR 959
Cdd:TIGR01553 872 TDEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKR 951
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721247069 960 IRALQSGGKTVHQVGIPIHWGYEGVAKKGFSANTLTPFVGDANTQTPEFKSFLVNVEK 1017
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 ... |
47-876 |
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: 972.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 47 RNTCPYCSVGCGILMYSLGDgaknakaDIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSNEYKRISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNG-------VWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 127 DEAFERIAAHMKRDRDANFVEKNADGVTVNRWLTTGFLAASASSNEAGWLTHKFTRSLGLLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 207 TFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 287 VIRYLLqtgkynkeytlaytnaallvnpdfkfddglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvinlmre 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 367 hvaRYTPEMVETLCGTPKDAFLKVCEYLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 447 GHSNIQGLTDIGLLSTSLPGYLNmpsekeptlesylskytskpladgqmnywqnypkffvslmkamwgdkatadnqwgyd 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 527 wlpkwdksydvlqyfelmhqgkingyfcqGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTSTFWKNHGeqndVKTAE 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 607 IQTEVFRLPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRLKAQYAKDGGKNAEAIMslSWAYGDPH 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPIT--KWNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 687 EPKPEELAKELNGKALADIPDPKNPGQfLAKKGEQLSGFALLQADGSTASGCWIFAGSWTQAGNqMARRDNSDPSGLGNT 766
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYTGQSPER-LKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLY 542
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 767 LGWAWAWPANRRVLYNRASCKPDGTPWDKKRTLIKWNGEK-WTGIDVPDFKADEPPGSAMGPFIMQAEGLGRLFALDKma 845
Cdd:cd02752 543 PGWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGLGwWWKGDVPDGPWPAAKEHGCGPFIMAPEGQARLFVWNF-- 620
|
810 820 830
....*....|....*....|....*....|.
gi 1721247069 846 EGPFPEHYEPFETPLGTNplHPKVVSNPAAR 876
Cdd:cd02752 621 DGPFPEHYEPLESPRPDL--HSKVAKNPTYK 649
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
15-1015 |
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: 932.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 15 GMAGTTIATLGFMPETALADTrsykllratETRNTCPYCSVGCGILMYslgdgAKNAKadIFHIEGDPDHPVNRGALCPK 94
Cdd:NF041513 21 GAAARSARTRALRPRTATADR---------VVRSVCPYCAVGCGQKVY-----VKDEK--VVQIEGDPDSPISRGRLCPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 95 GAGLIDFIHSPNRLRYPEVREAGSNEYKRISWDEAFERIAAHMKRDRDANFVEKNADGVTVNRWLTTGFLAASASSNEAG 174
Cdd:NF041513 85 GSASLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEEN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 175 WLTHKFTRSLGLLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTRNkAK 254
Cdd:NF041513 165 YLIKKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAKARG-AT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 255 LIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAALLVNPDFKfD----DGLFSGYNADK 330
Cdd:NF041513 244 VIHVDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFR-DtedlDGLFSGFDPET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 331 HSYDKSTWTYQLDD----------------------------------KGMAKRDDSLSDPRCVINLMREHVARYTPEMV 376
Cdd:NF041513 323 GSYDPASWQYEGVEvaaaagqrdqlydsrggahesargeehgsggapvAGAPRRDETLQDPRCVFQILKRHFARYTPEMV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 377 ETLCGTPKDAFLKVCEYLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTD 456
Cdd:NF041513 403 EEICGIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 457 IGLLSTSLPGYLNMP-SEKEPTLESYLSKytskplADGQMNYWQNYPKFFVSLMKAMWGDKATADNQWGYDWLPKWDKSY 535
Cdd:NF041513 483 IPTLFNLLPGYLPMPhAHKHEDLDSYVEA------NASQKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDH 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 536 DVLQYFELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTSTFWKNHGE--QNDVKTAEIQTEVFR 613
Cdd:NF041513 557 STYQTVMAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEieTGELRTEDIGTEVFF 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 614 LPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRLKAQYAKDGGKNAEAIMSLSWAYG--DPH-EPKP 690
Cdd:NF041513 637 FPAAAHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLDLTWDYPteGPHgEPDA 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 691 EELAKELNGKALAdipdpknpgqflakkGEQLSGFALLQADGSTASGCWIFAGSWTQAGNQMARRDnsdPSGLGNTLG-- 768
Cdd:NF041513 717 EAVLAEINGYDLS---------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWVAae 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 769 WAWAWPANRRVLYNRASCKPDGTPWDKKRTLIKWNGEK--WTGIDVPDFKADEPPG-----SAMG--------PFIMQAE 833
Cdd:NF041513 779 WGWAWPANRRILYNRASADPEGRPWSERKKYVWWDAEAgrWTGYDVPDFPVDKPPDyrpppGATGpaalsgddPFIMQAD 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 834 GLGRLFALDKMAEGPFPEHYEPFETPLGtNPLHPKvVSNPAARVFPADREQMGKH------DAFPYAATTYRLTEHFHG- 906
Cdd:NF041513 859 GKGWLFAPAGLVDGPLPTHYEPQESPVR-NPLYGQ-QRNPARKVYPREDNRYHPSggepgaEVYPYVFTTYRLTEHHTAg 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 907 ----WTKH-ARLnaiaQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRALQSGGKTVHQVGIPIHWGY 981
Cdd:NF041513 937 gmsrWLPYlAEL----QPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGP 1012
|
1050 1060 1070
....*....|....*....|....*....|....
gi 1721247069 982 EGVAkKGFSANTLTPFVGDANTQTPEFKSFLVNV 1015
Cdd:NF041513 1013 NGLV-TGDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
44-1018 |
1.19e-148 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 458.19 E-value: 1.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 44 TETRNTCPYCSVGCGILMYSLGDGaknakadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGsnEYKR 123
Cdd:COG3383 5 KKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 124 ISWDEAFERIAAHMKRDRDanfvEKNADGVtvnrwlttGFLAASASSNEAGWLTHKFTRS-LGLLAVDNQARVUHGPTVA 202
Cdd:COG3383 76 VSWDEALDLVAERLREIQA----EHGPDAV--------AFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 203 SLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIA 282
Cdd:COG3383 144 GLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 283 FLSGVIRYLLQTGKYNKEYTLAYTNAallvnpdfkFDDglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvin 362
Cdd:COG3383 223 LLNGLLHVIIEEGLVDEDFIAERTEG---------FEE------------------------------------------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 363 lMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGV 442
Cdd:COG3383 252 -LKASVAKYTPERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 443 NALRGHSNIQGLTDIGLLSTSLPGYlnmpsekeptlesylskytsKPLADGQmnywqnypkffvslmkamwgDKATADNQ 522
Cdd:COG3383 327 FPLTGQNNVQGGRDMGALPNVLPGY--------------------RDVTDPE--------------------HRAKVADA 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 523 WGYDWLPKWdKSYDVLQYFELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTStfwknhgEQNDV 602
Cdd:COG3383 367 WGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETA-------EYADV 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 603 ktaeiqtevfRLPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRlkaqyakdggknaeaiMSLSWAY 682
Cdd:COG3383 439 ----------VLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARR----------------LGYGFDY 492
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 683 GDphepkPEELAKELngKALAdiPDpknpgqflakkgeqLSG--FALLQADGStasgcwifagswtqagnqmarrdnsdp 760
Cdd:COG3383 493 DS-----PEEVFDEI--ARLT--PD--------------YSGisYERLEALGG--------------------------- 522
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 761 sglgntlgwaWAWPANrrvlynrasckpdgtpwdkkrtlikwngekwtgidvpdfkADEPPGSAmgpfimqaeglgRLFA 840
Cdd:COG3383 523 ----------VQWPCP----------------------------------------SEDHPGTP------------RLFT 540
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 841 ldkmaegpfpehyEPFETPLGTNPLHPKVVSNPAARVfpaDREqmgkhdaFPYAATTYRLTEHFHGWTKHAR---LNAIA 917
Cdd:COG3383 541 -------------GRFPTPDGKARFVPVEYRPPAELP---DEE-------YPLVLTTGRLLDQWHTGTRTRRsprLNKHA 597
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 918 qPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRAlqsggktvHQVGIPIHWGYEGvakkgfsANTLTPF 997
Cdd:COG3383 598 -PEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTND 661
|
970 980
....*....|....*....|.
gi 1721247069 998 VGDANTQTPEFKSFLVNVEKV 1018
Cdd:COG3383 662 ALDPVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1009 |
4.24e-128 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 404.16 E-value: 4.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYslgdgAKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGsnEYKRISWDE 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD--KFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 129 AFERIAAHMKRDRDANFVEknadgvtvnrwlTTGFLAASASSNEAGWLTHKFTRS-LGLLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKEIKEKYGPD------------SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 208 FGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 288 IRYLLQTGKYNKEYtlaytnaallvnpdfkfddglfsgynadkhsydkstwtyqlddkgMAKRDDSLSDprcvinlMREH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAF---------------------------------------------IEKRTEGFEE-------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 368 VARYTPEMVETLCGTPKDAFLKvceyLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIRE----AARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 448 HSNIQGLTDIGLLSTSLPGYlnmpsekeptlesylskytsKPLADgqmnywQNYPKFFVSLmkamwgdkatadnqWGYDW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGY--------------------QPVSD------EEVREKFAKA--------------WGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 528 LPKwDKSYDVLQYFELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTSTFwknhgeqndvktaei 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 608 qTEVFrLPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRlkaqyakdggknaeaiMSLSWAYGDPHE 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANA----------------LGLDWNYNHPQE 489
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 688 PKPEelakelngkaladipdpknpgqflakkgeqlsgfallqadgsTASGCWIFAGswtqagnqMARRDNSDPSGLgntl 767
Cdd:TIGR01591 490 IMDE------------------------------------------IRELTPLFAG--------LTYERLDELGSL---- 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 768 gwawAWPANRRvlynrascKPDGTPWDKKrtlikwngekwTGIDVPDfkadeppgsamgpfimqaeGLGRLFALDKMAeg 847
Cdd:TIGR01591 516 ----QWPCNDS--------DASPTSYLYK-----------DKFATPD-------------------GKAKFIPLEWVA-- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 848 pfpehyePFETPlgtnplhpkvvsnpaarvfpadreqmgkHDAFPYAATTYRLTEHFHGWTKHARLNAIAQ--PEQFVEI 925
Cdd:TIGR01591 552 -------PIEEP----------------------------DDEYPLILTTGRVLTHYNVGEMTRRVAGLRRlsPEPYVEI 596
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 926 GEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqsGGKTVhqvgIPIHWGYEgvakkgfSANTLTPFVGDANTQT 1005
Cdd:TIGR01591 597 NTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVN----KGAIY----ITMHFWDG-------AVNNLTTDDLDPISGT 661
|
....
gi 1721247069 1006 PEFK 1009
Cdd:TIGR01591 662 PEYK 665
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1018 |
7.82e-127 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 400.76 E-value: 7.82e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 43 ATETRNTCPYCSVGCGILMYSLGDGAKnakadifHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR--EAGSNE 120
Cdd:COG0243 21 TKTVKTTCPGCGVGCGLGVKVEDGRVV-------RVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRvgPRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 121 YKRISWDEAFERIAAHMKRDRDanfvEKNADGVtvnrWLTTGFLAASASSNEAGWLTHKFTRSLGLLAVDNQARVUHGPT 200
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIID----EYGPEAV----AFYTSGGSAGRLSNEAAYLAQRFARALGTNNLDDNSRLCHESA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 201 VASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRTGTD 280
Cdd:COG0243 166 VAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 281 IAFLSGVIRYLLQTGKYNKEYTLAYTNAallvnpdfkFDDglfsgynadkhsydkstwtyqlddkgmakrddslsdprcv 360
Cdd:COG0243 246 AALLLALAHVLIEEGLYDRDFLARHTVG---------FDE---------------------------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 361 inlMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGG 440
Cdd:COG0243 277 ---LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 441 GVNALRGHSniqgltdigllstslpgylnmpsekeptlesylskytskpLADGqmnywQNYPkffvslMKAMWgdkatad 520
Cdd:COG0243 350 GPFSLTGEA----------------------------------------ILDG-----KPYP------IKALW------- 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 521 nqwgydwlpkwdksydvlqyfelmhqgkingyfCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTSTFwknhgeqN 600
Cdd:COG0243 372 ---------------------------------VYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY-------A 411
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 601 DVktaeiqtevfRLPTTCFAEEDGAVVNSG-RWLQWHWKGADAPGEAITDAEILAGIFTRLKAQYAKDGGKNAEAIMSLS 679
Cdd:COG0243 412 DI----------VLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLREL 481
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 680 WAYGDPHEPKPEELaKELNGKALADIPDPK--NPGQFlakkgeqlsgfallqadgSTASGcwifagswtqagnqmarrdn 757
Cdd:COG0243 482 LEATRGRGITFEEL-REKGPVQLPVPPEPAfrNDGPF------------------PTPSG-------------------- 522
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 758 sdpsglgntlgwawawpanrrvlynrasckpdgtpwdkkrtlikwngekwtgidvpdfKADeppgsamgpfimqaeglgr 837
Cdd:COG0243 523 ----------------------------------------------------------KAE------------------- 525
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 838 lFALDKMAEGPFPEHYEPFEtplGTNPLHPKvvsnpaarvfpadreqmgkhdaFPYAATTYRLTEHFHGWT-KHARLNAI 916
Cdd:COG0243 526 -FYSETLALPPLPRYAPPYE---GAEPLDAE----------------------YPLRLITGRSRDQWHSTTyNNPRLREI 579
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 917 aQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRAlqsggktvHQVGIPIHWGYEGVAKKGFSANTLTP 996
Cdd:COG0243 580 -GPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GVVFAPHGWWYEPADDKGGNVNVLTP 650
|
970 980
....*....|....*....|..
gi 1721247069 997 FVGDANTQTPEFKSFLVNVEKV 1018
Cdd:COG0243 651 DATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-687 |
1.22e-117 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 371.16 E-value: 1.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYSLGDgaknakaDIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGsnEYKRISWDE 128
Cdd:cd02753 3 VCPYCGVGCGLELWVKDN-------KIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 129 AFERIAAHMKRDRDANfvekNADGVtvnrwlttGFLAASASSNEAGWLTHKFTRSLGLL-AVDNQARVUHGPTVASLAPT 207
Cdd:cd02753 74 ALSLVASRLKEIKDKY----GPDAI--------AFFGSAKCTNEENYLFQKLARAVGGTnNVDHCARLCHSPTVAGLAET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 208 FGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGV 287
Cdd:cd02753 142 LGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAK-RNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 288 IRYLLQTGKYNKEYTLAYTNaallvnpdfkfddglfsGYNADkhsydkstwtyqlddkgmakrddslsdprcvinlmREH 367
Cdd:cd02753 221 AHVIIEEGLYDEEFIEERTE-----------------GFEEL-----------------------------------KEI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 368 VARYTPEMVETLCGTPKDAFLKVceylAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02753 249 VEKYTPEYAERITGVPAEDIREA----ARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 448 HSNIQGLTDIGLLSTSLPGYLnmpsekeptlesylskytskpladgqmnywqnypkffvslmKAMwgdkatadnqwgydw 527
Cdd:cd02753 325 QNNVQGACDMGALPNVLPGYV-----------------------------------------KAL--------------- 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 528 lpkwdksydvlqyfelmhqgkingyFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTstfwknhGEQNDVktaei 607
Cdd:cd02753 349 -------------------------YIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTET-------AELADV----- 391
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 608 qteVfrLPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRlkaqyakdggknaeaiMSLSWAYGDPHE 687
Cdd:cd02753 392 ---V--LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANR----------------LGYPGFYSHPEE 450
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-662 |
5.20e-88 |
|
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: 293.75 E-value: 5.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 47 RNTCPYCSVGCGILMYSLGDGAKNAKadifhieGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSnEYKRISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 127 DEAFERIAAHMKRDRDanfvEKNADGVTVnrwLTTGFLaasasSNEAGWLTHKFTRS-LGLLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFKAIQA----EYGPDSVAF---YGSGQL-----LTEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 206 PTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAK-TRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 285 SGVIRYLLQTGKYNKEYTLAYTNAallvnpdfkFDDglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvinlM 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTEG---------FEE-------------------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 365 REHVARYTPEMVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 445 LRGHSNIQGLTDIGLLSTSLPGYLNMPSEKeptlesylskytskpladgqmnywqnypkffvslmkamwgDKATADNQWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 525 --YDWLPKWdKSYDVLQYFELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLA-TDTSTFwknhgeqnd 601
Cdd:cd02754 365 vpEGTIPPK-PGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEY--------- 434
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721247069 602 vktAEIqtevfRLPTTCFAEEDGAVVNSGRWLQwHWKGA-DAPGEAITDAEILAGIFTRLKA 662
Cdd:cd02754 435 ---ADL-----VLPAASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRLGF 487
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-660 |
6.83e-85 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 278.83 E-value: 6.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 47 RNTCPYCSVGCGILMYSlgdgaKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSNEYKRISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 127 DEAFERIAAHMKRDRDANFVEKnadgvtvnrwltTGFLAASASSNEAGWLTHKFTRSLGLLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDA------------IAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 207 TFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 287 viryllqtgkynkeytlaytnaallvnpdfkfddglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvinlmre 366
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 367 hvarytpEMVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 220 -------EWAAEITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 447 ghsniqgltdigllstslpgylnmpsekeptlesylskytskpladgqmnywqnypkffvslmkamwgdkatadnqwgyd 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 527 wlpkwdksydvlqyfelmhqgkingyfcqGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTstfwknhGEQNDVktae 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTET-------AAYADV---- 326
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1721247069 607 iqtevfRLPTTCFAEEDGAVVNSGRWLQWHWKGADAPGEAITDAEILAGIFTRL 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 ... |
891-1017 |
8.74e-56 |
|
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: 188.59 E-value: 8.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 891 FPYAATTYRLTEHFHGW--TKHARLNAIAQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqsggk 968
Cdd:cd02792 3 FPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK------- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1721247069 969 tVHQVGIPIHWGYEGVAkKGFSANTLTPFVGDANTQTPEFKSFLVNVEK 1017
Cdd:cd02792 76 -PHEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
1.81e-46 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 173.64 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 48 NTCPYCSVGCGILMYslgdgAKNAKAdiFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR--EAGSNEYKRIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGRV--VKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRvgERGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 126 WDEAFERIAAHMKRDRDANFVEKNA--DGVTVNRWLTTGFLAASASSNeagWLTHkftrslgllavdnqARVUHGP-TVA 202
Cdd:cd02755 76 WDEALQYIASKLKEIKEQHGPESVLfgGHGGCYSPFFKHFAAAFGSPN---IFSH--------------ESTCLASkNLA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 203 SLAPTFGRGAMTNhwVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIA 282
Cdd:cd02755 139 WKLVIDSFGGEVN--PDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 283 FLSGVIRYLLQTGKYNKEYTLAYTNAallvnpdfkFDdglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvin 362
Cdd:cd02755 217 FVLALIHVLISENLYDAAFVEKYTNG---------FE------------------------------------------- 244
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721247069 363 LMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETGAHDKTTSFLYALgWTQHSIgsQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02755 245 LLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGT-FYSNSF--QTRRAIAIINALLGNIDKRGG 319
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-661 |
2.26e-46 |
|
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: 175.96 E-value: 2.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 107 RLRYPEVREAGSNEYKRISWDEAFERIAAHMKRDRDanfveknadgvtvNRwltTGFLAASASSNEAGWLTHKFTRSLGL 186
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRALDP-------------DR---AAFYTSGRASNEAAYLYQLFARAYGT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDP------ 260
Cdd:cd02767 128 NNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlrepgl 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 261 -RF----------TRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEytlaytnaalLVNPDFkfddglfsgynAD 329
Cdd:cd02767 207 eRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERDDEPGN----------VLDHDF-----------IA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 330 KHsydkstwTYQLDDkgmakrddslsdprcvinlMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYA 409
Cdd:cd02767 266 EH-------TSGFEE-------------------YVAALRALSWDEIERASGLSREEIEAFAAMYAKS----ERVVFVWG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 410 LGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGltdigllstslpgylnmpsekeptlesylskytskp 489
Cdd:cd02767 316 MGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQG------------------------------------ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 490 laDGQMNYWqnyPKFFVSLMKAMwgdkataDNQWGYDwLPKWdKSYDVLQYFELMHQGKINGYFCQGFNPILAFPDKNKV 569
Cdd:cd02767 360 --DRTMGIT---EKPFPEFLDAL-------EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAAT 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 570 VASLSKLKYLVIMDpLATDTSTFWknHGEQN-----------DVKTAEIQTEVFRLPTTCFAEEDGAVVNSGRWLQ---- 634
Cdd:cd02767 426 EEALRRLDLTVHVA-TKLNRSHLV--HGEEAlilpclgrteiDMQAGGAQAVTVEDSMSMTHTSRGRLKPASRVLLseea 502
|
570 580
....*....|....*....|....*...
gi 1721247069 635 -WHWKGADAPGEAITDAEILAGIFTRLK 661
Cdd:cd02767 503 iVAGIAGARLGEAKPEWEILVEDYDRIR 530
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-454 |
1.86e-45 |
|
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: 171.66 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 47 RNTCPY-CSVGCGILMYSLGDGAKNakadifhIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR-EAGSNEYKRI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRvGRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 125 SWDEAFERIAAHMKRDRDanfvEKNADGVTVNRWL-TTGFLAASAssneagwlTHKFTRSLGLLAVDNQarVUHGPTVAS 203
Cdd:cd02766 74 SWDEALDTIAAKLKEIKA----EYGPESILPYSYAgTMGLLQRAA--------RGRFFHALGASELRGT--ICSGAGIEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 204 LAPTFGRgAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAF 283
Cdd:cd02766 140 QKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGTDGAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 284 LSGVIRYLLQTGKYNKEYTLAYTNaallvnpdfkfddglfsGYNAdkhsydkstwtyqlddkgmakrddslsdprcvinl 363
Cdd:cd02766 218 ALGVAKVLFREGLYDRDFLARHTE-----------------GFEE----------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 364 MREHVARYTPEMVETLCGTPKDAFlkvcEYLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVN 443
Cdd:cd02766 246 LKAHLETYTPEWAAEITGVSAEEI----EELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGAF 321
|
410
....*....|.
gi 1721247069 444 ALRGHSNIQGL 454
Cdd:cd02766 322 YSNSGPPVKAL 332
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
1.05e-43 |
|
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: 165.94 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYslgdgAKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYP--EVREAGSNEYKRISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPlkRVGERGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 127 DEAFERIAAHMKRDRDanfvEKNADGVTVnrWLTTGFLAASASSNEAGWLTHKFTRSLGLLAVDnqarVUHGPT-VASLA 205
Cdd:cd02759 76 DEALDEIAEKLAEIKA----EYGPESIAT--AVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGE----SCYWPRdMAHAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 206 PTFGRGAMTNHwvDIKNANLIVVMGGNAAEAHPVGF-RWAIEAKTRNkAKLIVIDPRFTRTASVADYYAPIRTGTDIAFL 284
Cdd:cd02759 146 TTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQgHWLVAAMKRG-AKLIVVDPRLTWLAARADLWLPIRPGTDAALA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 285 SGVIRYLLQTGKYNKEYTlaytnaallvnpdfkfddglfsgYNadkhsydkstWTYQLDDkgmakrddslsdprcvinlM 364
Cdd:cd02759 223 LGMLNVIINEGLYDKDFV-----------------------EN----------WCYGFEE-------------------L 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 365 REHVARYTPEMVETLCGTPKDAFLKVCEYLAetgahdktTSFLYALGWT---QHSI-GSQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02759 251 AERVQEYTPEKVAEITGVPAEKIRKAARLYA--------TAKPACIQWGlaiDQQKnGTQTSRAIAILRAITGNLDVPGG 322
|
....
gi 1721247069 441 GVNA 444
Cdd:cd02759 323 NLLI 326
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
889-1017 |
8.97e-43 |
|
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: 151.51 E-value: 8.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 889 DAFPYAATTYRLTEHFHGW--TKHARLNAIAQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqsg 966
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1721247069 967 gktVHQVGIPIHWGYEGvakKGFSANTLTPFVGDANTQTPEFKSFLVNVEK 1017
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-599 |
3.10e-41 |
|
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: 163.06 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 107 RLRYPEVREAGSNEYKRISWDEAFERIAAHMKrDRDANFVEknadgvtvnrwlttgFLAASASSNEAGWLTHKFTRSLGL 186
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIAAKLN-SLDPKQVA---------------FYTSGRTSNEAAYLYQLFARSLGS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTRNkAKLIVIDP------ 260
Cdd:TIGR01701 163 NNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRG-AKIIAINPlrergl 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 261 -RFTRTAS-----------VADYYAPIRTGTDIAFLSGVIRYLLQTGKYNK------EYTLAYTNAallvnpdfkfddgl 322
Cdd:TIGR01701 242 eRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDAQPgslidhEFIANHTNG-------------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 323 FSGYnadkhsydkstwtyqlddkgmakrddslsdprcvinlmREHVARYTPEMVETLCGTPKDAFLKVceylAETGAHDK 402
Cdd:TIGR01701 308 FDEL--------------------------------------RRHVLQLNWNDIERSSGLSQEEILEF----AKLLANSR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 403 TTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGltdigllstslpgylnmpsekeptlesyl 482
Cdd:TIGR01701 346 RVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQG----------------------------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 483 skytskplaDGQMNYWQNYPKFFvslmkamwgdKATADNQWGYDwLPKWdKSYDVLQYFELMHQGKINGYFCQGFNPILA 562
Cdd:TIGR01701 397 ---------DRTMGITEKPEEEF----------LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNFLEA 455
|
490 500 510
....*....|....*....|....*....|....*..
gi 1721247069 563 FPDKNKVVASLSKLKYLVimdPLATDTSTFWKNHGEQ 599
Cdd:TIGR01701 456 MPDTAAIERALRQLDLRV---HVATKLNRSHVLAKEE 489
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
49-440 |
2.78e-37 |
|
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: 147.97 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYSLGDGAKNakadifhIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR------EAGSNEYK 122
Cdd:cd02757 5 TCQGCTAWCGLQAYVEDGRVTK-------VEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRtnprkgRDVDPKFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 123 RISWDEAFERIAAHMKRDRDANfvEKNADGVTVNRWLTTGFLaasassneagwLTHKFTRSLGLLAVDNQARVUhgptva 202
Cdd:cd02757 78 PISWDEALDTIADKIRALRKEN--EPHKIMLHRGRYGHNNSI-----------LYGRFTKMIGSPNNISHSSVC------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 203 SLAPTFGRGAMTNHW----VDIKNANLIVVMGGNAAEA-HPVGFRWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRT 277
Cdd:cd02757 139 AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 278 GTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAALLVNPDFKFDDGLFSgynaDKHSYDKSTWtyqlddkgmakrddslsdp 357
Cdd:cd02757 219 GEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGETVDEESFK----EKSTEGLVKW------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 358 rcvinlMREHVARYTPEMVETLCGTPKDAFLKVCEYLAETGAhdKTTSFLYAlGWTQHSIGSQNIRTMAMIQLLLGNMGM 437
Cdd:cd02757 276 ------WNLELKDYTPEWAAKISGIPAETIERVAREFATAAP--AAAAFTWR-GATMQNRGSYNSMACHALNGLVGSIDS 346
|
...
gi 1721247069 438 AGG 440
Cdd:cd02757 347 KGG 349
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
82-453 |
2.90e-36 |
|
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: 145.70 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 82 PDHPVNRGalCPKGAGLIDFIHSPNRLRYPEVR--EAGSNEYKRISWDEAFERIAAHMKRDRDanfveknadgvtvnRWL 159
Cdd:cd02765 32 PDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRvgERGEGKFERITWDEALDTIADKLTEAKR--------------EYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 160 TTGFLAASASSNEA--GWLTHKFtrSLGLLAVDNQARVUHGPTVA-SLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEA 236
Cdd:cd02765 96 GKSILWMSSSGDGAilSYLRLAL--LGGGLQDALTYGIDTGVGQGfNRVTGGGFMPPTNEITDWVNAKTIIIWGSNILET 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 237 HPVGFRWAIEAKtRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAALLVnpdf 316
Cdd:cd02765 174 QFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLKSNTSAPFLV---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 317 KFDDGLF-----SGYNADKHSY---DKSTWTYQ-LDDKGM--AKRDDSLSDP---RCVINLMREHVARYTPEMVETLCGT 382
Cdd:cd02765 249 REDNGTLlrqadVTATPAEDGYvvwDTNSDSPEpVAATNInpALEGEYTINGvkvHTVLTALREQAASYPPKAAAEICGL 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721247069 383 PKDAFLKVCEYLAETGAhdkttSFLYALGWTQHSIGSQNI-RTMAMIQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 329 EEAIIETLAEWYATGKP-----SGIWGFGGVDRYYHSHVFgRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-662 |
5.36e-35 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 141.38 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYSlgDGAKNAKadifhIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSneYKRISWDE 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 129 AFERIAAHMK--RDRDAN----FVEKNADGVTVNRWLTTG-FLAASASSNeagwlthKFTRSLgllaVDNQarvuhgPTV 201
Cdd:cd02762 74 AFDEIAERLRaiRARHGGdavgVYGGNPQAHTHAGGAYSPaLLKALGTSN-------YFSAAT----ADQK------PGH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 202 ASLAPTFGRGaMTNHWVDIKNANLIVVMGGNAAEAHpvGFRWAI-EAKTRNKA------KLIVIDPRFTRTASVADYYAP 274
Cdd:cd02762 137 FWSGLMFGHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTApDRVLRLKAakdrggSLVVIDPRRTETAKLADEHLF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 275 IRTGTDIAFLSGVIRYLLQtgkynkeytlaytnaallvnpdfkfdDGLFsgynadkhsydkstwtyqlDDKGMAKRDDSL 354
Cdd:cd02762 214 VRPGTDAWLLAAMLAVLLA--------------------------EGLT-------------------DRRFLAEHCDGL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 355 SDprcvinlMREHVARYTPEMVETLCGTPKDaflkVCEYLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGN 434
Cdd:cd02762 249 DE-------VRAALAEFTPEAYAPRCGVPAE----TIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGN 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 435 MGMAGGgvnalrghsniqgltdiGLLSTSLPGYLNMPSEKEPTLESYLSKYTSKPLADGQmnywqnYPkffVSlmkamwg 514
Cdd:cd02762 318 LDRPGG-----------------AMFTTPALDLVGQTSGRTIGRGEWRSRVSGLPEIAGE------LP---VN------- 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 515 dkATADNqwgydwlpkwdksydvlqyFELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTStfwk 594
Cdd:cd02762 365 --VLAEE-------------------ILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETT---- 419
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721247069 595 NHGEQNDVKTAEIQTEVFrlpTTCFAEedgAVVNSGRWLQwhwKGADAPGEAITDAEILAGIFTRLKA 662
Cdd:cd02762 420 RHADYILPPASQLEKPHA---TFFNLE---FPRNAFRYRR---PLFPPPPGTLPEWEILARLVEALDA 478
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
4.12e-32 |
|
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: 134.19 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMYsLGDGaknakaDIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR--EAGSNEYKRISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDG------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRkgPRGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 127 DEAFErIAAhmkrDRDANFVEKNADGVTVnrwlttgFLAASASSNEAGWLTHKFtrslGLLAVDNQARVUHGPTVASLAP 206
Cdd:cd02763 76 EEAFS-IAT----KRLKAARATDPKKFAF-------FTGRDQMQALTGWFAGQF----GTPNYAAHGGFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 207 TFGRGAMTNHWVDIKNANLIvVMGGNAAEAHPVGFRWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSG 286
Cdd:cd02763 140 SIGGSFWEFGGPDLEHTKYF-MMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 287 VIRYLLQTGKYNKEYTLAYTNAALLVNpdfkfddglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvinlmre 366
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTNAAELVD----------------------------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 367 hvarYTPEMVETLCGTPKDAFLKVCEYLAETG-----------------AHDKTT----SFLYALGWTQHSIGSQNIRTM 425
Cdd:cd02763 246 ----YTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrKHEKITgrpvSFHAMRGIAAHSNGFQTIRAL 321
|
410
....*....|....*
gi 1721247069 426 AMIQLLLGNMGMAGG 440
Cdd:cd02763 322 FVLMMLLGTIDRPGG 336
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-459 |
1.14e-29 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 126.70 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 102 IHSPNRLRYPEVREAGSNEYKRISWDEAFERIAAHMKRDRDANFVEknadgvtvnrwlttgFLAASASSNEAGWLTHKFT 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVE---------------FYTSGRTSNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 182 RSLGLLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRwAIEAKTRNKAKLIVIDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 261 ------RFT-----------RTASVADYYAPIRTGTDIAFLSGVIRYLLQtgkyNKEYTLAYTNAALLvnpDFKFDDGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIE----RDDAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 324 SGYNADKHSYDKSTWtyqlddkgmakrddslSDPRCVINLMREHVARYTpemvetlcgtpkDAFlkvceylaetgAHDKT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEW----------------KDIERISGLSQTQIAELA------------DAY-----------AAAER 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721247069 404 TSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDIGL 459
Cdd:PRK09939 361 TIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI 416
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
4.66e-29 |
|
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: 123.97 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 79 EGDPDHPVNRGalCPKGAGLIDFIHSPNRLRYP--EVREAGSNEYKRISWDEAFERIAAHMKR----------------- 139
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPmkRVGKRGEGKFVRISWDEALDTIASELKRiiekygneaiyvnygtg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 140 DRDANFVEKNADGVTVNrwLTTGFLAASASSNEAGWLThkftrslgllavdnqarvuhgptvaSLAPTFGRGAMTNHWVD 219
Cdd:cd02770 111 TYGGVPAGRGAIARLLN--LTGGYLNYYGTYSWAQITT-------------------------ATPYTYGAAASGSSLDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 220 IKNANLIVVMGGNAAEAHPVGFR---WAIEAKtRNKAKLIVIDPRFTRTASV-ADYYAPIRTGTDIAFLSGVIRYLLqtg 295
Cdd:cd02770 164 LKDSKLVVLFGHNPAETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMI--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 296 kynkeyTLAYTNAALLVNPDFKFD-DGLFSGYNADKHSYDkstwtYqlddkgmakrddslsdprcVINLMREHVARyTPE 374
Cdd:cd02770 240 ------TENLHDQAFLDRYCVGFDaEHLPEGAPPNESYKD-----Y-------------------VLGTGYDGTPK-TPE 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721247069 375 MVETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 289 WASEITGVPAETIRRLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-480 |
3.45e-28 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 122.44 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 2 QVSRRQFFKLCA-GGMAGTTIA-TLGFMPETALADTRSYKllRATEtRNTCPYCSVGCGI---LMYSLGDGAknakadIF 76
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAMASSAlTLPFSRIAHAVDSAIPT--KSDE-KVIWSACTVNCGSrcpLRMHVVDGE------IK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 77 HIEGDPDHPVNRGAL-----CPKGAGLIDFIHSPNRLRYP--EVREAGSNEYKRISWDEAFERIAAHMKR--------DR 141
Cdd:PRK14990 84 YVETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPmkRVGARGEGKFERISWEEAYDIIATNMQRlikeygneSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 142 DANFVEKNADGVTVNRWLTTGFLAASASSNEAGWLTHKFTRSLGLLAvdnqarvuhgptvASLAPTFGRGAMTNHWVDIK 221
Cdd:PRK14990 164 YLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA-------------EGLNYTYGGWADGNSPSDIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 222 NANLIVVMGGNAAEAHPVG---FRWAIEAKTRNKAKLIVIDPRFTRT-ASVADYYAPIRTGTDIAFLSGViryllqtgky 297
Cdd:PRK14990 231 NSKLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGL---------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 298 nkEYTLAYTNaalLVNPDFkfddglfsgynADKH--SYDKSTWTYQLDDKGMAKrddslsdpRCVINLMREHVARyTPEM 375
Cdd:PRK14990 301 --AYVMITEN---LVDQPF-----------LDKYcvGYDEKTLPASAPKNGHYK--------AYILGEGPDGVAK-TPEW 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 376 VETLCGTPKDAFLKVCEYLAETgahdKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGhsniqglt 455
Cdd:PRK14990 356 ASQITGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG-------- 423
|
490 500
....*....|....*....|....*
gi 1721247069 456 digllSTSLPgYLNMPSEKEPTLES 480
Cdd:PRK14990 424 -----SYSLP-FVRMPTLENPIQTS 442
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
46-447 |
6.02e-27 |
|
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: 115.49 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 46 TRNTC-PYCSVGCGILMYsLGDG---AKNAKADIFHIEGD-PDH-PvnRGalCPKGAGLIDFIHSPNRLRYPEVR--EAG 117
Cdd:cd02750 4 VRSTHgVNCTGSCSWNVY-VKNGivtREEQATDYPETPPDlPDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRvgARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 118 SNEYKRISWDEAFERIAAHMKRdrdaNFVEKNADGVTvnrwLTTGFLAASASSNEAGwltHKFTRSLGLLAVDNQARVUH 197
Cdd:cd02750 79 EGKWKRISWDEALELIADAIID----TIKKYGPDRVI----GFSPIPAMSMVSYAAG---SRFASLIGGVSLSFYDWYGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 198 GPTVASLapTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGFRWAIEAKTrNKAKLIVIDPRFTRTASVADYYAPIRT 277
Cdd:cd02750 148 LPPGSPQ--TWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARY-NGAKVVVVSPDYSPSAKHADLWVPIKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 278 GTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAALLVnpdfkfddglfsgynadkhsydkstwtyqlddkgmakrddslsdp 357
Cdd:cd02750 225 GTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLV--------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 358 rcvinlmrehvarYTPEMVETLCGTPKDAFLKVCEYLAETGAhdktTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGM 437
Cdd:cd02750 260 -------------YTPAWQEAITGVPRETVIRLAREFATNGR----SMIIVGAGINHWYHGDLCYRALILLLALTGNEGK 322
|
410
....*....|
gi 1721247069 438 AGGGVNALRG 447
Cdd:cd02750 323 NGGGWAHYVG 332
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-592 |
1.45e-26 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 117.08 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 1 MQVSRRQFFKLCAGGMAGTTIA-----TLGFMPETALADTrsykllrATETRNTCPYCSVGCGILMYSLGDgaKNakadI 75
Cdd:PRK15488 1 MSLSRRDFLKGAGAGCAACALGsllpgALAANEIAQLKGK-------TKLTPSICEMCSTRCPIEARVVNG--KN----V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 76 FhIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVR--EAGSNEYKRISWDEAFERIAAHMKRDRDanfvEKNADGV 153
Cdd:PRK15488 68 F-IQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLNAIKQ----QHGPESV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 154 TVnrwlttgflaASASSNEAGWLTHkFTRSLGLLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANLIVVMGGNA 233
Cdd:PRK15488 143 AF----------SSKSGSLSSHLFH-LATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 234 AEAHPVGF-RWAIEAKTRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYTLAYTNAallv 312
Cdd:PRK15488 208 YEGINMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSG---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 313 npdfkFDDglfsgynadkhsydkstwtyqlddkgmakrddslsdprcvinlMREHVARYTPEMVETLCGTPKDAFLKVCE 392
Cdd:PRK15488 284 -----FEE-------------------------------------------LAASVKEYTPEWAEAISDVPADDIRRIAR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 393 YLAETGAHdKTTSFLYALGWTQHSIgsQNIRTMAMIQLLLGNMGMAGG--------GVNALRGHSNIQGLTDigllstsl 464
Cdd:PRK15488 316 ELAAAAPH-AIVDFGHRATFTPEEF--DMRRAIFAANVLLGNIERKGGlyfgknasVYNKLAGEKVAPTLAK-------- 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 465 PGYLNMPSEKEPTLEsylskytskpLADgqmnywqnyPKFFvsLMKAMWG-----DKATADnqwgydwlpkwDKSYdvlq 539
Cdd:PRK15488 385 PGVKGMPKPTAKRID----------LVG---------EQFK--YIAAGGGvvqsiIDATLT-----------QKPY---- 428
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1721247069 540 yfelmhqgKINGYFCQGFNPILAFPDKNKVVASLSKLKYLVIMDPLATDTSTF 592
Cdd:PRK15488 429 --------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAY 473
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
2.18e-26 |
|
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: 116.29 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILmyslgdgAK--NAKADIFHIEGDPDHPVN---------------------------RGALCPKGAGLI 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 100 DFIHSPNRLRYPEVREA--GSNEYKRISWDEAFERIA--------AHMKRDRDANFVEKNAD------GVTVNRWLTTGf 163
Cdd:cd02758 76 QYLYDPYRVLQPLKRVGprGSGKWKPISWEQLIEEVVeggdlfgeGHVEGLKAIRDLDTPIDpdhpdlGPKANQLLYTF- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 164 laasaSSNE--AGWLTHKFTRSLGLLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANLIVVMGGNAAEAHPvG 240
Cdd:cd02758 155 -----GRDEgrTPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 241 FRWA----IEAKTRNKAKLIVIDPRFTRTASVAD---YYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYtLAYTNAAllvn 313
Cdd:cd02758 229 FKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEY-LSIPSKE---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 314 pdfkfddglfSGYNADKHSYDKSTWTYQlddkgMAKRDDSLSdprcvinLMREHVARYTPEMVETLCGTPKDaflKVCEY 393
Cdd:cd02758 304 ----------AAKAAGEPSWTNATHLVI-----TVRVKSALQ-------LLKEEAFSYSLEEYAEICGVPEA---KIIEL 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1721247069 394 LAETGAHDKTTSFLYAlGWTQHSIGSQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02758 359 AKEFTSHGRAAAVVHH-GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-653 |
1.87e-25 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 109.41 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 107 RLRYPEVREaGSNEYKRISWDEAFERIAAHMKRDRDanfvEKNADGVTVNrwlttgFLAASASSNEAGWLTHKFTRSLG- 185
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIK----KYGPDAIAIN------GGSGGLTDVESLYALKKLLNRLGs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 186 --LLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIVVMGGNAAEAHPVGfrWAIEAKT--RNKAKLIVIDPR 261
Cdd:pfam00384 70 knGNTEDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIL--NARIRKAalKGKAKVIVIGPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 262 FTRTasVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEYTlayTNAALLVnpdfkfddglfsgynadkhsydkstwtyq 341
Cdd:pfam00384 148 LDLT--YADEHLGIKPGTDLALALAGAHVFIKELKKDKDFA---PKPIIIV----------------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 342 lddkGMakrddslsdprcvinlmrehvarytpemvetlcgtpkdaflkvceylaetgahdkttsflyalGWTQHSIGSQN 421
Cdd:pfam00384 194 ----GA---------------------------------------------------------------GVLQRQDGEAI 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 422 IRTMAMIQLLLGNMGMAGGGVNALR---GHSNIQGLTDIGLLStslpgylnmpsekeptlesylskytskpladgqmnyw 498
Cdd:pfam00384 207 FRAIANLADLTGNIGRPGGGWNGLNilqGAASPVGALDLGLVP------------------------------------- 249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 499 qnyPKFFVSLMkamwgdkatadnqwgydwlpkwdksydvlqyfELMHQGKINGYFCQGFNPILAFPDKNKVVASLSKLKY 578
Cdd:pfam00384 250 ---GIKSVEMI--------------------------------NAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDL 294
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721247069 579 LVIMDPlatdtstFWKNHGEQN-DVktaeiqtevfRLPTTCFAEEDGAVVNSGRWLQwHWKGA-DAPGEAITDAEIL 653
Cdd:pfam00384 295 FVVYDG-------HHGDKTAKYaDV----------ILPAAAYTEKNGTYVNTEGRVQ-STKQAvPPPGEAREDWKIL 353
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
900-1009 |
7.24e-25 |
|
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: 99.70 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 900 LTEHFHGW--TKHARLNAIaQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqsggktVHQVGIPI 977
Cdd:cd02775 1 LRDHFHSGtrTRNPWLREL-APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVP--------PGVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 1721247069 978 HWGYEGvaKKGFSANTLTPFVGDANTQTPEFK 1009
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
3.67e-24 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 108.47 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 92 CPKGAGLIDFIHSPNRLRYPEVREA------------GSNEYKRISWDEAFERIAAHMKRDRDAnfveknadgvtvnrwl 159
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsrelrGEGEFVRISWDEALDLVASELKRIREK---------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 160 ttgFLAASASSNEAGWLTHK-FTRSLGLLavdnqARV--UHGPTVASLAP---------------TFGRGAMTNHWVDI- 220
Cdd:cd02751 96 ---YGNEAIFGGSYGWASAGrLHHAQSLL-----HRFlnLIGGYLGSYGTystgaaqvilphvvgSDEVYEQGTSWDDIa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 221 KNANLIVVMGGNAAE---------AHPVGFRWAiEAKtRNKAKLIVIDPRFTRTAS-VADYYAPIRTGTDIAFLSGVIRY 290
Cdd:cd02751 168 EHSDLVVLFGANPLKtrqgggggpDHGSYYYLK-QAK-DAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 291 LLQTGKYNKEYTLAYTnaallvnpdfkfddglfSGYNADKhsydkstwTYQL--DDkGMAKrddslsdprcvinlmrehv 368
Cdd:cd02751 246 LITEDLHDQAFLARYT-----------------VGFDEFK--------DYLLgeSD-GVPK------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 369 aryTPEMVETLCGTPKDAFLKvceyLAETGAhDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRGH 448
Cdd:cd02751 281 ---TPEWAAEITGVPAETIRA----LAREIA-SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGY 352
|
410
....*....|....*..
gi 1721247069 449 SNIQGLTDIGLLSTSLP 465
Cdd:cd02751 353 SNGGGPPRGGAGGPGLP 369
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
889-1018 |
3.28e-22 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 93.02 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 889 DAFPYAATTYRLTEHFHGWT---KHARLNAIAqPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqS 965
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVR---P 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1721247069 966 GgktvhQVGIPIHWGYEGVAKKGfsANTLTPFVGDANTQTPEFKSFLVNVEKV 1018
Cdd:cd02791 77 G-----EVFVPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-447 |
8.26e-21 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 98.43 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 1 MQVSRRQFFK----LCAGGMAGTTI-ATLGFMPETALADTRSYKllratetrNTCPYCSVGCGILMyslgdGAKNAKadI 75
Cdd:PRK13532 1 MKLSRRDFMKanaaAAAAAAAGLSLpAVANAVVGSAQTAIKWDK--------APCRFCGTGCGVLV-----GTKDGR--V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 76 FHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAG-----SNEYKRISWDEAFERIAAHMKRdrdaNFVEKNA 150
Cdd:PRK13532 66 VATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMKDgkydkEGEFTPVSWDQAFDVMAEKFKK----ALKEKGP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 151 DGVTV---NRW-LTTGFlaASASSNEAGWLTHkftrslgllAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLI 226
Cdd:PRK13532 142 TAVGMfgsGQWtIWEGY--AASKLMKAGFRSN---------NIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 227 VVMGGNAAEAHPVgfRWAIEAKTR---NKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEY-- 301
Cdd:PRK13532 211 VLWGSNMAEMHPI--LWSRVTDRRlsnPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFvn 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 302 -----TLAYTNAALLVNPDFKFDDGLFSGYNADKHsydkstWTYQLDDkgmakrddslsdprcvinlMREHVARYTPEMV 376
Cdd:PRK13532 289 khtnfRKGATDIGYGLRPTHPLEKAAKNPGTAGKS------EPISFEE-------------------FKKFVAPYTLEKT 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721247069 377 ETLCGTPKDAFLKVCEYLAETGAhdKTTSFlYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK13532 344 AKMSGVPKEQLEQLAKLYADPNR--KVVSF-WTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTG 411
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-396 |
2.35e-20 |
|
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: 96.96 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 50 CPYCSVGCGILMYSLGDGAknakadIFHIEGDPD----HPVnRGALCPKGAGLIDFIHSPNRLRYPEVR---EAGSNE-- 120
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRtnpKKGRNEdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 121 -YKRISWDEAFERIAAHMKRDRDANFVEKNA---DGVTVNRWLTTGFLAASASSNEAGWLTHKFTRSLGLLAVDNQARVU 196
Cdd:cd02760 77 gFVPISWDEALDLVAAKLRRVREKGLLDEKGlprLAATFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQGVKCVHSEHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 197 HGptvaslaptfgrGAMTNHWV---DIKNANLIVVMGGNA-AEAHPVGFRWAIEAKTRNkAKLIVIDPRFTRTASVADYY 272
Cdd:cd02760 157 YG------------EFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVRG-YKRVQVEPHLSVTGACSAEW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 273 APIRTGTDIAFLSGVIRYLLQT---GKYNKEYTLAYTNAALLVNPD----------------------FKFDDGLFSGYN 327
Cdd:cd02760 224 VPIRPKTDPAFMFAMIHVMVHEqglGKLDVPFLRDRTSSPYLVGPDglylrdaatgkplvwdersgraVPFDTRGAVPAV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 328 ADKHSYDKStwtYQLDDKGmAKRDDSLSDPRCVINLMREHVARYTPEMVETLCGTPKDAFLKVC-EYLAE 396
Cdd:cd02760 304 AGDFAVDGA---VSVDADD-ETAIHQGVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIArEFLEN 369
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
896-1012 |
5.88e-20 |
|
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: 86.17 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 896 TTYRLTEHFHGWTKHARLNAIAQPEQ-FVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRAlqsGgktvhQVG 974
Cdd:pfam01568 4 ITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP---G-----VVF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1721247069 975 IPIHWGYEgvaKKGFSANTLTPFVGDANTQTPEFKSFL 1012
Cdd:pfam01568 76 MPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
889-1017 |
3.28e-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: 84.21 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 889 DAFPYAATTYRLTEHFHGW--TKHAR-LNAIAqPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIralQS 965
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGtmTRRAEgLDAIA-PEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRV---PE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1721247069 966 GgktvhQVGIPIHWgYEGvakkgfSANTLTPFVGDANTQTPEFKSFLVNVEK 1017
Cdd:cd02790 77 G-----VVFMPFHF-AEA------AANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
44-104 |
1.80e-18 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 79.99 E-value: 1.80e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721247069 44 TETRNTCPYCSVGCGILMYSlgdgaKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHS 104
Cdd:smart00926 2 KWVPTVCPLCGVGCGLLVEV-----KDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
44-104 |
5.91e-18 |
|
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: 78.49 E-value: 5.91e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721247069 44 TETRNTCPYCSVGCGILMYSlgdgaKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHS 104
Cdd:pfam04879 2 KVVKTICPYCGVGCGLEVHV-----KDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
49-259 |
4.64e-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: 75.89 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCGILMyslgdGAKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVReaGSNEYKRISWDE 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 129 AFERIAAHMKRDRDAnfveknADGVTVNRwlttgflaasaSSNEAGWLTHKFTR-SLGLLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK------VGGIGSPR-----------ASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721247069 208 FGRGAMTNHwvDIKNANLIVVMGGNAAEAHPVGFrWAIEAKTRNKAKLIVID 259
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPRIA-LALRQAARRKAVELAAL 181
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-309 |
2.85e-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: 72.70 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 50 CPYCSVGCGILMyslgdGAKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVReaGSNEYKRISWDEA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 130 FERIAAHMKrdrdanfvEKNADGVtvnrwlttGFLAASASSNEAGWLTHKFTRSLGLLAVDNQARvuhGPTVASLAPTFG 209
Cdd:cd02768 75 LKTVAEGLK--------AVKGDKI--------GGIAGPRADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 210 RGAMTNHWVDIKNANLIVVMGGNAAEAHPVgfrwaIEAK-----TRNKAKLIVIDPRFTRTASVADY-YAPIrtGTDIAF 283
Cdd:cd02768 136 NYLFNTSIAEIEEADAVLLIGSNLRKEAPL-----LNARlrkavKKKGAKIAVIGPKDTDLIADLTYpVSPL--GASLAT 208
|
250 260
....*....|....*....|....*.
gi 1721247069 284 LSGVIryllqTGKYNKEYTLAYTNAA 309
Cdd:cd02768 209 LLDIA-----EGKHLKPFAKSLKKAK 229
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
43-294 |
7.09e-12 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 69.43 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 43 ATETRNTCPYCSVGCGILMYSLGDGAKNAKA--------DI---------------------------FHIEGDPDH--P 85
Cdd:cd02756 10 AERYNVTCHFCIVGCGYHVYVWPVGEEGGPSpgqnaigyDLvdqvpplnlqwypktmhyvvvtqdgreVYIVIVPDKecP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 86 VNRGALCPKGAGLIDFIHSP------NRLRYPEVREAGsnEYKRISWDEAFERIAAHMKRDRDAnfvEKNADGVTVNRWL 159
Cdd:cd02756 90 VNSGNYSTRGGTNAERIWSPdnrvgeTRLTTPLVRRGG--QLQPTTWDDAIDLVARVIKGILDK---DGNDDAVFASRFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 160 TTGflaaSASSNEAGWLTHKFTRSLglLAVDNQA---RVUHGPTVASLAPTfGRGAMTNHWVDIKNANLIVVMGGNAAEA 236
Cdd:cd02756 165 HGG----GGGGFENNWGVGKFFFMA--LQTPFVRihnRPAYNSEVHATREM-GVGELNNSYEDARLADTIVLWGNNPYET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 237 HPVGF-----------------RWAIEAKTRNKAKLIVIDPRFTRTASVADYYA--------PIRTGTDIAFLSGVIRYL 291
Cdd:cd02756 238 QTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEAAAgkdrvlhlQVNPGTDTALANAIARYI 317
|
...
gi 1721247069 292 LQT 294
Cdd:cd02756 318 YES 320
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
5-295 |
7.25e-11 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 65.97 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 5 RRQFFKLCAGGMAGTTIATLGFmPETALADtrsYKLLRATE-TRNTCPYCS------VGCGILMySLGDGAKnakadiFH 77
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRY-PVEKIVP---YVIWPENIvPGETVYYATslvpagEGQGVLV-KTVDGRP------IK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 78 IEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGSNEYKrISWDEAFERIAAHMKrdrdanfveKNADGVTVnR 157
Cdd:cd02764 70 IEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGAYVA-SDWADFDAKVAEQLK---------AVKDGGKL-A 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 158 WLTTGFLAASASSNEAGWLTHKF-TRSLGLLAVDNQarvuhgPTVASLAPTFGRGAMTNHwvDIKNANLIVVMGGNAAE- 235
Cdd:cd02764 139 VLSGNVNSPTTEALIGDFLKKYPgAKHVVYDPLSAE------DVNEAWQASFGKDVVPGY--DFDKAEVIVSIDADFLGs 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721247069 236 -AHPVGFRWAIEA-----KTRNKAKLIVIDPRFTRTASVADYYAPIRTGTDIAFLSGVIRYLLQTG 295
Cdd:cd02764 211 wISAIRHRHDFAAkrrlgAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKG 276
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-285 |
1.97e-10 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 64.28 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 49 TCPYCSVGCgilmyslgdgaknakaDIFHIEGDPDHPVNRGALCPKGAGLidFIHSPNRLRYPEVREagsneyKRISWDE 128
Cdd:cd02761 3 VCPFCGLLC----------------DDIEVEVEDNKITKVRNACRIGAAK--FARYERRITTPRIDG------KPVSLEE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 129 AFERIAAHMKRDRDANFVeknadgvtvnrwlttGFlaaSASSNEAgwlthkfTRSLGLLA------VDNQARVUHGPTVA 202
Cdd:cd02761 59 AIEKAAEILKEAKRPLFY---------------GL---GTTVCEA-------QRAGIELAeklgaiIDHAASVCHGPNLL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 203 SLAPtfgRGAMTNHWVDIKN-ANLIVVMGGNAAEAHPVGF-RWAIEAK------TRNKAKLIVIDPRFTRTASVADYYAP 274
Cdd:cd02761 114 ALQD---SGWPTTTLGEVKNrADVIVYWGTNPMHAHPRHMsRYSVFPRgffregGREDRTLIVVDPRKSDTAKLADIHLQ 190
|
250
....*....|.
gi 1721247069 275 IRTGTDIAFLS 285
Cdd:cd02761 191 IDPGSDYELLA 201
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-306 |
2.26e-10 |
|
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: 64.59 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 79 EGDPDhPvnrgalCPKGAGLIDFIHSPNRLRYPEVREA-------------GSNEYKRISWDEAFERIAAHMKRDRDanf 145
Cdd:cd02769 25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrslrGKEEFVRVSWDEALDLVAAELKRVRK--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 146 veknadgvtvnrwlTTGFLAASASSneAGWlthkftRSLGLL--AVDNQARV--UHGPTVAS----------------LA 205
Cdd:cd02769 95 --------------TYGNEAIFGGS--YGW------SSAGRFhhAQSLLHRFlnLAGGYVGSvgdystgaaqvilphvVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 206 PTFGRGAMTNHWVDI-KNANLIVVMGGNA----------AEAHPVGFRWAiEAKTRNKaKLIVIDPRFTRTASVADY-YA 273
Cdd:cd02769 153 SMEVYTEQQTSWPVIaEHTELVVAFGADPlknaqiawggIPDHQAYSYLK-ALKDRGI-RFISISPLRDDTAAELGAeWI 230
|
250 260 270
....*....|....*....|....*....|...
gi 1721247069 274 PIRTGTDIAFLSGVIRYLLQTGKYNKEYTLAYT 306
Cdd:cd02769 231 AIRPGTDVALMLALAHTLVTEGLHDKAFLARYT 263
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-153 |
2.71e-10 |
|
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: 63.71 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 41 LRATETrnTCPYCSVGCGILMyslgdGAKNAKadIFHIEGDPDHPVNRGALCPKGAGLIDFIHSPNRLRYPEVREAGsnE 120
Cdd:COG1034 215 LKKTPS--ICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG--E 283
|
90 100 110
....*....|....*....|....*....|...
gi 1721247069 121 YKRISWDEAFERIAAHMKRDRDAnfveKNADGV 153
Cdd:COG1034 284 LVEASWEEALAAAAEGLKALKKA----ENSVGA 312
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
891-986 |
1.78e-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: 57.30 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 891 FPYAATTYRLTEHFHGWTKHARLNAIaQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRalqsggKTV 970
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEI-KPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVR------PGV 73
|
90
....*....|....*....
gi 1721247069 971 hqVGIPI---HWGYEGVAK 986
Cdd:cd02780 74 --VAIEHgygHWAYGAVAS 90
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
891-961 |
6.04e-08 |
|
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: 52.37 E-value: 6.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721247069 891 FPYAATTYRLTEHFHgwTKHARLNAI--AQPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIR 961
Cdd:cd02785 2 YPLACIQRHSRFRVH--SQFSNVPWLleLQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
889-1017 |
7.28e-08 |
|
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: 52.31 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 889 DAFPYAATTYRLTEHFHgwTKHARLNAIAQ--PEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRAlqsg 966
Cdd:cd02781 1 EYPLILTTGARSYYYFH--SEHRQLPSLRElhPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRP---- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721247069 967 gKTVH-QVGipiHWGYEGVAKKGFS-------ANTLT------PFVGDANtqtpeFKSFLVNVEK 1017
Cdd:cd02781 75 -GVVRaEHG---WWYPEREAGEPALggvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
930-1017 |
1.22e-06 |
|
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: 48.35 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 930 AKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIR----ALQSGGktvhqvgipihWgYEGVAKKGF----SANTLTPFVGda 1001
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIMpgvvALPEGA-----------W-YDPDDNGGLdkggNPNVLTSDIP-- 108
|
90 100
....*....|....*....|..
gi 1721247069 1002 ntqTPEF------KSFLVNVEK 1017
Cdd:cd02777 109 ---TSKLaqgnpaNTCLVEIEK 127
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
897-1017 |
1.34e-06 |
|
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: 48.42 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 897 TYRLTEHFHGWTKH-ARLNAIAqPEQFVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIRAlqsggKTV---HQ 972
Cdd:cd02778 6 YGKSPVHTHGHTANnPLLHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP-----DTVfmpHG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1721247069 973 VGipiHWGYEGVAK--KGFSANTLTPFVGDANTQTPEFKSFLVNVEK 1017
Cdd:cd02778 80 FG---HWAPALSRAygGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
70-440 |
1.74e-06 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 52.31 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 70 NAKADIFHIEGDPDHPV--------------------------NRGALCPKGAGLIDFIHSPNRLRYP--EVREAGSNEY 121
Cdd:PRK14991 94 NATNKILRIAGNPYHPLstdhhidmstpvkeafeslsgesgleGRSTACARGNAMLEQLDSPYRVLQPlkRVGKRGSGKW 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 122 KRISwdeaFERIAAHMKRDRDAnFVEKNADGVTVNRWLTTGF-------------LAASASSNEA-GWLTHKFTR-SLGL 186
Cdd:PRK14991 174 QRIS----FEQLVEEVVEGGDL-FGEGHVDGLRAIRDLDTPIdaknpeygpkanqLLVTNASDEGrDAFIKRFAFnSFGT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 187 LAVDNQARVUhgptvaSLAPTFGRGAMTN------HWV-DIKNANLIVVMGGNAAEA-HPvgF----RWAIEAKTRNKAK 254
Cdd:PRK14991 249 RNFGNHGSYC------GLAYRAGSGALMGdldknpHVKpDWDNVEFALFIGTSPAQSgNP--FkrqaRQLANARTRGNFE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 255 LIVIDPRFTRTASVA----DYYAPIRTGTDIAFLSGVIRYLLQTGKYNKEY-------------TLAYTNAALLV--NPD 315
Cdd:PRK14991 321 YVVVAPALPLSSSLAagdnNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYlaqpgvaamqaagEASWTNATHLViaDPG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 316 FK--------FDDGLfsGYNADKHSYDKSTWTYQLDDKGMA------------KRDDSLSDPRCV-----INLMREHVAR 370
Cdd:PRK14991 401 HPrygqflraSDLGL--PFEGEARGDGEDTLVVDAADGELVpatqaqparlfvEQYVTLADGQRVrvkssLQLLKEAARK 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 371 YTPEMVETLCGTPkdafLKVCEYLAETGAHDKTTSFLYALGWTQHSIGSQNIRTMAMIQLLLGNMGMAGG 440
Cdd:PRK14991 479 LSLAEYSEQCGVP----EAQIIALAEEFTSHGRKAAVISHGGTMSGNGFYNAWAIMMLNALIGNLNLKGG 544
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
905-1017 |
5.50e-06 |
|
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: 46.86 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 905 HGWtkHARLNAIAQPEQfVEIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIR----ALQSGGktvhqvgipihW- 979
Cdd:cd02793 20 HGS--LSRAYKVQGREP-IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMpgvvQLPTGA-----------Wy 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1721247069 980 ------GYEGVAKKGfSANTLTPFVGDAN-TQTPEFKSFLVNVEK 1017
Cdd:cd02793 86 dpddpgEPGPLCKHG-NPNVLTLDIGTSSlAQGCSAQTCLVQIEK 129
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
3-129 |
1.27e-04 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 46.20 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 3 VSRRQFFKlcagGMAGTTIATLG----FMPETALADTRSykllrATETRNTcpYCSVGCGIlmyslgdGAKNAK------ 72
Cdd:PRK15102 1 ASRRRFLK----GLGGLSAAGMLgpslLTPRSALAAQAA-----AAETTKE--WILTGSHW-------GAFRAKvkngrf 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 73 ADIFHIEGDpDHPvnrgalCPKGAGLIDFIHSPNRLRYPEVR-------------EAGSNEYKRISWDEA 129
Cdd:PRK15102 63 VEAKPFELD-KYP------TKMINGIKGHVYNPSRIRYPMVRldwlrkrhksdtsQRGDNRFVRVSWDEA 125
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
917-1017 |
2.26e-03 |
|
The MopB_CT_DmsA-EC CD 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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 39.20 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721247069 917 AQPEQFVeIGEALAKEKGIAHGDTVKVSSKRGYIKAKAVVTKRIR----ALQSGGktvhqvgipihWgYE----GVAKKG 988
Cdd:cd02794 27 AFPQEVW-INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMpgvvALPQGA-----------W-YEpdanGIDKGG 93
|
90 100 110
....*....|....*....|....*....|....
gi 1721247069 989 fSANTLT-----PFVGdANTQtpefKSFLVNVEK 1017
Cdd:cd02794 94 -CINTLTglrpsPLAK-GNPQ----HTNLVQVEK 121
|
|
| |
