|
Name |
Accession |
Description |
Interval |
E-value |
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
2-1014 |
0e+00 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 1512.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 2 QVSRRQFFKICAGGMAGTTVAALGFAPEVALAETRQYKLLRARETRNTCTYCSVGCGLLMYSLGDGAKNAKESIFHIEGD 81
Cdd:TIGR01553 1 LISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 82 PDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGSDKWQRISWDDAFTRIAKLVKEDRDANFIKTNDQGVTVNRWLTT 161
Cdd:TIGR01553 81 PDHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 162 GMLCASAASNETGFLSQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGF 241
Cdd:TIGR01553 161 ASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 242 RWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTNASLLVREDFAFEDG 321
Cdd:TIGR01553 241 KWAIRAK-KKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYTNASFIVGEGFAFEDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 322 LFSGYDAENRKYDKTTWNYQFDENGFAKRDVTLQDPRCVWNLLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETCVAD 401
Cdd:TIGR01553 320 LFAGYNKETRKYDKSKWGYEFDENGNPKRDETLKHPRCVFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKTGKPN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 402 KTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLLSQSLPGYLTLPSEKQTDLDTY 481
Cdd:TIGR01553 400 KAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPRASIPTYEQY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 482 LKANTPKALLPGQVNYWGNYPKFFVSMMKTFYGDKAQKDNSWGFDWLPKWDKGYD-VLQYFEMMAQGKVNGYFCQGFNPV 560
Cdd:TIGR01553 480 TKKFTPVSKDPQSANYWSNFPKFFASYIKSMWGDAATNENGWAYDYLPKGEDGYDsWLTLFDDMFQGKIKGFFAWGQNPL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 561 ASFPNKNKVVASLSKLKFLVTIDPLNTETSNFWQNHGefneVDPSQIQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGA 640
Cdd:TIGR01553 560 NSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPG----MDPKEIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGP 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 641 DAPGEALNDGEILAGIFSRLREMYARDGGAVPEQVLNMTWDYLTPDNPAPEEVAQENNGKALADLldADGKVLVKKGELL 720
Cdd:TIGR01553 636 DPPGNAIPDGDIIVELAKRVQELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKEINGYALKDF--KVGDVEYKKGQQI 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 721 SSFAQLRDDGTTASGCWIFAGSWTPAGNQMARRDNADPSGLGNTLGWAWAWPLNRRILYNRASADPQGKPWDPKRQLLEW 800
Cdd:TIGR01553 714 ATFGHLRDDGSTTSGCWLYTGSYTEKGNMAARRDKSDPAGLGLYPGWTWAWPANRRVLYNRASVDLNGKPWDPERALVEW 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 801 DGA--KWVGaDIPDY-STAAPGSDVGPFIMQPEGMGRLFATDKMAEGPFPEHYEPFETPLGTNPLHPNVVSNPAARVFKD 877
Cdd:TIGR01553 794 NAAekKWVG-DIPDYpPTAPPEKGKGAFIMKPEGYGRLFAPGKREDGPLPEHYEPMESPVITNPFHPNVLHNPTALHYKT 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 878 DLAAMGKSDKFPYVGTTYRLTEHFHYWTKHARLNAIAQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRI 957
Cdd:TIGR01553 873 DEKAVGDPKRYPFVATTYRLTEHWHTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRI 952
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1778702115 958 RTLQVHGQEVDTIGIPIHWGYEGVAKKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1014
Cdd:TIGR01553 953 KPLAIQGQQVHMIGIPIHWGWSFLKNGGDATNILTPSVGDPNTGTPETKAFLVNIEK 1009
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
47-873 |
0e+00 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 993.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 47 RNTCTYCSVGCGLLMYSLGdgaknakESIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGSDKWQRISW 126
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQN-------GVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 127 DDAFTRIAKLVKEDRDANFIKTNDQGVTVNRWLTTGMLCASAASNETGFLSQKFSRALGMLAVDNQARVUHGPTVASLAP 206
Cdd:cd02752 74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 207 TFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSG 286
Cdd:cd02752 154 TFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 287 VLLYLMtnnkfnreyveaytnasllvredfafedglfsgydaenrkydkttwnyqfdengfakrdvtlqdprcvwnllkq 366
Cdd:cd02752 234 MINYII-------------------------------------------------------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 367 hvsRYTPDVVSNICGTPKDDFLKVCEYIAETCVADKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02752 240 ---RYTPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 447 GHSNIQGLTDLGLLSQSLPGYLTlpsekqtdldtylkantpkallpgqvnywgnypkffvsmmktfygdkaqkdnswgfd 526
Cdd:cd02752 317 GHSNVQGATDLGLLSHNLPGYLG--------------------------------------------------------- 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 527 wlpkwdkgydvlqyfemmaqgkvngyfcqGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFWQNHGefneVDPSQ 606
Cdd:cd02752 340 -----------------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKNPG----MDPKS 386
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 607 IQTEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILAGIFSRLREMYARDGGAVPEQVLNmtWDYLTPD 686
Cdd:cd02752 387 IQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITK--WNYGYGD 464
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 687 NPAPEEVAQENNGKALADLL-DADGKVLVKKGELLSSFAQLRDDGTTASGCWIFAGSWTPAGNqMARRDNADPSGLGNTL 765
Cdd:cd02752 465 EPTPEEIAREINGGALTDGYtGQSPERLKAHGQNVHTFDTLRDDGSTACGCWIYSGSYTEEGR-MARRDTSDPDGLGLYP 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 766 GWAWAWPLNRRILYNRASADPQGKPWDPKRQLLEWDGAK-WVGADIPDY-STAAPGSDVGPFIMQPEGMGRLFATDKmaE 843
Cdd:cd02752 544 GWPWPWPVNRRILYNRASVDMEGKPGYPERPLVEWDGLGwWWKGDVPDGpWPAAKEHGCGPFIMAPEGQARLFVWNF--D 621
|
810 820 830
....*....|....*....|....*....|
gi 1778702115 844 GPFPEHYEPFETPLGTNplHPNVVSNPAAR 873
Cdd:cd02752 622 GPFPEHYEPLESPRPDL--HSKVAKNPTYK 649
|
|
| formate_DH_Act |
NF041513 |
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type ... |
24-1012 |
0e+00 |
|
formate dehydrogenase; Members of this family are the enzyme formate dehydrogenase, of a type found in the Actinomycetota, as in the genera Streptomyces, Nocardiopsis, Gordonia, and Saccharomonospora. Many are selenoproteins.
Pssm-ID: 469399 [Multi-domain] Cd Length: 1066 Bit Score: 921.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 24 LGFAPEVALAETRQyklLRARE------TRNTCTYCSVGCGLLMYslgdgAKNakESIFHIEGDPDHPVNRGALCPKGAG 97
Cdd:NF041513 18 LGRGAAARSARTRA---LRPRTatadrvVRSVCPYCAVGCGQKVY-----VKD--EKVVQIEGDPDSPISRGRLCPKGSA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 98 LVDFIHSESRLKYPEYRAPGSDKWQRISWDDAFTRIAKLVKEDRDANFIKTNDQGVTVNRWLTTGMLCASAASNETGFLS 177
Cdd:NF041513 88 SLQLVTGPTRVTTVLYRRPYGTEWEELDLDTAMDMIADRVLDTRRETWQDEDDDGRRLRRTMGIASLGGATLDNEENYLI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 178 QKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIV 257
Cdd:NF041513 168 KKLFTALGAVQVENQARIUHSSTVPGLGTSFGRGGATTFLQDLANSDCIVIQGSNMAEAHPVGFQWVMEAK-ARGATVIH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 258 IDPRFTRTASVADFYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTNASLLVREDFAFE---DGLFSGYDAENRKYD 334
Cdd:NF041513 247 VDPRFTRTSALADLHVPIRAGSDIAFLGGLINHVLSNELYFREYVLAYTNAATIVSEDFRDTedlDGLFSGFDPETGSYD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 335 KTTWNYQFDEN----------------------------------GFAKRDVTLQDPRCVWNLLKQHVSRYTPDVVSNIC 380
Cdd:NF041513 327 PASWQYEGVEVaaaagqrdqlydsrggahesargeehgsggapvaGAPRRDETLQDPRCVFQILKRHFARYTPEMVEEIC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 381 GTPKDDFLKVCEYIAETCVADKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLL 460
Cdd:NF041513 407 GIPRELFLKVADALTANSGRERTTAFCYAVGWTQHTVGVQYIRAASILQLLLGNIGRPGGGIMALRGHASIQGSTDIPTL 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 461 SQSLPGYLTLP-SEKQTDLDTYLKANTPkallpgQVNYWGNYPKFFVSMMKTFYGDKAQKDNSWGFDWLPKWDKGYDVLQ 539
Cdd:NF041513 487 FNLLPGYLPMPhAHKHEDLDSYVEANAS------QKGFWANMRAYTVSLLKAWWGDAATAENDFCFDYLPRLTGDHSTYQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 540 YFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFWQNHGEFN--EVDPSQIQTEVFRLPST 617
Cdd:NF041513 561 TVMAMLDGKVKGYFLMGENPAVGSANGRLQRLGMANLDWLVVRDFSLIESATFWKDGPEIEtgELRTEDIGTEVFFFPAA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 618 CFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILAGIFSRLREMYARDGGAVPEQVLNMTWDYLTP---DNPAPEEVA 694
Cdd:NF041513 641 AHTEKSGTFTNTQRLLQWRHQAVEPPGDARSDLWFFYHLGRRIREKLAGSTDPRDRPLLDLTWDYPTEgphGEPDAEAVL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 695 QENNGKALAdlldadgkvlvkkGELLSSFAQLRDDGTTASGCWIFAGSWTPAGNQMARRDnadPSGLGNTLG--WAWAWP 772
Cdd:NF041513 721 AEINGYDLS-------------GRPLSAYTELKDDGSTSCGCWIYCGVYADGVNQAARRK---PGREQDWVAaeWGWAWP 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 773 LNRRILYNRASADPQGKPWDPKRQLLEWD--GAKWVGADIPDY-STAAPG-------------SDVGPFIMQPEGMGRLF 836
Cdd:NF041513 785 ANRRILYNRASADPEGRPWSERKKYVWWDaeAGRWTGYDVPDFpVDKPPDyrpppgatgpaalSGDDPFIMQADGKGWLF 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 837 ATDKMAEGPFPEHYEPFETPLGtNPLHPnVVSNPAARVF--KDDLAA----MGKSDKFPYVGTTYRLTEHF-----HYWT 905
Cdd:NF041513 865 APAGLVDGPLPTHYEPQESPVR-NPLYG-QQRNPARKVYprEDNRYHpsggEPGAEVYPYVFTTYRLTEHHtaggmSRWL 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 906 KH-ARLnaiaQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTLQVHGQEVDTIGIPIHWGYEGVAkK 984
Cdd:NF041513 943 PYlAEL----QPEMFCEVSPELAAERGLENGGWATIVTARGAIEARVLVTDRMTPLRVQGRTVHQIGLPYHWGPNGLV-T 1017
|
1050 1060
....*....|....*....|....*...
gi 1778702115 985 GFIANTLTPFVGDANTQTPEFKAFLVNV 1012
Cdd:NF041513 1018 GDAANELLGITLDPNVHIQESKALTCDI 1045
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
44-1015 |
4.16e-151 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 464.36 E-value: 4.16e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 44 RETRNTCTYCSVGCGLLMYSLGDGaknakesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGsdKWQR 123
Cdd:COG3383 5 KKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 124 ISWDDAFTRIAKLVKEDRDanfiKTNDQGVtvnrwlttGMLCASAASNETGFLSQKFSRA-LGMLAVDNQARVUHGPTVA 202
Cdd:COG3383 76 VSWDEALDLVAERLREIQA----EHGPDAV--------AFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLCMASAVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 203 SLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIA 282
Cdd:COG3383 144 GLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPRRTETARLADLHLQIKPGTDLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 283 FLSGVLLYLMTNNKFNREYVEAYTNasllvredfafedglfsGYDAenrkydkttwnyqfdengfakrdvtlqdprcvwn 362
Cdd:COG3383 223 LLNGLLHVIIEEGLVDEDFIAERTE-----------------GFEE---------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 363 lLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGV 442
Cdd:COG3383 252 -LKASVAKYTPERVAEITGVPAEDIREAARLIAEA----KRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 443 NALRGHSNIQGLTDLGLLSQSLPGYLTLPSEKqtdldtylkantpkallpgqvnywgnypkffvsmmktfygDKAQKDNS 522
Cdd:COG3383 327 FPLTGQNNVQGGRDMGALPNVLPGYRDVTDPE----------------------------------------HRAKVADA 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 523 WGFDWLPKWdKGYDVLQYFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFwqnhgefnev 602
Cdd:COG3383 367 WGVPPLPDK-PGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEY---------- 435
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 603 dpsqiqTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILAGIFSRlremyardggavpeqvLNMTWDY 682
Cdd:COG3383 436 ------ADVV-LPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARR----------------LGYGFDY 492
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 683 ltpdnPAPEEVAQEnngkaladlldadgkvlvkkgellssfaqlrddgttasgcwifagswtpagnqmarrdnadpsglg 762
Cdd:COG3383 493 -----DSPEEVFDE------------------------------------------------------------------ 501
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 763 ntlgWAWAWPLNRRILYNRasadpqgkpwdpkrqLLEWDGAKWvgadiPDYSTAAPGSDvgpfimqpegmgRLFAtdkma 842
Cdd:COG3383 502 ----IARLTPDYSGISYER---------------LEALGGVQW-----PCPSEDHPGTP------------RLFT----- 540
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 843 egpfpehyEPFETPLGTNPLHPNVVSNPAARVfkddlaamgkSDKFPYVGTTYRLTEHFHYWTKHAR---LNAIAqPEQF 919
Cdd:COG3383 541 --------GRFPTPDGKARFVPVEYRPPAELP----------DEEYPLVLTTGRLLDQWHTGTRTRRsprLNKHA-PEPF 601
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 920 VEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTlqvhgqevDTIGIPIHWGYEGvakkgfiANTLTPFVGDAN 999
Cdd:COG3383 602 VEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRP--------GTVFMPFHWGEGA-------ANALTNDALDPV 666
|
970
....*....|....*.
gi 1778702115 1000 TQTPEFKAFLVNVEKV 1015
Cdd:COG3383 667 SKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-1012 |
1.94e-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: 404.93 E-value: 1.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYslgdgAKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRApgSDKWQRISWDD 128
Cdd:TIGR01591 2 VCPYCGVGCSLNLV-----VKDGK--IVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIRE--GDKFREVSWDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 129 AFTRIAKLVKEdrdanfIKTNdQGVTvnrwlTTGMLCASAASNETGFLSQKFSRA-LGMLAVDNQARVUHGPTVASLAPT 207
Cdd:TIGR01591 73 AISYIAEKLKE------IKEK-YGPD-----SIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCHGPSVAGLKQT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 208 FGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSGV 287
Cdd:TIGR01591 141 VGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAK-RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 288 LLYLMTNNKFNREYVEAYTNasllvredfafedglfsgydaenrkydkttwnyQFDEngfakrdvtlqdprcvwnlLKQH 367
Cdd:TIGR01591 220 ANVIIEEGLYDKAFIEKRTE---------------------------------GFEE-------------------FREI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 368 VSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:TIGR01591 248 VKGYTPEYVEDITGVPADLIREAARMYAKA----GSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 448 HSNIQGLTDLGLLSQSLPGYltLPSEKQTDLDTYLKAntpkallpgqvnywgnypkffvsmmktfygdkaqkdnsWGFDW 527
Cdd:TIGR01591 324 QNNVQGACDMGALPDFLPGY--QPVSDEEVREKFAKA--------------------------------------WGVVK 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 528 LPKwDKGYDVLQYFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFwqnhgefnevdpsqi 607
Cdd:TIGR01591 364 LPA-EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY--------------- 427
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 608 qTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILagifsrlrEMYARDGGAvpeqvlnmTWDYltpDN 687
Cdd:TIGR01591 428 -ADVV-LPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII--------QELANALGL--------DWNY---NH 486
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 688 PApeEVAQEnngkaladlldadgkvlvkkgellssfaqlrddgtTASGCWIFAGswtpagnqMARRDNADPSGLgntlgw 767
Cdd:TIGR01591 487 PQ--EIMDE-----------------------------------IRELTPLFAG--------LTYERLDELGSL------ 515
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 768 awAWPLNrrilynraSADPQGKPwdpkrqLLEWDGakwvgadipdystaapgsdvgpfIMQPEGMGRLFATDKMAegpfp 847
Cdd:TIGR01591 516 --QWPCN--------DSDASPTS------YLYKDK-----------------------FATPDGKAKFIPLEWVA----- 551
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 848 ehyePFETPlgtnplhpnvvsnpaarvfkddlaamgkSDKFPYVGTTYRLTEHFHYWTKHARLNAIAQ--PEQFVEIGEK 925
Cdd:TIGR01591 552 ----PIEEP----------------------------DDEYPLILTTGRVLTHYNVGEMTRRVAGLRRlsPEPYVEINTE 599
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 926 LAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRtlqvhgqeVDTIGIPIHWGYEGVakkgfiaNTLTPFVGDANTQTPEF 1005
Cdd:TIGR01591 600 DAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVN--------KGAIYITMHFWDGAV-------NNLTTDDLDPISGTPEY 664
|
....*..
gi 1778702115 1006 KAFLVNV 1012
Cdd:TIGR01591 665 KYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-1015 |
8.10e-124 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 392.67 E-value: 8.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 43 ARETRNTCTYCSVGCGLLMYSLGDGAKnakesifHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYR--APGSDK 120
Cdd:COG0243 21 TKTVKTTCPGCGVGCGLGVKVEDGRVV-------RVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRvgPRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 121 WQRISWDDAFTRIAKLVKEDRDanfiKTNDQGVtvnrWLTTGMLCASAASNETGFLSQKFSRALGMLAVDNQARVUHGPT 200
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIID----EYGPEAV----AFYTSGGSAGRLSNEAAYLAQRFARALGTNNLDDNSRLCHESA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 201 VASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTD 280
Cdd:COG0243 166 VAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTETAAIADEWLPIRPGTD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 281 IAFLSGVLLYLMTNNKFNREYVEAYTNasllvredfafedglfsGYDAenrkydkttwnyqfdengfakrdvtlqdprcv 360
Cdd:COG0243 246 AALLLALAHVLIEEGLYDRDFLARHTV-----------------GFDE-------------------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 361 wnlLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:COG0243 277 ---LAAYVAAYTPEWAAEITGVPAEDIRELAREFATA----KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 441 GVNALRGHsniqgltdlgllsqslpgyltlpsekqtdldtylkantpkALLPGQvnywgNYPkffvsmmktfygdkaqkd 520
Cdd:COG0243 350 GPFSLTGE----------------------------------------AILDGK-----PYP------------------ 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 521 nswgfdwlpkwdkgydvlqyfemmaqgkVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFwqnhgefn 600
Cdd:COG0243 367 ----------------------------IKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY-------- 410
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 601 eVDpsqiqtevFRLPSTCFAEENGSIVNSG-RWLQWHWKGADAPGEALNDGEILAGIFSRLremyardggAVPEQVlnmt 679
Cdd:COG0243 411 -AD--------IVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRL---------GFEEAF---- 468
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 680 wdyltPDNPAPEEVaqenngkaLADLLDADGKVLVkkgellsSFAQLRDDGttasgcwifagswtpagnqmarrdnadps 759
Cdd:COG0243 469 -----PWGRTEEDY--------LRELLEATRGRGI-------TFEELREKG----------------------------- 499
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 760 glgntlgwAWAWPLnrrilynrasadPQGKPWdpkrqllEWDGAkwvgadipdYSTAApgsdvgpfimqpegmGRL-FAT 838
Cdd:COG0243 500 --------PVQLPV------------PPEPAF-------RNDGP---------FPTPS---------------GKAeFYS 528
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 839 DKMAEGPFPEHYEPFEtplgtnplhpnvvsnpaarvfkddlAAMGKSDKFPYVGTTYRLTEHFHYWT-KHARLNAIaQPE 917
Cdd:COG0243 529 ETLALPPLPRYAPPYE-------------------------GAEPLDAEYPLRLITGRSRDQWHSTTyNNPRLREI-GPR 582
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 918 QFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTlqvhgqevDTIGIPIHWGYEGVAKKGFIANTLTPFVGD 997
Cdd:COG0243 583 PVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--------GVVFAPHGWWYEPADDKGGNVNVLTPDATD 654
|
970
....*....|....*...
gi 1778702115 998 ANTQTPEFKAFLVNVEKV 1015
Cdd:COG0243 655 PLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-660 |
1.74e-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: 370.39 E-value: 1.74e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYSlgdgaKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGsdKWQRISWDD 128
Cdd:cd02753 3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 129 AFTRIA-KL--VKEDRDANFIktndqgvtvnrwlttGMLCASAASNETGFLSQKFSRA-LGMLAVDNQARVUHGPTVASL 204
Cdd:cd02753 74 ALSLVAsRLkeIKDKYGPDAI---------------AFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCHSPTVAGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 205 APTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKIhNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFL 284
Cdd:cd02753 139 AETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKR-NGAKLIVADPRRTELARFADLHLQLRPGTDVALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 285 SGVLLYLMTNNKFNREYVEAYTNasllvredfafedglfsGYDAenrkydkttwnyqfdengfakrdvtlqdprcvwnlL 364
Cdd:cd02753 218 NAMAHVIIEEGLYDEEFIEERTE-----------------GFEE-----------------------------------L 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 365 KQHVSRYTPDVVSNICGTPKDDFLKVCEYIAEtcvADKTAsFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02753 246 KEIVEKYTPEYAERITGVPAEDIREAARMYAT---AKSAA-ILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 445 LRGHSNIQGLTDLGLLSQSLPGYltlpsekqtdldtylkantpkallpgqvnywgnypkffvsmmktfygdkaqkdnswg 524
Cdd:cd02753 322 LRGQNNVQGACDMGALPNVLPGY--------------------------------------------------------- 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 525 fdwlpkwdkgydvlqyfemmaqgkVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFwqnhgefnevdp 604
Cdd:cd02753 345 ------------------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAEL------------ 388
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1778702115 605 sqiqTEVFrLPSTCFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILAGIFSRL 660
Cdd:cd02753 389 ----ADVV-LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRL 439
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
47-660 |
3.16e-86 |
|
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: 288.74 E-value: 3.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 47 RNTCTYCSVGCGLLMYSLGDGAKNAKesifhieGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGSdKWQRISW 126
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 127 DDAFTRIAKLVKEDRDanfiktnDQGVTVNRWLTTGMLCasaasNETGFLSQKFSRA-LGMLAVDNQARVUHGPTVASLA 205
Cdd:cd02754 73 DEALDLIAERFKAIQA-------EYGPDSVAFYGSGQLL-----TEEYYAANKLAKGgLGTNNIDTNSRLCMASAVAGYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 206 PTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAK-IHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFL 284
Cdd:cd02754 141 RSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKkANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 285 SGVLLYLMTNNKFNREYVEAYTNasllvredfafedglfsGYDAenrkydkttwnyqfdengfakrdvtlqdprcvwnlL 364
Cdd:cd02754 221 NGLLHVLIEEGLIDRDFIDAHTE-----------------GFEE-----------------------------------L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 365 KQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02754 249 KAFVADYTPEKVAEITGVPEADIREAARLFGEA----RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFS 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 445 LRGHSNIQGLTDLGLLSQSLPGYLTLPSEKqtdldtylkantpkallpgqvnywgnypkffvsmmktfygDKAQKDNSWG 524
Cdd:cd02754 325 LTGQPNAMGGREVGGLANLLPGHRSVNNPE----------------------------------------HRAEVAKFWG 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 525 FDWLPKWDK-GYDVLQYFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDP-LNTETsnfwqnhGEFNEV 602
Cdd:cd02754 365 VPEGTIPPKpGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAfADTET-------AEYADL 437
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1778702115 603 dpsqiqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGEALNDGEILAGIFSRL 660
Cdd:cd02754 438 ----------VLPAASWGEKEGTMTNSERRVS-LLRAAvEPPGEARPDWWILADVARRL 485
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-660 |
1.10e-84 |
|
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: 278.06 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 47 RNTCTYCSVGCGLLMYSlgdgaKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGSDKWQRISW 126
Cdd:cd00368 1 PSVCPFCGVGCGILVYV-----KDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 127 DDAFTRIAKLVKEDRDANfikTNDQgvtvnrwltTGMLCASAASNETGFLSQKFSRALGMLAVDNQARVUHGPTVASLaP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREKY---GPDA---------IAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAAL-K 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 207 TFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSG 286
Cdd:cd00368 141 AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 287 vllylmtnnkfnrEYVEAytnasllvredfafedglfsgydaenrkydkttwnyqfdengfakrdvtlqdprcvwnllkq 366
Cdd:cd00368 220 -------------EWAAE-------------------------------------------------------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 367 hvsrytpdvvsnICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNAlr 446
Cdd:cd00368 225 ------------ITGVPAETIRALAREFAAA----KRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 447 ghsniqgltdlgllsqslpgyltlpsekqtdldtylkantpkallpgqvnywgnypkffvsmmktfygdkaqkdnswgfd 526
Cdd:cd00368 --------------------------------------------------------------------------------
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 527 wlpkwdkgydvlqyfemmaqgkvngyfcqGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETSNFwqnhgefnevdpsq 606
Cdd:cd00368 287 -----------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY-------------- 323
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1778702115 607 iqtEVFRLPSTCFAEENGSIVNSGRWLQWHWKGADAPGEALNDGEILAGIFSRL 660
Cdd:cd00368 324 ---ADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
886-1014 |
3.52e-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: 189.74 E-value: 3.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 886 DKFPYVGTTYRLTEHFHYW--TKHARLNAIAQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRtlqvh 963
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGnmTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 964 gqeVDTIGIPIHWGYEGVAkKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1014
Cdd:cd02792 76 ---PHEVGIPYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
107-661 |
2.05e-48 |
|
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: 182.12 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 107 RLKYPEYRAPGSDKWQRISWDDAFTRIAKLVKedrdanfiKTNDQGVTvnrWLTTGmlcasAASNETGFLSQKFSRALGM 186
Cdd:cd02767 64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLR--------ALDPDRAA---FYTSG-----RASNEAAYLYQLFARAYGT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDP------ 260
Cdd:cd02767 128 NNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK-KRGGKIIVINPlrepgl 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 261 -RF----------TRTASVADFYTPIRSGTDIAFLSGVLLYLMTN-----NKFNREYVEAYTNasllvredfafedglfs 324
Cdd:cd02767 207 eRFanpqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTS----------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 325 GYDAENRKYDKTTWnyqfdengfakrdvtlqdprcvwnllkqhvsrytpDVVSNICGTPKDDFLKVceyiAETCVADKTA 404
Cdd:cd02767 270 GFEEYVAALRALSW-----------------------------------DEIERASGLSREEIEAF----AAMYAKSERV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 405 SFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgyltlpsekqtdldtylka 484
Cdd:cd02767 311 VFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 485 nTPKALlpgqvnywgnyPKFFVSMmktfygdkaqkDNSWGFDwLPKWdKGYDVLQYFEMMAQGKVNGYFCQGFNPVASFP 564
Cdd:cd02767 366 -TEKPF-----------PEFLDAL-----------EEVFGFT-PPRD-PGLDTVEAIEAALEGKVKAFISLGGNFAEAMP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 565 NKNKVVASLSKLKFLVTID-PLNteTSNFWqnHGEFN---------EVD--PSQIQTEVFRLPSTCFAEENGSIVNSGRW 632
Cdd:cd02767 421 DPAATEEALRRLDLTVHVAtKLN--RSHLV--HGEEAlilpclgrtEIDmqAGGAQAVTVEDSMSMTHTSRGRLKPASRV 496
|
570 580 590
....*....|....*....|....*....|....
gi 1778702115 633 LQ-----WHWKGADAPGEALNDGEILAGIFSRLR 661
Cdd:cd02767 497 LLseeaiVAGIAGARLGEAKPEWEILVEDYDRIR 530
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-440 |
3.47e-45 |
|
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: 169.79 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 48 NTCTYCSVGCGLLMYslgdgAKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQRIS 125
Cdd:cd02755 3 SICEMCSSRCGILAR-----VEDGR--VVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 126 WDDAFTRIAKLVKEDRDanfiKTNDQGVTVNRWLTTGMlcasaasnetgFLSQKFSRALGMLAVDNQARVUHGP-TVASL 204
Cdd:cd02755 76 WDEALQYIASKLKEIKE----QHGPESVLFGGHGGCYS-----------PFFKHFAAAFGSPNIFSHESTCLASkNLAWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 205 APTFGRGAMTNhwVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFL 284
Cdd:cd02755 141 LVIDSFGGEVN--PDFENARYIILFGRNLAEAIIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 285 SGVLLYLMTNNKFNREYVEAYTNAsllvredfafedglfsgydaenrkydkttwnyqFDEngfakrdvtlqdprcvwnlL 364
Cdd:cd02755 219 LALIHVLISENLYDAAFVEKYTNG---------------------------------FEL-------------------L 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778702115 365 KQHVSRYTPDVVSNICGTPKDDFLKVCEYIAeTCVADKTASFLYALGWTQHSVGAQniRTMAMIQLLLGNMGMAGG 440
Cdd:cd02755 247 KAHVKPYTPEWAAQITDIPADTIRRIAREFA-AAAPHAVVDPGWRGTFYSNSFQTR--RAIAIINALLGNIDKRGG 319
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-454 |
5.24e-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: 170.51 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 47 RNTCTY-CSVGCGLLMYSLGDGAKNakesifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRA-PGSDKWQRI 124
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVR-------VEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 125 SWDDAFTRIAKLVKEdrdanfiktndqgvTVNRWLTTGMLCASAASNeTGFLSQK----FSRALGMLAVDNQarVUHGPT 200
Cdd:cd02766 74 SWDEALDTIAAKLKE--------------IKAEYGPESILPYSYAGT-MGLLQRAargrFFHALGASELRGT--ICSGAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 201 VASLAPTFGRgAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTD 280
Cdd:cd02766 137 IEAQKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR-KRGAKVVVIDPYRTATAARADLHIQIRPGTD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 281 IAFLSGVLLYLMTNNKFNREYVEAYTNasllvredfafedglfsGYDAenrkydkttwnyqfdengfakrdvtlqdprcv 360
Cdd:cd02766 215 GALALGVAKVLFREGLYDRDFLARHTE-----------------GFEE-------------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 361 wnlLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02766 246 ---LKAHLETYTPEWAAEITGVSAEEIEELARLYGEA----KPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGG 318
|
410
....*....|....
gi 1778702115 441 GVNALRGHSNIQGL 454
Cdd:cd02766 319 GAFYSNSGPPVKAL 332
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
107-589 |
1.89e-43 |
|
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: 169.99 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 107 RLKYPEYRAPGSDKWQRISWDDAFTRIAklvkedRDANFIKTNdQGVtvnrWLTTGMlcasaASNETGFLSQKFSRALGM 186
Cdd:TIGR01701 99 RLTYPLSLRPGSDHYTPISWDDAYQEIA------AKLNSLDPK-QVA----FYTSGR-----TSNEAAYLYQLFARSLGS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 187 LAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDP------ 260
Cdd:TIGR01701 163 NNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAK-KRGAKIIAINPlrergl 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 261 -RFTRTAS-----------VADFYTPIRSGTDIAFLSGVLLYLMTNNK------FNREYVEAYTNasllvredfafedgl 322
Cdd:TIGR01701 242 eRFWIPQIpesmltgggtqISSEYYQVRIGGDIALFNGVMKLLIEAEDaqpgslIDHEFIANHTN--------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 323 fsgydaenrkydkttwnyqfdenGFAKrdvtlqdprcvwnlLKQHVSRYTPDVVSNICGTPKDDFLKVceyiAETCVADK 402
Cdd:TIGR01701 307 -----------------------GFDE--------------LRRHVLQLNWNDIERSSGLSQEEILEF----AKLLANSR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 403 TASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGLlsqslpgyltlpsekqtdldtyl 482
Cdd:TIGR01701 346 RVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGI----------------------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 483 kantpkallpgqvnyWGNYPKFFvsmmktfygdKAQKDNSWGFDwLPKWdKGYDVLQYFEMMAQGKVNGYFCQGFNPVAS 562
Cdd:TIGR01701 403 ---------------TEKPEEEF----------LARLSQIYGFT-PPDW-PGDTTVAMIEAILTGKVRAFICLGGNFLEA 455
|
490 500
....*....|....*....|....*..
gi 1778702115 563 FPNKNKVVASLSKLKFLVTIDPLNTET 589
Cdd:TIGR01701 456 MPDTAAIERALRQLDLRVHVATKLNRS 482
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
886-1014 |
1.71e-42 |
|
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: 150.74 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 886 DKFPYVGTTYRLTEHFHYW--TKHARLNAIAQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRtlqvh 963
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGtmTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 964 gqeVDTIGIPIHWGYEGvakKGFIANTLTPFVGDANTQTPEFKAFLVNVEK 1014
Cdd:cd00508 76 ---PGTVFMPFHWGGEV---SGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-444 |
3.00e-42 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 161.70 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYslgdgAKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRA--PGSDKWQRISW 126
Cdd:cd02759 3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 127 DDAFTRIA-KLvkedrdaNFIKTNDQGVTVNRWLTTGMLCASAASNETGFLSQKFSRALGMLAVDnqarVUHGPT-VASL 204
Cdd:cd02759 76 DEALDEIAeKL-------AEIKAEYGPESIATAVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGE----SCYWPRdMAHA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 205 APTFGRGAMTNHwvDIKNANLIIVMGGNAAEAHPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFL 284
Cdd:cd02759 145 LTTGFGLGYDEP--DWENPECIVLWGKNPLNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 285 SGVLLYLMTNNKFNREYVEaytnasllvredfafedglfsgydaenrkydktTWNYQFDEngfakrdvtlqdprcvwnlL 364
Cdd:cd02759 223 LGMLNVIINEGLYDKDFVE---------------------------------NWCYGFEE-------------------L 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 365 KQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNA 444
Cdd:cd02759 251 AERVQEYTPEKVAEITGVPAEKIRKAARLYATA----KPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLI 326
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-453 |
3.43e-40 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 157.26 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 51 TYCSVGCG---LLMYSLGDGaknakeSIFHIEGD--PDHPVNRGalCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQR 123
Cdd:cd02765 2 TACPPNCGgrcPLKCHVRDG------KIVKVEPNewPDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 124 ISWDDAFTRIAKLVKEDRD-------ANFIKTNDQGVTvnRWLTTGMLCASAASNETgfLSQKFSRALGMlavdnqarvu 196
Cdd:cd02765 74 ITWDEALDTIADKLTEAKReyggksiLWMSSSGDGAIL--SYLRLALLGGGLQDALT--YGIDTGVGQGF---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 197 hgptvaSLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIR 276
Cdd:cd02765 140 ------NRVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDAR-ENGAKIVVIDPVYSTTAAKADQWVPIR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 277 SGTDIAFLSGVLLYLMTNNKFNREYVEAYTNASLLVREDfafeDGLF---SGYDAENRKYDKTTWNYQFDENG------- 346
Cdd:cd02765 213 PGTDPALALGMINYILEHNWYDEAFLKSNTSAPFLVRED----NGTLlrqADVTATPAEDGYVVWDTNSDSPEpvaatni 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 347 -FAKR-DVTLQDPRC--VWNLLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAEtcvadKTASFLYALGWTQHSV-GAQN 421
Cdd:cd02765 289 nPALEgEYTINGVKVhtVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYAT-----GKPSGIWGFGGVDRYYhSHVF 363
|
410 420 430
....*....|....*....|....*....|....*.
gi 1778702115 422 IRTMAMIQLLLGNMGMAGGGVNALRG----HSNIQG 453
Cdd:cd02765 364 GRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-663 |
7.55e-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: 140.61 E-value: 7.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYSlgDGAKNAKesifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAPGSdkWQRISWDD 128
Cdd:cd02762 3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 129 AFTRIAKLVKEDRDAN------FIKTNDQ-----GVTVNRWLTTGMLCASAASNETGflSQKfsralgmlavdnqarvuh 197
Cdd:cd02762 74 AFDEIAERLRAIRARHggdavgVYGGNPQahthaGGAYSPALLKALGTSNYFSAATA--DQK------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 198 gPTVASLAPTFGRGaMTNHWVDIKNANLIIVMGGNAAEAHpvGFRWAMEAKIHNNA-------KLIVIDPRFTRTASVAD 270
Cdd:cd02762 134 -PGHFWSGLMFGHP-GLHPVPDIDRTDYLLILGANPLQSN--GSLRTAPDRVLRLKaakdrggSLVVIDPRRTETAKLAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 271 FYTPIRSGTDIAFLSGvLLYLMtnnkfnreyveaytnasllvredfaFEDGLfsgydaenrkydkttwnyqFDENGFAKR 350
Cdd:cd02762 210 EHLFVRPGTDAWLLAA-MLAVL-------------------------LAEGL-------------------TDRRFLAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 351 DVTlqdprcvWNLLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAetcvADKTASFLYALGWTQHSVGAQNIRTMAMIQL 430
Cdd:cd02762 245 CDG-------LDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFA----AAPSAAVYGRLGVQTQLFGTLCSWLVKLLNL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 431 LLGNMGMAGGgvnalrghsniqgltdlGLLSQSLpgyltLPSEKQTDLDTYLKANTPKAllpgqvnywgnypkffVSMMK 510
Cdd:cd02762 314 LTGNLDRPGG-----------------AMFTTPA-----LDLVGQTSGRTIGRGEWRSR----------------VSGLP 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 511 TFYGDkaqkdnswgfdwLPkwdkGYDVLQYFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKFLVTIDPLNTETS 590
Cdd:cd02762 356 EIAGE------------LP----VNVLAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETT 419
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778702115 591 nfwqNHGEFNEVDPSQIQTEVFRLPSTCFAeengsiVNSGRWLQwhwKGADAPGEALNDGEILAGIFSRLREM 663
Cdd:cd02762 420 ----RHADYILPPASQLEKPHATFFNLEFP------RNAFRYRR---PLFPPPPGTLPEWEILARLVEALDAV 479
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
49-440 |
5.53e-32 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 131.79 E-value: 5.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYSLGDGAKNakesifhIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRA------PGSDKWQ 122
Cdd:cd02757 5 TCQGCTAWCGLQAYVEDGRVTK-------VEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrDVDPKFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 123 RISWDDAFT----RIAKLVKEDRDANFIktndqgVTVNRWlttgmlcasaaSNETGFLSQKFSRALGMLAVDNQARVUhg 198
Cdd:cd02757 78 PISWDEALDtiadKIRALRKENEPHKIM------LHRGRY-----------GHNNSILYGRFTKMIGSPNNISHSSVC-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 199 ptvaSLAPTFGRGAMTNHW----VDIKNANLIIVMGGNAAEA-HPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYT 273
Cdd:cd02757 139 ----AESEKFGRYYTEGGWdynsYDYANAKYILFFGADPLESnRQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 274 PIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTNASLLVREDFAFEDGLFsgydaenrkydKTTWNYQFDEngfakrdvt 353
Cdd:cd02757 215 PIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGETVDEESF-----------KEKSTEGLVK--------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 354 lqdprcvWnlLKQHVSRYTPDVVSNICGTPKDDFLKVCEYIAETcvADKTASFLYAlGWTQHSVGAQNIRTMAMIQLLLG 433
Cdd:cd02757 275 -------W--WNLELKDYTPEWAAKISGIPAETIERVAREFATA--APAAAAFTWR-GATMQNRGSYNSMACHALNGLVG 342
|
....*..
gi 1778702115 434 NMGMAGG 440
Cdd:cd02757 343 SIDSKGG 349
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
79-449 |
5.28e-31 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 130.14 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 79 EGDPDHPVNRGalCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQRISWDDAFTRIAKLVKEdrdanfIKTN--DQGVT 154
Cdd:cd02770 33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIASELKR------IIEKygNEAIY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 155 VNrwlttgmlCASAASNETGFLSQKFSRALGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGN 232
Cdd:cd02770 105 VN--------YGTGTYGGVPAGRGAIARLLNLTGgyLNYYGTYSWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 233 AAEAHPVGFR---WAMEAKiHNNAKLIVIDPRFTRTASV-ADFYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTna 308
Cdd:cd02770 177 PAETRMGGGGstyYYLQAK-KAGAKFIVIDPRYTDTAVTlADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYC-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 309 sllVREDfafEDGLFSGYDAENRKYDkttwnYQF--DENGFAKrdvtlqdprcvwnllkqhvsryTPDVVSNICGTPKDD 386
Cdd:cd02770 254 ---VGFD---AEHLPEGAPPNESYKD-----YVLgtGYDGTPK----------------------TPEWASEITGVPAET 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778702115 387 FLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGvNALRGHS 449
Cdd:cd02770 301 IRRLAREIATT----KPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGN-TGARPGG 358
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
2-447 |
7.61e-29 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 124.37 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 2 QVSRRQFFKICA-GGMA-GTTVAALGFAPEVALAETRQYKLLRARETRNTCTY-CSVGCGLLMYSLgDGAknakesIFHI 78
Cdd:PRK14990 13 EVSRRGLVKTTAiGGLAmASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVnCGSRCPLRMHVV-DGE------IKYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 79 EGDPDHPVNRGAL-----CPKGAGLVDFIHSESRLKYPEYR--APGSDKWQRISWDDAFTRIA----KLVKEDRDANFI- 146
Cdd:PRK14990 86 ETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYDIIAtnmqRLIKEYGNESIYl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 147 --KTNDQGVTVNR-WLTTGMLCASAASNETGFLSQKFSRALGMLAvdnqarvuhgptvASLAPTFGRGAMTNHWVDIKNA 223
Cdd:PRK14990 166 nyGTGTLGGTMTRsWPPGNTLVARLMNCCGGYLNHYGDYSSAQIA-------------EGLNYTYGGWADGNSPSDIENS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 224 NLIIVMGGNAAEAHPVG---FRWAMEAKIHNNAKLIVIDPRFTRT-ASVADFYTPIRSGTDIAFLSGVLLYLMTNNKFNR 299
Cdd:PRK14990 233 KLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 300 EYVEAYTNAsllvredfafedglfsgydaenrkYDKTTWNYQFDENGFAKRDVTLQDPRCVWNllkqhvsryTPDVVSNI 379
Cdd:PRK14990 313 PFLDKYCVG------------------------YDEKTLPASAPKNGHYKAYILGEGPDGVAK---------TPEWASQI 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778702115 380 CGTPKDDFLKVCEYIAETcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK14990 360 TGVPADKIIKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREG 423
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
102-459 |
1.44e-26 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 117.07 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 102 IHSESRLKYPEYRAPGSDKWQRISWDDAFTRIAKLVKEDRDANFIKTNDQGVTvnrwlttgmlcasaaSNETGFLSQKFS 181
Cdd:PRK09939 103 LEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRT---------------SNEAAFLYQLFA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 182 RALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGFRwAMEAKIHNNAKLIVIDP- 260
Cdd:PRK09939 168 REYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLT-SLRALVKRGAKMIAINPl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 261 ------RFT-----------RTASVADFYTPIRSGTDIAFLSGVLLYLMTNNkfnrEYVEAYTNASLLvreDFAFEDGLF 323
Cdd:PRK09939 247 qergleRFTapqnpfemltnSETQLASAYYNVRIGGDMALLKGMMRLLIERD----DAASAAGRPSLL---DDEFIQTHT 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 324 SGYDAENRKYDKTTWnyqfdengfakrdvtlQDprcvwnllkqhvsrytpdvVSNICGTPKDDFLKVCEYIAetcVADKT 403
Cdd:PRK09939 320 VGFDELRRDVLNSEW----------------KD-------------------IERISGLSQTQIAELADAYA---AAERT 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1778702115 404 AsFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRGHSNIQGLTDLGL 459
Cdd:PRK09939 362 I-ICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI 416
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-440 |
5.25e-26 |
|
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: 114.93 E-value: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYsLGDGaknakeSIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQRISW 126
Cdd:cd02763 3 TCYMCACRCGIRVH-LRDG------KVRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 127 DDAFTRIAKLVKEDRDAN-----FIKTNDQGVTVNRWLTTGMLCASAASNeTGFLSqkFSRALGMLAvdnqarvuhgpTV 201
Cdd:cd02763 76 EEAFSIATKRLKAARATDpkkfaFFTGRDQMQALTGWFAGQFGTPNYAAH-GGFCS--VNMAAGGLY-----------SI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 202 ASLAPTFGRGamtnhwvDIKNANLiIVMGGNAAEAHPVGFRWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTDI 281
Cdd:cd02763 142 GGSFWEFGGP-------DLEHTKY-FMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 282 AFLSGVLLYLMTNNKFNREYVEAYTNASLLVredfafedglfsgydaenrkydkttwnyqfdengfakrdvtlqdprcvw 361
Cdd:cd02763 214 AFILALAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 362 nllkqhvsRYTPDVVSNICGTPKDDFLKVCEYIAETC---------------------VADKTASFLYALGWTQHSVGAQ 420
Cdd:cd02763 245 --------DYTPEWVEKITGIPADTIRRIAKELGVTArdqpielpiawtdvwgrkhekITGRPVSFHAMRGIAAHSNGFQ 316
|
410 420
....*....|....*....|
gi 1778702115 421 NIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02763 317 TIRALFVLMMLLGTIDRPGG 336
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
49-440 |
9.76e-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: 114.36 E-value: 9.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLmyslgdgAK--NAKESIFHIEGDPDHPVN---------------------------RGALCPKGAGLV 99
Cdd:cd02758 3 SCLGCWTQCGIR-------VRvdKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 100 DFIHSESRLKYPEYRA--PGSDKWQRISWDDAFTRIA---KL-----VKEDRDANFIKT------NDQGVTVNrwlttgM 163
Cdd:cd02758 76 QYLYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVVeggDLfgeghVEGLKAIRDLDTpidpdhPDLGPKAN------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 164 LCASAASNE--TGFLSQKFSRALGMLAVDNQARVUHGPTVASLAPTFGRGAMTNHW-VDIKNANLIIVMGGNAAEAHPvG 240
Cdd:cd02758 150 LLYTFGRDEgrTPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGYPHVkPDFDNAEFALFIGTSPAQAGN-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 241 FRWA----MEAKIHNNAKLIVIDPRFTRTASVAD---FYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVE---------- 303
Cdd:cd02758 229 FKRQarrlAEARTEGNFKYVVVDPVLPNTTSAAGeniRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSipskeaakaa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 304 ---AYTNASLLV---REDFAFEdglfsgydaenrkydkttwnyqfdengfakrdvtlqdprcvwnLLKQHVSRYTPDVVS 377
Cdd:cd02758 309 gepSWTNATHLVitvRVKSALQ-------------------------------------------LLKEEAFSYSLEEYA 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778702115 378 NICGTPKDDFLKVCEYIAE--TCVADKTAsflyalGWTQHSVGAQNIRTMAMIQLLLGNMGMAGG 440
Cdd:cd02758 346 EICGVPEAKIIELAKEFTShgRAAAVVHH------GGTMHSNGFYNAYAIRMLNALIGNLNWKGG 404
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-440 |
8.20e-25 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 111.30 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 1 MQVSRRQFFKicaGGMAGTTVAALGFAPEVALAETRQYKLL-RARETRNTCTYCSVGCGLLMYSLGDgaKNakesIFhIE 79
Cdd:PRK15488 1 MSLSRRDFLK---GAGAGCAACALGSLLPGALAANEIAQLKgKTKLTPSICEMCSTRCPIEARVVNG--KN----VF-IQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQRISWDDAFTRIAKlvkedrDANFIKTNDQGVTVnr 157
Cdd:PRK15488 71 GNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAA------KLNAIKQQHGPESV-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 158 wlttgmlcasAASNETGFLSQ---KFSRALGMLAVDNQARVUHGPTVASLAPTFGrGAMTNhwvDIKNANLIIVMGGNAA 234
Cdd:PRK15488 143 ----------AFSSKSGSLSShlfHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 235 EAHPVGF-RWAMEAKIHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTnasllvr 313
Cdd:PRK15488 209 EGINMSDtRGLMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYT------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 314 edfafedglfSGYDAenrkydkttwnyqfdengfakrdvtlqdprcvwnlLKQHVSRYTPDVVSNICGTPKDDFLKVCEY 393
Cdd:PRK15488 282 ----------SGFEE-----------------------------------LAASVKEYTPEWAEAISDVPADDIRRIARE 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1778702115 394 IAET---CVAD--KTASFlyalgwTQHSVgaQNIRTMAMIQLLLGNMGMAGG 440
Cdd:PRK15488 317 LAAAaphAIVDfgHRATF------TPEEF--DMRRAIFAANVLLGNIERKGG 360
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
897-1006 |
1.22e-24 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 98.93 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 897 LTEHFH--YWTKHARLNAIaQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRtlqvhgqeVDTIGIPI 974
Cdd:cd02775 1 LRDHFHsgTRTRNPWLREL-APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVP--------PGVVFLPH 71
|
90 100 110
....*....|....*....|....*....|..
gi 1778702115 975 HWGYEGvaKKGFIANTLTPFVGDANTQTPEFK 1006
Cdd:cd02775 72 GWGHRG--GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
107-653 |
1.57e-24 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 106.33 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 107 RLKYPEYRApGSDKWQRISWDDAFTRIAKLVKEDRDANfiktNDQGVTVNRWlttgmlCASAASNETGFLSQKFSRALGM 186
Cdd:pfam00384 1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIKKY----GPDAIAINGG------SGGLTDVESLYALKKLLNRLGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 187 LAV---DNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMGGNAAEAHPVGfrWAME--AKIHNNAKLIVIDPR 261
Cdd:pfam00384 70 KNGnteDHNGDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPIL--NARIrkAALKGKAKVIVIGPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 262 FTRTasVADFYTPIRSGTDIAFLSGVLLYLMTNNkfnreyveaytnasllvredfafedglfsgydaenrKYDKTtwnyq 341
Cdd:pfam00384 148 LDLT--YADEHLGIKPGTDLALALAGAHVFIKEL------------------------------------KKDKD----- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 342 fdengFAKRdvtlqdprcvwnllkqhvsrytpdvvsnicgtpkddflkvceyiaetcvadktASFLYALGWTQHSVGAQN 421
Cdd:pfam00384 185 -----FAPK-----------------------------------------------------PIIIVGAGVLQRQDGEAI 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 422 IRTMAMIQLLLGNMGMAGGGVNALR---GHSNIQGLTDLGLlsqslpgyltlpsekqtdldtylkantpkallpgqvnyw 498
Cdd:pfam00384 207 FRAIANLADLTGNIGRPGGGWNGLNilqGAASPVGALDLGL--------------------------------------- 247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 499 gnypkffvsmmktfygdkaqkdnswgfdwlpkwDKGYDVLQYFEMMAQGKVNGYFCQGFNPVASFPNKNKVVASLSKLKF 578
Cdd:pfam00384 248 ---------------------------------VPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDL 294
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778702115 579 LVTIDP-LNTETSNFwqnhgefnevdpSQIqtevfRLPSTCFAEENGSIVNSGRWLQwHWKGA-DAPGEALNDGEIL 653
Cdd:pfam00384 295 FVVYDGhHGDKTAKY------------ADV-----ILPAAAYTEKNGTYVNTEGRVQ-STKQAvPPPGEAREDWKIL 353
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-447 |
7.27e-24 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 108.45 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 1 MQVSRRQFFKICAggmAGTTVAALGFA-PEVALAETRQyKLLRARETRNTCTYCSVGCGLLMyslgdGAKNAKesIFHIE 79
Cdd:PRK13532 1 MKLSRRDFMKANA---AAAAAAAAGLSlPAVANAVVGS-AQTAIKWDKAPCRFCGTGCGVLV-----GTKDGR--VVATQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKYP-------EYRAPGsdKWQRISWDDAFTRIAKLVKEdrdanfiKTNDQG 152
Cdd:PRK13532 70 GDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFKK-------ALKEKG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 153 VTvnrwlTTGMLCASAASNETGFLSQKFSRAlGMLA--VDNQARVUHGPTVASLAPTFGRGAMTNHWVDIKNANLIIVMG 230
Cdd:PRK13532 141 PT-----AVGMFGSGQWTIWEGYAASKLMKA-GFRSnnIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 231 GNAAEAHPVgfRWA--MEAKI-HNNAKLIVIDPRFTRTASVADfyTPI--RSGTDIAFLSGVLLYLMTNNKFNREYVEAY 305
Cdd:PRK13532 215 SNMAEMHPI--LWSrvTDRRLsNPDVKVAVLSTFEHRSFELAD--NGIifTPQTDLAILNYIANYIIQNNAVNWDFVNKH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 306 TNASLLVrEDFAF----EDGLFSgyDAENRKYDKTTWNYQFDEngFAKrdvtlqdprcvwnllkqHVSRYTPDVVSNICG 381
Cdd:PRK13532 291 TNFRKGA-TDIGYglrpTHPLEK--AAKNPGTAGKSEPISFEE--FKK-----------------FVAPYTLEKTAKMSG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778702115 382 TPKDDFLKVCEYIAETCVadKTASFlYALGWTQHSVG--AQNIrtMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:PRK13532 349 VPKEQLEQLAKLYADPNR--KVVSF-WTMGFNQHTRGvwANNL--VYNIHLLTGKISTPGNGPFSLTG 411
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
82-447 |
3.94e-21 |
|
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: 97.77 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 82 PDH-PvnRGalCPKGAGLVDFIHSESRLKYPEYRAP--GSDKWQRISWDDAFTRIAklvkeDRDANFIKTN--DQGVTVN 156
Cdd:cd02750 44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELIA-----DAIIDTIKKYgpDRVIGFS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 157 RWLTTGMLCASAASnetgflsqKFSRALGMLAVDNQARVUHGPTVASLapTFGRGAMTNHWVDIKNANLIIVMGGNAAEA 236
Cdd:cd02750 115 PIPAMSMVSYAAGS--------RFASLIGGVSLSFYDWYGDLPPGSPQ--TWGEQTDVPESADWYNADYIIMWGSNVPVT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 237 HPVGFRWAMEAKiHNNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSGVLLYLMTNNKFNREYVEAYTNASLLVredf 316
Cdd:cd02750 185 RTPDAHFLTEAR-YNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDLPFLV---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 317 afedglfsgydaenrkydkttwnyqfdengfakrdvtlqdprcvwnllkqhvsrYTPDVVSNICGTPKDDFLKVCEYIAE 396
Cdd:cd02750 260 ------------------------------------------------------YTPAWQEAITGVPRETVIRLAREFAT 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 397 TcvadKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALRG 447
Cdd:cd02750 286 N----GRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG 332
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
886-1015 |
6.56e-21 |
|
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: 89.17 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 886 DKFPYVGTTYRLTEHFHYWT---KHARLNAIAqPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTLQV 962
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTrtgRVPRLNAHV-PEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1778702115 963 HgqevdtigIPIHWGYEGVAKKGfiANTLTPFVGDANTQTPEFKAFLVNVEKV 1015
Cdd:cd02791 80 F--------VPMHWGDQFGRSGR--VNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
92-465 |
7.28e-21 |
|
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: 98.07 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 92 CPKGAGLVDFIHSESRLKYPEYR------------APGSDKWQRISWDDAFTRIAKLVKEDRDA--Nfiktndqgvtvnr 157
Cdd:cd02751 32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLVASELKRIREKygN------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 158 wltTGMLCASAasneTGFLSQKFSRALGMLAvdnqaRV--UHGPTVASLAP---------------TFGRGAMTNHWVDI 220
Cdd:cd02751 99 ---EAIFGGSY----GWASAGRLHHAQSLLH-----RFlnLIGGYLGSYGTystgaaqvilphvvgSDEVYEQGTSWDDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 221 -KNANLIIVMGGNAAE--------AHPVGFRWAMEAKiHNNAKLIVIDPRFTRTASV-ADFYTPIRSGTDIAFLSGVLLY 290
Cdd:cd02751 167 aEHSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAK-DAGVRFICIDPRYTDTAAVlAAEWIPIRPGTDVALMLAMAHT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 291 LMTNNKFNREYVEAYTnasllvredfafedglfSGYDAENR----KYDKTtwnyqfdengfAKrdvtlqdprcvwnllkq 366
Cdd:cd02751 246 LITEDLHDQAFLARYT-----------------VGFDEFKDyllgESDGV-----------PK----------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 367 hvsryTPDVVSNICGTPKDDFLKVCEYIaetcvADKTASFLYALGWTQHSVGAQNIRTMAMIQLLLGNMGMAGGGVNALR 446
Cdd:cd02751 281 -----TPEWAAEITGVPAETIRALAREI-----ASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY 350
|
410
....*....|....*....
gi 1778702115 447 GHSNIQGLTDLGLLSQSLP 465
Cdd:cd02751 351 GYSNGGGPPRGGAGGPGLP 369
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
886-1014 |
2.47e-19 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 84.60 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 886 DKFPYVGTTYRLTEHFHYW--TKHAR-LNAIAqPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTLQV 962
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGtmTRRAEgLDAIA-PEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1778702115 963 HgqevdtigIPIHWgYEGVakkgfiANTLTPFVGDANTQTPEFKAFLVNVEK 1014
Cdd:cd02790 80 F--------MPFHF-AEAA------ANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
893-1009 |
2.18e-18 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 81.55 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 893 TTYRLTEHFHYWTKHARLNAIAQPEQ-FVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTlqvhgqevDTIG 971
Cdd:pfam01568 4 ITGRVLGQYHSQTRTRRVLRLAKPEPeVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--------GVVF 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1778702115 972 IPIHWGYEgvaKKGFIANTLTPFVGDANTQTPEFKAFL 1009
Cdd:pfam01568 76 MPFGWWYE---PRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
44-104 |
6.38e-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: 78.45 E-value: 6.38e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 44 RETRNTCTYCSVGCGLLMYSlgdgaKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 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 |
3.87e-17 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 76.18 E-value: 3.87e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 44 RETRNTCTYCSVGCGLLMYSlgdgaKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHS 104
Cdd:pfam04879 2 KVVKTICPYCGVGCGLEVHV-----KDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
50-399 |
5.95e-15 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 79.63 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 50 CTYCSVGCGLLMYSLGDGAknakesIFHIEGDPD----HPVnRGALCPKGAGLVDFIHSESRLKYPEYRA---------P 116
Cdd:cd02760 4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 117 GsdkWQRISWDDAFTRIAKLVKEDRDANFikTNDQGV-----TVNRWLTTGMLCASAASNETGFLSQKFSRALGMLAVDN 191
Cdd:cd02760 77 G---FVPISWDEALDLVAAKLRRVREKGL--LDEKGLprlaaTFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQGVKCV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 192 QARVUHGptvaslaptfgrGAMTNHWV---DIKNANLIIVMGGNA-AEAHPVGFRWAMEAKIHNnAKLIVIDPRFTRTAS 267
Cdd:cd02760 152 HSEHLYG------------EFWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVRG-YKRVQVEPHLSVTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 268 VADFYTPIRSGTDIAF---LSGVLLYLMTNNKFNREYVEAYTNASLLVRedfafEDGLFSgYDAENRKydKTTWNYQ--- 341
Cdd:cd02760 219 CSAEWVPIRPKTDPAFmfaMIHVMVHEQGLGKLDVPFLRDRTSSPYLVG-----PDGLYL-RDAATGK--PLVWDERsgr 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 342 ---FDENGF--------------------AKRDVTLQDPRCVWNLLKQHVSRYTPDVVSNICGTPKDDFLKVC-EYIAET 397
Cdd:cd02760 291 avpFDTRGAvpavagdfavdgavsvdaddETAIHQGVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIArEFLENA 370
|
..
gi 1778702115 398 CV 399
Cdd:cd02760 371 SI 372
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
50-288 |
1.98e-14 |
|
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: 76.17 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 50 CTYCSVGCGLLMyslgdGAKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRapGSDKWQRISWDDA 129
Cdd:cd02768 4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 130 FTRIAKLVKEdrdanfIKTNDQGVTVNrwlttgmlcaSAASNETGFLSQKFSRALGMLAVDNQARvuhGPTVASLAPTFG 209
Cdd:cd02768 75 LKTVAEGLKA------VKGDKIGGIAG----------PRADLESLFLLKKLLNKLGSNNIDHRLR---QSDLPADNRLRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 210 RGAMTNHWVDIKNANLIIVMGGNAAEAHPVgfrwaMEAKI-----HNNAKLIVIDPRFTRTasVADF-YTPIRSGTDIAF 283
Cdd:cd02768 136 NYLFNTSIAEIEEADAVLLIGSNLRKEAPL-----LNARLrkavkKKGAKIAVIGPKDTDL--IADLtYPVSPLGASLAT 208
|
....*
gi 1778702115 284 LSGVL 288
Cdd:cd02768 209 LLDIA 213
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
43-291 |
6.87e-14 |
|
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: 75.98 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 43 ARETRNTCTYCSVGCGLLMYS---LGDGAKNAKESIF--------------------------------HIEGDPDH--P 85
Cdd:cd02756 10 AERYNVTCHFCIVGCGYHVYVwpvGEEGGPSPGQNAIgydlvdqvpplnlqwypktmhyvvvtqdgrevYIVIVPDKecP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 86 VNRGALCPKGAGLVDFIHS------ESRLKYPEYRApgSDKWQRISWDDAFTRIAKLVKEDRDAnfiKTNDQGVTVNRW- 158
Cdd:cd02756 90 VNSGNYSTRGGTNAERIWSpdnrvgETRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGILDK---DGNDDAVFASRFd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 159 -----------LTTGMLCASAasnetgfLSQKFSRalgmlaVDNqaRVUHGPTVASLAPTfGRGAMTNHWVDIKNANLII 227
Cdd:cd02756 165 hggggggfennWGVGKFFFMA-------LQTPFVR------IHN--RPAYNSEVHATREM-GVGELNNSYEDARLADTIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 228 VMGGNAAEAHPVGF-----------------RWAMEAKIHNNAKLIVIDPRFTRTASVAD--------FYTPIRSGTDIA 282
Cdd:cd02756 229 LWGNNPYETQTVYFlnhwlpnlrgatvsekqQWFPPGEPVPPGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTA 308
|
....*....
gi 1778702115 283 FLSGVLLYL 291
Cdd:cd02756 309 LANAIARYI 317
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
49-239 |
8.85e-14 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 75.12 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMyslgdGAKNAKesIFHIEGDPDHPVNRGALCPKGAGLVDFIHSESRLKYPEYRapGSDKWQRISWDD 128
Cdd:cd02771 3 ICHHCSVGCNISL-----GERYGE--LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 129 AFTRIAKLVKEDRDAnfiktndqgvtvnrwltTGMLCASAASNETGFLSQKFSR-ALGMLAVDNQARvuhgPTVASLAPT 207
Cdd:cd02771 74 ALDVAAARLKEAKDK-----------------VGGIGSPRASNESNYALQKLVGaVLGTNNVDHRAR----RLIAEILRN 132
|
170 180 190
....*....|....*....|....*....|..
gi 1778702115 208 FGRGAMTNHwvDIKNANLIIVMGGNAAEAHPV 239
Cdd:cd02771 133 GPIYIPSLR--DIESADAVLVLGEDLTQTAPR 162
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
888-983 |
2.96e-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: 56.53 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 888 FPYVGTTYRLTEHFHYWTKHARLNAIaQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTlqvhgqev 967
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEI-KPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRP-------- 71
|
90
....*....|....*....
gi 1778702115 968 DTIGIPI---HWGYEGVAK 983
Cdd:cd02780 72 GVVAIEHgygHWAYGAVAS 90
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
5-288 |
3.97e-09 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 60.20 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 5 RRQFFKICAGGMAGTTVAALG-----FAPEVALAETRQykLLRARETRNTCTYCSVGCGLLMySLGDGAKnakesiFHIE 79
Cdd:cd02764 1 RRGFLKLMGASLAMASAAACRypvekIVPYVIWPENIV--PGETVYYATSLVPAGEGQGVLV-KTVDGRP------IKIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 80 GDPDHPVNRGALCPKGAGLVDFIHSESRLKYPeYRAPGSDKWQRISWDDAftriAKLVKEDRDANfiktNDQGVTVnrwL 159
Cdd:cd02764 72 GNPDHPASLGGTSARAQASVLSLYDPDRAQGP-LRRGIDGAYVASDWADF----DAKVAEQLKAV----KDGGKLA---V 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 160 TTGMLCASAASNETGFLSQKFSRALGMLAVDNQArvuhGPTVASLAPTFGRGAMTNHwvDIKNANLIIVMGGNAAEAHPV 239
Cdd:cd02764 140 LSGNVNSPTTEALIGDFLKKYPGAKHVVYDPLSA----EDVNEAWQASFGKDVVPGY--DFDKAEVIVSIDADFLGSWIS 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1778702115 240 GFRWA---MEAKIH----NNAKLIVIDPRFTRTASVADFYTPIRSGTDIAFLSGVL 288
Cdd:cd02764 214 AIRHRhdfAAKRRLgaeePMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLA 269
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
888-1014 |
2.61e-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: 53.47 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 888 FPYVGTTYRLTEHFHywTKHARLNAIAQ--PEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTLQVHGQ 965
Cdd:cd02781 3 PLILTTGARSYYYFH--SEHRQLPSLRElhPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1778702115 966 EvdtiGipiHWGYEGVAKKGFI-------ANTLT------PFVGDANtqtpeFKAFLVNVEK 1014
Cdd:cd02781 81 H----G---WWYPEREAGEPALggvwesnANALTsddwndPVSGSSP-----LRSMLCKIYK 130
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
910-1014 |
1.89e-07 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 50.74 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 910 LNAIAqPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIRTlqvhgqevDTIGIPIHWGYegVAKKGFIA- 988
Cdd:cd02778 23 LHELT-PENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--------DTVFMPHGFGH--WAPALSRAy 91
|
90 100 110
....*....|....*....|....*....|..
gi 1778702115 989 ------NTLTPFVGDANTQTPEFKAFLVNVEK 1014
Cdd:cd02778 92 gggvndNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-306 |
2.19e-07 |
|
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: 54.96 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 79 EGDPDhPvnrgalCPKGAGLVDFIHSESRLKYPEYR-------------APGSDKWQRISWDDAFTRIAKLVKEDRDA-- 143
Cdd:cd02769 25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTyg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 144 -NFIKTNDQGvtvnrWLTTGML------------CASAASNETGFLSQKFSRA-----LGMLAVDNQARVUHgPTVAS-- 203
Cdd:cd02769 98 nEAIFGGSYG-----WSSAGRFhhaqsllhrflnLAGGYVGSVGDYSTGAAQVilphvVGSMEVYTEQQTSW-PVIAEht 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 204 -LAPTFGRGAMTNHWVdiknanliivmGGNAAEAHPV--GFRWAMEAKIhnnaKLIVIDPRFTRTASVADF-YTPIRSGT 279
Cdd:cd02769 172 eLVVAFGADPLKNAQI-----------AWGGIPDHQAysYLKALKDRGI----RFISISPLRDDTAAELGAeWIAIRPGT 236
|
250 260
....*....|....*....|....*..
gi 1778702115 280 DIAFLSGVLLYLMTNNKFNREYVEAYT 306
Cdd:cd02769 237 DVALMLALAHTLVTEGLHDKAFLARYT 263
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
887-958 |
5.57e-07 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 49.29 E-value: 5.57e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778702115 887 KFPYVGTTYRLTEHFHywTKHARLNAI--AQPEQFVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIR 958
Cdd:cd02785 1 KYPLACIQRHSRFRVH--SQFSNVPWLleLQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQ 72
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
49-285 |
6.40e-07 |
|
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: 53.11 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 49 TCTYCSVGCGLLMYSLGDGAKNAKESIfhiegdpdhpvnrgalCPKG-AGLVDFIHSesrlkYPEYRAPGSDkwqrISWD 127
Cdd:cd02761 3 VCPFCGLLCDDIEVEVEDNKITKVRNA----------------CRIGaAKFARYERR-----ITTPRIDGKP----VSLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 128 DAFTRIAKLVKEDRDANFiktndqgvtvnrwlttGMLCASaaSNETgflsQKFSRALGMLA---VDNQARVUHGPTVASL 204
Cdd:cd02761 58 EAIEKAAEILKEAKRPLF----------------YGLGTT--VCEA----QRAGIELAEKLgaiIDHAASVCHGPNLLAL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 205 APtfgRGAMTNHWVDIKN-ANLIIVMGGNAAEAHP------VGFRWAMEAKIHNNA-KLIVIDPRFTRTASVADFYTPIR 276
Cdd:cd02761 116 QD---SGWPTTTLGEVKNrADVIVYWGTNPMHAHPrhmsrySVFPRGFFREGGREDrTLIVVDPRKSDTAKLADIHLQID 192
|
....*....
gi 1778702115 277 SGTDIAFLS 285
Cdd:cd02761 193 PGSDYELLA 201
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
104-260 |
3.37e-06 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 50.82 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 104 SESRLKYPEYRAPGsdKWQRISWDDAFTRIA---KLVKEDRDANFIktndqgvtvnrwlttGMLCASAASNETGFLSQKF 180
Cdd:cd02772 51 SEDRLTKPMIKKDG--QWQEVDWETALEYVAeglSAIIKKHGADQI---------------GALASPHSTLEELYLLQKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 181 SRALGMLAVDNQARVUHGPTVASLAPTFGrgaMTNHWVDIKNANLIIVMGGNAAEAHP-VGFRWAMEAKihNNAKLIVID 259
Cdd:cd02772 114 ARGLGSDNIDHRLRQSDFRDDAKASGAPW---LGMPIAEISELDRVLVIGSNLRKEHPlLAQRLRQAVK--KGAKLSAIN 188
|
.
gi 1778702115 260 P 260
Cdd:cd02772 189 P 189
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
927-1014 |
1.28e-05 |
|
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: 45.65 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778702115 927 AEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIR--TLQV-HGQEVDTIGIPihwgyeGVAKKGFIaNTLTPFVGD------ 997
Cdd:cd02777 43 AAARGIKDGDIVRVFNDRGAVLAGARVTDRIMpgVVALpEGAWYDPDDNG------GLDKGGNP-NVLTSDIPTsklaqg 115
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90
....*....|....*....
gi 1778702115 998 --ANTQtpefkafLVNVEK 1014
Cdd:cd02777 116 npANTC-------LVEIEK 127
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
905-963 |
2.07e-04 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 42.24 E-value: 2.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778702115 905 TKHARLNAIAQPEQfVEIGEKLAEKKGIKQGDTVKVSSNRGYIKAKAVVTKRIR--TLQVH 963
Cdd:cd02793 21 GSLSRAYKVQGREP-IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMpgVVQLP 80
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| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
927-957 |
2.07e-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: 2.07e-03
10 20 30
....*....|....*....|....*....|.
gi 1778702115 927 AEKKGIKQGDTVKVSSNRGYIKAKAVVTKRI 957
Cdd:cd02794 39 AAARGIKDGDRVLVFNDRGKVIRPVKVTERI 69
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