|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
112-860 |
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: 894.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNG--KYQRISWDQALDEI 189
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 190 SAKLKQIRQET------------GPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVANTWGYGAM 257
Cdd:cd02752 81 ARKMKDIRDASfveknaagvvvnRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARIUHSPTVAGLANTFGRGAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 258 TNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKES-GCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFq 336
Cdd:cd02752 161 TNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKnGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMINYII- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 337 ngwedkkyladrvygmdkvkeevlaKWTPDKVEEVCGVPEAEVRYVAETMAKN----RPSTLVWCMGQTQHTIGNAIVRA 412
Cdd:cd02752 240 -------------------------RYTPEEVEDICGVPKEDFLKVAEMFAATgrpdKPGTILYAMGWTQHTVGSQNIRA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 413 SCIVQLALGNIGVSGGGANIFRGHDNVQGATDVGPNPDSLPGYYGlaagawkhfatvwgvdyewikkqfasqammeksgt 492
Cdd:cd02752 295 MCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG----------------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 493 tvsrwidivtekpelidqdhnvrgvffwGHAPNSQTRGL-EMKRALDKLDLLVVIDPYPSATAAMANMPATegDTPNPNR 571
Cdd:cd02752 340 ----------------------------GQNPNSSFPNAnKVRRALDKLDWLVVIDPFPTETAAFWKNPGM--DPKSIQT 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 572 AVYLLPACTQFETSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFANELSKNYKLVEV-KRAGRTWREPETE 650
Cdd:cd02752 390 EVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPItKWNYGYGDEPTPE 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 651 SILREINAGNWTIGYTGQSPERLKAHMRNMHMFDvrSLRCKGGKDPVTGY-------------------DITGDYFGLPW 711
Cdd:cd02752 470 EIAREINGGALTDGYTGQSPERLKAHGQNVHTFD--TLRDDGSTACGCWIysgsyteegrmarrdtsdpDGLGLYPGWPW 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 712 PCYGTpelkhpgSPNLYDTSRNVMDGggnfranfgverdgvsllaadgshslgadiTTGYPEFDAVLLKKLGWWdeltda 791
Cdd:cd02752 548 PWPVN-------RRILYNRASVDMEG------------------------------KPGYPERPLVEWDGLGWW------ 584
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737919411 792 ekkaadgknWKTDLSGGIQRvVMKNHGCHPFGNAR---ARAVVWNFPDPIPQHREPLYSTRPD---MVAKYPTHD 860
Cdd:cd02752 585 ---------WKGDVPDGPWP-AAKEHGCGPFIMAPegqARLFVWNFDGPFPEHYEPLESPRPDlhsKVAKNPTYK 649
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
112-1025 |
9.62e-172 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 518.28 E-value: 9.62e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQRISWDQALDEISA 191
Cdd:COG3383 8 KTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALDLVAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 192 KLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWV-SFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAA 270
Cdd:COG3383 88 RLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLArGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 271 LYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVY 350
Cdd:COG3383 168 LVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 351 GMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGA 430
Cdd:COG3383 248 GFEELKASV-AKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 431 NIFRGHDNVQGATDVGPNPDSLPGYYGLA-AGAWKHFATVWGVDyewikkqfasqAMMEKSGTTVsrwidivtekPELID 509
Cdd:COG3383 327 FPLTGQNNVQGGRDMGALPNVLPGYRDVTdPEHRAKVADAWGVP-----------PLPDKPGLTA----------VEMFD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 510 QDHN--VRGVFFWG-----HAPNSQtrglEMKRALDKLDLLVVIDPYPSATAAMANMpategdtpnpnravyLLPACTQF 582
Cdd:COG3383 386 AIADgeIKALWIIGenpavSDPDAN----HVREALEKLEFLVVQDIFLTETAEYADV---------------VLPAASWA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 583 ETSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFAnelsknyklvevkragrtWREPETESILREINAGnwT 662
Cdd:COG3383 447 EKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLGYG------------------FDYDSPEEVFDEIARL--T 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 663 IGYTGQSPERLKAHMrnmhmfdvrslrckggkdpvtgyditgdyfGLPWPCygtPELKHPGSPNLYDtsrnvmdggGNFr 742
Cdd:COG3383 507 PDYSGISYERLEALG------------------------------GVQWPC---PSEDHPGTPRLFT---------GRF- 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 743 anfgverdgvsllaadgshslgadittgypefdavllkklgwwdeltdaekkaadgknwktdlsggiqrvvmknhgCHPF 822
Cdd:COG3383 544 ----------------------------------------------------------------------------PTPD 547
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 823 GNARARAVvwnfpdpipQHREPlySTRPDmvakypthddkmafwrlptlyktvqqrnienkvyEKFPIILTSGRLVEYEG 902
Cdd:COG3383 548 GKARFVPV---------EYRPP--AELPD----------------------------------EEYPLVLTTGRLLDQWH 582
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 903 GGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPFHFSgwwqgkdlkp 982
Cdd:COG3383 583 TGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRG-EVVLRARVTDRVRPGTVFMPFHWG---------- 651
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 737919411 983 yypegampivrGEAVNTATTYGYDSVTMMQETKTTVCQIERFA 1025
Cdd:COG3383 652 -----------EGAANALTNDALDPVSKQPEYKACAVRVEKVA 683
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
112-743 |
7.52e-151 |
|
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: 457.83 E-value: 7.52e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQRISWDQALDEISA 191
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 192 KLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWV-SFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAA 270
Cdd:cd02753 81 RLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLArAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 271 LYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVY 350
Cdd:cd02753 161 LVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 351 GMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGA 430
Cdd:cd02753 241 GFEELKEIV-EKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 431 NIFRGHDNVQGATDVGPNPDSLPGYyglaagawkhfatvwgvdyewIKkqfasqAMMeksgttvsrwidIVTEKPELIDq 510
Cdd:cd02753 320 NPLRGQNNVQGACDMGALPNVLPGY---------------------VK------ALY------------IMGENPALSD- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 511 dhnvrgvffwghaPNSQtrglEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGSCTA 590
Cdd:cd02753 360 -------------PNTN----HVRKALESLEFLVVQDIFLTETAELAD---------------VVLPAASFAEKDGTFTN 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 591 SNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFanelsknyklvevkragrTWREPETESILREINAgnWTIGYTGQSP 670
Cdd:cd02753 408 TERRVQRVRKAVEPPGEARPDWEIIQELANRLGY------------------PGFYSHPEEIFDEIAR--LTPQYAGISY 467
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737919411 671 ERLKAHMrnmhmfdvrslrckggkdpvtgyditgdyfGLPWPCygtPELKHPGSPNLYDTSRNVMDGGGNFRA 743
Cdd:cd02753 468 ERLERPG------------------------------GLQWPC---PDEDHPGTPILHTERFATPDGKARFMP 507
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
113-1021 |
6.80e-145 |
|
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: 448.07 E-value: 6.80e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQRISWDQALDEISAK 192
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAISYIAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 193 LKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWV-SFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAAL 271
Cdd:TIGR01591 81 LKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLArAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENADLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 272 YIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVYG 351
Cdd:TIGR01591 161 IIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKRTEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 352 MDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGAN 431
Cdd:TIGR01591 241 FEEFREIV-KGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 432 IFRGHDNVQGATDVGPNPDSLPGYYGLAAGAW-KHFATVWGVdyewikkqfasqammEKSGTTVSRWIdivtekPELIDQ 510
Cdd:TIGR01591 320 PLRGQNNVQGACDMGALPDFLPGYQPVSDEEVrEKFAKAWGV---------------VKLPAEPGLRI------PEMIDA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 511 --DHNVRGVFFWGHAP-NSQTRGLEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGS 587
Cdd:TIGR01591 379 aaDGDVKALYIMGEDPlQSDPNTSKVRKALEKLELLVVQDIFMTETAKYAD---------------VVLPAAAWLEKEGT 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 588 CTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFanelsknyklvevkragrTWREPETESILREINagNWTIGYTG 667
Cdd:TIGR01591 444 FTNAERRIQRFFKAVEPKGESKPDWEIIQELANALGL------------------DWNYNHPQEIMDEIR--ELTPLFAG 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 668 QSPERLkahmrnmhmfdvrslrckggkdpvtgyditGDYFGLPWPCygTPELKHPgSPNLYdtsrnvmdgggnfranfgv 747
Cdd:TIGR01591 504 LTYERL------------------------------DELGSLQWPC--NDSDASP-TSYLY------------------- 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 748 erdgvsllaadgshslgadittgypefdavllkklgwwdeltdaekkaadgknwktdlsggiqrvvmKNHGCHPFGNARA 827
Cdd:TIGR01591 532 -------------------------------------------------------------------KDKFATPDGKAKF 544
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 828 RAVVWNFPDpipqhreplystrpdmvakypthddkmafwrlptlyktvqqrnieNKVYEKFPIILTSGRLVEYEGGGEET 907
Cdd:TIGR01591 545 IPLEWVAPI---------------------------------------------EEPDDEYPLILTTGRVLTHYNVGEMT 579
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 908 RSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPFHFsgwwqgkdlkpyypeg 987
Cdd:TIGR01591 580 RRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRG-EITLRAKVSDRVNKGAIYITMHF---------------- 642
|
890 900 910
....*....|....*....|....*....|....
gi 737919411 988 ampivRGEAVNTATTYGYDSVTMMQETKTTVCQI 1021
Cdd:TIGR01591 643 -----WDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
110-1023 |
2.14e-144 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 446.98 E-value: 2.14e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 110 VRRTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVN----GKYQRISWDQA 185
Cdd:COG0243 23 TVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGKFERISWDEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 186 LDEISAKLKQIRQETGPDSLFFIGSSKH----SNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSY 261
Cdd:COG0243 103 LDLIAEKLKAIIDEYGPEAVAFYTSGGSagrlSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 262 NDMQNAKAALYIGSNAAEAHPVSMLHLLHA-KESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWE 340
Cdd:COG0243 183 EDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVLIEEGLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 341 DKKYLADRVYGMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLAL 420
Cdd:COG0243 263 DRDFLARHTVGFDELAAYV-AAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 421 GNIGVSGGGANIFRGHdnvqgatdvgpnpdslpgyyglaagawkhfatvwgvdyewikkqfasqAMMEKsgttvsrwidi 500
Cdd:COG0243 342 GNIGKPGGGPFSLTGE------------------------------------------------AILDG----------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 501 vtekpelidQDHNVRGVFFWG-----HAPNSQtrglEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYL 575
Cdd:COG0243 363 ---------KPYPIKALWVYGgnpavSAPDTN----RVREALRKLDFVVVIDTFLTETARYAD---------------IV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 576 LPACTQFETSG-SCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFANELsknyklvevkragrTWREPEtESILR 654
Cdd:COG0243 415 LPATTWLERDDiVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAF--------------PWGRTE-EDYLR 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 655 EinagnwtigytgqsperlkahmrnmhmfdvrslrckggkdpvtgyditgdyfglpwpcygtpelkhpgspnLYDTSRnv 734
Cdd:COG0243 480 E-----------------------------------------------------------------------LLEATR-- 486
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 735 mdgggnfranfgverdgvsllaadgshslGADITtgypeFDAvlLKKLGWWDELTDAEKKAADGKNWKTDlSGgiqrvvm 814
Cdd:COG0243 487 -----------------------------GRGIT-----FEE--LREKGPVQLPVPPEPAFRNDGPFPTP-SG------- 522
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 815 knhgchpfgnaRAR-AVVWNFPDPIPQHREPLYSTRPDmvakypthddkmafwrlptlyktvqqrnienkvYEKFPIILT 893
Cdd:COG0243 523 -----------KAEfYSETLALPPLPRYAPPYEGAEPL---------------------------------DAEYPLRLI 558
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 894 SGRLVE-YEGGgeeTRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPFhfs 972
Cdd:COG0243 559 TGRSRDqWHST---TYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRG-EVLARAKVTEGIRPGVVFAPH--- 631
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 737919411 973 GWWQGKDLKpyypegampivRGEAVNTATTYGYDSVTMMQETKTTVCQIER 1023
Cdd:COG0243 632 GWWYEPADD-----------KGGNVNVLTPDATDPLSGTPAFKSVPVRVEK 671
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
112-622 |
1.05e-120 |
|
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: 373.97 E-value: 1.05e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVN--GKYQRISWDQALDEI 189
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 190 SAKLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVAnTWGYGAMTNSYNDMQNAKA 269
Cdd:cd00368 81 AEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALK-AFGGGAPTNTLADIENADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 270 ALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGvlyhifqngwedkkyladrv 349
Cdd:cd00368 160 ILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA-------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 350 ygmdkvkeevlakwtpDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGG 429
Cdd:cd00368 220 ----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 430 anIFRGHDNVQgatdvgpnpdslpgyyglaagawkhfatvwgvdyewikkqfasqammeksgttvsrwidivtekpelid 509
Cdd:cd00368 284 --LGPGGNPLV--------------------------------------------------------------------- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 510 qdhnvrgvffwgHAPNSQtrglEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGSCT 589
Cdd:cd00368 293 ------------SAPDAN----RVRAALKKLDFVVVIDIFMTETAAYAD---------------VVLPAATYLEKEGTYT 341
|
490 500 510
....*....|....*....|....*....|...
gi 737919411 590 ASNRSLQWREKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd00368 342 NTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
112-732 |
1.17e-107 |
|
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: 346.52 E-value: 1.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPM-KLVNGKYQRISWDQALDEIS 190
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLlRRNGGELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 191 AKLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWV-SFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKA 269
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAkGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDIEHADC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 270 ALYIGSNAAEAHPVSMLHLLHAKES--GCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLAD 347
Cdd:cd02754 161 FFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 348 RVYGMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSG 427
Cdd:cd02754 241 HTEGFEELKAFV-ADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 428 GGANIFRGHDNVQGATDVGPNPDSLPGYYGLAAGA-WKHFATVWGVDYEWI--KKQFASQAMMEK--SGTTVSRWIdIVT 502
Cdd:cd02754 320 SGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEhRAEVAKFWGVPEGTIppKPGLHAVEMFEAieDGEIKALWV-MCT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 503 ekpelidqdHNVRGVffwghaPNSQtrglEMKRALDKLDLLVVIDPYP-SATAAMANMpategdtpnpnravyLLPACTQ 581
Cdd:cd02754 399 ---------NPAVSL------PNAN----RVREALERLEFVVVQDAFAdTETAEYADL---------------VLPAASW 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 582 FETSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFANELSKNyklvevkragrtwrepetesilreinagnw 661
Cdd:cd02754 445 GEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYT------------------------------ 494
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737919411 662 tigytgqSPERLKAHMRnmhmfdvrslRCKGGkdpvTGYDITG------DYFGLPWPCygtPELKHPGSPNLYDTSR 732
Cdd:cd02754 495 -------SPEEVFEEYR----------RLSRG----RGADLSGlsyerlRDGGVQWPC---PDGPPEGTRRLFEDGR 547
|
|
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
67-1023 |
3.08e-105 |
|
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: 352.29 E-value: 3.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 67 RRSFLKRSGIGVGAGLAATqltMMRRADADDGKGGAGGKGDIVVRRTVCGHCSVGCAV---------DAVVQNGVWVRQE 137
Cdd:TIGR01553 4 RRAFLKLTAGGATLSAFGG---LGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLlvyssshtgDNKTNRAIHVEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 138 PvfDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNG--KYQRISWDQALDEISAKLKQIRQET-------GP-----D 203
Cdd:TIGR01553 81 P--DHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGsdQWEEISWDWAIDTIARRVKDTRDATfvtkdakGQvvnrcD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 204 SLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPV 283
Cdd:TIGR01553 159 GIASVGSSAMDNEECWLYQKWLRSLGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 284 SMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKY---------LADRVYGM-- 352
Cdd:TIGR01553 239 GFKWAIRAKKKGAKIIHIDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYvvnytnasfIVGEGFAFed 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 353 -------------DKVK---------------------------EEVLAKWTPDKVEEVCGVPEAEVRYVAETMAK---- 388
Cdd:TIGR01553 319 glfagynketrkyDKSKwgyefdengnpkrdetlkhprcvfnilKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKtgkp 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 389 NRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGANIFRGHDNVQGATDVGPNPDSLPGYYGLA--------- 459
Cdd:TIGR01553 399 NKAMTILYALGWTQHSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGSTDHGLLMHILPGYLGTPrasiptyeq 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 460 --------------AGAWKHFAtvwgvdyewikKQFAS--QAMMEKSGTTVSRWIDIVTEKPE--------LIDQ--DHN 513
Cdd:TIGR01553 479 ytkkftpvskdpqsANYWSNFP-----------KFFASyiKSMWGDAATNENGWAYDYLPKGEdgydswltLFDDmfQGK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 514 VRGVFFWGHAP-NSQTRGLEMKRALDKLDLLVVIDPYPSATAAMANMPATegDTPNPNRAVYLLPACTQFETSGSCTASN 592
Cdd:TIGR01553 548 IKGFFAWGQNPlNSGPNSNKTREALTKLKWMVVMDPFDNETGSFWRGPGM--DPKEIKTEVFFLPTAVFIEKEGSISNSG 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 593 RSLQWREKVIEPLFESMPDHAIMQAFAEKLG--FANELSKNYKLVEvkraGRTW-----REPETESILREINaGNWTIGY 665
Cdd:TIGR01553 626 RWMQWRYKGPDPPGNAIPDGDIIVELAKRVQelYAKEGGKLAEPVT----KLKWdywvpDHPDAHEIAKEIN-GYALKDF 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 666 TGQSPERLKAHMRNM--HMFDVRSLRCKggkdpvtGYDITGDYfglpwpcygTPElkhpgspnlydtsrnvmdggGNFRA 743
Cdd:TIGR01553 701 KVGDVEYKKGQQIATfgHLRDDGSTTSG-------CWLYTGSY---------TEK--------------------GNMAA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 744 NfgverdgvsllaADGSHSLGADITTGY----PEFDAVLLKKLGW------WDELTDAEKKAADGKNWKTDLS------- 806
Cdd:TIGR01553 745 R------------RDKSDPAGLGLYPGWtwawPANRRVLYNRASVdlngkpWDPERALVEWNAAEKKWVGDIPdypptap 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 807 --GGIQRVVMKnhgchPFGNARARAVVWNFPDPIPQHREPLYSTrpdmVAKYPTHDDKMafwRLPTL--YKTVQQRNIEN 882
Cdd:TIGR01553 813 peKGKGAFIMK-----PEGYGRLFAPGKREDGPLPEHYEPMESP----VITNPFHPNVL---HNPTAlhYKTDEKAVGDP 880
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 883 KvyeKFPIILTSGRLVEYEggGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVG- 961
Cdd:TIGR01553 881 K---RYPFVATTYRLTEHW--HTWTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRG-KIWAKAIVTKRIKp 954
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737919411 962 -------VDTAFIPFHFSgwWQGkdlkpyypegamPIVRGEAVNTATTYGYDSVTMMQETKTTVCQIER 1023
Cdd:TIGR01553 955 laiqgqqVHMIGIPIHWG--WSF------------LKNGGDATNILTPSVGDPNTGTPETKAFLVNIEK 1009
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
113-630 |
7.88e-67 |
|
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: 231.80 E-value: 7.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQALDE 188
Cdd:cd02755 3 SICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgergEGKFREASWDEALQY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 189 ISAKLKQIRQETGPDSLFFIGsskHSNEQSYLLRKWVSFFGTNNTDHQARICH-STTVAGVANTWGYGAMTNSynDMQNA 267
Cdd:cd02755 83 IASKLKEIKEQHGPESVLFGG---HGGCYSPFFKHFAAAFGSPNIFSHESTCLaSKNLAWKLVIDSFGGEVNP--DFENA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 268 KAALYIGSNAAEA-HPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLA 346
Cdd:cd02755 158 RYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 347 DRVYGMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLV---WCMGQTQHTIGnaIVRASCIVQLALGNI 423
Cdd:cd02755 238 KYTNGFELLKAHV-KPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVdpgWRGTFYSNSFQ--TRRAIAIINALLGNI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 424 GVSGGganifrghdnvqgatdvgpnpdslpGYYGLAAgawkhfatvwgvdyewikkqfasqammeksgttvsrwidivte 503
Cdd:cd02755 315 DKRGG-------------------------LYYAGSA------------------------------------------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 504 KPelidqdHNVRGVFFWGHAP-NSQTRGLEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQF 582
Cdd:cd02755 327 KP------YPIKALFIYRTNPfHSMPDRARLIKALKNLDLVVAIDILPSDTALYAD---------------VILPEATYL 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 737919411 583 E-------TSGSCTASnrslQWREKVIEPLFESMPDHAIMQAFAEKLGFANELSK 630
Cdd:cd02755 386 ErdepfsdKGGPAPAV----ATRQRAIEPLYDTRPGWDILKELARRLGLFGTPSG 436
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
113-623 |
2.84e-66 |
|
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: 231.04 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVN----GKYQRISWDQALDE 188
Cdd:cd02759 2 GTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 189 ISAKLKQIRQETGPDSL-FFIGSSKHSNEQSYLLrkWVSF---FGTNNTDHQARICHSTTVAGVANTWGYGAmTNSYNDM 264
Cdd:cd02759 82 IAEKLAEIKAEYGPESIaTAVGTGRGTMWQDSLF--WIRFvrlFGSPNLFLSGESCYWPRDMAHALTTGFGL-GYDEPDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 265 QNAKAALYIGSNAAEAHPVSMLH-LLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKK 343
Cdd:cd02759 159 ENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGLYDKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 344 YLADRVYGMDKVKEEVlAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGqTQHTI-GNAIVRASCIVQLALGN 422
Cdd:cd02759 239 FVENWCYGFEELAERV-QEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLA-IDQQKnGTQTSRAIAILRAITGN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 423 IGVSGGGAnifrghdnvqgatdVGPNPdslpgyyglaagawkhfatvwgvdyewIKkqfasqAMMEKSGTTVSRWIDivt 502
Cdd:cd02759 317 LDVPGGNL--------------LIPYP---------------------------VK------MLIVFGTNPLASYAD--- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 503 EKPELidqdhnvrgvffwghapnsqtrglemkRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQF 582
Cdd:cd02759 347 TAPVL---------------------------EALKALDFIVVVDLFMTPTAMLAD---------------IVLPVAMSL 384
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 737919411 583 ETSGSCTASNRS--LQWREKVIEPLFESMPDHAIMQAFAEKLG 623
Cdd:cd02759 385 ERPGLRGGFEAEnfVQLRQKAVEPYGEAKSDYEIVLELGKRLG 427
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
112-628 |
6.94e-66 |
|
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: 230.60 E-value: 6.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 112 RTVCGH-CSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGK---YQRISWDQALD 187
Cdd:cd02766 1 RSVCPLdCPDTCSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKggqWERISWDEALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 188 EISAKLKQIRQETGPDSLFFIgssKHSNEQSYLLRKWVSFF----GTNNTDHQarICHSTTVAgvANTWGYGAMT-NSYN 262
Cdd:cd02766 81 TIAAKLKEIKAEYGPESILPY---SYAGTMGLLQRAARGRFfhalGASELRGT--ICSGAGIE--AQKYDFGASLgNDPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 263 DMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDK 342
Cdd:cd02766 154 DMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 343 KYLADRVYGMDKVKEEVLAkWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRA-SCIVQLaLG 421
Cdd:cd02766 234 DFLARHTEGFEELKAHLET-YTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAiDALPAL-TG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 422 NIGVSGGGANifrgHDNVQGatdvgpnpdslpgyyglaagawkhfatvwgvdyewikkqfasqammeksgttvsrwidiv 501
Cdd:cd02766 312 NIGVPGGGAF----YSNSGP------------------------------------------------------------ 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 502 tekpelidqdhNVRGVFFWGH-----APNSQTrgleMKRAL-DKLDLLVVIDPYPSATAAMANmpategdtpnpnravYL 575
Cdd:cd02766 328 -----------PVKALWVYNSnpvaqAPDSNK----VRKGLaREDLFVVVHDQFMTDTARYAD---------------IV 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 737919411 576 LPACTQFE-----TSGsctaSNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFANEL 628
Cdd:cd02766 378 LPATTFLEhedvyASY----WHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPP 431
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
156-469 |
6.60e-64 |
|
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: 227.19 E-value: 6.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 156 LREHGhgeyRLKYPMKLVNG--KYQRISWDQALDEISAKLkqirQETGPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNT 233
Cdd:cd02767 59 LEHLG----RLTYPMRYDAGsdHYRPISWDEAFAEIAARL----RALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 234 DHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDP-------RY- 305
Cdd:cd02767 131 PDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPlrepgleRFa 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 306 ---------TRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQN-----GWEDKKYLADRVYGMDKVKEEVLA-KWtpDKVEE 370
Cdd:cd02767 211 npqnpesmlTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRAlSW--DEIER 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 371 VCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRAscIVQLAL--GNIGVSGGGANIFRGHDNVQGATDVG-- 446
Cdd:cd02767 289 ASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRA--IVNLALlrGNIGRPGAGLMPIRGHSNVQGDRTMGit 366
|
330 340
....*....|....*....|....*...
gi 737919411 447 PNP-----DSLPGYYGLAAGAWKHFATV 469
Cdd:cd02767 367 EKPfpeflDALEEVFGFTPPRDPGLDTV 394
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
117-646 |
4.43e-59 |
|
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: 214.01 E-value: 4.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 117 HCSVGCAVDAVVQNGVWVRQEPvFDSpiNLGAHCAKGAALREHGHGEYRLKYPMKLV--------------NGKYQRISW 182
Cdd:cd02751 2 TACHWGPFKAHVKDGVIVRVEP-DDT--DQPRPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrgEGEFVRISW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 183 DQALDEISAKLKQIRQETGPDSLfFIGSSKHS------NEQSyLLRKWVSFFG----TNNTDhqarichSTTVAGVAN-- 250
Cdd:cd02751 79 DEALDLVASELKRIREKYGNEAI-FGGSYGWAsagrlhHAQS-LLHRFLNLIGgylgSYGTY-------STGAAQVILph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 251 ---TWGYGAMTNSYNDM-QNAKAALYIGSNAAE--------AHPVSMLHLLHAKESGCKVIVVDPRYTRTAA-KSDHYVR 317
Cdd:cd02751 150 vvgSDEVYEQGTSWDDIaEHSDLVVLFGANPLKtrqgggggPDHGSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 318 IRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVYGMDKVKEEVL------AKwTPDKVEEVCGVPEAEVRYVAETMAKNRp 391
Cdd:cd02751 230 IRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLgesdgvPK-TPEWAAEITGVPAETIRALAREIASKR- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 392 stlvwcmgqTQHTIGNAIVRASC-------IVQLA--LGNIGVSGGGanifrghdnvqgatdVGPNPDSLPGYYGLAAGA 462
Cdd:cd02751 308 ---------TMIAQGWGLQRAHHgeqpawmLVTLAamLGQIGLPGGG---------------FGFGYGYSNGGGPPRGGA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 463 wkhfatvWGVDYEWIKKQFasqammeKSGTTVSRWIDIVTEKPELIDQDH------NVRGVFFWGHAPNSQTRGL-EMKR 535
Cdd:cd02751 364 -------GGPGLPQGKNPV-------KDSIPVARIADALLNPGKEFTANGklktypDIKMIYWAGGNPLHHHQDLnRLIK 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 536 ALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFET---SGSCTASNRSLQWREKVIEPLFESMPDH 612
Cdd:cd02751 430 ALRKDETIVVHDIFWTASARYAD---------------IVLPATTSLERndiGLTGNYSNRYLIAMKQAVEPLGEARSDY 494
|
570 580 590
....*....|....*....|....*....|....
gi 737919411 613 AIMQAFAEKLGFANELSKnyklvevkraGRTWRE 646
Cdd:cd02751 495 EIFAELAKRLGVEEEFTE----------GRDEME 518
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
886-1023 |
2.10e-57 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 193.21 E-value: 2.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 886 EKFPIILTSGRLVEYEGGGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTA 965
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRG-KIKVKALVTDRVKPHEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 737919411 966 FIPFHFSGWWQgkdlkpyypegampiVRGEAVNTATTYGYDSVTMMQETKTTVCQIER 1023
Cdd:cd02792 80 GIPYHWGGMGL---------------VIGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
156-469 |
3.07e-55 |
|
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: 205.43 E-value: 3.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 156 LREHGhgeyRLKYPMKLVNG--KYQRISWDQALDEISAKLKQIrqetGPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNT 233
Cdd:TIGR01701 94 LEKLG----RLTYPLSLRPGsdHYTPISWDDAYQEIAAKLNSL----DPKQVAFYTSGRTSNEAAYLYQLFARSLGSNNL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 234 DHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDP-------RYT 306
Cdd:TIGR01701 166 PDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPlrergleRFW 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 307 RTAAK-----------SDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVY------GMDKVKEEVLA-KWtpDKV 368
Cdd:TIGR01701 246 IPQIPesmltgggtqiSSEYYQVRIGGDIALFNGVMKLLIEAEDAQPGSLIDHEFianhtnGFDELRRHVLQlNW--NDI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 369 EEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGANIFRGHDNVQGATDVG-- 446
Cdd:TIGR01701 324 ERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGit 403
|
330 340
....*....|....*....|....*...
gi 737919411 447 --PNP---DSLPGYYGLAAGAWKHFATV 469
Cdd:TIGR01701 404 ekPEEeflARLSQIYGFTPPDWPGDTTV 431
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
113-627 |
2.96e-51 |
|
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: 191.38 E-value: 2.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGH-CSVGCAVDAVVQNGVWVRQEPVFDSPINLGAH----CAKGAALREHGHGEYRLKYPMKLVN----GKYQRISWD 183
Cdd:cd02770 2 SACTVnCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHqiraCLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 184 QALDEISAKLKQIRQETGPDSLFF-------IGSSKHSNEQSYLLRKWVSFFGTNNTDHQARIchSTTVAGVANTWGYGa 256
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAIYVnygtgtyGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQI--TTATPYTYGAAASG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 257 mtNSYNDMQNAKAALYIGSNAAE-----AHPVsmLHLLHAKESGCKVIVVDPRYTRTAA-KSDHYVRIRSGTDIAFLFGV 330
Cdd:cd02770 159 --SSLDDLKDSKLVVLFGHNPAEtrmggGGST--YYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 331 LYHIFQNGWEDKKYLADRVYGMDK------------VKEEVLAKW------TPDKVEEVCGVPEAEVRYVAETMAKNRPS 392
Cdd:cd02770 235 AYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYVLGTGydgtpkTPEWASEITGVPAETIRRLAREIATTKPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 393 TLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGANIFRGHDNVQGA-TDVGPNP--DSLPGYyglaagawkhfatv 469
Cdd:cd02770 315 AILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAgLPAGKNPvkTSIPCF-------------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 470 wgvdyewikkqfasqammeksgttvsRWIDIVTEKPELIDQDHNVRGV--------FFWGHAPNS--QTRGlEMKRALDK 539
Cdd:cd02770 381 --------------------------MWTDAIERGEEMTADDGGVKGAdklksnikMIWNYAGNTliNQHS-DDNNTTRA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 540 L-------DLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGSCTASNRS----LQWREKVIEPLFES 608
Cdd:cd02770 434 LlddeskcEFIVVIDNFMTPSARYAD---------------ILLPDTTELEREDIVLTSNAGmmeyLIYSQKAIEPLYEC 498
|
570
....*....|....*....
gi 737919411 609 MPDHAIMQAFAEKLGFANE 627
Cdd:cd02770 499 KSDYEICAELAKRLGVEDQ 517
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
65-971 |
2.65e-50 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 191.03 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 65 MDRRSFLKRSGIGvGAGLAATQL---TMMRRADADDGKGGAGGkgdivvrRTVCGHCSVGCAVDAVVQNG--VWVRQEPv 139
Cdd:PRK15488 3 LSRRDFLKGAGAG-CAACALGSLlpgALAANEIAQLKGKTKLT-------PSICEMCSTRCPIEARVVNGknVFIQGNP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 140 fDSPINLGAHCAKGAAlrehGHG----EYRLKYPMKLV----NGKYQRISWDQALDEISAKLKQIRQETGPDSLFFigSS 211
Cdd:PRK15488 74 -KAKSFGTKVCARGGS----GHSllydPQRIVKPLKRVgergEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAF--SS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 212 KhSNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVANTWGyGAMTNsynDMQNAKAALYIGSNAAEAHPVSMLHLL-- 289
Cdd:PRK15488 147 K-SGSLSSHLFHLATAFGSPNTFTHASTCPAGYAIAAKVMFG-GKLKR---DLANSKYIINFGHNLYEGINMSDTRGLmt 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 290 HAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVYGMDKVKEEVlAKWTPDKVE 369
Cdd:PRK15488 222 AQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASV-KEYTPEWAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 370 EVCGVPEAEVRYVAETMAKNRPSTLV-WCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGganIFRGHD----NVQGATD 444
Cdd:PRK15488 301 AISDVPADDIRRIARELAAAAPHAIVdFGHRATFTPEEFDMRRAIFAANVLLGNIERKGG---LYFGKNasvyNKLAGEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 445 VGPnpdslpgyyGLAAGAWKHFATVWGVDYEWIKKQFasqAMMEKSGTTVSRWID-IVTEKPelidqdHNVRGVFFWGHA 523
Cdd:PRK15488 378 VAP---------TLAKPGVKGMPKPTAKRIDLVGEQF---KYIAAGGGVVQSIIDaTLTQKP------YQIKGWVMSRHN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 524 P-NSQTRGLEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGSCTAS---NRSLQWRE 599
Cdd:PRK15488 440 PmQTVTDRADVVKALKKLDLVVVCDVYLSESAAYAD---------------VVLPESTYLERDEEISDKsgkNPAYALRQ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 600 KVIEPLFESMPDHAIMQAFAEKLGfaneLSKNYklvevkragrTWREPETesiLREINAGNwtigytgqSPERLKAhmrn 679
Cdd:PRK15488 505 RVVEPIGDTKPSWQIFKELGEKMG----LGQYY----------PWQDMET---LQLYQVNG--------DHALLKE---- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 680 mhmfdvrsLRCKGgkdpvtgyditgdyfglpWPCYGTPELkhpgspnlydtsrnvmdgggnFRanfgvERDGVsllaadg 759
Cdd:PRK15488 556 --------LKKKG------------------YVSFGVPLL---------------------LR-----EPKMV------- 576
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 760 shslgADITTGYPEFDAVllkklgwwdeltDAEKKAADGKNWKTDlSGGIQrvvmknhgchpfgnararavvwnfpdpip 839
Cdd:PRK15488 577 -----AKFVARYPNAKAV------------DEDGTYGSQLKFKTP-SGKIE----------------------------- 609
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 840 qhrepLYStrPDMVAKYPThddkmafwrlptlYKTVQQRNIenKVYEKFPIILTSGRLVEYEGGGeeTRSNPWLAELQQE 919
Cdd:PRK15488 610 -----LFS--AKLEALAPG-------------YGVPRYRDV--ALKKEDELYFIQGKVAVHTNGA--TQNVPLLANLMSD 665
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 737919411 920 NFVEINPKAASERGIRNGDYCWVKTPTGARiKVRALVTERVGVDTAFIPFHF 971
Cdd:PRK15488 666 NAVWIHPQTAGKLGIKNGDEIRLENSVGKE-KGKALVTPGIRPDTLFAYMGF 716
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-622 |
1.46e-47 |
|
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: 178.74 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQRISWDQALDEISAK 192
Cdd:cd02762 2 RACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGSFEEIDWDEAFDEIAER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 193 LKQIRQETGPDSLFFIGSSKHSNEQS------YLLR--KWVSFFgTNNTDHQarICHSTTVAGVantwgYG-AMTNSYND 263
Cdd:cd02762 82 LRAIRARHGGDAVGVYGGNPQAHTHAggayspALLKalGTSNYF-SAATADQ--KPGHFWSGLM-----FGhPGLHPVPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 264 MQNAKAALYIGSNAAEAH------PVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQN 337
Cdd:cd02762 154 IDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVLLAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 338 GWEDKKYLADRVYGMDKVKeEVLAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMG---QTQHTIGNAIVRAsc 414
Cdd:cd02762 234 GLTDRRFLAEHCDGLDEVR-AALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGvqtQLFGTLCSWLVKL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 415 iVQLALGNIGvSGGGANIFrghdnvQGATDVGPNPDSlpgyYGLAAGAWKhfatvwgvdyewikkqfasqammeksgTTV 494
Cdd:cd02762 311 -LNLLTGNLD-RPGGAMFT------TPALDLVGQTSG----RTIGRGEWR---------------------------SRV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 495 SRWIDIVTEKP-----ELIDQDH--NVRGVFFWG-----HAPNSQtrglEMKRALDKLDLLVVIDPYPSATAAMANmpat 562
Cdd:cd02762 352 SGLPEIAGELPvnvlaEEILTDGpgRIRAMIVVAgnpvlSAPDGA----RLEAALGGLEFMVSVDVYMTETTRHAD---- 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737919411 563 egdtpnpnravYLLPACTQFE----TSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd02762 424 -----------YILPPASQLEkphaTFFNLEFPRNAFRYRRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
113-668 |
3.05e-46 |
|
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: 175.36 E-value: 3.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVC-GHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQALD 187
Cdd:cd02765 2 TACpPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVgergEGKFERITWDEALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 188 EISAKLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKwvSFFGTNNTDHQARICHSTTvAGVANTWGYGAM--TNSYNDMQ 265
Cdd:cd02765 82 TIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLA--LLGGGLQDALTYGIDTGVG-QGFNRVTGGGFMppTNEITDWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 266 NAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYL 345
Cdd:cd02765 159 NAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 346 ADRV-----------------------------------------------------YGMDKVK--------EEVLAKWT 364
Cdd:cd02765 239 KSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeYTINGVKvhtvltalREQAASYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 365 PDKVEEVCGVPEAEVRYVAETMAKNRPStLVWCMGQTQHTI-GNAIVRASCIVQLALGNIGVSGGGAnifrGHdnvqgat 443
Cdd:cd02765 319 PKAAAEICGLEEAIIETLAEWYATGKPS-GIWGFGGVDRYYhSHVFGRTAAILAALTGNIGRVGGGV----GQ------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 444 dvgpnpdsLPGYYGLaagawkhfatvwgvdyewikkqfasqammeksgttvsrwidivtekpelidqdhnvrGVFFWGHA 523
Cdd:cd02765 387 --------IKFMYFM---------------------------------------------------------GSNFLGNQ 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 524 PNSQTrgleMKRALDKLDLLVVIDPYPSATAAMANMpategdtpnpnravyLLPACTQFETSGSCTASNRS--LQWREKV 601
Cdd:cd02765 402 PDRDR----WLKVMKNLDFIVVVDIFHTPTVRYADI---------------VLPAAHWFEVEDLLVRYTTHphVLLQQKA 462
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737919411 602 IEPLFESMPDHAIMQAFAEKLGFANELSKNYKlvEVKRA----------GRTWREPETESILREINA-GNWTIGYTGQ 668
Cdd:cd02765 463 IEPLFESKSDFEIEKGLAERLGLGDYFPKTPE--DYVRAfmnsddpaldGITWEALKEEGIIMRLATpEDPYVAYLDQ 538
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
165-621 |
7.22e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 163.34 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 165 RLKYPM-KLVNGKYQRISWDQALDEISAKLKQIRQETGPDSLFFIGSS--KHSNEQSYLLRKWVSFFGTNNT---DHQAR 238
Cdd:pfam00384 1 RLKYPMvRRGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSggLTDVESLYALKKLLNRLGSKNGnteDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 239 ICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHA-KESGCKVIVVDPRYTRTAAksDHYVR 317
Cdd:pfam00384 81 LCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRLDLTYA--DEHLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 318 IRSGTDIAFLFGVLYHIFQNGWEDKKYladrvygmdkvkeevlakwtpdkveevcgvpeaevryvaetmaknRPSTLV-W 396
Cdd:pfam00384 159 IKPGTDLALALAGAHVFIKELKKDKDF---------------------------------------------APKPIIiV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 397 CMGQTQHTIGNAIVRASCIVQLALGNIGVSGGG---ANIFRGHDNVQGATDVGPNPDslpgyyglaagawkhfatvwgvd 473
Cdd:pfam00384 194 GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGwngLNILQGAASPVGALDLGLVPG----------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 474 yewikKQFASQAMMEKSGttvsrwidivtekpelidqdhNVRGVFFWGHAP-NSQTRGLEMKRALDKLDLLVVIDPYP-S 551
Cdd:pfam00384 251 -----IKSVEMINAIKKG---------------------GIKVLYLLGNNPfVTHADENRVVKALQKLDLFVVYDGHHgD 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 552 ATAAMANmpategdtpnpnravYLLPACTQFETSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEK 621
Cdd:pfam00384 305 KTAKYAD---------------VILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
886-1023 |
9.73e-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: 148.42 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 886 EKFPIILTSGRLVEYEGGGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTA 965
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRG-SVVVRARVTDRVRPGTV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 737919411 966 FIPFHFSGWwqgkdlkpyypegampiVRGEAVNTATTYGYDSVTMMQETKTTVCQIER 1023
Cdd:cd00508 80 FMPFHWGGE-----------------VSGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
113-622 |
9.85e-40 |
|
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: 155.29 E-value: 9.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVN--------GKYQRISWDQ 184
Cdd:cd02757 4 STCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKFVPISWDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 185 ALDEISAKLKQIRQETGPDS-LFFIGSSKHSNEQSY--LLRKWVSffgTNNTDHQArICHSTTVAGVANTWGYGAMtNSY 261
Cdd:cd02757 84 ALDTIADKIRALRKENEPHKiMLHRGRYGHNNSILYgrFTKMIGS---PNNISHSS-VCAESEKFGRYYTEGGWDY-NSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 262 nDMQNAKAALYIGSNAAEA-HPVSM-LHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGW 339
Cdd:cd02757 159 -DYANAKYILFFGADPLESnRQNPHaQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHVILTEGL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 340 EDKKYLADRVYGMDKVKEE---------------VLAKW-------TPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWC 397
Cdd:cd02757 238 WDKDFVGDFVDGKNYFKAGetvdeesfkekstegLVKWWnlelkdyTPEWAAKISGIPAETIERVAREFATAAPAAAAFT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 398 M-GQTQHTIGNAIVRASCIVQLALGNIGVSGgganifrghdnvqgatdvgpnpdslpgyyGLAAGAWkhfatvwgvdyew 476
Cdd:cd02757 318 WrGATMQNRGSYNSMACHALNGLVGSIDSKG-----------------------------GLCPNMG------------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 477 ikkqfasqamMEKSGTTVSRWIDivtekpelidqdhnvrgvFFWghapnSQTRGLEMKRALDKLDLLVVIDPYPSATAAM 556
Cdd:cd02757 356 ----------VPKIKVYFTYLDN------------------PVF-----SNPDGMSWEEALAKIPFHVHLSPFMSETTYF 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737919411 557 ANmpategdtpnpnravYLLPACTQFETSGSCTASNRSLQW---REKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd02757 403 AD---------------IVLPDGHHFERWDVMSQENNLHPWlsiRQPVVKSLGEVREETEILIELAKKL 456
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
126-627 |
1.26e-38 |
|
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: 153.19 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 126 AVVQNGVWVRQEPvFD-----SPInlgahcakGAALREHGHGEYRLKYPMK----LVNGK-----------YQRISWDQA 185
Cdd:cd02769 11 ARVKDGRIVGVRP-FEedpdpSPL--------LDGVPDAVYSPTRIKYPMVrrgwLEKGPgsdrslrgkeeFVRVSWDEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 186 LDEISAKLKQIRQETGPDSLFfiGSS---KHS----NEQSYLLRkwvsFFGT--NNTDHQARicHSTTVAGV------AN 250
Cdd:cd02769 82 LDLVAAELKRVRKTYGNEAIF--GGSygwSSAgrfhHAQSLLHR----FLNLagGYVGSVGD--YSTGAAQVilphvvGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 251 TWGYGAMTNSY---------------NDMQNAKaalyIGSNAAEAHPVSmLHLLHAKESGCKVIVVDPRYTRTAA--KSD 313
Cdd:cd02769 154 MEVYTEQQTSWpviaehtelvvafgaDPLKNAQ----IAWGGIPDHQAY-SYLKALKDRGIRFISISPLRDDTAAelGAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 314 HyVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVYGMDKVKEEVL------AKwTPDKVEEVCGVPEAEVRYVAETMA 387
Cdd:cd02769 229 W-IAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLgesdgvPK-TPEWAAAICGIPAETIRELARRFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 388 KNRpsTLV---WCMGQTQH---TIGNAIVRASCivqlaLGNIGVSGGGANIFRGHDNVQGATDVGPNPDSLPgyyglaag 461
Cdd:cd02769 307 SKR--TMImagWSLQRAHHgeqPHWMAVTLAAM-----LGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALP-------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 462 awkhfatvWGvdyewikkqfasqammEKSGTT---VSRWIDIVTEKPELIdqDHN--------VRGVFFWGHAPNSQTRG 530
Cdd:cd02769 372 --------QG----------------RNPVSSfipVARIADMLLNPGKPF--DYNgkkltypdIKLVYWAGGNPFHHHQD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 531 L-EMKRALDKLDLLVVIDPYPSATAAMANMpategdtpnpnravyLLPACTQFETSG-SCTASNRSLQWREKVIEPLFES 608
Cdd:cd02769 426 LnRLIRAWQKPETVIVHEPFWTATARHADI---------------VLPATTSLERNDiGGSGDNRYIVAMKQVVEPVGEA 490
|
570
....*....|....*....
gi 737919411 609 MPDHAIMQAFAEKLGFANE 627
Cdd:cd02769 491 RDDYDIFADLAERLGVEEQ 509
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
109-622 |
1.66e-36 |
|
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: 144.38 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 109 VVRRTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSP---INLGAH----CAKGAALREHGHGEYRLKYPMKLV----NGKY 177
Cdd:cd02750 3 VVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPetpPDLPDYnprgCQRGASFSWYLYSPDRVKYPLKRVgargEGKW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 178 QRISWDQALDEISAKLKQIRQETGPDSLFFIGSSKHSNEQSYL-------LRKWVSF-FGTNNTDHQArichsttvaGVA 249
Cdd:cd02750 83 KRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAagsrfasLIGGVSLsFYDWYGDLPP---------GSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 250 NTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFG 329
Cdd:cd02750 154 QTWGEQTDVPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 330 VLYHIFQNgwedkkYLADRVYgmdkVKEEV---LAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIG 406
Cdd:cd02750 234 MAHVIIKE------KLYDEDY----LKEYTdlpFLVYTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 407 NAIVRAsCIVQLAL-GNIGVSGGGanifrghdnvqgatdvgpnpdslpgyyglaagaWKHFAtvwgvdyewikkqfasqa 485
Cdd:cd02750 304 DLCYRA-LILLLALtGNEGKNGGG---------------------------------WAHYV------------------ 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 486 mmeksgttvsrwidivtekpelidqdHNVRGVFFWGHAP-NSQTRGLEM-KRALD-KLDLLVVIDPYPSATAAMANmpat 562
Cdd:cd02750 332 --------------------------GQPRVLFVWRGNLfGSSGKGHEYfEDAPEgKLDLIVDLDFRMDSTALYSD---- 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737919411 563 egdtpnpnravYLLPACTQFE-TSGSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd02750 382 -----------IVLPAATWYEkHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
65-630 |
3.35e-34 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 141.32 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 65 MDRRSFLKRSGIGvGAGLAATQLTM-MRRADADDGKGGAGGKGDIVVRRTVCGHCSVGCAVDAVVQNGV--WVRQEPVFD 141
Cdd:PRK14990 14 VSRRGLVKTTAIG-GLAMASSALTLpFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEikYVETDNTGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 142 SPINlGAH----CAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQALDEISAKLKQIRQETGPDSLFF---IGS 210
Cdd:PRK14990 93 DNYD-GLHqvraCLRGRSMRRRVYNPDRLKYPMKRVgargEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLnygTGT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 211 SKHSNEQSY-----LLRKWVSFFGtNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVS- 284
Cdd:PRK14990 172 LGGTMTRSWppgntLVARLMNCCG-GYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGg 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 285 --MLHLLHAKE-SGCKVIVVDPRYTRT-AAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRVYGMDK------ 354
Cdd:PRK14990 251 gvTYYLEQARQkSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEktlpas 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 355 ------VKEEVLAKW------TPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGN 422
Cdd:PRK14990 331 apknghYKAYILGEGpdgvakTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 423 IGVSGGganifrghdnvqgatdvgpNPDSLPGYYGLAagawkhfatvwgvdyewikkqFASQAMME---KSGTTVSRWID 499
Cdd:PRK14990 411 VGINGG-------------------NSGAREGSYSLP---------------------FVRMPTLEnpiQTSISMFMWTD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 500 IVTEKPELIDQDHNVRG--------VFFWGHAPN-------SQTRGLEMKRALDKLDLLVVIDPYPSATAAMANMpateg 564
Cdd:PRK14990 451 AIERGPEMTALRDGVRGkdkldvpiKMIWNYAGNclinqhsEINRTHEILQDDKKCELIVVIDCHMTSSAKYADI----- 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737919411 565 dtpnpnravyLLPACT-----QFETSGSCtaSNRS-LQWREKVIEPLFESMPDHAIMQAFAEKLGFANELSK 630
Cdd:PRK14990 526 ----------LLPDCTaseqmDFALDASC--GNMSyVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTE 585
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
134-623 |
1.03e-30 |
|
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: 130.15 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 134 VRQEPVFDSPINLGAH-----CAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQALDEISAK-----------L 193
Cdd:cd02758 47 LKESLYLSLVGENGLKarataCARGNAGLQYLYDPYRVLQPLKRVgprgSGKWKPISWEQLIEEVVEGgdlfgeghvegL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 194 KQIRQET----------GPDS--LFFIGSSkhSNEQSYLLRKWVSF-FGTNNTDHQARIC-HSTTVAGVANTWGYGAMTN 259
Cdd:cd02758 127 KAIRDLDtpidpdhpdlGPKAnqLLYTFGR--DEGRTPFIKRFANQaFGTVNFGGHGSYCgLSYRAGNGALMNDLDGYPH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 260 SYNDMQNAKAALYIGSNAAEAHP----VSMLHLLHAKESGCKVIVVDPRYTRT---AAKSDHYVRIRSGTDIAFLFGVLY 332
Cdd:cd02758 205 VKPDFDNAEFALFIGTSPAQAGNpfkrQARRLAEARTEGNFKYVVVDPVLPNTtsaAGENIRWVPIKPGGDGALAMAMIR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 333 HIFQNGWEDKKYLAD-RVYGMDKV------------------------KEEVLAKwTPDKVEEVCGVPEAEVRYVAETMA 387
Cdd:cd02758 285 WIIENERYNAEYLSIpSKEAAKAAgepswtnathlvitvrvksalqllKEEAFSY-SLEEYAEICGVPEAKIIELAKEFT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 388 KNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGAnifrghdnvqgATDVGPNPDSLPGYYGLAAGAWKhfA 467
Cdd:cd02758 364 SHGRAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGLL-----------MSGGGFADNSAGPRYDFKKFFGE--V 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 468 TVWGV-------DYE-----WIKKQFASQAMMEK------SGTTVSRWI-DIVTEKPELIDQDHNVRGVFFWGhAPNSQT 528
Cdd:cd02758 431 KPWGVpidrskkAYEktseyKRKVAAGENPYPAKrpwyplTPELYTEVIaSAAEGYPYKLKALILWMANPVYG-APGLVK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 529 RGLEMKRALDKLDLLVVIDPYPSATAAMANmpategdtpnpnravYLLPACTQFETSGSCTASNRSL----QWREKVIEP 604
Cdd:cd02758 510 QVEEKLKDPKKLPLFIAIDAFINETSAYAD---------------YIVPDTTYYESWGFSTPWGGVPtkasTARWPVIAP 574
|
570 580
....*....|....*....|....*
gi 737919411 605 LFESMPD-HAI-MQAF----AEKLG 623
Cdd:cd02758 575 LTEKTANgHPVsMESFlidlAKALG 599
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
63-637 |
1.80e-30 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 129.63 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 63 PTMDRRSFLKRSGIGVGAGLAATQLTmmrradADDGKGGAGGKGDIVVRRTVCGHCSVGCAVDAVVQNG--VWVRQEPvf 140
Cdd:PRK13532 1 MKLSRRDFMKANAAAAAAAAAGLSLP------AVANAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGrvVATQGDP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 141 DSPINLGAHCAKGAALREHGHGEYRLKYPMKLV-------NGKYQRISWDQALDEISAKLKQIRQETGPDSLFFIGSSKH 213
Cdd:PRK13532 73 DAPVNRGLNCIKGYFLSKIMYGKDRLTQPLLRMkdgkydkEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 214 SNEQSYLLRK-WVSFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAK 292
Cdd:PRK13532 153 TIWEGYAASKlMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 293 ES--GCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYLADRV----------YGM------DK 354
Cdd:PRK13532 233 LSnpDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTnfrkgatdigYGLrpthplEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 355 VKEEV-----------------LAKWTPDKVEEVCGVPEAEVRYVAETMA-KNRPSTLVWCMGQTQHTIGNAIVRASCIV 416
Cdd:PRK13532 313 AAKNPgtagksepisfeefkkfVAPYTLEKTAKMSGVPKEQLEQLAKLYAdPNRKVVSFWTMGFNQHTRGVWANNLVYNI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 417 QLALGNIGVSGGGANIFRGHDNVQG-ATDVGPNPDSLPGyyGLAAGAWKHFAT---VW----GVDYEWIKKQFASQAMME 488
Cdd:PRK13532 393 HLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPA--DMVVTNPKHREIaekIWklpeGTIPPKPGYHAVAQDRML 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 489 KSGTTVSRWIdivtekpelidQDHNVrgvffWGHAPNSQTRGLEMKRALDklDLLVVIDPYPSATAAMANMpategdtpn 568
Cdd:PRK13532 471 KDGKLNAYWV-----------MCNNN-----MQAGPNINEERLPGWRNPD--NFIVVSDPYPTVSALAADL--------- 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737919411 569 pnravyLLPACTQFETSGSC-TASNRSLQWREKVIEPlFESMPD-HAIMqafaeklgfanELSKNYKLVEV 637
Cdd:PRK13532 524 ------ILPTAMWVEKEGAYgNAERRTQFWRQQVKAP-GEAKSDlWQLV-----------EFSKRFKTEEV 576
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
165-446 |
2.18e-30 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 129.01 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 165 RLKYPMKL--VNGKYQRISWDQALDEISAKLKQIRQetgPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHS 242
Cdd:PRK09939 108 RLTQPLKYdaVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 243 TTVAGVANTWGYGAMTNSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDP-------RYT--------- 306
Cdd:PRK09939 185 PTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTapqnpfeml 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 307 ---RTAAKSDHYvRIRSGTDIAFLFGVLYHIF----------QNGWEDKKYLADRVYGMDKVKEEVL-AKWtpDKVEEVC 372
Cdd:PRK09939 265 tnsETQLASAYY-NVRIGGDMALLKGMMRLLIerddaasaagRPSLLDDEFIQTHTVGFDELRRDVLnSEW--KDIERIS 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737919411 373 GVPEAEVRYVAETMAKNRPSTLVWCMGQTQHTIGNAIVRASCIVQLALGNIGVSGGGANIFRGHDNVQGATDVG 446
Cdd:PRK09939 342 GLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG 415
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-627 |
1.09e-28 |
|
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: 123.40 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNG--VWVRQEPvfDSPINLGAHCAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQAL 186
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGkvRYIKGNP--DHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIEWEEAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 187 DEISAKLKQIRQeTGPDSL-FFIGsskhsNEQSYLLRKW-VSFFGTNNTDHQARICHSTTVAGVANTWGYGAMTNSYNDM 264
Cdd:cd02763 80 SIATKRLKAARA-TDPKKFaFFTG-----RDQMQALTGWfAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGPDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 265 QNAKAALYIGSnaAEAH---PVSmLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWED 341
Cdd:cd02763 154 EHTKYFMMIGV--AEDHhsnPFK-IGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLID 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 342 KKYLadrvygMDKVKEEVLAKWTPDKVEEVCGVPEAEVRYVAETMA-------------------------KNRPSTLVW 396
Cdd:cd02763 231 WEFL------KRYTNAAELVDYTPEWVEKITGIPADTIRRIAKELGvtardqpielpiawtdvwgrkhekiTGRPVSFHA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 397 CMGQTQHTIGNAIVRASCIVQLALGNIGVSGGganiFRGHDNVQGATDVGPNPDSLPgyyglaaGAWKHFATVWGVDYEW 476
Cdd:cd02763 305 MRGIAAHSNGFQTIRALFVLMMLLGTIDRPGG----FRHKPPYPRHIPPLPKPPKIP-------SADKPFTPLYGPPLGW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 477 -----------------IKKQFASQAMMEKSGTTVSRWIDIVTEKPELIDqdhnVRGVFFWGHAPNSQTRGLEMKRALD- 538
Cdd:cd02763 374 paspddllvdedgnplrIDKAYSWEYPLAAHGCMQNVITNAWRGDPYPID----TLMIYMANMAWNSSMNTPEVREMLTd 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 539 -------KLDLLVVIDPYPSATAAMANMpategdtpnpnravyLLPACTQFETSGSCTASNRSLQ--------WREKVIE 603
Cdd:cd02763 450 kdasgnyKIPFIIVCDAFYSEMVAFADL---------------VLPDTTYLERHDAMSLLDRPISeadgpvdaIRVPIVE 514
|
570 580
....*....|....*....|....*..
gi 737919411 604 PLFESMPDHAIMQAFAEKL---GFANE 627
Cdd:cd02763 515 PKGDVKPFQEVLIELGTRLglpGFTNE 541
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
65-631 |
8.42e-28 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 120.93 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 65 MDRRSFLKRSGIGVGAGLAATQLTMMRRADADDGKGGAGGKGDIVVrrtvcghcsvGC---AVDAVVQNGVWVRQEPvFD 141
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLLTPRSALAAQAAAAETTKEWILT----------GShwgAFRAKVKNGRFVEAKP-FE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 142 spinLGAHCAKG-AALREHGHGEYRLKYPMKLV---------------NGKYQRISWDQALDEISAKLKQIRQETGPDSL 205
Cdd:PRK15102 70 ----LDKYPTKMiNGIKGHVYNPSRIRYPMVRLdwlrkrhksdtsqrgDNRFVRVSWDEALDLFYEELERVQKTYGPSAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 206 FFIGSSKHSNEQ-----SYLLRKwVSFFGTNNT---DHQA--------RICHSTTVAGVANTWGYgAMTNS------YND 263
Cdd:PRK15102 146 HTGQTGWQSTGQfhsatGHMQRA-IGMHGNSVGtvgDYSTgagqvilpYVLGSTEVYEQGTSWPL-ILENSktivlwGSD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 264 M-QNakaaLYIGSNAAEAHPVSMLHLLHAK--ESGCKVIVVDPRYTRTAA--KSDHyVRIRSGTDIAFLFGVLYHIFQNG 338
Cdd:PRK15102 224 PvKN----LQVGWNCETHESYAYLAQLKEKvaKGEINVISIDPVVTKTQNylGCEH-LYVNPQTDVPLMLALAHTLYSEN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 339 WEDKKYLADRVYGMDKV------KEEVLAKwTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLV-WCMGQTQHtiGNAIVR 411
Cdd:PRK15102 299 LYDKKFIDNYCLGFEQFlpyllgEKDGVPK-TPEWAEKICGIDAETIRELARQMAKGRTQIIAgWCIQRQQH--GEQPYW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 412 ASCIVQLALGNIGVSGGGANiFRGHDNVQGA-TDVGPNPDSLPGyyglaagawkhfatvwGVDyEWIKKQFASQAMMEKS 490
Cdd:PRK15102 376 MGAVLAAMLGQIGLPGGGIS-YGHHYSGIGVpSSGGAIPGGFPG----------------NLD-TGQKPKHDNSDYKGYS 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 491 GTT-VSRWIDIVTEKPELIdqDHNVRGVFF-------------WGHapnSQTRGlEMKRALDKLDLLVVIDPYPSATAAM 556
Cdd:PRK15102 438 STIpVARFIDAILEPGKTI--NWNGKKVTLpplkmmifsgtnpWHR---HQDRN-RMKEAFRKLETVVAIDNQWTATCRF 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 557 ANMpategdtpnpnravyLLPACTQFETS-----GSctASNRSLQWREKVIEPLFESMPDHAIMQAFAEKLGFANELSKN 631
Cdd:PRK15102 512 ADI---------------VLPACTQFERNdidqyGS--YSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRG 574
|
|
| 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 ... |
113-623 |
2.91e-24 |
|
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: 107.47 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQRISWDQALDEISAK 192
Cdd:cd02771 2 SICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 193 LKQIRQETGPdslffIGSSKHSNEQSYLLRKWV-SFFGTNNTDHQARICHSTTVAgvantwGYGAMTNSYNDMQNAKAAL 271
Cdd:cd02771 82 LKEAKDKVGG-----IGSPRASNESNYALQKLVgAVLGTNNVDHRARRLIAEILR------NGPIYIPSLRDIESADAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 272 YIGSNAAEAHPVSMLHLlhakesgckvivvdprytRTAAKSDH-YVRIRSGTDIAFLFGVLYHIFQNGWE-------DKK 343
Cdd:cd02771 151 VLGEDLTQTAPRIALAL------------------RQAARRKAvELAALSGIPKWQDAAVRNIAQGAKSPlfivnalATR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 344 Y--LADRVYGMDKVKE----EVLAKWTPDKVEEVCGV--PEAEVRYVAETMAKNRPSTLVWCMGQtqhtiGNAIVRASCI 415
Cdd:cd02771 213 LddIAAESIRASPGGQarlgAALARAVDASAAGVSGLapKEKAARIAARLTGAKKPLIVSGTLSG-----SLELIKAAAN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 416 VQLALGNIGVSGGganifrghdnVQGATDVGpnpdSLPGYYGLAAGAWKHFATVWGvdyewikkqfASQAMMEKSGTTVs 495
Cdd:cd02771 288 LAKALKRRGENAG----------LTLAVEEG----NSPGLLLLGGHVTEPGLDLDG----------ALAALEDGSADAL- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 496 rwidIVTEKpELIDqdhnvrgvffwgHAPNSqtrglEMKRALDKLDLLVVIDPYPSATAAmanmpategdtpnpnRAVYL 575
Cdd:cd02771 343 ----IVLGN-DLYR------------SAPER-----RVEAALDAAEFVVVLDHFLTETAE---------------RADVV 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 737919411 576 LPACTQFETSGSCTASNRSLQWREKVI-EPLFESMPDHAIMQAFAEKLG 623
Cdd:cd02771 386 LPAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLG 434
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
113-622 |
7.69e-23 |
|
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: 101.98 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGaalR---EHGHGEYRLKYPMKLVNGKYQRISWDQALDEI 189
Cdd:cd02768 2 SIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKG---RfgyDGLNSRQRLTQPLIKKGGKLVPVSWEEALKTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 190 SAKLKQIRqetgPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHSTTVAGVANTWGYGamtNSYNDMQNAKA 269
Cdd:cd02768 79 AEGLKAVK----GDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFN---TSIAEIEEADA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 270 ALYIGSNAAEAHPVSMLHLLHA-KESGCKVIVVDPRYTRTAAKSDHYVrIRSGTDIAFLFGVLyhifqngwedkkyladr 348
Cdd:cd02768 152 VLLIGSNLRKEAPLLNARLRKAvKKKGAKIAVIGPKDTDLIADLTYPV-SPLGASLATLLDIA----------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 349 vygmdkvkeevlakwtpdkveevcgVPEAEVRYVAETMAKNRPSTLVwcmGQ-TQHTIGNAIVRAscIVQLAlgniGVSG 427
Cdd:cd02768 214 -------------------------EGKHLKPFAKSLKKAKKPLIIL---GSsALRKDGAAILKA--LANLA----AKLG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 428 GGANIFrghdnvqgatdVGPNPDSLPGYYGLAAGAWKHFAtvwgvdyewikkqfasqammeksgttvsrwidivTEKPEL 507
Cdd:cd02768 260 TGAGLW-----------NGLNVLNSVGARLGGAGLDAGLA----------------------------------LLEPGK 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 508 IDqdhnvrgvFFWGHAPNSQTRGLEMKRALDKLDLLVVIDPYPSATAAMANMpategdtpnpnravyLLPACTQFETSGS 587
Cdd:cd02768 295 AK--------LLLLGEDELDRSNPPAAVALAAADAFVVYQGHHGDTGAQADV---------------ILPAAAFTEKSGT 351
|
490 500 510
....*....|....*....|....*....|....*
gi 737919411 588 CTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd02768 352 YVNTEGRVQRFKKAVSPPGDAREDWKILRALSNLL 386
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
904-1015 |
5.41e-21 |
|
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: 88.53 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 904 GEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPFHFSGWwqgkdlkpy 983
Cdd:cd02775 7 SGTRTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRG-SVVLRAKVTDGVPPGVVFLPHGWGHR--------- 76
|
90 100 110
....*....|....*....|....*....|..
gi 737919411 984 ypegampIVRGEAVNTATTYGYDSVTMMQETK 1015
Cdd:cd02775 77 -------GGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
113-622 |
3.29e-20 |
|
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: 96.40 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAVV------------QNG--------------------------------VWVRQEPVFDSPINLGA 148
Cdd:cd02756 15 VTCHFCIVGCGYHVYVwpvgeeggpspgQNAigydlvdqvpplnlqwypktmhyvvvtqdgreVYIVIVPDKECPVNSGN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 149 HCAKGAALREH------GHGEYRLKYPMKLVNGKYQRISWDQALDEISAKLKQIRQETGPDSLFFIGSSKHSNEQSYLLR 222
Cdd:cd02756 95 YSTRGGTNAERiwspdnRVGETRLTTPLVRRGGQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFASRFDHGGGGGGFEN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 223 KWVS---FFGTNNTDHqARI---------CHSTTVAGVantwgyGAMTNSYNDMQNAKAALYIGSNAAEAHPVSML-HLL 289
Cdd:cd02756 175 NWGVgkfFFMALQTPF-VRIhnrpaynseVHATREMGV------GELNNSYEDARLADTIVLWGNNPYETQTVYFLnHWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 290 ------------HAKESG-----CKVIVVDPRYTRTAAKSDH--------YVRIRSGTDIAFLFGVLYHIfqngwedkky 344
Cdd:cd02756 248 pnlrgatvsekqQWFPPGepvppGRIIVVDPRRTETVHAAEAaagkdrvlHLQVNPGTDTALANAIARYI---------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 345 ladrVYGMDKVKEEvlakwtpdkVEEVCGVPEAEVRYVAETMAK-----NRPST-------LVWCMGQTQhTIGNaivra 412
Cdd:cd02756 318 ----YESLDEVLAE---------AEQITGVPRAQIEKAADWIAKpkeggYRKRVmfeyekgIIWGNDNYR-PIYS----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 413 scIVQLAL--GNIGVSGGGANIFRGHDnvQGATDVGPNPDSLPGYYG--------LAAGAWKhFATVWGVDYewIKKQFA 482
Cdd:cd02756 379 --LVNLAIitGNIGRPGTGCVRQGGHQ--EGYVRPPPPPPPWYPQYQyapyidqlLISGKGK-VLWVIGCDP--YKTTPN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 483 SQAMMEksgtTVSRWIDIVTEkpelidqdhnvrGVFFWGHAPNSQTRglEMKRALDKLD-----LLVVIDPYPSATAAMA 557
Cdd:cd02756 452 AQRLRE----TINHRSKLVTD------------AVEAALYAGTYDRE--AMVCLIGDAIqpgglFIVVQDIYPTKLAEDA 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737919411 558 NMpategdtpnpnravyLLPACTQFETS-GSCTASNRSLQWREKVIEPLFESMPDHAIMQAFAEKL 622
Cdd:cd02756 514 HV---------------ILPAAANGEMNeTSMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI 564
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
109-442 |
1.82e-19 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 92.22 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 109 VVRRTVCGHCSVGC-----AVD----AVVQNGvwvrqepvfdspinlgahCAKGAALREHGHGEYRLKYPMklVNGKYqr 179
Cdd:COG1029 4 VVKNVVCPFCGCLCddlevEVEggkiVVVKNA------------------CAIGAAKFERAVSDHRITSPR--IRGKE-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 180 ISWDQALDEISAKLKQIRQetgPdsLFFIGSSKHSNEQSYLLRKWVSFFGTnnTDHQARICHSTTVAGVANTwgyGAMTN 259
Cdd:COG1029 62 VSLEEAIDKAAEILANAKR---P--LIYGLSSTDCEAMRAGLALAERVGAV--VDNTASVCHGPSLLALQDV---GWPTC 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 260 SYNDMQN-AKAALYIGSNAAEAHPVSMLHLLHAKES--------GCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAfLFGV 330
Cdd:COG1029 132 TLGEVKNrADVIIYWGCNPVHAHPRHMSRYSVFPRGfftpkgrkDRTVIVVDPRPTDTAKVADLHLQVKPGRDYE-VLSA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 331 LyhifqngwedkkyladrvygmdkvkeEVLAKWTPDKVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTQ-----HTI 405
Cdd:COG1029 211 L--------------------------RALVRGKELSPEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQspgkhLNV 264
|
330 340 350
....*....|....*....|....*....|....*..
gi 737919411 406 GNAIvrasCIVQlALGNIGVSGGGANifRGHDNVQGA 442
Cdd:COG1029 265 DAAI----ELVR-DLNRYTKFSILPL--RGHYNVAGA 294
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
886-1023 |
7.85e-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: 83.06 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 886 EKFPIILTSGRLVEYEGGGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGArIKVRALVTERVGVDTA 965
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGS-VEVRARVTDRVPEGVV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 737919411 966 FIPFHFsgwwqgkdlkpyyPEGampivrgeAVNTATTYGYDSVTMMQETKTTVCQIER 1023
Cdd:cd02790 80 FMPFHF-------------AEA--------AANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
890-1017 |
1.90e-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: 81.94 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 890 IILTSGRLVEYEGGGEETRSNPWLAELQQEnFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPF 969
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPE-VVEIHPEDAAALGIKDGDLVEVTSRRG-SVVVRAKVTDRVRPGVVFMPF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 737919411 970 HfsgWWQGkdlkpyypegampiVRGEAVNTATTYGYDSVTMMQETKTT 1017
Cdd:pfam01568 79 G---WWYE--------------PRGGNANALTDDATDPLSGGPEFKTC 109
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
113-348 |
2.13e-18 |
|
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: 90.80 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 113 TVCGHCSVGCAVDAV-VQNGVWVRQEPVF---DSPINLGAHCAKGAALREHGHGEYRLKYPMKLVNGKYQR--------I 180
Cdd:cd02760 2 TYCYNCVAGPDFMAVkVVDGVATEIEPNFaaeDIHPARGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKKGRnedpgfvpI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 181 SWDQALDEISAKLKQIRQE-TGPDSLF--FIGSSKHSNEQSYLLRKWVSF---FGTNNTDHQArichSTTVAGVANTWGY 254
Cdd:cd02760 82 SWDEALDLVAAKLRRVREKgLLDEKGLprLAATFGHGGTPAMYMGTFPAFlaaWGPIDFSFGS----GQGVKCVHSEHLY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 255 GA-MTNSYN---DMQNAKAALYIGSNA-AEAHPVSMLHLLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFG 329
Cdd:cd02760 158 GEfWHRAFTvaaDTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPAFMFA 237
|
250 260
....*....|....*....|..
gi 737919411 330 ---VLYHIFQNGWEDKKYLADR 348
Cdd:cd02760 238 mihVMVHEQGLGKLDVPFLRDR 259
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
165-303 |
4.02e-16 |
|
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: 82.02 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 165 RLKYPMKLVNGKYQRISWDQALDEISAKLKQIRQETGPDSLFFIGSSKHSNEQSYLLRKWVSFFGTNNTDHQARICHSTT 244
Cdd:cd02772 54 RLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDFRD 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 737919411 245 VAGVANTWGYGAmtnSYNDMQNAKAALYIGSNAAEAHPVSMLHLLHAKESGCKVIVVDP 303
Cdd:cd02772 134 DAKASGAPWLGM---PIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINP 189
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
886-1024 |
5.60e-16 |
|
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: 74.92 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 886 EKFPIILTSGRLVEYEGGGEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTA 965
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRG-EVVLRVRVTDRVRPGEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 737919411 966 FIPFHFSGWWQgkdlkpyypegampivRGEAVNTATTYGYDSVTMMQETKTTVCQIERF 1024
Cdd:cd02791 80 FVPMHWGDQFG----------------RSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
906-1018 |
2.01e-15 |
|
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: 73.46 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 906 ETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTAFIPFHFSGWWQGKDLKPYyp 985
Cdd:cd02778 16 HTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARG-KVTGKARLTEGIRPDTVFMPHGFGHWAPALSRAYG-- 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 737919411 986 egampivRGEAVNTATTYGYDSVT---MMQETKTTV 1018
Cdd:cd02778 93 -------GGVNDNNLLPGSTEPVSggaGLQEFTVTV 121
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
886-1023 |
6.00e-15 |
|
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: 72.34 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 886 EKFPIILTSGRLVEYEGggEETRSNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTA 965
Cdd:cd02781 1 EYPLILTTGARSYYYFH--SEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRG-RARQKARLTPGIRPGVV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737919411 966 FIPFhfsGWWQGKDlkpyypEGAMPIVRGEA---VNTATT-YGYDSVTMMQETKTTVCQIER 1023
Cdd:cd02781 78 RAEH---GWWYPER------EAGEPALGGVWesnANALTSdDWNDPVSGSSPLRSMLCKIYK 130
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
110-159 |
2.40e-14 |
|
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: 68.04 E-value: 2.40e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 737919411 110 VRRTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREH 159
Cdd:smart00926 3 WVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQ 52
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
114-445 |
3.73e-12 |
|
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: 69.67 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 114 VCGHCSVGCAvDAVVQngvwvrqepVFDSPINLGAH-CAKGAALREHGhgEYRLKYPMklVNGKyqRISWDQALDEISAK 192
Cdd:cd02761 3 VCPFCGLLCD-DIEVE---------VEDNKITKVRNaCRIGAAKFARY--ERRITTPR--IDGK--PVSLEEAIEKAAEI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 193 LKQIRQetgpdSLFFIGSSKHSNEQSYLLR---KwvsffgTNNT-DHQARICHSTTVAGVANTwgyGAMTNSYNDMQN-A 267
Cdd:cd02761 67 LKEAKR-----PLFYGLGTTVCEAQRAGIElaeK------LGAIiDHAASVCHGPNLLALQDS---GWPTTTLGEVKNrA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 268 KAALYIGSNAAEAHPVSMLH--------LLHAKESGCKVIVVDPRYTRTAAKSDHYVRIRSGTDIAFLFGvlyhifqngw 339
Cdd:cd02761 133 DVIVYWGTNPMHAHPRHMSRysvfprgfFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAA---------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 340 edkkyLADRVYGMDKVkeevlakwtpdkVEEVCGVPEAEVRYVAETMAKNRPSTLVWCMGQTqHTIGNA--IVRASCIVQ 417
Cdd:cd02761 203 -----LRALLRGAGLV------------PDEVAGIPAETILELAERLKNAKFGVIFWGLGLL-PSRGAHrnIEAAIRLVK 264
|
330 340
....*....|....*....|....*...
gi 737919411 418 lALGNIGVSGGGAniFRGHDNVQGATDV 445
Cdd:cd02761 265 -ALNEYTKFALLP--LRGHYNVRGFNQV 289
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
910-984 |
2.09e-11 |
|
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: 62.70 E-value: 2.09e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737919411 910 NPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGArIKVRALVTERVGVDTAFIPFHFSGWWQGKDLKPYY 984
Cdd:cd02780 20 APWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGS-VVGKAKVTEGVRPGVVAIEHGYGHWAYGAVASTID 93
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
150-346 |
4.50e-11 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 67.33 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 150 CAKGAALREHGHGEYRLKYPMKLV----NGKYQRISWDQALDEIS-----------AKLKQIRQ----------ETGPDS 204
Cdd:PRK14991 142 CARGNAMLEQLDSPYRVLQPLKRVgkrgSGKWQRISFEQLVEEVVeggdlfgeghvDGLRAIRDldtpidaknpEYGPKA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 205 --LFFIGSSkhsNE--QSYLLRKWVSFFGTNNTDHQARIChsttvaGVANTWGYGAMTNSYN-------DMQNAKAALYI 273
Cdd:PRK14991 222 nqLLVTNAS---DEgrDAFIKRFAFNSFGTRNFGNHGSYC------GLAYRAGSGALMGDLDknphvkpDWDNVEFALFI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 274 GSNAAEA-HPVSMLHLLHAK---ESGCKVIVVDPRYTRT----AAKSDHYVRIRSGTDIAFLFGVLYHIFQNGWEDKKYL 345
Cdd:PRK14991 293 GTSPAQSgNPFKRQARQLANartRGNFEYVVVAPALPLSsslaAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYL 372
|
.
gi 737919411 346 A 346
Cdd:PRK14991 373 A 373
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
111-198 |
4.91e-11 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 66.02 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 111 RRTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGaalR---EHGHGEYRLKYPMKLVNGKYQRISWDQALD 187
Cdd:COG1034 218 TPSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKG---RfgyDGLNSPDRLTRPLVRKDGELVEASWEEALA 294
|
90
....*....|.
gi 737919411 188 EISAKLKQIRQ 198
Cdd:COG1034 295 AAAEGLKALKK 305
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
110-162 |
8.40e-10 |
|
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: 55.38 E-value: 8.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 737919411 110 VRRTVCGHCSVGCAVDAVVQNGVWVRQEPVFDSPINLGAHCAKGAALREHGHG 162
Cdd:pfam04879 3 VVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
909-987 |
1.04e-08 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 54.29 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 909 SNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTE--RVGVDTAfipfhFSGWWqgkdlKPYYPE 986
Cdd:cd02785 21 NVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRG-SVVCKAKVDDgiQPGVVTA-----EQGWW-----SRYFQE 89
|
.
gi 737919411 987 G 987
Cdd:cd02785 90 G 90
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
910-1003 |
2.98e-05 |
|
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: 44.59 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 910 NPWLAELQQENFVeINPKAASERGIRNGDYCWVKTPTGARIkVRALVTERV--GVdtafIPFHFSGWWQgkdlkpyyPEG 987
Cdd:cd02794 21 VPWLREAFPQEVW-INPLDAAARGIKDGDRVLVFNDRGKVI-RPVKVTERImpGV----VALPQGAWYE--------PDA 86
|
90
....*....|....*.
gi 737919411 988 AmPIVRGEAVNTATTY 1003
Cdd:cd02794 87 N-GIDKGGCINTLTGL 101
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
910-965 |
5.64e-05 |
|
The MopB_CT_2 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: 239184 [Multi-domain] Cd Length: 156 Bit Score: 44.37 E-value: 5.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 737919411 910 NPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGaRIKVRALVTERVGVDTA 965
Cdd:cd02783 22 NAWLRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNG-RVKGQARFTETVEPGTV 76
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
909-975 |
1.02e-04 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 42.65 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737919411 909 SNPWLAELQQENFVEINPKAASERGIRNGDYCWVKTPTGArIKVRALVTERV--GVDTAfipfhFSGWW 975
Cdd:cd02786 20 NLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGS-VTLRAKVTDDVppGVVVA-----EGGWW 82
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
910-1003 |
1.12e-03 |
|
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: 39.88 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737919411 910 NPWLAELQQENFVE---INPKAASERGIRNGDYCWVKTPTGARIkVRALVTERV--GVdtafIPFHFSGWWQgkdlkpyy 984
Cdd:cd02777 21 VPWLREAYKVKGREpvwINPLDAAARGIKDGDIVRVFNDRGAVL-AGARVTDRImpGV----VALPEGAWYD-------- 87
|
90
....*....|....*....
gi 737919411 985 PEGAMPIVRGEAVNTATTY 1003
Cdd:cd02777 88 PDDNGGLDKGGNPNVLTSD 106
|
|
| |
