|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
7-695 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 906.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEArqrsgFQATGVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALD 85
Cdd:COG3383 9 TVCPYCGVGCGIDLEVKDGKI-----VKVEGDPDHpVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 86 TVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRFCMSAAASAGVKTFGIDrGLTNQLSEIP 165
Cdd:COG3383 84 LVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSD-APPNSYDDIE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 166 LAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDSAFI 245
Cdd:COG3383 163 EADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 246 QSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIGRE 325
Cdd:COG3383 243 AERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 326 GCGYGAVTGQGNGQGGREHGQKADQLPGYRSIENENDRAFVAKVWGIPPeeLPGK-GVSAYEMMELVHQEQIKALFVMGS 404
Cdd:COG3383 323 GTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKpGLTAVEMFDAIADGEIKALWIIGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 405 NPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQILC 484
Cdd:COG3383 401 NPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 485 SVAEKLGRGayFPYKDAEEIFNELRKASqggiADYFGITYERLRREEGIYWPCPSTDHPGTGRLFEYSFAHADGLARFQT 564
Cdd:COG3383 481 ELARRLGYG--FDYDSPEEVFDEIARLT----PDYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFPTPDGKARFVP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 565 VPVALQGEETNSEYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSR 644
Cdd:COG3383 555 VEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRAR 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2306680097 645 YSDKIREDTVFIPMHWGDAqNVNLATNPELDPYCKMPDFKVSAVRVRPLAE 695
Cdd:COG3383 635 VTDRVRPGTVFMPFHWGEG-AANALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
7-567 |
0e+00 |
|
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: 725.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEArqrsgFQATGVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVRKNG-ELVRSSWEEAL 84
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKV-----VAVRGDPEHpVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 85 DTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRFCMSAAASAGVKTFGIDrGLTNQLSEI 164
Cdd:cd02754 77 DLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGAD-GPPGSYDDI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 165 PLAECIILAGTNIAECQPTLMPYFIRAKEN--GAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDS 242
Cdd:cd02754 156 EHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 243 AFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKI 322
Cdd:cd02754 236 DFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 323 GREGCGYGAVTGQGNGQGGREHGQKADQLPGYRSIENENDRAFVAKVWGIPPEELPGK-GVSAYEMMELVHQEQIKALFV 401
Cdd:cd02754 316 GRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVEMFEAIEDGEIKALWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 402 MGSNPVVSNPHASLVEEGIRKLDFLVVADMFL-SETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDW 480
Cdd:cd02754 396 MCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 481 QILCSVAEKLGRGAYFPYKDAEEIFNELRKASQGGIADYFGITYERLRReEGIYWPCPSTDHPGTGRLFE-YSFAHADGL 559
Cdd:cd02754 476 WILADVARRLGFGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEdGRFPTPDGR 554
|
....*...
gi 2306680097 560 ARFQTVPV 567
Cdd:cd02754 555 ARFVAVPY 562
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
7-690 |
0e+00 |
|
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: 610.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARQRSGFQAtgvpNAASEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALDT 86
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQG----HKANRGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAISY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 87 VAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRFCMSAAASAGVKTFGIDRGlTNQLSEIPL 166
Cdd:TIGR01591 77 IAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAM-SNTISEIEN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 167 AECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDSAFIQ 246
Cdd:TIGR01591 156 ADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 247 SRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIGREG 326
Cdd:TIGR01591 236 KRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 327 CGYGAVTGQGNGQGGREHGQKADQLPGYRSIENENDRAFVAKVWGIppEELPGK-GVSAYEMMELVHQEQIKALFVMGSN 405
Cdd:TIGR01591 316 GGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGV--VKLPAEpGLRIPEMIDAAADGDVKALYIMGED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 406 PVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQILCS 485
Cdd:TIGR01591 394 PLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 486 VAEKLgrGAYFPYKDAEEIFNELRKASQggiaDYFGITYERLRREEGIYWPCPSTDHPGTGRLFEYSFAHADGLARFQTV 565
Cdd:TIGR01591 474 LANAL--GLDWNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKFIPL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 566 PVALQGEETNSEYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRY 645
Cdd:TIGR01591 548 EWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKV 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2306680097 646 SDKIREDTVFIPMHWGDAQnVNLATNPELDPYCKMPDFKVSAVRV 690
Cdd:TIGR01591 628 SDRVNKGAIYITMHFWDGA-VNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
4-695 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 573.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 4 TMNTQCPFCSVQCKMTVEITPGEARQrsgfqATGVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVRKN----GELVRS 78
Cdd:COG0243 23 TVKTTCPGCGVGCGLGVKVEDGRVVR-----VRGDPDHpVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGKFERI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 79 SWEEALDTVAARFSVIQEAYGRDAVGVYGGGS----LTNETAYALGKFARvALRSRYIDYNGRFCMSAAASAGVKTFGID 154
Cdd:COG0243 98 SWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGsagrLSNEAAYLAQRFAR-ALGTNNLDDNSRLCHESAVAGLPRTFGSD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 155 RGlTNQLSEIPLAECIILAGTNIAECQPTLMPYFIRA-KENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKV 233
Cdd:COG0243 177 KG-TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 234 ILDENLIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFL 313
Cdd:COG0243 256 LIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 314 NMVLATGKIGREGCGYGAVTGqgngqggrehgqkadqlpgyrsienendrafvakvwgippeelpgkgvsayEMMELVHQ 393
Cdd:COG0243 336 NLALLTGNIGKPGGGPFSLTG---------------------------------------------------EAILDGKP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 394 EQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLE-GRVLLREAARSA 472
Cdd:COG0243 365 YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 473 PGETRHDWQILCSVAEKLGRGAYFPY-KDAEEIFNELRKASQGGiadyfGITYERLRREEGIYWPCPstdhPGTGRLFEY 551
Cdd:COG0243 445 PGEARSDWEIFAELAKRLGFEEAFPWgRTEEDYLRELLEATRGR-----GITFEELREKGPVQLPVP----PEPAFRNDG 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 552 SFAHADGLARF-----------QTVPVALQGEETNSEYPLMMTNGRVLPHYLTgvQTRRSPVLAAKFVESFMEIHPLTAR 620
Cdd:COG0243 516 PFPTPSGKAEFysetlalpplpRYAPPYEGAEPLDAEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPEDAA 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 621 KHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMHWG------DAQNVNLATNPELDPYCKMPDFKVSAVRVRPLA 694
Cdd:COG0243 594 ALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKAA 673
|
.
gi 2306680097 695 E 695
Cdd:COG0243 674 A 674
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
7-565 |
0e+00 |
|
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: 529.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEArqrsgFQATGVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALD 85
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKI-----VGVEPVKGHpVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 86 TVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRFCMSAAASAGVKTFGIDRGlTNQLSEIP 165
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAM-TNSIADIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 166 LAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDSAFI 245
Cdd:cd02753 156 EADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 246 QSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIGRE 325
Cdd:cd02753 236 EERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 326 GCGYGAVTGQGNGQGGREHGQKADQLPGYrsienendrafvakvwgippeelpgkgvsayemmelvhqeqIKALFVMGSN 405
Cdd:cd02753 316 GTGVNPLRGQNNVQGACDMGALPNVLPGY-----------------------------------------VKALYIMGEN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 406 PVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQILCS 485
Cdd:cd02753 355 PALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 486 VAEKLG-RGAYFpykDAEEIFNELRKAsqggIADYFGITYERLRREEGIYWPCPSTDHPGTGRLFEYSFAHADGLARFQT 564
Cdd:cd02753 435 LANRLGyPGFYS---HPEEIFDEIARL----TPQYAGISYERLERPGGLQWPCPDEDHPGTPILHTERFATPDGKARFMP 507
|
.
gi 2306680097 565 V 565
Cdd:cd02753 508 V 508
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
7-490 |
7.17e-113 |
|
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: 345.08 E-value: 7.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARQrsgfqATGVPN-AASEGRLCVKGMNAHQHASSRDRLLFPLVRKN--GELVRSSWEEA 83
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVR-----IEGDPNhPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 84 LDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARvALRSRYIDYNGRFCMSAAAsAGVKTFGIDrGLTNQLSE 163
Cdd:cd00368 77 LDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAV-AALKAFGGG-APTNTLAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 164 IPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGmlkvildenlidsa 243
Cdd:cd00368 154 IENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA-------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 244 fiqsrtkdfdqlkadllridlEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIG 323
Cdd:cd00368 220 ---------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 324 REGCGYGAvtgqgngqggrehgqkadqlpgyrsienendrafvakvwgippeelpgkgvsayemmelvhqeqikalfvmG 403
Cdd:cd00368 279 RPGGGLGP-----------------------------------------------------------------------G 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 404 SNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQIL 483
Cdd:cd00368 288 GNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEIL 367
|
....*..
gi 2306680097 484 CSVAEKL 490
Cdd:cd00368 368 RELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
9-562 |
1.60e-88 |
|
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: 286.07 E-value: 1.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPF-CSVQCKMTVEITPGEArqrsgFQATGVP-NAASEGRLCVKGMNAHQHASSRDRLLFPLVR---KNGELVRSSWEEA 83
Cdd:cd02766 4 CPLdCPDTCSLLVTVEDGRI-----VRVEGDPaHPYTRGFICAKGARYVERVYSPDRLLTPLKRvgrKGGQWERISWDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 84 LDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNgrFCMSAAASAGVKTFGIDRGltNQLSE 163
Cdd:cd02766 79 LDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGT--ICSGAGIEAQKYDFGASLG--NDPED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 164 IPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDSA 243
Cdd:cd02766 155 MVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 244 FIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVR--NFLNMVlaTGK 321
Cdd:cd02766 235 FLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRaiDALPAL--TGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 322 IGREGCGYGAVTGQgngqggrehgqkadqlpgyrsienendrafvakvwgiPPeelpgkgvsayemmelvhqeqIKALFV 401
Cdd:cd02766 313 IGVPGGGAFYSNSG-------------------------------------PP---------------------VKALWV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 402 MGSNPVVSNPHASLVEEG-IRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGR-VLLREAARSAPGETRHD 479
Cdd:cd02766 335 YNSNPVAQAPDSNKVRKGlAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYyLQYNEPAIPPPGEARSN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 480 WQILCSVAEKLGRGAYFPYKDAEEIfneLRKASQGGIADYFGITYERLRreegiywPCPSTDHPGTgRLFEYSFAHADGL 559
Cdd:cd02766 415 TEIFRELAKRLGFGEPPFEESDEEW---LDQALDGTGLPLEGIDLERLL-------GPRKAGFPLV-AWEDRGFPTPSGK 483
|
...
gi 2306680097 560 ARF 562
Cdd:cd02766 484 FEF 486
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
63-489 |
5.35e-80 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 259.25 E-value: 5.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 63 RLLFPLVRKN-GELVRSSWEEALDTVAARFSVIQEAYGRDAVGVYG--GGSLTNETAYALGKFARV--ALRSRYIDYNGR 137
Cdd:pfam00384 1 RLKYPMVRRGdGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGgsGGLTDVESLYALKKLLNRlgSKNGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 138 FCMSAAASAGVkTFGIDRGLTNQLSEIPLAECIILAGTNIAECQPTLMPYFI-RAKENGAFIIVIDPRATATaeLADLHL 216
Cdd:pfam00384 81 LCTAAAAAFGS-DLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGPRLDLT--YADEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 217 QVKPGTDSALVSGMLKVILDENLIDSAFiqsrtkdfdqlkadllridlegiaeltgvrieqirtaavtyakAGTGMVFTA 296
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 297 RGVEQHADGHMAVRNFLNMVLATGKIGREGCGYGAVTgqgNGQG-GREHGQKADQLPgyrsienendrafvakvwgippe 375
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGaASPVGALDLGLV----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 376 elpgKGVSAYEMMELVHQEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFL-SETAKYADVVLPVTSYMENEG 454
Cdd:pfam00384 249 ----PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
410 420 430
....*....|....*....|....*....|....*
gi 2306680097 455 TLTNLEGRVLLREAARSAPGETRHDWQILCSVAEK 489
Cdd:pfam00384 325 TYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-490 |
1.53e-74 |
|
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: 250.39 E-value: 1.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGE-ARQRsgfqatGVP-NAASEGRLCVKG--MNAHQHasSRDRLLFPLVRKNGELVRSSWEE 82
Cdd:cd02762 2 RACILCEANCGLVVTVEDGRvASIR------GDPdDPLSKGYICPKAaaLGDYQN--DPDRLRTPMRRRGGSFEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 83 ALDTVAARFSVIQEAYGRDAVGVYGGGSLTNEtaYALGKFARVALRSryIDYNGRFcmsAAASAGVKT--------FGid 154
Cdd:cd02762 74 AFDEIAERLRAIRARHGGDAVGVYGGNPQAHT--HAGGAYSPALLKA--LGTSNYF---SAATADQKPghfwsglmFG-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 155 RGLTNQLSEIPLAECIILAGTNIAECQ--PTLMPYFIR----AKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVS 228
Cdd:cd02762 145 HPGLHPVPDIDRTDYLLILGANPLQSNgsLRTAPDRVLrlkaAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 229 GMLKVILDENLIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMA 308
Cdd:cd02762 225 AMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 309 --VRNFLNmvLATGKIGREG---CGYGAVTGQGN-GQGGREHGQKADQLPGYRSIENEndrafvakvwgIPPEELPgkgv 382
Cdd:cd02762 305 swLVKLLN--LLTGNLDRPGgamFTTPALDLVGQtSGRTIGRGEWRSRVSGLPEIAGE-----------LPVNVLA---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 383 sayEMMELVHQEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMEN-EGTLTNLE- 460
Cdd:cd02762 368 ---EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKpHATFFNLEf 444
|
490 500 510
....*....|....*....|....*....|..
gi 2306680097 461 --GRVLLREAARSAPGETRHDWQILCSVAEKL 490
Cdd:cd02762 445 prNAFRYRRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
7-491 |
5.27e-72 |
|
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: 246.16 E-value: 5.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEArqrsgFQATGVP-NAASEGRLCVKGMNAHQHASSRDRLLFPLVRKNG--ELVRSSWEEA 83
Cdd:cd02752 2 TICPYCSVGCGLIAYVQNGVW-----VHQEGDPdHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 84 LDTVAARFSVIQEA------------YGRDAVGVYGGGSLTNETAYALGKFARvALRSRYIDYNGRFCMSAAASAGVKTF 151
Cdd:cd02752 77 LDEIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLANTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 152 GidRG-LTNQLSEIPLAECIILAGTNIAECQPTLMPYFIRAKE-NGAFIIVIDPRATATAELADLHLQVKPGTDSALVSG 229
Cdd:cd02752 156 G--RGaMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 230 MLKVIldenlidsafiqsrtkdfdqlkadlLRIDLEGIAELTGVRIEQIRTAAVTYAKAG----TGMVFTARGVEQHADG 305
Cdd:cd02752 234 MINYI-------------------------IRYTPEEVEDICGVPKEDFLKVAEMFAATGrpdkPGTILYAMGWTQHTVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 306 HMAVRNFLNMVLATGKIGREGCGYGAVTGQGNGQGGREHGQKADQLPGYRSienendrafvakvwgippeelpgkgvsay 385
Cdd:cd02752 289 SQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG----------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 386 emmelvhqeqikalfvmGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYAD-------------VVLPVTSYMEN 452
Cdd:cd02752 340 -----------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEK 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2306680097 453 EGTLTNlEGRVL-LREAARSAPGETRHDWQILCSVAEKLG 491
Cdd:cd02752 403 EGSITN-SGRWLqWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
9-517 |
1.24e-71 |
|
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: 240.67 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEITPGEARQRSGFQATGVPNaaseGRLCVKGMNAHQHASSRDRLLFPLVRKN----GELVRSSWEEAL 84
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNK----GRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERISWDEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 85 DTVAARFSVIQEAYGRDAVGVYGGGSltNETAYALGKFARVALR---SRYIDYNGRFC-MSAAASAGVKTFGidrGLTNQ 160
Cdd:cd02759 80 DEIAEKLAEIKAEYGPESIATAVGTG--RGTMWQDSLFWIRFVRlfgSPNLFLSGESCyWPRDMAHALTTGF---GLGYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 161 LSEIPLAECIILAGTNIAECQPTLMPY-FIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENL 239
Cdd:cd02759 155 EPDWENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIINEGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 240 IDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVlat 319
Cdd:cd02759 235 YDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 320 gkigregcgygAVTGQGNGQGGrehgqkadqlpgyrsienendrafvaKVWGIPPeelpgkgvsayemmelvhqeqIKAL 399
Cdd:cd02759 312 -----------AITGNLDVPGG--------------------------NLLIPYP---------------------VKML 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 400 FVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGR--VLLREAARSAPGETR 477
Cdd:cd02759 334 IVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPYGEAK 413
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2306680097 478 HDWQILCSVAEKLGRG--AYFPYKdaeeiFNELRKASQGGIA 517
Cdd:cd02759 414 SDYEIVLELGKRLGPEeaEYYKYE-----KGLLRPDGQPGFN 450
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
9-690 |
1.01e-70 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 246.35 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVeitpgeARQRSGFQAT-GVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVR-------KNGELVRSS 79
Cdd:PRK13532 47 CRFCGTGCGVLV------GTKDGRVVATqGDPDApVNRGLNCIKGYFLSKIMYGKDRLTQPLLRmkdgkydKEGEFTPVS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 80 WEEALDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRFCMSAAASAGVKTFGIDR--GL 157
Cdd:PRK13532 121 WDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEpmGC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 158 TNqlsEIPLAECIILAGTNIAECQPTLMPYFI--RAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVIL 235
Cdd:PRK13532 201 YD---DIEAADAFVLWGSNMAEMHPILWSRVTdrRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 236 DENLIDSAFIQSRTK----------------------------------DFDQLKADLLRIDLEGIAELTGVRIEQIRTA 281
Cdd:PRK13532 278 QNNAVNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 282 AVTYAKAGTGMV-FTARGVEQHADGHMAVRNFLNMVLATGKIGREGCGYGAVTGQGNGQG-GREHGQKADQLPGYRSIEN 359
Cdd:PRK13532 358 AKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPADMVVTN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 360 ENDRAFVAKVWGIPPEELPGK-GVSAYEMMELVHQEQIKALFVMGSNPVVSNPHASlvEEGI---RKLD-FLVVADMFLS 434
Cdd:PRK13532 438 PKHREIAEKIWKLPEGTIPPKpGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgwRNPDnFIVVSDPYPT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 435 ETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHD-WQI----------------------------LCS 485
Cdd:PRK13532 516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLvefskrfkteevwpeellakkpeyrgktLYD 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 486 VAEKLGRGAYFPYKDAEE-----------------IFNELRKASQG---GIADYfgITYERLRreeGIYWPC-------- 537
Cdd:PRK13532 596 VLFANGQVDKFPLSELAEgylndeakhfgfyvqkgLFEEYASFGRGhghDLAPF--DTYHKVR---GLRWPVvdgketlw 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 538 ---PSTD---HPGTGRLFeysFAHADGLARFQTVPVALQGEETNSEYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESF 611
Cdd:PRK13532 671 ryrEGYDpyvKAGEGFKF---YGKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELYRAFPEAV 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 612 MEIHPLTARKHRIEEGALVRVSSKRGTVTVR--SRYSDKIREDTVFIPmhWGDA-QNVNLATNPELDPYCKMPDFKVSAV 688
Cdd:PRK13532 748 CFMHPEDAKARGLRRGDEVKVVSRRGEVKSRveTRGRNKPPRGLVFVP--FFDAaQLINKLTLDATDPLSKQTDFKKCAV 825
|
..
gi 2306680097 689 RV 690
Cdd:PRK13532 826 KI 827
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
46-534 |
2.17e-64 |
|
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: 224.89 E-value: 2.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 46 RLCVKGMNAHQHASSRDRLLFPLVRKN----GELVRSSWEEALDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGK 121
Cdd:cd02770 42 RACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 122 FARV-ALRSRYIDYNGRFCMSAAASAGVKTFGIDrGLTNQLSEIPLAECIILAGTNIAEcqpTLMP------YFIRAKEN 194
Cdd:cd02770 122 IARLlNLTGGYLNYYGTYSWAQITTATPYTYGAA-ASGSSLDDLKDSKLVVLFGHNPAE---TRMGgggstyYYLQAKKA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 195 GAFIIVIDPRATATAE-LADLHLQVKPGTDSALVSGMLKVILDENLIDSAFIQSRTKDFDQ------------LKADLLR 261
Cdd:cd02770 198 GAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYVLG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 262 IDLEGI-------AELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFlnMVLA--TGKIGREGCGYGAV 332
Cdd:cd02770 278 TGYDGTpktpewaSEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAI--MMLAamTGNVGIPGGNTGAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 333 TGQGNGQGgrehgqkadqlPGYRSIENENDRAFVAKVW--GIppeeLPGKGVSAYEMMELVHQE---QIKALFVMGSNpV 407
Cdd:cd02770 356 PGGSAYNG-----------AGLPAGKNPVKTSIPCFMWtdAI----ERGEEMTADDGGVKGADKlksNIKMIWNYAGN-T 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 408 VSNPHASL------VEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTN----LEGRVLLREAARSAPGETR 477
Cdd:cd02770 420 LINQHSDDnnttraLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnagMMEYLIYSQKAIEPLYECK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2306680097 478 HDWQILCSVAEKLGRGAYFPY-KDAEEIFNELrkASQGGIADYFGITYERLrREEGIY 534
Cdd:cd02770 500 SDYEICAELAKRLGVEDQFTEgKTEQEWLEEL--YGQTRAKEPGLPTYEEF-REKGIY 554
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
39-534 |
1.33e-61 |
|
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: 217.10 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 39 PNAASEGRLCVKGMNAHQHASSRDRLLFPLVRK--------------NGELVRSSWEEALDTVAARFSVIQEAYGRDAV- 103
Cdd:cd02751 23 PDDTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVgwlgngpgsrelrgEGEFVRISWDEALDLVASELKRIREKYGNEAIf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 104 GVYGGGSLTNETAYALGKFAR-VALRSRYIDYNGRFCMSAAASAGVKTFGIDRGLTNQLSeIPL----AECIILAGTNIA 178
Cdd:cd02751 103 GGSYGWASAGRLHHAQSLLHRfLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYEQGTS-WDDiaehSDLVVLFGANPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 179 ECQP--------TLMPYFIRAKENGAFIIVIDPRATATAE-LADLHLQVKPGTDSALVSGMLKVILDENLIDSAFIQSRT 249
Cdd:cd02751 182 KTRQgggggpdhGSYYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 250 KDFDQLKADLL-RIDleGI-------AELTGVRIEQIRTAAVTYAKaGTGMVFTARGVEQHADGHMAVRNFlnMVLA--T 319
Cdd:cd02751 262 VGFDEFKDYLLgESD--GVpktpewaAEITGVPAETIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWML--VTLAamL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 320 GKIGREGCGYGAVTGQGNGQGGrehGQKADQLPGYRSIENENDRAF-VAKVW-GI--PPEELPGKGvsayemmELVHQEQ 395
Cdd:cd02751 337 GQIGLPGGGFGFGYGYSNGGGP---PRGGAGGPGLPQGKNPVKDSIpVARIAdALlnPGKEFTANG-------KLKTYPD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 396 IKALFVMGSNPVVSnpHASLVE--EGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENE--GTLTNLEGRVLLREAARS 471
Cdd:cd02751 407 IKMIYWAGGNPLHH--HQDLNRliKALRKDETIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYSNRYLIAMKQAV 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306680097 472 AP-GETRHDWQILCSVAEKLGRGAYFPY-KDAEE----IFNELRKASQGGIADYfgITYERLrREEGIY 534
Cdd:cd02751 485 EPlGEARSDYEIFAELAKRLGVEEEFTEgRDEMEwlehLYEETRAKAAGPGPEL--PSFEEF-WEKGIV 550
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-490 |
2.49e-60 |
|
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: 212.55 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 63 RLLFPLVRKNGE--LVRSSWEEALDTVAARFSVIQEaygrDAVGVYGGGSLTNETAYALGKFARvALRSRYIDYNGRFCM 140
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRALDP----DRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 141 SAAASAGVKTFGIDRGlTNQLSEIPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDP----------------- 203
Cdd:cd02767 139 EPSSVGLKKSIGVGKG-TVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPlrepglerfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 204 RATATAELADLHLQVKPGTDSALVSGMLKVILDE-----NLIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQI 278
Cdd:cd02767 218 MLTGGTKIADEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 279 RTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIGREGCGYGAVTGQGNGQGGREHG-------QKADQL 351
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGitekpfpEFLDAL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 352 pgyrsienendrafvAKVWGIPPEELPGKGVSayEMMELVHQEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADM 431
Cdd:cd02767 378 ---------------EEVFGFTPPRDPGLDTV--EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVAT 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 432 FLSETA---KYADVVLPVTS--------------YMENEGTLTNL-------EGRVLLREAARSA------PGETRHDWQ 481
Cdd:cd02767 441 KLNRSHlvhGEEALILPCLGrteidmqaggaqavTVEDSMSMTHTsrgrlkpASRVLLSEEAIVAgiagarLGEAKPEWE 520
|
....*....
gi 2306680097 482 ILCSVAEKL 490
Cdd:cd02767 521 ILVEDYDRI 529
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
9-533 |
7.32e-57 |
|
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: 203.09 E-value: 7.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPF-CSVQCKMTVEITPGEarqrsgfqatgvPNAASEGRLCVKGMNAHQHASSRDRLLFPLVR----KNGELVRSSWEEA 83
Cdd:cd02765 12 CPLkCHVRDGKIVKVEPNE------------WPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFERITWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 84 LDTVAARFSVIQEAYGRDAVGVYGGgsltnetAYALGKFARVALRSryidyngrfcmSAAASAGVKTFGIDRGL------ 157
Cdd:cd02765 80 LDTIADKLTEAKREYGGKSILWMSS-------SGDGAILSYLRLAL-----------LGGGLQDALTYGIDTGVgqgfnr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 158 ---------TNQLSEIPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVS 228
Cdd:cd02765 142 vtgggfmppTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 229 GMLKVILDENLIDSAFIQSRTKDFDQLKAD---LLRIDLEGIA----------ELTGVrIEQIRTAAVTYAKAGTgmvFT 295
Cdd:cd02765 222 GMINYILEHNWYDEAFLKSNTSAPFLVREDngtLLRQADVTATpaedgyvvwdTNSDS-PEPVAATNINPALEGE---YT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 296 ARGVEQHAdGHMAVRNflNMVLATGKIGREGCGYGAVT--------GQGNGQGGREHGqkadqlpGYRSIENENDRAFVA 367
Cdd:cd02765 298 INGVKVHT-VLTALRE--QAASYPPKAAAEICGLEEAIietlaewyATGKPSGIWGFG-------GVDRYYHSHVFGRTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 368 KVWGIPPEEL--PGKGVSayemmelvhqeQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLP 445
Cdd:cd02765 368 AILAALTGNIgrVGGGVG-----------QIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 446 VTSYMENEGTLTNLEGR--VLLREAARSAPGETRHDWQILCSVAEKLGRGAYFPyKDAEEIFNELRKASQGGIAdyfGIT 523
Cdd:cd02765 437 AAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFP-KTPEDYVRAFMNSDDPALD---GIT 512
|
570
....*....|
gi 2306680097 524 YERLrREEGI 533
Cdd:cd02765 513 WEAL-KEEGI 521
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
9-492 |
7.04e-54 |
|
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: 192.13 E-value: 7.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEITPGEARQRSGFQAtgvpNAASEGRLCVKGMNAHQHASSRDRLLFPLVR--KNGE--LVRSSWEEAL 84
Cdd:cd02755 5 CEMCSSRCGILARVEDGRVVKIDGNPL----SPLSRGKLCARGNAGIQLLYDPDRLKKPLIRvgERGEgkFREASWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 85 DTVAARFSVIQEAYGRDAVgVYGGGSLTNETAyaLGKFARvALRSRYIDYNGRFCMSAAASAGVKTFGIDRG-----LTN 159
Cdd:cd02755 81 QYIASKLKEIKEQHGPESV-LFGGHGGCYSPF--FKHFAA-AFGSPNIFSHESTCLASKNLAWKLVIDSFGGevnpdFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 160 qlseiplAECIILAGTNIAEC-QPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDEN 238
Cdd:cd02755 157 -------ARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISEN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 239 LIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFtargveqhADGHMAVRN------- 311
Cdd:cd02755 230 LYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVV--------DPGWRGTFYsnsfqtr 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 312 ---FLNMVLaTGKIGREGcgygavtgqgngqggrehgqkadqlpgyrsienendrafvakvwGIPPEELPGKGvsayemm 388
Cdd:cd02755 302 raiAIINAL-LGNIDKRG--------------------------------------------GLYYAGSAKPY------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 389 elvhqeQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEG---RVLL 465
Cdd:cd02755 330 ------PIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGpapAVAT 403
|
490 500
....*....|....*....|....*..
gi 2306680097 466 REAARSAPGETRHDWQILCSVAEKLGR 492
Cdd:cd02755 404 RQRAIEPLYDTRPGWDILKELARRLGL 430
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
9-674 |
6.54e-53 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 195.27 E-value: 6.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEITPGEARqrsgFqATGVPNAAS-EGRLCVKGMNAHQHASSRDRLLFPLVRK----NGELVRSSWEEA 83
Cdd:PRK15488 48 CEMCSTRCPIEARVVNGKNV----F-IQGNPKAKSfGTKVCARGGSGHSLLYDPQRIVKPLKRVgergEGKWQEISWDEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 84 LDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKfarvALRSRYIDYNGRFCMSAAASAGVKTFG--IDRGLTNql 161
Cdd:PRK15488 123 YQEIAAKLNAIKQQHGPESVAFSSKSGSLSSHLFHLAT----AFGSPNTFTHASTCPAGYAIAAKVMFGgkLKRDLAN-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 162 seiplAECII------LAGTNIAECQpTLMPYfirAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVIL 235
Cdd:PRK15488 197 -----SKYIInfghnlYEGINMSDTR-GLMTA---QMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 236 DENLIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTArgveqhadGHMA------- 308
Cdd:PRK15488 268 EENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDF--------GHRAtftpeef 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 309 -VRNFLNMVLA-TGKIGREGCGYGAVTGQGNGQGGREhgQKADQL-----PGYRSIENEN-DRA-----FVAKVWG---- 371
Cdd:PRK15488 340 dMRRAIFAANVlLGNIERKGGLYFGKNASVYNKLAGE--KVAPTLakpgvKGMPKPTAKRiDLVgeqfkYIAAGGGvvqs 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 372 IPPEELPGKgvsAYemmelvhqeQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYME 451
Cdd:PRK15488 418 IIDATLTQK---PY---------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 452 NEGTLTNLEGRV---LLREAARSAPGETRHDWQILCSVAEKLGRGAYFPYKDAEE-----------IFNELRK---ASQG 514
Cdd:PRK15488 486 RDEEISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWQDMETlqlyqvngdhaLLKELKKkgyVSFG 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 515 --------GIADYFGITY--ERLRREEGIYWPCPS-TDHPGTGRLFEYSF-AHADGLARFQTVPVALQgeetnSEYPLMM 582
Cdd:PRK15488 566 vplllrepKMVAKFVARYpnAKAVDEDGTYGSQLKfKTPSGKIELFSAKLeALAPGYGVPRYRDVALK-----KEDELYF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 583 TNGRVLPHylTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMHWGd 662
Cdd:PRK15488 641 IQGKVAVH--TNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFG- 717
|
730
....*....|..
gi 2306680097 663 aqnvnlATNPEL 674
Cdd:PRK15488 718 ------SKNKEL 723
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
577-692 |
2.93e-49 |
|
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: 168.45 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 577 EYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFI 656
Cdd:cd00508 2 EYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFM 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 2306680097 657 PMHWGD---AQNVNLATNPELDPYCKMPDFKVSAVRVRP 692
Cdd:cd00508 82 PFHWGGevsGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| 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 ... |
9-515 |
1.01e-48 |
|
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: 178.35 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEITPGEARQRSGfqatGVPNAASEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALDTVA 88
Cdd:cd02771 4 CHHCSVGCNISLGERYGELRRVEN----RYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 89 ARFSVIqeaygRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGRfcMSAAASagVKTFGIDRGltnQLSEIPLAE 168
Cdd:cd02771 80 ARLKEA-----KDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRAR--RLIAEI--LRNGPIYIP---SLRDIESAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 169 CIILAGTNIAECQPtLMPYFIR-AKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDenlIDSAFIQS 247
Cdd:cd02771 148 AVLVLGEDLTQTAP-RIALALRqAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD---IAAESIRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 248 RTKDFDQLKADLLR-IDLEGIAELTGVRIEQIRTAAVTYAKAGTgmVFTARGVEQHADGhmAVRNFLNMVLATGKIGrEG 326
Cdd:cd02771 224 SPGGQARLGAALARaVDASAAGVSGLAPKEKAARIAARLTGAKK--PLIVSGTLSGSLE--LIKAAANLAKALKRRG-EN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 327 CGYGAVTGQGNgqggrehgqkadqLPGYRSIENENDRAfvakvwgippeelpgkGVSAYEMMELVHQEQIKALFVMGSNP 406
Cdd:cd02771 299 AGLTLAVEEGN-------------SPGLLLLGGHVTEP----------------GLDLDGALAALEDGSADALIVLGNDL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 407 VVSNPHASlVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRV-LLREAARSAPGETRHDWQILCS 485
Cdd:cd02771 350 YRSAPERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAqRFFKAYDDPAGDARSDWRWLHA 428
|
490 500 510
....*....|....*....|....*....|.
gi 2306680097 486 VAEKLGRG-AYFPYKDAEEIFNELRKASQGG 515
Cdd:cd02771 429 LAAKLGGKlVPSDAAILDEIIALVPGKAPVG 459
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
37-508 |
1.20e-44 |
|
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: 166.34 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 37 GVPNAasEGRLCVKGMNAHQHASSRDRLLFPLVRK----NGELVRSSWEEALDTVAARFSVIQEAYGRDAVGVYGGGSLT 112
Cdd:cd02750 42 DLPDY--NPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 113 NETAYALGkfarvalrSRYIDYNGRFCMSAAA------SAGVKTFGiDRGLTNQLSEIPLAECIILAGTNIAECQPTLMP 186
Cdd:cd02750 120 SMVSYAAG--------SRFASLIGGVSLSFYDwygdlpPGSPQTWG-EQTDVPESADWYNADYIIMWGSNVPVTRTPDAH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 187 YFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVILDENLIDSAFIQSRTkDFdqlkaDLLRIDLEG 266
Cdd:cd02750 191 FLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT-DL-----PFLVYTPAW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 267 IAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNMVLATGKIGRegcgygavtgqgngqggrehgq 346
Cdd:cd02750 265 QEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGK---------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 347 kadqlpgyrsienendrafvakvwgippeelPGKGVSAYEmmelvhqEQIKALFVMGSNPVVSNPHASLVEEGI--RKLD 424
Cdd:cd02750 323 -------------------------------NGGGWAHYV-------GQPRVLFVWRGNLFGSSGKGHEYFEDApeGKLD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 425 FLVVADMFLSETAKYADVVLP-VTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQILCSVAEKL------GRGAYfp 497
Cdd:cd02750 365 LIVDLDFRMDSTALYSDIVLPaATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKVpwrtltGRQQF-- 442
|
490
....*....|.
gi 2306680097 498 YKDaEEIFNEL 508
Cdd:cd02750 443 YLD-HDWFLEL 452
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
576-692 |
3.58e-42 |
|
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: 148.54 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 576 SEYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVF 655
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2306680097 656 IPMHWGDAqNVNLATNPELDPYCKMPDFKVSAVRVRP 692
Cdd:cd02790 81 MPFHFAEA-AANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
12-649 |
1.43e-38 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 153.26 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 12 CSVQCKMTVEITPGEARQRSGfQATGVPN--AASEGRLCVKGMNAHQHASSRDRLLFPL----VRKNGELVRSSWEEALD 85
Cdd:PRK14990 67 CGSRCPLRMHVVDGEIKYVET-DNTGDDNydGLHQVRACLRGRSMRRRVYNPDRLKYPMkrvgARGEGKFERISWEEAYD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 86 TVAARFSVIQEAYGRDAVGV-YGGGSL--TNETAYALGKFARVALRS---RYIDYNGRFCmSAAASAGVK-TFGidrGLT 158
Cdd:PRK14990 146 IIATNMQRLIKEYGNESIYLnYGTGTLggTMTRSWPPGNTLVARLMNccgGYLNHYGDYS-SAQIAEGLNyTYG---GWA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 159 --NQLSEIPLAECIILAGTNIAECQPTL--MPYFI---RAKENgAFIIVIDPRATAT-AELADLHLQVKPGTDSALVSGM 230
Cdd:PRK14990 222 dgNSPSDIENSKLVVLFGNNPGETRMSGggVTYYLeqaRQKSN-ARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 231 LKVILDENLIDSAFIQSRTKDFDQ------------LKADLLRIDLEGIA-------ELTGVRIEQIRTAAVTYAKAGTG 291
Cdd:PRK14990 301 AYVMITENLVDQPFLDKYCVGYDEktlpasapknghYKAYILGEGPDGVAktpewasQITGVPADKIIKLAREIGSTKPA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 292 MVFTARGVEQHADGHMAVRNFLNMVLATGKIGREGcgygavtgqGNgQGGREHGQKadqLPGYR--SIENENDRAFVAKV 369
Cdd:PRK14990 381 FISQGWGPQRHANGEIATRAISMLAILTGNVGING---------GN-SGAREGSYS---LPFVRmpTLENPIQTSISMFM 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 370 WGIPPEELPG-----KGVSAYEMMELvhqeQIKALFVMGSNPVVsNPHASL-----VEEGIRKLDFLVVADMFLSETAKY 439
Cdd:PRK14990 448 WTDAIERGPEmtalrDGVRGKDKLDV----PIKMIWNYAGNCLI-NQHSEInrtheILQDDKKCELIVVIDCHMTSSAKY 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 440 ADVVLPVTSYMEN-----EGTLTNLEgRVLLREAARSAPGETRHDWQILCSVAEKLGRGAYFPY-KDAEEIFNELRKASQ 513
Cdd:PRK14990 523 ADILLPDCTASEQmdfalDASCGNMS-YVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEgRTQEEWMRHLYAQSR 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 514 GGIADYfgITYERLRREeGIYWPCPSTDH--------------PGT---GRLFEYSFAHADGLARFQ--------TVPVA 568
Cdd:PRK14990 602 EAIPEL--PTFEEFRKQ-GIFKKRDPQGHhvaykafredpqanPLTtpsGKIEIYSQALADIAATWElpegdvidPLPIY 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 569 LQGEET-----NSEYPLMMTNGrvlpHYLTGVQTRRSPVLAAKFV-ESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVR 642
Cdd:PRK14990 679 TPGFESyqdplNKQYPLQLTGF----HYKSRVHSTYGNVDVLKAAcRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIE 754
|
....*..
gi 2306680097 643 SRYSDKI 649
Cdd:PRK14990 755 AKVTPRM 761
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
9-490 |
2.26e-38 |
|
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: 146.66 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEITPGEARQRsgfqatgVP---NAASEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALD 85
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEVMRI-------LPrenEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 86 TVAARFSviqeAYGRDAVGVYGGGSLTNETAYALGKFARvALRSRYIDYNGRFcMSAAASAGVKTFGIdrgLTNQLSEIP 165
Cdd:cd02768 77 TVAEGLK----AVKGDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQ-SDLPADNRLRGNYL---FNTSIAEIE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 166 LAECIILAGTNIAECQPtLMPYFIR--AKENGAFIIVIDPraTATAELADLHLQVKPGTDSalvsgmLKVILDenlidsa 243
Cdd:cd02768 148 EADAVLLIGSNLRKEAP-LLNARLRkaVKKKGAKIAVIGP--KDTDLIADLTYPVSPLGAS------LATLLD------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 244 fiqsrtkdfdqlkadllriDLEGIAeltgvrieqIRTAAVTYAKAGTGMVFTARGVEQHaDGHMAVRNFLNMVLATGKIG 323
Cdd:cd02768 212 -------------------IAEGKH---------LKPFAKSLKKAKKPLIILGSSALRK-DGAAILKALANLAAKLGTGA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 324 REGCGYGAVtgqgngqggrehgqkadQLPGYRSIENENDRAFVAKvwgippeelpgkgvsayemmelvHQEQIKALFVMG 403
Cdd:cd02768 263 GLWNGLNVL-----------------NSVGARLGGAGLDAGLALL-----------------------EPGKAKLLLLGE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 404 SNPVVSNPHASLVeegIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQIL 483
Cdd:cd02768 303 DELDRSNPPAAVA---LAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKIL 379
|
....*..
gi 2306680097 484 CSVAEKL 490
Cdd:cd02768 380 RALSNLL 386
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
577-692 |
6.74e-38 |
|
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: 136.93 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 577 EYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFI 656
Cdd:cd02791 2 EYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2306680097 657 PMHWGD----AQNVNLATNPELDPYCKMPDFKVSAVRVRP 692
Cdd:cd02791 82 PMHWGDqfgrSGRVNALTLDATDPVSGQPEFKHCAVRIEK 121
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
577-692 |
7.27e-36 |
|
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: 131.19 E-value: 7.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 577 EYPLMMTNGRVLPHYLTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFI 656
Cdd:cd02792 2 EFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2306680097 657 PMHWGDA-----QNVNLATNPELDPYCKMPDFKVSAVRVRP 692
Cdd:cd02792 82 PYHWGGMglvigDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
7-503 |
2.15e-35 |
|
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: 141.04 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARQrsgfqATGVPNA-ASEGRLCVKGMNAHQHASSRDRLLFPLVRKN--------GELVR 77
Cdd:cd02757 4 STCQGCTAWCGLQAYVEDGRVTK-----VEGNPLHpGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdvdPKFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 78 SSWEEALDTVAARFSVIQEA---------YGR-------------DAVGVYGGGSLTNETAYAlGKFARVALrSRYIDYN 135
Cdd:cd02757 79 ISWDEALDTIADKIRALRKEnephkimlhRGRyghnnsilygrftKMIGSPNNISHSSVCAES-EKFGRYYT-EGGWDYN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 136 grfcmsaaasagvktfgiDRGLTNqlseiplAECIILAGTNIAECQPTLmPYFIR---AKENGAFIIVIDPRATATAELA 212
Cdd:cd02757 157 ------------------SYDYAN-------AKYILFFGADPLESNRQN-PHAQRiwgGKMDQAKVVVVDPRLSNTAAKA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 213 DLHLQVKPGTDSALVSGMLKVILDENLIDSAFI----------------------QSRTKDFDQ-LKADLLRIDLEGIAE 269
Cdd:cd02757 211 DEWLPIKPGEDGALALAIAHVILTEGLWDKDFVgdfvdgknyfkagetvdeesfkEKSTEGLVKwWNLELKDYTPEWAAK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 270 LTGVRIEQIRTAAVTYAKAGT-GMVFTARGVEQHADGHMAVR--NFLNMVlaTGKIGREGcgyGAVTGQGNGqggrehgq 346
Cdd:cd02757 291 ISGIPAETIERVAREFATAAPaAAAFTWRGATMQNRGSYNSMacHALNGL--VGSIDSKG---GLCPNMGVP-------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 347 kadqlpgyrsienendrafvakvwgippeelpgkgvsayemmelvhqeQIKALFVMGSNPVVSNPHASLVEEGIRKLDFL 426
Cdd:cd02757 358 ------------------------------------------------KIKVYFTYLDNPVFSNPDGMSWEEALAKIPFH 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 427 VVADMFLSETAKYADVVLPVTSYMENEGTL---TNLEGRVLLREAARSAPGETRHDWQILCSVAEKL------GRGAYFP 497
Cdd:cd02757 390 VHLSPFMSETTYFADIVLPDGHHFERWDVMsqeNNLHPWLSIRQPVVKSLGEVREETEILIELAKKLdpkgsdGMKRYAP 469
|
....*...
gi 2306680097 498 --YKDAEE 503
Cdd:cd02757 470 gqFKDPET 477
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
62-562 |
5.16e-35 |
|
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: 141.47 E-value: 5.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 62 DRLLFPLVRKNGELVRSSWEEALDTVA-ARFSVIQEAYGRDAVGV----YGGGSLTNETAYALGKFARVALRSRYIDYNG 136
Cdd:cd02756 116 TRLTTPLVRRGGQLQPTTWDDAIDLVArVIKGILDKDGNDDAVFAsrfdHGGGGGGFENNWGVGKFFFMALQTPFVRIHN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 137 RFCMS----AAASAGVKTfgidrgLTNQLSEIPLAECIILAGTNIAECQPTlmpYFI----------------RAKENG- 195
Cdd:cd02756 196 RPAYNsevhATREMGVGE------LNNSYEDARLADTIVLWGNNPYETQTV---YFLnhwlpnlrgatvsekqQWFPPGe 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 196 ----AFIIVIDPRATATAELAD--------LHLQVKPGTDSALVSGMLKVIldenlidsafiqsrtkdfdqlkADLLRID 263
Cdd:cd02756 267 pvppGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYI----------------------YESLDEV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 264 LEGIAELTGVRIEQIRTAAVTYAKAGTG------MVFTARGVEQHADGHMAVRNFLNMVLATGKIGREGCGYGAvtgqgn 337
Cdd:cd02756 325 LAEAEQITGVPRAQIEKAADWIAKPKEGgyrkrvMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVR------ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 338 gQGGREHGQKADQLPGYRSIENENDRAFVAK-----------VWGIPPEELpgkGVSAYEMMELVHQEQ---IKALFVMG 403
Cdd:cd02756 399 -QGGHQEGYVRPPPPPPPWYPQYQYAPYIDQllisgkgkvlwVIGCDPYKT---TPNAQRLRETINHRSklvTDAVEAAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 404 SNPVVSNPHASLVEEGIRKLD--FLVVADMFLSETAKYADVVLPVTSYME-NEGTLTNLEGRVLLREAARSAPGETRHDW 480
Cdd:cd02756 475 YAGTYDREAMVCLIGDAIQPGglFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRLRLYEKFMDPPGEAMPDW 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 481 QILCSVAEKL-------GRGAY-------FPYKDAEEIFNE-LRKASQGGIADYF----------GITYERLRREEGIYW 535
Cdd:cd02756 555 WIAAMIANRIyelyqeeGKGGSaqyqffgFIWKTEEDNFMDgSQEFADGGEFSEDyyvlgqeryeGVTYNRLKAVGVNGI 634
|
570 580 590
....*....|....*....|....*....|...
gi 2306680097 536 PCPSTDHPGTGRL------FEYSFAHADGLARF 562
Cdd:cd02756 635 QLPVTTDTVTKILvtnvlrTEGVFDTEDGKAYV 667
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
60-511 |
1.60e-33 |
|
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: 136.62 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 60 SRDRLLFPLVRK---------------NGELVRSSWEEALDTVAARFSVIQEAYGRDAV--GVYGGGSLtnetayalGKF 122
Cdd:cd02769 43 SPTRIKYPMVRRgwlekgpgsdrslrgKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIfgGSYGWSSA--------GRF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 123 --ARVALRsRYIDYNGRFC-----MSAAASAGV--KTFGIDRGLTNQLSEIPL----AECIILAGTNIAECQPT------ 183
Cdd:cd02769 115 hhAQSLLH-RFLNLAGGYVgsvgdYSTGAAQVIlpHVVGSMEVYTEQQTSWPViaehTELVVAFGADPLKNAQIawggip 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 184 ---LMPYFIRAKENGAFIIVIDPRATATAELADL-HLQVKPGTDSALVSGMLKVILDENLIDSAFIQSRTKDFDQLKADL 259
Cdd:cd02769 194 dhqAYSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 260 L------RIDLEGIAELTGVRIEQIRTAAVTYAKAGTgMVFTARGVEQHADGHMAVrnFLNMVLAT--GKIGREGCGYGA 331
Cdd:cd02769 274 LgesdgvPKTPEWAAAICGIPAETIRELARRFASKRT-MIMAGWSLQRAHHGEQPH--WMAVTLAAmlGQIGLPGGGFGF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 332 VTGQGNGQGGREHGQKADQLP-GYRSIenendRAF--VAKVwgipPEEL--PGKgVSAYEMMELVHQEqIKALFVMGSNP 406
Cdd:cd02769 351 GYHYSNGGGPPRGAAPPPALPqGRNPV-----SSFipVARI----ADMLlnPGK-PFDYNGKKLTYPD-IKLVYWAGGNP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 407 VVSnpHASLVE--EGIRKLDFLVVADMFLSETAKYADVVLPVTSYME-NEGTLTNLEGRVL-LREAArsAP-GETRHDWQ 481
Cdd:cd02769 420 FHH--HQDLNRliRAWQKPETVIVHEPFWTATARHADIVLPATTSLErNDIGGSGDNRYIVaMKQVV--EPvGEARDDYD 495
|
490 500 510
....*....|....*....|....*....|....*
gi 2306680097 482 ILCSVAEKLGRGAYFPY-KDAEE----IFNELRKA 511
Cdd:cd02769 496 IFADLAERLGVEEQFTEgRDEMEwlrhLYEESRAQ 530
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
48-659 |
1.38e-32 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 134.69 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 48 CVKGMNAHQHASSRDRLLFPLVR-KNGELVRSSWEEALDTVAARFsviqeAYGRDAVGVYGGGSLTNETAYALGKFARVA 126
Cdd:PRK07860 263 CDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGL-----AAARGRVGVLVGGRLTVEDAYAYAKFARVA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 127 LRSRYIDYNGR--------FCmsAAASAGvktfgidRGLTNQLSEIPLAECIILAGTNIAECQPTLmpyFIR----AKEN 194
Cdd:PRK07860 338 LGTNDIDFRARphsaeeadFL--AARVAG-------RGLGVTYADLEKAPAVLLVGFEPEEESPIV---FLRlrkaARKH 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 195 GAFIIVIDPRAT-ATAELADLHLQVKPGTDSALVSGMLKVILDEnlidsafiqsrtkdfdqlkADLLRidLEGIAELTGV 273
Cdd:PRK07860 406 GLKVYSIAPFATrGLEKMGGTLLRTAPGGEAAALDALATGAPDV-------------------AELLR--TPGAVILVGE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 274 RIEQIR---TAAVTYAKAgTGmvftARgveqhadghmavrnflnmvLATgkIGREGCGYGAVtgqgngqggrEHGQKADQ 350
Cdd:PRK07860 465 RLATVPgalSAAARLADA-TG----AR-------------------LAW--VPRRAGERGAL----------EAGALPTL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 351 LPGYRSIENENDRAFVAKVWGIPpeELPGK-GVSAYEMMELVHQEQIKALFVMGSNPV-VSNPHASLveEGIRKLDFLVV 428
Cdd:PRK07860 509 LPGGRPVADPAARAEVAAAWGVD--ELPAApGRDTAGILAAAAAGELGALLVGGVEPAdLPDPAAAL--AALDAAGFVVS 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 429 ADMFLSETAKYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRhDWQILCSVAEKLGRGAYFPykDAEEIFNEL 508
Cdd:PRK07860 585 LELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTGALS-DLRVLDALADEMGVDLGLP--TVAAARAEL 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 509 rkasqggiadyfgityERLRREEGIYWPCPSTDHPgtgrlfeysfahadglarfqTVPVALQGEETNSEYPLMMTNGRVL 588
Cdd:PRK07860 662 ----------------ARLGAWDGARAAAPAVPAA--------------------APPQPGAGEAVLATWRMLLDDGRLQ 705
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306680097 589 ---PHyLTGvqTRRSPVLaakfvesfmEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDkIREDTVFIPMH 659
Cdd:PRK07860 706 dgePH-LAG--TARPPVA---------RLSAATAAEIGVADGDAVTVSTERGSITLPLAITD-MPDRVVWLPLN 766
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
79-451 |
2.34e-29 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 124.39 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 79 SWEEALDTVAARfsvIQEAYGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGrFCMSAAASAGVKTFGIDRGlT 158
Cdd:PRK09939 126 SWQQAFDEIGAR---LQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSN-MCHEPTSVGLAASIGVGKG-T 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 159 NQLSEIPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDP-------RATA-----------TAELADLHLQVKP 220
Cdd:PRK09939 201 VLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqnpfemltnsETQLASAYYNVRI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 221 GTDSALVSGMLKVILDEN----------LIDSAFIQSRTKDFDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGT 290
Cdd:PRK09939 281 GGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAER 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 291 GMVFTARGVEQHADGHMAVRNFLNMVLATGKIGREGCGYGAVTGQGNGQGGREHGqkadqlpgyrsIENENDRAFVAKV- 369
Cdd:PRK09939 361 TIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG-----------ITEKPSAEFLARLg 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 370 --WGIPPEELPGKgvSAYEMMELVHQEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSE----TAKYAdVV 443
Cdd:PRK09939 430 erYGFTPPHAPGH--AAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRshllTARHS-YI 506
|
....*...
gi 2306680097 444 LPVTSYME 451
Cdd:PRK09939 507 LPVLGRSE 514
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
580-687 |
5.53e-29 |
|
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: 111.21 E-value: 5.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 580 LMMTNGRVLPHYLTGVQTRRSPVLAaKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMH 659
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLA-KPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 2306680097 660 WGD---AQNVNLATNPELDPYCKMPDFKVSA 687
Cdd:pfam01568 80 WWYeprGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
383-511 |
8.62e-29 |
|
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: 120.33 E-value: 8.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 383 SAYEMMELVHQEQIKALFVMGSNPVVSNPhaSLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLEGR 462
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDP--AAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2306680097 463 VLLREAARSAPGETRHDWQILCSVAEKLGRGayFPYKDAEEIFNELRKA 511
Cdd:COG1034 398 VQRFNAAVPPPGEARPDWRVLRALANALGAG--LPYDSLEEVRAELAAE 444
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
54-483 |
4.16e-25 |
|
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: 108.60 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 54 AHQHASSRDRLLFPLVRKNGELVRSSWEEALDTVAARFSVIQEAYGRDAVGVYGGGSLTNETAYALGKFARvALRSRYID 133
Cdd:cd02772 45 SYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLAR-GLGSDNID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 134 YNGR---FCMSAAASAGvktfgidRGLTNQLSEIPLAECIILAGTNIAECQPTLMPYFIRAKENGAFIIVIDPraTATAE 210
Cdd:cd02772 124 HRLRqsdFRDDAKASGA-------PWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINP--ADDDF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 211 LADLHLQ--VKPgtdSALVSGMLKVIldenlidsafiqsrtKDFDQLKADLLRIDLEGIAELtgvriEQIRTAAVTYAKA 288
Cdd:cd02772 195 LFPLSGKaiVAP---SALANALAQVA---------------KALAEEKGLAVPDEDAKVEAS-----EEARKIAASLVSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 289 GTGMVFTARGVEQHADG---HMAVRNFLNMVLATGkigregcgyGAVTGQGNGQGGREHGQkadqlpgyrsienendraf 365
Cdd:cd02772 252 ERAAVFLGNLAQNHPQAatlRALAQEIAKLTGATL---------GVLGEGANSVGAYLAGA------------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 366 vakvwgippeeLPGKGVSAYEMMElvhqEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAK-YADVVL 444
Cdd:cd02772 304 -----------LPHGGLNAAAMLE----QPRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVLL 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 2306680097 445 PVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQIL 483
Cdd:cd02772 369 PIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
590-684 |
4.63e-24 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 97.01 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 590 HYLTGVQTRrSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMHWGDA----QN 665
Cdd:cd02775 4 HFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRggrgGN 82
|
90
....*....|....*....
gi 2306680097 666 VNLATNPELDPYCKMPDFK 684
Cdd:cd02775 83 ANVLTPDALDPPSGGPAYK 101
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
9-455 |
3.32e-21 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 96.84 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQC-KMTVEITPGearqrsgfQATGVPNAasegrlCVKGMNAHQHASSRDRLLFPLVRkngeLVRSSWEEALDTV 87
Cdd:COG1029 10 CPFCGCLCdDLEVEVEGG--------KIVVVKNA------CAIGAAKFERAVSDHRITSPRIR----GKEVSLEEAIDKA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 88 AarfSVIQEAygrDAVGVYGGGSLTNETAYALgkfARVALRSR-YIDYNgrfcmsAAASAGVKTFGI-DRGLTNQ-LSEI 164
Cdd:COG1029 72 A---EILANA---KRPLIYGLSSTDCEAMRAG---LALAERVGaVVDNT------ASVCHGPSLLALqDVGWPTCtLGEV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 165 P-LAECIILAGTNIAECQPTLM--------PYFIRAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSGMLKVIL 235
Cdd:COG1029 137 KnRADVIIYWGCNPVHAHPRHMsrysvfprGFFTPKGRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEVLSALRALVR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 236 DENLIdsafiqsrtkdfdqlkadllridlegIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLNM 315
Cdd:COG1029 217 GKELS--------------------------PEEVAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIEL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 316 VLATGKIGRegCGYGAVTGQGNGQGgrehgqkADQLPGYRSienendrafvakvwGIP---------PEELPGKgvsaYE 386
Cdd:COG1029 271 VRDLNRYTK--FSILPLRGHYNVAG-------ANQVASWQT--------------GYPfrvdfsrgyPRYNPGE----TS 323
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 387 MMELVHQEQIKALFVMGSNPVVSNPHASLveEGIRKLDfLVVADMFLSETAKYADVVLPVTSY-MENEGT 455
Cdd:COG1029 324 AVDLLARGEVDALLWVASDPGAHFPPDAV--EHLAKIP-TIVIDPHGTPTTEVADVVIPVAIPgIEHGGT 390
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
45-491 |
1.64e-20 |
|
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: 96.64 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 45 GRLCVKGMNAHQHASSRDRLLFPLVR--KNGE--LVRSSWEEALDTVAARfSVIQEAYGRDAV-GVY-----------GG 108
Cdd:cd02758 65 ATACARGNAGLQYLYDPYRVLQPLKRvgPRGSgkWKPISWEQLIEEVVEG-GDLFGEGHVEGLkAIRdldtpidpdhpDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 109 GSLTNETAYALG----------KFARVALRSRYIDYNGRFC---MSAAASAGVKTFGidrGLTNQLSEIPLAECIILAGT 175
Cdd:cd02758 144 GPKANQLLYTFGrdegrtpfikRFANQAFGTVNFGGHGSYCglsYRAGNGALMNDLD---GYPHVKPDFDNAEFALFIGT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 176 NIAECQP---TLMPYFIRAKENGAF-IIVIDPRATATAELADLH---LQVKPGTDSALVSGMLKVILDENLIDSAF---- 244
Cdd:cd02758 221 SPAQAGNpfkRQARRLAEARTEGNFkYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENERYNAEYlsip 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 245 --------------------IQSRTKD-FDQLKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHA 303
Cdd:cd02758 301 skeaakaagepswtnathlvITVRVKSaLQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 304 DGH---MAVRNfLNMVLatGKIGREGcgyGAVTGQG----NGQGGREHGQKADQLPGYRSI----------ENENDRAFV 366
Cdd:cd02758 381 NGFynaYAIRM-LNALI--GNLNWKG---GLLMSGGgfadNSAGPRYDFKKFFGEVKPWGVpidrskkayeKTSEYKRKV 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 367 AKVWGIPPEELPGKGVSAYEMMELV--HQE----QIKALFVMGSNPVVSNPHA-SLVEEGIR---KLDFLVVADMFLSET 436
Cdd:cd02758 455 AAGENPYPAKRPWYPLTPELYTEVIasAAEgypyKLKALILWMANPVYGAPGLvKQVEEKLKdpkKLPLFIAIDAFINET 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2306680097 437 AKYADVVLPVTSYMENEGTLTNLEGRVLLREAARS----------APGETRHDWQILCSVAEKLG 491
Cdd:cd02758 535 SAYADYIVPDTTYYESWGFSTPWGGVPTKASTARWpviapltektANGHPVSMESFLIDLAKALG 599
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
9-490 |
4.56e-20 |
|
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: 93.17 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCK-MTVEitpgearqRSGFQATGVPNAASEGrlcvkgmNAHqHASSRDRLLFPLVRKngelVRSSWEEALDTv 87
Cdd:cd02761 4 CPFCGLLCDdIEVE--------VEDNKITKVRNACRIG-------AAK-FARYERRITTPRIDG----KPVSLEEAIEK- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 88 AARfsVIQEAygRDAVgVYGGGSLTNE---TAYALGKFARValrsrYIDYNGRFCMSAAASAGvktfgIDRGL-TNQLSE 163
Cdd:cd02761 63 AAE--ILKEA--KRPL-FYGLGTTVCEaqrAGIELAEKLGA-----IIDHAASVCHGPNLLAL-----QDSGWpTTTLGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 164 IP-LAECIILAGTNIAECQPTLMP---YFIRAKENGAF-----IIVIDPRATATAELADLHLQVKPGTDSALVSGMLkvi 234
Cdd:cd02761 128 VKnRADVIVYWGTNPMHAHPRHMSrysVFPRGFFREGGredrtLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALR--- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 235 ldenlidsafiqsrtkdfdqlkaDLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVFTARGVEQHADGHMAVRNFLN 314
Cdd:cd02761 205 -----------------------ALLRGAGLVPDEVAGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAAIR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 315 MVLATGKIGREGCgyGAVTGQGNGQGgreHGQKADQLPGYrsienendrAFVAKVWGIPPEELPGkgvsAYEMMELVHQE 394
Cdd:cd02761 262 LVKALNEYTKFAL--LPLRGHYNVRG---FNQVLTWLTGY---------PFRVDFSRGYPRYNPG----EFTAVDLLAEG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 395 QIKALFVMGSNPVVSNPhASLVEEGIRKLdfLVVADMFLSETAKYADVVLPV-TSYMENEGTLTNLEGRVLLREAARsaP 473
Cdd:cd02761 324 EADALLIIASDPPAHFP-QSAVKHLAEIP--VIVIDPPPTPTTRVADVVIPVaIPGIEAGGTAYRMDGVVVLPLKAV--E 398
|
490
....*....|....*..
gi 2306680097 474 GETRHDWQILCSVAEKL 490
Cdd:cd02761 399 TERLPDEEILKQLLEKV 415
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-460 |
8.84e-17 |
|
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: 84.50 E-value: 8.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARQRSGFQATGVpnaaSEGRLCVKGMNAHQHASSRDRLLFPLVRK----NGELVRSSWEE 82
Cdd:cd02763 2 TTCYMCACRCGIRVHLRDGKVRYIKGNPDHPL----NKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEIEWEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 83 ALDTVAARFSVIQEA--------YGRDAVGvygggSLTNETAYALGKFARVAlrsryidyNGRFCMSAAASAGVKTFGid 154
Cdd:cd02763 78 AFSIATKRLKAARATdpkkfaffTGRDQMQ-----ALTGWFAGQFGTPNYAA--------HGGFCSVNMAAGGLYSIG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 155 rGLTNQLSEIPL--AECIILAGTniAECQPTlMPYFI---RAKENGAFIIVIDPRATATAELADLHLQVKPGTDSALVSG 229
Cdd:cd02763 143 -GSFWEFGGPDLehTKYFMMIGV--AEDHHS-NPFKIgiqKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 230 MLKVILDENLIDSAFIQSRTKdfdqlKADLLRIDLEGIAELTGVRIEQIRTAAVTYAKA--------------------- 288
Cdd:cd02763 219 LAHELLKAGLIDWEFLKRYTN-----AAELVDYTPEWVEKITGIPADTIRRIAKELGVTardqpielpiawtdvwgrkhe 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 289 ---GTGMVFTA-RGVEQHADGHMAVRNFLNMVLATGKIGREG--------------CGYGAVTGQGNGQGGREHG----- 345
Cdd:cd02763 294 kitGRPVSFHAmRGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppyprhippLPKPPKIPSADKPFTPLYGpplgw 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 346 -QKADQLpgyrSIENEN-----DRAFvakVWGIPpeelpgkgVSAYEMMELVHQEQ-------IKALFVMGSN------- 405
Cdd:cd02763 374 pASPDDL----LVDEDGnplriDKAY---SWEYP--------LAAHGCMQNVITNAwrgdpypIDTLMIYMANmawnssm 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2306680097 406 --PVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYMENEGTLTNLE 460
Cdd:cd02763 439 ntPEVREMLTDKDASGNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLD 495
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
9-222 |
3.16e-16 |
|
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: 81.81 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 9 CPFCSVQCKMTVEitpgeARQRSGFQATGVPNAA-SEGRLCVKGMNAHQHASSRDRLLFPLVRKNGELVRSSWEEALDTV 87
Cdd:COG1034 222 CPHCSVGCNIRVD-----VRGGKVYRVLPRENEAvNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEALAAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 88 AARFSVIQEAYGRdaVGVYGGGSLTNETAyalgkfarvalrsryidyngrfcMSAAASAGvktfgidrgltnqlseipLA 167
Cdd:COG1034 297 AEGLKALKKAENS--VGAALLGALPDAAA-----------------------ILEAAEAG------------------KL 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306680097 168 ECIILAGTNIAECQPTLmpyFIRAKENGAFIIVIDPRATATAELADLHLQVKPGT 222
Cdd:COG1034 334 KALVLLGADPYDLDPAA---ALAALAKADFVVVLDHFGSATAERADVVLPAAAFA 385
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
49-514 |
8.15e-14 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 75.09 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 49 VKGMNAHQHASSRDRllFPLVR----KNGEL-----------VRSSWEEALDTVAARFSVIQEAYGRDA-----VGVYGG 108
Cdd:PRK15102 78 INGIKGHVYNPSRIR--YPMVRldwlRKRHKsdtsqrgdnrfVRVSWDEALDLFYEELERVQKTYGPSAlhtgqTGWQST 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 109 GSLTNETAYalgkFAR-VALRSRYI----DYngrfcmSAAASAGVKTFGIdrGLTN---QLSEIPL----AECIILAGTN 176
Cdd:PRK15102 156 GQFHSATGH----MQRaIGMHGNSVgtvgDY------STGAGQVILPYVL--GSTEvyeQGTSWPLilenSKTIVLWGSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 177 -IAECQ-----PTLMP--YFIRAKE---NGAF-IIVIDPRATATAE-LADLHLQVKPGTDSALVSGMLKVILDENLIDSA 243
Cdd:PRK15102 224 pVKNLQvgwncETHESyaYLAQLKEkvaKGEInVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 244 FIQSRTKDFDQL------KADLLRIDLEGIAELTGVRIEQIRTAAVTYAKAGTGMVF---TARgvEQHADGH--MAVrnf 312
Cdd:PRK15102 304 FIDNYCLGFEQFlpyllgEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAgwcIQR--QQHGEQPywMGA--- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 313 lnmVLAT--GKIGREGCGY---------GAVTGQGNGQGGREHGQKADQLPGYRSieneNDRAFVAKVwgIPPEEL---- 377
Cdd:PRK15102 379 ---VLAAmlGQIGLPGGGIsyghhysgiGVPSSGGAIPGGFPGNLDTGQKPKHDN----SDYKGYSST--IPVARFidai 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 378 --PGKGVSAYEmmELVHQEQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTSYME-NE- 453
Cdd:PRK15102 450 lePGKTINWNG--KKVTLPPLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFErNDi 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 454 ---GTLTNlegRVLLREAARSAP-GETRHDWQILCSVAEKLGR-GAYFPYKDA----EEIFNELRKASQG 514
Cdd:PRK15102 528 dqyGSYSN---RGIIAMKKVVEPlFESRSDFDIFRELCRRFGReKEYTRGMDEmgwlKRLYQECKQQNKG 594
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
577-660 |
1.80e-12 |
|
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: 65.02 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 577 EYPLMMTNG-RVLPHylTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVF 655
Cdd:cd02781 1 EYPLILTTGaRSYYY--FHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
....*
gi 2306680097 656 IPMHW 660
Cdd:cd02781 79 AEHGW 83
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
7-249 |
2.22e-12 |
|
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: 70.38 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 7 TQCPFCSVQCK-MTVEITPGEARQRSG-FQATGVPNAasEGRLCVKGMNAHQHASSRDRLLFPLVRKNGE--------LV 76
Cdd:cd02760 2 TYCYNCVAGPDfMAVKVVDGVATEIEPnFAAEDIHPA--RGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 77 RSSWEEALDTVAARFSVIQEAYGRDAVGV------YGGGSLtneTAYALGKFarVALRSRYidynGRFCMSAAASAGVKT 150
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREKGLLDEKGLprlaatFGHGGT---PAMYMGTF--PAFLAAW----GPIDFSFGSGQGVKC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 151 FGID--------RGLTnQLSEIPLAECIILAGTNI-AECQPTLMPYFIRAKENGAFIIVIDPRATATAELADLHLQVKPG 221
Cdd:cd02760 151 VHSEhlygefwhRAFT-VAADTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPK 229
|
250 260 270
....*....|....*....|....*....|.
gi 2306680097 222 TDSALVSGMLKVILDE---NLIDSAFIQSRT 249
Cdd:cd02760 230 TDPAFMFAMIHVMVHEqglGKLDVPFLRDRT 260
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
579-661 |
9.76e-12 |
|
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: 62.68 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 579 PLMMTNGRVLPHylTGVQTRRSPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPM 658
Cdd:cd02778 1 EFRLIYGKSPVH--THGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
...
gi 2306680097 659 HWG 661
Cdd:cd02778 79 GFG 81
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
45-490 |
1.28e-11 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase 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 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 Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 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: 239174 [Multi-domain] Cd Length: 375 Bit Score: 66.90 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 45 GRLCVKGMNahqhassRDRLLFPLVRKNGELVRSSWEEALDTVAARfsvIQEAYGRDAVGVygGGSLTN-ETAYALGKFA 123
Cdd:cd02773 42 TRFAYDGLK-------RQRLDKPYIRKNGKLKPATWEEALAAIAKA---LKGVKPDEIAAI--AGDLADvESMVALKDLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 124 RvALRSRYIDYNGRFcmsAAASAGVKTFGIdrgLTNQLSEIPLAECIILAGTNIAECQPTLMPYFIRA-KENGAFIIVID 202
Cdd:cd02773 110 N-KLGSENLACEQDG---PDLPADLRSNYL---FNTTIAGIEEADAVLLVGTNPRFEAPVLNARIRKAwLHGGLKVGVIG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 203 PRATATAELADLhlqvkpGTDsalvsgmLKVILDenlidsafIQSRTKDFDQ-LKadllridlegiaeltgvrieqirta 281
Cdd:cd02773 183 PPVDLTYDYDHL------GTD-------AKTLQD--------IASGKHPFSKaLK------------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 282 avtyaKAGTGMVFTARGVEQHADGhmavrnflNMVLATgkIGREGCGYGAVTGQGNG----QggrehgQKADQLPGYrsi 357
Cdd:cd02773 217 -----DAKKPMIIVGSGALARKDG--------AAILAA--VAKLAKKNGVVREGWNGfnvlH------RAASRVGAL--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 358 enenDRAFVAKVWGIppeelpgkgvsayemmelVHQEQIKALFVMGSNPVVSNPhaslveegIRKLDFLVVADMFLSETA 437
Cdd:cd02773 273 ----DLGFVPGAGAI------------------RKSGPPKVLYLLGADEIDITP--------IPKDAFVVYQGHHGDRGA 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2306680097 438 KYADVVLPVTSYMENEGTLTNLEGRVLLREAARSAPGETRHDWQILCSVAEKL 490
Cdd:cd02773 323 QIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
62-454 |
1.36e-10 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 64.43 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 62 DRLLFPLVR-KNGELVRSSWEEALDTVAARFSVIQeayGRDAVGVYGGGSLTNETAYALGKFARVALRSRYIDYNGrfcM 140
Cdd:cd02764 98 DRAQGPLRRgIDGAYVASDWADFDAKVAEQLKAVK---DGGKLAVLSGNVNSPTTEALIGDFLKKYPGAKHVVYDP---L 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 141 SA--AASAGVKTFGIDrglTNQLSEIPLAECIILAGTNIAECQPTLMPY---FI-----RAKENGAFIIVIDPRATATAE 210
Cdd:cd02764 172 SAedVNEAWQASFGKD---VVPGYDFDKAEVIVSIDADFLGSWISAIRHrhdFAakrrlGAEEPMSRLVAAESVYTLTGA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 211 LADLHLQVKPGTDSALVSGMLKVILDENLIDSAFIQSRTKDFDQLKADllridlegIAELTGVRIEQIRTAAVTYAKAGT 290
Cdd:cd02764 249 NADVRLAIRPSQEKAFALGLAHKLIKKGAGSSLPDFFRALNLAFKPAK--------VAELTVDLDKALAALAKALAAAGK 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 291 GMVFT--ARGVEQHADGHMAVrNFLNMVLatgkiGREGCGYGAVTGQGNGQGGREHGQKAdqlpgyrsienendrAFVAK 368
Cdd:cd02764 321 SLVVAgsELSQTAGADTQVAV-NALNSLL-----GNDGKTVDHARPIKGGELGNQQDLKA---------------LASRI 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 369 VWGippeelpgkgvsayemmelvhqeQIKALFVMGSNPVVSNPHASLVEEGIRKLDFLVVADMFLSETAKYADVVLPVTS 448
Cdd:cd02764 380 NAG-----------------------KVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSH 436
|
....*.
gi 2306680097 449 YMENEG 454
Cdd:cd02764 437 GLESWG 442
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
7-60 |
2.11e-08 |
|
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: 50.75 E-value: 2.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARqrsgfQATGVPNA-ASEGRLCVKGMNAHQHASS 60
Cdd:pfam04879 6 TICPYCGVGCGLEVHVKDGKIV-----KVEGDPDHpVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
7-60 |
1.47e-07 |
|
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: 48.40 E-value: 1.47e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2306680097 7 TQCPFCSVQCKMTVEITPGEARqrsgfQATGVPN-AASEGRLCVKGMNAHQHASS 60
Cdd:smart00926 6 TVCPLCGVGCGLLVEVKDGRVV-----RVRGDPDhPVNRGRLCPKGRAGLEQVYS 55
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
610-696 |
1.88e-06 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 47.54 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 610 SFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMH-WGdaqnvNLATNPELDPyCKMPDFKVSAV 688
Cdd:COG1153 31 AVCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGpWA-----NAVVPPETHS-TGMPDFKGVPV 104
|
....*...
gi 2306680097 689 RVRPLAEE 696
Cdd:COG1153 105 EVEPTDEE 112
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
612-693 |
6.95e-06 |
|
The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 45.85 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 612 MEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMHWGDAQ------------NVNLATNPE-LDPYC 678
Cdd:cd02782 35 LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpgvsgagsrpgvNVNDLTDDTqRDPLS 114
|
90
....*....|....*
gi 2306680097 679 KMPDFKVSAVRVRPL 693
Cdd:cd02782 115 GNAAHNGVPVRLARV 129
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
600-677 |
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: 42.27 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 600 SPVLAAKFVESFMEIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMHW-----GDAQNVNLATNPEL 674
Cdd:cd02786 21 LPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGWwrehsPDGRGVNALTSARL 100
|
....
gi 2306680097 675 -DPY 677
Cdd:cd02786 101 tDLG 104
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
190-245 |
2.29e-04 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 44.60 E-value: 2.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306680097 190 RAKENGAF-IIVIDPRATATAEL-ADLH---LQVKPGTDSALVSGMLKVILDENLIDSAFI 245
Cdd:PRK14991 312 NARTRGNFeYVVVAPALPLSSSLaAGDNnrwLPIRPGTDSALAMGMIRWIIDNQRYNADYL 372
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
614-657 |
2.53e-04 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2306680097 614 IHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIP 657
Cdd:cd02793 37 INPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
613-684 |
3.77e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), 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 superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 40.49 E-value: 3.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306680097 613 EIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIREDTVFIPMH-WgdaqnvnlaTNPELDPY---CKMPDFK 684
Cdd:cd02789 34 EINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGpW---------ANVVVDPYtdsTGSPIFK 100
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
578-657 |
7.20e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 40.26 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306680097 578 YPLMMTNgrvlPHYLTGV--QTRRSPVLAAKFVESFME---IHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKIRED 652
Cdd:cd02777 1 YPLQLIS----PHPKRRLhsQLDNVPWLREAYKVKGREpvwINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPG 76
|
....*
gi 2306680097 653 TVFIP 657
Cdd:cd02777 77 VVALP 81
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
578-649 |
5.43e-03 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 37.27 E-value: 5.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306680097 578 YPLMMTNgrvlPHYLtgvqtRRS-------PVLAAKFVESFMeIHPLTARKHRIEEGALVRVSSKRGTVTVRSRYSDKI 649
Cdd:cd02794 1 YPLQLIG----WHYK-----RRThstfdnvPWLREAFPQEVW-INPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERI 69
|
|
| |
