|
Name |
Accession |
Description |
Interval |
E-value |
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
10-811 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 1456.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 10 VSRRALLK-STALGSLALAAGGLTLPFTlrRAAAAVQQATGDTTRIVWGACSVNCGSRCALRLHVRDDEVVYVETDNTGD 88
Cdd:TIGR02166 1 ISRRHFLKtSAALGGLAAASGALSLPFS--VNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 89 DRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYINYSSGIVG 168
Cdd:TIGR02166 79 DEYGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 169 GNITRSSPSaSPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYG-SNDGNSTSDIENSKLVVMFGNNPAETRMSGGGITW 247
Cdd:TIGR02166 159 GTMSRSWPP-TAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYGiSADGSSLDDIENSKLVVMFGNNPAETRMSGGGQTY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 248 YLEQARERSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEKTLPAGAPAN 327
Cdd:TIGR02166 238 YFLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 328 GHYKAYILGEGDDGIAKTPQWASRITGIPTERIIKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGIN 407
Cdd:TIGR02166 318 GSYKDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 408 GGNSGARESTYTITIERLPVLENPVKTAISCFTWTDAIARGPEMTASRDGVRGKEKLDVPIKFLWNYAGNTIINQHSDIN 487
Cdd:TIGR02166 398 GGNNGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 488 KTHEILQDESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIPNDYAGNMGYLIFIQPATSAKFERKPIYWILSEVA 567
Cdd:TIGR02166 478 RTHKILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 568 KRLGddVHQRFTEGRTQEQWLQYLYAKMVAKDPALPAYEDLKRMGIYKRKDPNGHFVAYRDFRRDPEAHPLKTPSGKIEI 647
Cdd:TIGR02166 558 KRLG--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEI 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 648 YSSRLAEIAARWQLEKDEVISPLPVYASTFEGWDDPLRSQYPLQLFGFHYKARTHSSYGNVDVLQAACRQEVWINPLDAE 727
Cdd:TIGR02166 636 YSERLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQ 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 728 KRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHDANmtGDRIDHGACMNTLTTHRPSPLAKGNPQHTNLVD 807
Cdd:TIGR02166 716 KRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVE 793
|
....
gi 490294727 808 IEKV 811
Cdd:TIGR02166 794 VEKA 797
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
10-811 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1300.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 10 VSRRALLKSTALGSLALAAGGLTLPFTLRRAAAAVQQATGDTTRIVWGACSVNCGSRCALRLHVRDDEVVYVETDNTGDD 89
Cdd:PRK14990 14 VSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNTGDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 90 RY-GDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYINYSSGIVG 168
Cdd:PRK14990 94 NYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 169 GNITRS-SPSASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGS-NDGNSTSDIENSKLVVMFGNNPAETRMSGGGIT 246
Cdd:PRK14990 174 GTMTRSwPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGNNPGETRMSGGGVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 247 WYLEQARERSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEKTLPAGAPA 326
Cdd:PRK14990 254 YYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLPASAPK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 327 NGHYKAYILGEGDDGIAKTPQWASRITGIPTERIIKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGI 406
Cdd:PRK14990 334 NGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 407 NGGNSGARESTYTITIERLPVLENPVKTAISCFTWTDAIARGPEMTASRDGVRGKEKLDVPIKFLWNYAGNTIINQHSDI 486
Cdd:PRK14990 414 NGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSEI 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 487 NKTHEILQDESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIPNDYAGNMGYLIFIQPATSAKFERKPIYWILSEV 566
Cdd:PRK14990 494 NRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSEL 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 567 AKRLGddVHQRFTEGRTQEQWLQYLYAKMVAKDPALPAYEDLKRMGIYKRKDPNGHFVAYRDFRRDPEAHPLKTPSGKIE 646
Cdd:PRK14990 574 AKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIE 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 647 IYSSRLAEIAARWQLEKDEVISPLPVYASTFEGWDDPLRSQYPLQLFGFHYKARTHSSYGNVDVLQAACRQEVWINPLDA 726
Cdd:PRK14990 652 IYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLDA 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 727 EKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHDANmtGDRIDHGACMNTLTTHRPSPLAKGNPQHTNLV 806
Cdd:PRK14990 732 QKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPSPLAKGNPSHTNLV 809
|
....*
gi 490294727 807 DIEKV 811
Cdd:PRK14990 810 QVEKV 814
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
56-679 |
0e+00 |
|
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: 969.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 56 WGACSVNCGSRCALRLHVRDDEVVYVETDNTGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISW 135
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 136 QEALDTLADRLKSVVAQYGNEAVYINYSSGIVGGNItrssPSASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSND 215
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVP----AGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 216 -GNSTSDIENSKLVVMFGNNPAETRMSGGGITWYLEQAReRSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIA 294
Cdd:cd02770 157 sGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 295 WVLINEDLVDQPFLDKYCVGYDEKTLPAGAPANGHYKAYILGEGDDGIAKTPQWASRITGIPTERIIKLAREIGMSKPAY 374
Cdd:cd02770 236 YVMITENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 375 ICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGARESTYTITIERLPVLENPVKTAISCFTWTDAIARGPEMTAS 454
Cdd:cd02770 316 ILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 455 RDGVRGKEKLDVPIKFLWNYAGNTIINQHSDINKTHE-ILQDESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIP 533
Cdd:cd02770 396 DGGVKGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRaLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 534 NDYAGNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGddVHQRFTEGRTQEQWLQYLYAKMVAKDPALPAYEDLKRMGI 613
Cdd:cd02770 476 TSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGI 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490294727 614 YKRKDPnGHFVAYRDFRRDPEAHPLKTPSGKIEIYSSRLAEIAArwQLEKDEVISPLPVYASTFEG 679
Cdd:cd02770 554 YRVPRA-LPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAK--TLPEGDEIPAIPKYVPAWEG 616
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
66-679 |
0e+00 |
|
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: 717.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 66 RCALRLHVRDDEVVYVETDNTgddrygdHQVRACLRGRSIRRRINHPDRLNYPMKRVGK----------RGEGKFVRISW 135
Cdd:cd02751 6 WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelRGEGEFVRISW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 136 QEALDTLADRLKSVVAQYGNEAVYINYSSGIVGGNITRSSpsaSPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGS-- 213
Cdd:cd02751 79 DEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQ---SLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSde 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 214 --NDGNSTSDI-ENSKLVVMFGNNPAETRMSGGGITW-----YLEQARERsNARMIVIDPRYTDTAAGREDEWIPIRPGT 285
Cdd:cd02751 156 vyEQGTSWDDIaEHSDLVVLFGANPLKTRQGGGGGPDhgsyyYLKQAKDA-GVRFICIDPRYTDTAAVLAAEWIPIRPGT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 286 DAALVAGIAWVLINEDLVDQPFLDKYCVGYDEktlpagapanghYKAYILGEgDDGIAKTPQWASRITGIPTERIIKLAR 365
Cdd:cd02751 235 DVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLGE-SDGVPKTPEWAAEITGVPAETIRALAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 366 EIgMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGARESTYT--------ITIERLPVLENPVKTAIS 437
Cdd:cd02751 302 EI-ASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNgggpprggAGGPGLPQGKNPVKDSIP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 438 CFTWTDAIAR-GPEMTAsrdgvRGKEKLDVPIKFLWNYAGNTIINQHsDINKTHEILQDEskcETIVVIDNFMTSSAKYA 516
Cdd:cd02751 381 VARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFWTASARYA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 517 DLLLPDLMTVEQEDIIPNDYAgNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGddVHQRFTEGRTQEQWLQYLYAKMV 596
Cdd:cd02751 452 DIVLPATTSLERNDIGLTGNY-SNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLEHLYEETR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 597 AK----DPALPAYEDLKRMGIYKRKDPNGHFVAYRDFRRDPEAHPLKTPSGKIEIYSSRLAEIAarwqlekDEVISPLPV 672
Cdd:cd02751 529 AKaagpGPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFG-------YDDCPGHPT 601
|
....*..
gi 490294727 673 YASTFEG 679
Cdd:cd02751 602 WIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
48-811 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 699.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 48 TGDTTRIVWGACSvNCGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGE 127
Cdd:COG0243 17 EAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGPRGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 128 GKFVRISWQEALDTLADRLKSVVAQYGNEAVYINYSsgivGGNITRSSPSASPVA-RLMNCYgGSLNQY--GTYSTAQIA 204
Cdd:COG0243 92 GKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTS----GGSAGRLSNEAAYLAqRFARAL-GTNNLDdnSRLCHESAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 205 CAMPYTYGSNDG-NSTSDIENSKLVVMFGNNPAETrmsGGGITWYLEQARERSNARMIVIDPRYTDTAAgREDEWIPIRP 283
Cdd:COG0243 167 AGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEWLPIRP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 284 GTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEktlpagapanghYKAYIlgegddgIAKTPQWASRITGIPTERIIKL 363
Cdd:COG0243 243 GTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAEDIREL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 364 AREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNsgarestytitierlpvlenpvktaiSCFTWTD 443
Cdd:COG0243 304 AREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGG--------------------------PFSLTGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 444 AIARGpemtasrdgvrgkekLDVPIKFLWNYAGNtIINQHSDINKTHEILQdesKCETIVVIDNFMTSSAKYADLLLPDL 523
Cdd:COG0243 358 AILDG---------------KPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 524 MTVEQEDIIPNdyaGNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGddVHQRFTEGRTQEQWLQYLYAKMvakDPALP 603
Cdd:COG0243 419 TWLERDDIVTN---SEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLG--FEEAFPWGRTEEDYLRELLEAT---RGRGI 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 604 AYEDLKRMGIYKRKDPNGHFvayrdFRRDpeaHPLKTPSGKIEIYSSRLAeiaarwqlekdevISPLPVYASTFEgWDDP 683
Cdd:COG0243 491 TFEELREKGPVQLPVPPEPA-----FRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE-GAEP 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 684 LRSQYPLQLFGFHYKARTHSSYGNVDVLQAACRQE-VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSA 762
Cdd:COG0243 549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 490294727 763 MGQGAWHDANMtgdriDHGACMNTLTTHRPSPLAKGNPQHTNLVDIEKV 811
Cdd:COG0243 629 APHGWWYEPAD-----DKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
102-653 |
7.16e-131 |
|
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: 403.18 E-value: 7.16e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 102 GRSIRRRINHPDRLNYPMKRVG-----------KRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYinyssgivGGN 170
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIF--------GGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 171 ITRSSP-----SASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSNDG----NSTSD--IENSKLVVMFGNNPAETR 239
Cdd:cd02769 106 YGWSSAgrfhhAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVyteqQTSWPviAEHTELVVAFGADPLKNA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 240 MSGGGIT------WYLEQARERsNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKYCV 313
Cdd:cd02769 186 QIAWGGIpdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 314 GYDEktlpagapanghYKAYILGEgDDGIAKTPQWASRITGIPTERIIKLAREIgMSKPAYICQGWGPQRQANGELTARA 393
Cdd:cd02769 265 GFDK------------FLPYLLGE-SDGVPKTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 394 IAMLPILTGNVGINGG--------NSGARESTYTITIERLPVLENPVKTAISCFTWTDAIARgPEMTASRDGvrgkEKLD 465
Cdd:cd02769 331 AVTLAAMLGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLN-PGKPFDYNG----KKLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 466 VP-IKFLWNyAGNTIINQHSDINKTHEILQdesKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIipnDYAGNMGYLI 544
Cdd:cd02769 406 YPdIKLVYW-AGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 545 FIQPATSAKFERKPIYWILSEVAKRLGddVHQRFTEGRTQEQWLQYLY----AKMVAKDPALPAYEDLKRMGIYKRKDPN 620
Cdd:cd02769 479 AMKQVVEPVGEARDDYDIFADLAERLG--VEEQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPE 556
|
570 580 590
....*....|....*....|....*....|...
gi 490294727 621 GHFVAYRDFRRDPEAHPLKTPSGKIEIYSSRLA 653
Cdd:cd02769 557 ADFVRLADFREDPEANPLGTPSGRIEIFSETIA 589
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
58-671 |
7.46e-110 |
|
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: 345.00 E-value: 7.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 58 ACSVNCGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGeGKFVRISWQE 137
Cdd:cd02766 3 VCPLDCPDTCSLLVTVEDGRIVRVE----GDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 138 ALDTLADRLKSVVAQYGNEAV-YINYSSGivGGNITRSSPsaspvaRLMNCYGGSLNQYGTY-STAQIAcAMPYTYGSND 215
Cdd:cd02766 78 ALDTIAAKLKEIKAEYGPESIlPYSYAGT--MGLLQRAAR------GRFFHALGASELRGTIcSGAGIE-AQKYDFGASL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 216 GNSTSDIENSKLVVMFGNNPAETRMSGGGItwyLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAW 295
Cdd:cd02766 149 GNDPEDMVNADLIVIWGINPAATNIHLMRI---IQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALGVAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 296 VLINEDLVDQPFLDKYCVGYDEktlpagapanghYKAYILgegddgiAKTPQWASRITGIPTERIIKLAREIGMSKPAYI 375
Cdd:cd02766 224 VLFREGLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKPPSI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 376 CQGWGPQRQANGELTARAIAMLPILTGNVGINGGnsGARESTYtitierlpvlenpvktaiscftwtdaiarGPemtasr 455
Cdd:cd02766 285 RLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGG--GAFYSNS-----------------------------GP------ 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 456 dgvrgkekldvPIKFLWNYAGNTiINQHSDINKTHEILQDEskCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIpnd 535
Cdd:cd02766 328 -----------PVKALWVYNSNP-VAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY--- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 536 yaGNMG--YLIFIQPATSAKFERKPIYWILSEVAKRLGDDVHqrFTEgRTQEQWLqylyaKMVAKDPALPAyedlkrMGI 613
Cdd:cd02766 391 --ASYWhyYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEP--PFE-ESDEEWL-----DQALDGTGLPL------EGI 454
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 490294727 614 YKRKDPNGHFVAYRDFRrdPEAHPLKTPSGKIEIYSsrlaEIAARWQLEkdevisPLP 671
Cdd:cd02766 455 DLERLLGPRKAGFPLVA--WEDRGFPTPSGKFEFYS----ERAAKRGLP------PLP 500
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
10-810 |
3.86e-106 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 345.12 E-value: 3.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 10 VSRRALLKS-TALGSLALAAGGLTLPFTLRRAAAAVQQATGD--TTRIVWGAcsvncgsrcaLRLHVRDDEVVYVETDNT 86
Cdd:PRK15102 1 ASRRRFLKGlGGLSAAGMLGPSLLTPRSALAAQAAAAETTKEwiLTGSHWGA----------FRAKVKNGRFVEAKPFEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 87 gdDRYGDHQVRAclrgrsIRRRINHPDRLNYPMKRV-----------GKRGEGKFVRISWQEALDTLADRLKSVVAQYGN 155
Cdd:PRK15102 71 --DKYPTKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 156 EAVYinysSGIVGGNITRSSPSA-SPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSND----GNSTSDI-ENSKLVV 229
Cdd:PRK15102 143 SALH----TGQTGWQSTGQFHSAtGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSWPLIlENSKTIV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 230 MFGNNP---------AETRMSGGgitwYLEQARER---SNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVL 297
Cdd:PRK15102 219 LWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 298 INEDLVDQPFLDKYCVGYDEkTLPagapanghykaYILGEgDDGIAKTPQWASRITGIPTERIIKLAREIgMSKPAYICQ 377
Cdd:PRK15102 295 YSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 378 GWGPQRQANGELTARAIAMLPILTGNVGINGG--------NSGARESTYTITIERLP-VLENPVK------------TAI 436
Cdd:PRK15102 361 GWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhySGIGVPSSGGAIPGGFPgNLDTGQKpkhdnsdykgysSTI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 437 SCFTWTDAIARgPEMTASRDGvrGKEKLDvPIKFLWnYAGNTIINQHSDINKTHEILQdesKCETIVVIDNFMTSSAKYA 516
Cdd:PRK15102 441 PVARFIDAILE-PGKTINWNG--KKVTLP-PLKMMI-FSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATCRFA 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 517 DLLLPDLMTVEQEDI-IPNDYAgNMGyLIFIQPATSAKFERKPIYWILSEVAKRLGDdvHQRFTEGRTQEQWLQYLYAKM 595
Cdd:PRK15102 513 DIVLPACTQFERNDIdQYGSYS-NRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGR--EKEYTRGMDEMGWLKRLYQEC 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 596 VAKDPA---LPAYEDLKRMGiYKRKDPNGHFVAYRDFRRDPEAHPLKTPSGKIEIYSSRLAEIAAR-------WqLEKDE 665
Cdd:PRK15102 589 KQQNKGkfhMPEFDEFWKKG-YVEFGEGQPWVRHADFREDPELNPLGTPSGLIEIYSRKIADMGYDdcqghpmW-FEKIE 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 666 visplpvyastfegwddplRS-------QYPLQLFGFHYKARTHSSYGNVDVLQA----ACRQEVWINPLDAEKRGIKNG 734
Cdd:PRK15102 667 -------------------RShggpgsdKYPLWLQSVHPDKRLHSQLCESEELREtytvQGREPVYINPQDAKARGIKDG 727
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490294727 735 DMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHDANMTGD--RIDHGACMNTLTTHRP-SPLAKGNPQHTNLVDIEK 810
Cdd:PRK15102 728 DVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEigALCTYGDPNTLTLDIGtSQLAQATSAHTCLVEIEK 806
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
60-570 |
3.16e-100 |
|
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: 315.42 E-value: 3.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 60 SVNCGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGegKFVRISWQEAL 139
Cdd:cd00368 4 CPFCGVGCGILVYVKDGKVVRIE----GDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 140 DTLADRLKSVVAQYGNEAVYINYSSGIVGGNitrsspSASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSNDGNST 219
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAFYGGGGASNEE------AYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 220 SDIENSKLVVMFGNNPAETRMSgggITWYLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGiawvlin 299
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 300 edlvdqpfldkycvgydektlpagapanghykayilgegddgiaktpQWASRITGIPTERIIKLAREIGMSKPAYICQGW 379
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 380 GPQRQANGELTARAIAMLPILTGNVGINGGNSGARestytitierlpvlENPVKTAiscftwtdaiargpemtasrdgvr 459
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA------------------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 460 gkekldvpikflwnyagntiinqhsdiNKTHEILQDESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIipndYAGN 539
Cdd:cd00368 295 ---------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGT----YTNT 343
|
490 500 510
....*....|....*....|....*....|.
gi 490294727 540 MGYLIFIQPATSAKFERKPIYWILSEVAKRL 570
Cdd:cd00368 344 EGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
63-674 |
9.06e-96 |
|
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: 307.31 E-value: 9.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTL 142
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVE----GDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEALDEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVYInySSGiVGGNITRSSPSASPvaRLMNCYGGSLNQYGTYStaqiaC------AMPYTYGSNDG 216
Cdd:cd02759 83 AEKLAEIKAEYGPESIAT--AVG-TGRGTMWQDSLFWI--RFVRLFGSPNLFLSGES-----CywprdmAHALTTGFGLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 NSTSDIENSKLVVMFGNNPAETRMSGGGITwyLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWV 296
Cdd:cd02759 153 YDEPDWENPECIVLWGKNPLNSNLDLQGHW--LVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 297 LINEDLVDQPFLDKYCVGYDEktLPAgapangHYKAYilgegddgiakTPQWASRITGIPTERIIKLAREIGMSKPAYIC 376
Cdd:cd02759 229 IINEGLYDKDFVENWCYGFEE--LAE------RVQEY-----------TPEKVAEITGVPAEKIRKAARLYATAKPACIQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 377 QGWGPQRQANGELTARAIAMLPILTGNVGINGGNsgaRESTYtitierlpvlenpvktaiscftwtdaiargpemtasrd 456
Cdd:cd02759 290 WGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGN---LLIPY-------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 457 gvrgkekldvPIKFLWNYAGNTIINQhSDINKTHEILQdesKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIPNDY 536
Cdd:cd02759 329 ----------PVKMLIVFGTNPLASY-ADTAPVLEALK---ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFE 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 537 AGNMGYLI--FIQPAtsakFERKPIYWILSEVAKRLGddvhqrftegrtQEQWLQYLYAKmvakdpalpayedlkrmgIY 614
Cdd:cd02759 395 AENFVQLRqkAVEPY----GEAKSDYEIVLELGKRLG------------PEEAEYYKYEK------------------GL 440
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 615 KRKDPNGHFVayrdfrrdpeahplkTPSGKIEIYSSRLaeiaarWQLEKDevisPLPVYA 674
Cdd:cd02759 441 LRPDGQPGFN---------------TPTGKVELYSTML------EELGYD----PLPYYR 475
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
57-658 |
2.85e-93 |
|
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: 303.63 E-value: 2.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 57 GACSVNCGSRCALRLHVRDDEVVYVETDNTGDDRYGdhqvRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQ 136
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYK----RGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 137 EALDTLADRLKSVVAQYGNEAVYINYSSGIVGGNITRSSPSASPVARLMNCYGGSLNQYGTYSTAQIACAMPytygsnDG 216
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMP------PT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 NSTSDIENSKLVVMFGNNPAETRMSggGITWYLEqARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWV 296
Cdd:cd02765 152 NEITDWVNAKTIIIWGSNILETQFQ--DAEFFLD-ARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 297 LINEDLVDQPFLDKYC-----VGYDEKTL--PAGAPANGHYKAYILGEGDDG---------------------------- 341
Cdd:cd02765 227 ILEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVWDTNSDspepvaatninpalegeytingvkvhtv 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 342 -------IAK-TPQWASRITGIPTERIIKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGA 413
Cdd:cd02765 307 ltalreqAASyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 414 restytitierlpvlenpvktaiscftwtdaiargpemtasrdgvrgkekldvpIKFLWNyAGNTIINQHSDINKTHEIL 493
Cdd:cd02765 387 ------------------------------------------------------IKFMYF-MGSNFLGNQPDRDRWLKVM 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 494 qdeSKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIIPNDYAGNmgYLIFIQPATSAKFERKPIYWILSEVAKRLGDD 573
Cdd:cd02765 412 ---KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLG 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 574 vhQRFTEgrTQEQWLQylyAKMVAKDPALPA--YEDLKRMGIYKRKD-PNGHFVAYRDfrrdpeaHPLKTPSGKIEIYSS 650
Cdd:cd02765 487 --DYFPK--TPEDYVR---AFMNSDDPALDGitWEALKEEGIIMRLAtPEDPYVAYLD-------QKFGTPSGKLEFYNE 552
|
....*...
gi 490294727 651 RLAEIAAR 658
Cdd:cd02765 553 AAPELEEA 560
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
63-797 |
4.65e-92 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 303.73 E-value: 4.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFVRISWQEALDTL 142
Cdd:COG3383 14 CGVGCGIDLEVKDGKIVKVE----GDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEALDLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVYInYSSG----------------IVG-GNITRSS--PSASPVARLMNCYGGSlnqygtystaqi 203
Cdd:COG3383 86 AERLREIQAEHGPDAVAF-YGSGqltneenyllqklargVLGtNNIDNNArlCMASAVAGLKQSFGSD------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 204 acAMPYTYgsndgnstSDIENSKLVVMFGNNPAETrmsgggITWYLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRP 283
Cdd:COG3383 153 --APPNSY--------DDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 284 GTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEktlpagapanghYKAYILGEgddgiakTPQWASRITGIPTERIIKL 363
Cdd:COG3383 218 GTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 364 AREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGING---------GNS-GARESTYTITieRLP---VLEN 430
Cdd:COG3383 279 ARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGtgpfpltgqNNVqGGRDMGALPN--VLPgyrDVTD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 431 PVKTAISCFTW-TDAIARGPEMTASR--DGVRGKEkldvpIKFLWNYAGNtIINQHSDINKTHEILqdeSKCETIVVIDN 507
Cdd:COG3383 357 PEHRAKVADAWgVPPLPDKPGLTAVEmfDAIADGE-----IKALWIIGEN-PAVSDPDANHVREAL---EKLEFLVVQDI 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 508 FMTSSAKYADLLLPDLMTVEQEdiipndyaGNM----GYLIFIQPATSAKFERKPIYWILSEVAKRLGddvhQRFTEGRT 583
Cdd:COG3383 428 FLTETAEYADVVLPAASWAEKD--------GTFtnteRRVQRVRKAVEPPGEARPDWEIIAELARRLG----YGFDYDSP 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 584 QEQWLQYlyaKMVAKDPALPAYEDLKRMG----IYKRKDPNGHFVAYRD-FrrdpeahplKTPSGKieiyssrlAEIAAR 658
Cdd:COG3383 496 EEVFDEI---ARLTPDYSGISYERLEALGgvqwPCPSEDHPGTPRLFTGrF---------PTPDGK--------ARFVPV 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 659 WQLEKDEVISPlpvyastfegwddplrsQYPLQL------FGFHYKARThssyGNVDVLQAACRQE-VWINPLDAEKRGI 731
Cdd:COG3383 556 EYRPPAELPDE-----------------EYPLVLttgrllDQWHTGTRT----RRSPRLNKHAPEPfVEIHPEDAARLGI 614
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490294727 732 KNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMgqgAWHDAnmtgdridhGACMNTLTTHRPSPLAK 797
Cdd:COG3383 615 KDGDLVRVSSRRGEVVLRARVTDRVRPGTVFM---PFHWG---------EGAANALTNDALDPVSK 668
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
63-654 |
1.65e-82 |
|
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: 271.48 E-value: 1.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTL 142
Cdd:cd02755 8 CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQYI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVyinyssgIVGGNITRSSPSASPVARLMncygGSLNQYGTYSTaqiaCAMPYTYGSND------G 216
Cdd:cd02755 84 ASKLKEIKEQHGPESV-------LFGGHGGCYSPFFKHFAAAF----GSPNIFSHEST----CLASKNLAWKLvidsfgG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 NSTSDIENSKLVVMFGNNPAEtrmsgGGIT---WYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGI 293
Cdd:cd02755 149 EVNPDFENARYIILFGRNLAE-----AIIVvdaRRLMKALENG-AKVVVVDPRFSELAS-KADEWIPIKPGTDLAFVLAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 294 AWVLINEDLVDQPFLDKYCVGYDEktlpagapANGHYKAYilgegddgiakTPQWASRITGIPTERIIKLAREIGMSKP- 372
Cdd:cd02755 222 IHVLISENLYDAAFVEKYTNGFEL--------LKAHVKPY-----------TPEWAAQITDIPADTIRRIAREFAAAAPh 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 373 AYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGnsgarestytitierlpvlenpvktaiscftWTDAIARGPemt 452
Cdd:cd02755 283 AVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG-------------------------------LYYAGSAKP--- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 453 asrdgvrgkekldVPIKFLWNYAGNTIINQhSDINKTHEILQdesKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDII 532
Cdd:cd02755 329 -------------YPIKALFIYRTNPFHSM-PDRARLIKALK---NLDLVVAIDILPSDTALYADVILPEATYLERDEPF 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 533 PNDYAGNMGYLIFiQPATSAKFERKPIYWILSEVAKRLGddvhqrftegrtqeqwlqylyakmvakdpalpayedlkrmg 612
Cdd:cd02755 392 SDKGGPAPAVATR-QRAIEPLYDTRPGWDILKELARRLG----------------------------------------- 429
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 490294727 613 iykrkdpnghfvayrdfrrdpeahPLKTPSGKIEIYSSRLAE 654
Cdd:cd02755 430 ------------------------LFGTPSGKIELYSPILAK 447
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
11-811 |
1.25e-77 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 266.53 E-value: 1.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 11 SRRALLKSTALGSlALAAGGLTLPFTLRRAAAAVQQATGDTTRIVwgaCSVnCGSRCALRLHVRDDEVVYVetdnTGDDR 90
Cdd:PRK15488 4 SRRDFLKGAGAGC-AACALGSLLPGALAANEIAQLKGKTKLTPSI---CEM-CSTRCPIEARVVNGKNVFI----QGNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 91 YGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYinYSSgivggn 170
Cdd:PRK15488 75 AKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVA--FSS------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 171 itRSSPSASPVARLMNCYGgSLNQYGTYSTAQIACAMP--YTYGsndGNSTSDIENSKLVVMFGNNPAEtrmsggGI--- 245
Cdd:PRK15488 147 --KSGSLSSHLFHLATAFG-SPNTFTHASTCPAGYAIAakVMFG---GKLKRDLANSKYIINFGHNLYE------GInms 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 246 -TWYLEQARERSNARMIVIDPRYTdTAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDE--KTLpa 322
Cdd:PRK15488 215 dTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEElaASV-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 323 gapanghyKAYilgegddgiakTPQWASRITGIPTERIIKLAREIGMSKPAYICQgWGPQ---RQANGELTaRAIAMLPI 399
Cdd:PRK15488 292 --------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRatfTPEEFDMR-RAIFAANV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 400 LTGNVGINGGNSGARE-STYT--ITIERLPVLENPVKTAISCFTWT--DAIARGPEMTASRDGVRGK------EKLDVPI 468
Cdd:PRK15488 351 LLGNIERKGGLYFGKNaSVYNklAGEKVAPTLAKPGVKGMPKPTAKriDLVGEQFKYIAAGGGVVQSiidatlTQKPYQI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 469 KFLWNYAGNTIINQhSDINKTHEILQdesKCETIVVIDNFMTSSAKYADLLLPDLMTVEQ-EDIipNDYAG-NMGYLIFi 546
Cdd:PRK15488 431 KGWVMSRHNPMQTV-TDRADVVKALK---KLDLVVVCDVYLSESAAYADVVLPESTYLERdEEI--SDKSGkNPAYALR- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 547 QPATSAKFERKPIYWILSEVAKRLGDDvhQRFTeGRTQEQWLQYlyakMVAKDPALpaYEDLKRMG--------IYKRKD 618
Cdd:PRK15488 504 QRVVEPIGDTKPSWQIFKELGEKMGLG--QYYP-WQDMETLQLY----QVNGDHAL--LKELKKKGyvsfgvplLLREPK 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 619 PNGHFVAyrdfrRDPEAHP------------LKTPSGKIEIYSSRLAEIAARWQlekdeVISPLPVyastfegwddPLRS 686
Cdd:PRK15488 575 MVAKFVA-----RYPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALAPGYG-----VPRYRDV----------ALKK 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 687 QYPLQLFGFHYKARTHSSYGNVDVL-QAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGV--SAM 763
Cdd:PRK15488 635 EDELYFIQGKVAVHTNGATQNVPLLaNLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTlfAYM 714
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 490294727 764 GQGAWHDANMTGDRidHGACMNTLTTHRPSPLAkGNPQHTNLVDIEKV 811
Cdd:PRK15488 715 GFGSKNKELTRATG--KGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
54-591 |
1.73e-76 |
|
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: 255.32 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 54 IVWGACSVNCGSRCALRLHVRDDEVVYVE--TD--NTGDDrYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGK 129
Cdd:cd02750 3 VVRSTHGVNCTGSCSWNVYVKNGIVTREEqaTDypETPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 130 FVRISWQEALDTLADRLKSVVAQYGNEAVYInySSGIVG-GNITRSSPSaspvaRLMNCYGGSL----NQYGTYSTAQia 204
Cdd:cd02750 82 WKRISWDEALELIADAIIDTIKKYGPDRVIG--FSPIPAmSMVSYAAGS-----RFASLIGGVSlsfyDWYGDLPPGS-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 205 camPYTYG-SNDGNSTSDIENSKLVVMFGNNPAETRMSGggiTWYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRP 283
Cdd:cd02750 153 ---PQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADLWVPIKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 284 GTDAALVAGIAWVLINEDLVDQPFLDKYcvgydeKTLPagapanghYKAYilgegddgiakTPQWASRITGIPTERIIKL 363
Cdd:cd02750 225 GTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPRETVIRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 364 AREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNsgarestytitierlpvlenpvktaiscftWTD 443
Cdd:cd02750 280 AREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGG------------------------------WAH 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 444 AIARgpemtasrdgvrgkekldvpIKFLWNYAGNTiINQHsdiNKTHEILQD--ESKCETIVVIDNFMTSSAKYADLLLP 521
Cdd:cd02750 330 YVGQ--------------------PRVLFVWRGNL-FGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLP 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490294727 522 DLMTVEQEDIIPNDYAgnmGYLIFIQPATSAKFERKPIYWILSEVAKRlgddVHQRFTEGRTQ----EQWLQYL 591
Cdd:cd02750 386 AATWYEKHDLSTTDMH---PFIHPFSPAVDPLWEAKSDWEIFKALAKK----VPWRTLTGRQQfyldHDWFLEL 452
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-569 |
1.43e-70 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 236.14 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 114 RLNYPMKRvgkRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVYINYSSGivGGNITRSSPSASP-VARLMNCYGGSL 192
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALKKlLNRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 193 NQYGTYSTAQIACA-MPYTYGSNDGNSTSDIENSKLVVMFGNNPAETRMSGGgitWYLEQARERSNARMIVIDPRYTdta 271
Cdd:pfam00384 76 DHNGDLCTAAAAAFgSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILN---ARIRKAALKGKAKVIVIGPRLD--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 272 AGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQPFLDKycvgydektlpagapanghykayilgegddgiaktpqwasr 351
Cdd:pfam00384 150 LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK----------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 352 itgipteriiklareigmskpAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGARESTYTITiERLPVLENP 431
Cdd:pfam00384 189 ---------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAA-SPVGALDLG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 432 VKTAISCFTWTDAIARGpemtasrdgvrgkekldvPIKFLWnYAGNTIINQHSDINKTHEILQdesKCETIVVIDNFM-T 510
Cdd:pfam00384 247 LVPGIKSVEMINAIKKG------------------GIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYDGHHgD 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490294727 511 SSAKYADLLLPDLMTVEQEDIIPNDyagnMGYLIFIQPATSAKFERKPIYWILSEVAKR 569
Cdd:pfam00384 305 KTAKYADVILPAAAYTEKNGTYVNT----EGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
63-582 |
3.94e-69 |
|
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: 238.66 E-value: 3.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVetdnTGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRvgkRGEGKFVRISWQEALDTL 142
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAV----RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVYInYSSGivggniTRSSPSASPVARLMNCYGGSlNQYGTYST---AQIACAMPYTYGSnDG--N 217
Cdd:cd02754 80 AERFKAIQAEYGPDSVAF-YGSG------QLLTEEYYAANKLAKGGLGT-NNIDTNSRlcmASAVAGYKRSFGA-DGppG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 218 STSDIENSKLVVMFGNNPAETRmsggGITW-YLEQARE-RSNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAW 295
Cdd:cd02754 151 SYDDIEHADCFFLIGSNMAECH----PILFrRLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIRPGTDLALLNGLLH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 296 VLINEDLVDQPFLDKYCVGYDEKTLpagapangHYKAYilgegddgiakTPQWASRITGIPTERIIKLAREIGMSKPAYI 375
Cdd:cd02754 226 VLIEEGLIDRDFIDAHTEGFEELKA--------FVADY-----------TPEKVAEITGVPEADIREAARLFGEARKVMS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 376 CQGWGPQRQANGELTARAIAMLPILTGNVG--------ING-GNS-GARESTYTITieRLP---VLENPVKTAISCFTW- 441
Cdd:cd02754 287 LWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREVGGLAN--LLPghrSVNNPEHRAEVAKFWg 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 442 TDAIARGPEMtaSRDGVRGKEKL-DVPIKFLWNYAGNtiiNQHS--DINKTHEILQdesKCETIVVIDNFMTS-SAKYAD 517
Cdd:cd02754 365 VPEGTIPPKP--GLHAVEMFEAIeDGEIKALWVMCTN---PAVSlpNANRVREALE---RLEFVVVQDAFADTeTAEYAD 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490294727 518 LLLPDLMTVEQEDIIpndyaGNM-GYLIFIQPATSAKFERKPIYWILSEVAKRLG----------DDV---HQRFTEGR 582
Cdd:cd02754 437 LVLPAASWGEKEGTM-----TNSeRRVSLLRAAVEPPGEARPDWWILADVARRLGfgelfpytspEEVfeeYRRLSRGR 510
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
688-810 |
3.26e-67 |
|
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: 218.31 E-value: 3.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPLQLFGFHYKARTHSSYGNVDVLQAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGA 767
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490294727 768 WHDanMTGDRIDHGACMNTLTTHRPSPLAKGNPQHTNLVDIEK 810
Cdd:cd02794 81 WYE--PDANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
62-654 |
4.56e-62 |
|
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: 218.08 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 62 NCGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRG----EGKFVRISWQE 137
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPKFVPISWDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 138 ALDTLADRLKSVVAQygNEAVYINYSSGIVGGNitrsspSASPVARLMNCYGGSLNQYGTYSTAQIA-CAMPYTYGSNDG 216
Cdd:cd02757 84 ALDTIADKIRALRKE--NEPHKIMLHRGRYGHN------NSILYGRFTKMIGSPNNISHSSVCAESEkFGRYYTEGGWDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 NStSDIENSKLVVMFGNNPAET--------RMSGGgitwyleqarERSNARMIVIDPRYTDTAAgREDEWIPIRPGTDAA 288
Cdd:cd02757 156 NS-YDYANAKYILFFGADPLESnrqnphaqRIWGG----------KMDQAKVVVVDPRLSNTAA-KADEWLPIKPGEDGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 289 LVAGIAWVLINEDLVDQPFLDKYCVGYD----EKTLPAGAPANGHYKAYILGEGDDGIAKTPQWASRITGIPTERIIKLA 364
Cdd:cd02757 224 LALAIAHVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKEKSTEGLVKWWNLELKDYTPEWAAKISGIPAETIERVA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 365 REIGMSKPAYICQGW-GPQRQANGELTARAIAMLPILTGNVGINGG-NSGARESTYTITIERlpvLENPVKTAISCFTWT 442
Cdd:cd02757 304 REFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGGlCPNMGVPKIKVYFTY---LDNPVFSNPDGMSWE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 443 DAIArgpemtasrdgvrgkeklDVPIkflwnyagntiinqhsdinktheilqdeskcetIVVIDNFMTSSAKYADLLLPD 522
Cdd:cd02757 381 EALA------------------KIPF---------------------------------HVHLSPFMSETTYFADIVLPD 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 523 LMTVEQEDIIPNdYAGNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGDDVHqrftegrtqEQWLQYLYAKMvaKDPal 602
Cdd:cd02757 410 GHHFERWDVMSQ-ENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDPKGS---------DGMKRYAPGQF--KDP-- 475
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 490294727 603 payEDLKRMGiykrkdpnGHFVAYrdfrrdpeahpLKTPSGKIEIYSSRLAE 654
Cdd:cd02757 476 ---ETGKNNR--------WEFENV-----------FPTETGKFEFYSETLKK 505
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
63-573 |
1.33e-59 |
|
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: 210.92 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVgkrgEGKFVRISWQEALDTL 142
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVYINYSSGivGGN--------ITRS---SPSASPVARLmnCYGGSLNqygtystaqiacAMPYTY 211
Cdd:cd02753 79 ASRLKEIKDKYGPDAIAFFGSAK--CTNeenylfqkLARAvggTNNVDHCARL--CHSPTVA------------GLAETL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 212 GSN-DGNSTSDIENSKLVVMFGNNPAETRMSgggITWYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALV 290
Cdd:cd02753 143 GSGaMTNSIADIEEADVILVIGSNTTEAHPV---IARRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 291 AGIAWVLINEDLVDQPFLDKYCVGYDEKTLpagapangHYKAYilgegddgiakTPQWASRITGIPTERIIKLAREIGMS 370
Cdd:cd02753 218 NAMAHVIIEEGLYDEEFIEERTEGFEELKE--------IVEKY-----------TPEYAERITGVPAEDIREAARMYATA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 371 KPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGnsGArestytitierlpvleNPVktaiscftwtdaiaRGpe 450
Cdd:cd02753 279 KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT--GV----------------NPL--------------RG-- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 451 mtasRDGVRGKEKLDVPIKFLWNYA------GNTIINQHSDINKTHEILqdeSKCETIVVIDNFMTSSAKYADLLLPDLM 524
Cdd:cd02753 325 ----QNNVQGACDMGALPNVLPGYVkalyimGENPALSDPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPAAS 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 490294727 525 TVEQEDIIPNdyagNMGYLIFIQPATSAKFERKPIYWILSEVAKRLGDD 573
Cdd:cd02753 398 FAEKDGTFTN----TERRVQRVRKAVEPPGEARPDWEIIQELANRLGYP 442
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-810 |
2.58e-55 |
|
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: 186.25 E-value: 2.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPLQLFGFHYKARTHSSYGNVDVLQAAC----RQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAM 763
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYkvkgREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 490294727 764 GQGAWHDANMTGDrIDHGACMNTLTTHRPSP-LAKGNPQHTNLVDIEK 810
Cdd:cd02777 81 PEGAWYDPDDNGG-LDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
59-530 |
1.90e-53 |
|
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: 194.54 E-value: 1.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 59 CSVNCGsrcaLRLHVRDDEVVYVEtdntGDDrygDHQVRA---CLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFVRISW 135
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIR----GDP---DDPLSKgyiCPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 136 QEALDTLADRLKSVVAQYGNEAVyinyssGIVGGNitrssPSASPVARLMncYGGSL------NQYGTYSTAQiacAMP- 208
Cdd:cd02762 72 DEAFDEIAERLRAIRARHGGDAV------GVYGGN-----PQAHTHAGGA--YSPALlkalgtSNYFSAATAD---QKPg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 209 -----YTYGSNDGNSTSDIENSKLVVMFGNNPAETR---MSGGGITWYLEQARERSnARMIVIDPRYTDTAAgREDEWIP 280
Cdd:cd02762 136 hfwsgLMFGHPGLHPVPDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 281 IRPGTDAALVAGIAWVLINEDLVDQPFLDKYCVGYDEkTLPAGAPAnghykayilgegddgiakTPQWASRITGIPTERI 360
Cdd:cd02762 214 VRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDE-VRAALAEF------------------TPEAYAPRCGVPAETI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 361 IKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGGNsgarestyTITIERLPVLENPVKTAISCFT 440
Cdd:cd02762 275 RRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGA--------MFTTPALDLVGQTSGRTIGRGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 441 WTDAIARGPEMTASRDGVRGKEKLDVP----IKFLWNYAGNTIinqHS--DINKTHEILQdesKCETIVVIDNFMTSSAK 514
Cdd:cd02762 347 WRSRVSGLPEIAGELPVNVLAEEILTDgpgrIRAMIVVAGNPV---LSapDGARLEAALG---GLEFMVSVDVYMTETTR 420
|
490
....*....|....*.
gi 490294727 515 YADLLLPDLMTVEQED 530
Cdd:cd02762 421 HADYILPPASQLEKPH 436
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
53-572 |
2.04e-42 |
|
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: 164.49 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 53 RIVWGACSVNCGsrcaLRLHVRDDEVVYVETDNtgddrygDHQVR---ACLRGRSIRRRINHPDRLNYPMKRVGkrGEGK 129
Cdd:cd02752 1 RTICPYCSVGCG----LIAYVQNGVWVHQEGDP-------DHPVNrgsLCPKGAALRDFVHSPKRLKYPMYRAP--GSGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 130 FVRISWQEALDTLADRLKSV------------VAQYGNEAVYINYSSGI--------------VGGNITRSS---PSASP 180
Cdd:cd02752 68 WEEISWDEALDEIARKMKDIrdasfveknaagVVVNRPDSIAFLGSAKLsneecylirkfaraLGTNNLDHQariUHSPT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 181 VARLMNCYGgslnqYGtystaqiacAMPytygsndgNSTSDIENSKLVVMFGNNPAETRMSGggITWYLEqARERSNARM 260
Cdd:cd02752 148 VAGLANTFG-----RG---------AMT--------NSWNDIKNADVILVMGGNPAEAHPVS--FKWILE-AKEKNGAKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 261 IVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWVLInedlvdqpfldKYcvgydektlpagapanghykayilgegdd 340
Cdd:cd02752 203 IVVDPRFTRTAA-KADLYVPIRSGTDIAFLGGMINYII-----------RY----------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 341 giakTPQWASRITGIPTERIIKLAREIG----MSKPAYI--CQGWgpQRQANGELTARAIAMLPILTGNVGINGGnsGAr 414
Cdd:cd02752 242 ----TPEEVEDICGVPKEDFLKVAEMFAatgrPDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGG--GV- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 415 estytitierlpvlenpvktaiscftwtdAIARGpemtasRDGVRGKEKLDVpikfLWN-----YAGNTIINQHSDINKT 489
Cdd:cd02752 313 -----------------------------NALRG------HSNVQGATDLGL----LSHnlpgyLGGQNPNSSFPNANKV 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 490 HEILqdeSKCETIVVIDNFMTSSAKYAD-------------LLLPDLMTVEQEDIIPN-DYAGNMGYLIfIQPAtsakFE 555
Cdd:cd02752 354 RRAL---DKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNsGRWLQWRYKV-VEPP----GE 425
|
570
....*....|....*..
gi 490294727 556 RKPIYWILSEVAKRLGD 572
Cdd:cd02752 426 AKSDGDILVELAKRLGF 442
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-571 |
1.30e-41 |
|
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: 162.31 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTL 142
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 143 ADRLKSVVAQYGNEAVYI---NYSSGIVGgnitrsspsaspvarLMNCYGGSLN--QYGTYSTAQIACAMPYTYGSNDGN 217
Cdd:cd02763 83 TKRLKAARATDPKKFAFFtgrDQMQALTG---------------WFAGQFGTPNyaAHGGFCSVNMAAGGLYSIGGSFWE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 218 -STSDIENSKLVVMFG------NNPAETRMsgggitwyleQARERSNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALV 290
Cdd:cd02763 148 fGGPDLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPVRTGYAA-IADEWVPIKPGTDGAFI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 291 AGIAWVLINEDLVDQPFLDKYcvgydektlpagapANGHYKayilgegddgIAKTPQWASRITGIPTERIIKLAREIGMS 370
Cdd:cd02763 217 LALAHELLKAGLIDWEFLKRY--------------TNAAEL----------VDYTPEWVEKITGIPADTIRRIAKELGVT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 371 K-------PAYICQGWGPQRQ------------------ANGELTARAIAMLPILTGNVGINGGNSgaRESTYTITIERL 425
Cdd:cd02763 273 ArdqpielPIAWTDVWGRKHEkitgrpvsfhamrgiaahSNGFQTIRALFVLMMLLGTIDRPGGFR--HKPPYPRHIPPL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 426 P--------VLE------------------------NPVKTAiSCFTWTDAIA-RGPEMTASRDGVRGKEkldVPIKFLW 472
Cdd:cd02763 351 PkppkipsaDKPftplygpplgwpaspddllvdedgNPLRID-KAYSWEYPLAaHGCMQNVITNAWRGDP---YPIDTLM 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 473 NYAGNTIINQHSDINKTHEILQD-----ESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDII------PNDYAGNMG 541
Cdd:cd02763 427 IYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMslldrpISEADGPVD 506
|
570 580 590
....*....|....*....|....*....|
gi 490294727 542 YLifIQPATSAKFERKPIYWILSEVAKRLG 571
Cdd:cd02763 507 AI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
97-571 |
3.82e-34 |
|
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: 140.17 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 97 RACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLAD----------------RLKSVVA-----QYG- 154
Cdd:cd02758 66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEggdlfgeghveglkaiRDLDTPIdpdhpDLGp 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 155 --NEAVYINyssgivggniTRSSPSASPVARLMNCYGGSLNQYGTYSTAQIACAMPYTYGSNDGNS----TSDIENSKLV 228
Cdd:cd02758 146 kaNQLLYTF----------GRDEGRTPFIKRFANQAFGTVNFGGHGSYCGLSYRAGNGALMNDLDGyphvKPDFDNAEFA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 229 VMFGNNPAEtrmSGGGITW---YLEQARERSNARMIVIDPRY--TDTAAGREDEWIPIRPGTDAALVAG-IAWVLINEdl 302
Cdd:cd02758 216 LFIGTSPAQ---AGNPFKRqarRLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAmIRWIIENE-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 303 vdqpfldkycvGYDEKTL----PAGAPANGhYKAY-----------------ILGEgdDGIAKT-PQWAsRITGIPTERI 360
Cdd:cd02758 291 -----------RYNAEYLsipsKEAAKAAG-EPSWtnathlvitvrvksalqLLKE--EAFSYSlEEYA-EICGVPEAKI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 361 IKLAREIG--MSKPAYICQgwGPQRQANGELTARAIAMLPILTGNVGINGG--NSGARESTYT----------------- 419
Cdd:cd02758 356 IELAKEFTshGRAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLNWKGGllMSGGGFADNSagprydfkkffgevkpw 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 420 ---ITIERLPVLENP-----VKTAISCF----TWTD-AIARGPEMTASrdgvrGKEKLDVPIKFLWNYAGNTIINQHSDI 486
Cdd:cd02758 434 gvpIDRSKKAYEKTSeykrkVAAGENPYpakrPWYPlTPELYTEVIAS-----AAEGYPYKLKALILWMANPVYGAPGLV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 487 NKTHEILQDESKCETIVVIDNFMTSSAKYADLLLPDLMTVEQEDIipndyAGNMGYLIF---------IQPATSAKFERK 557
Cdd:cd02758 509 KQVEEKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGF-----STPWGGVPTkastarwpvIAPLTEKTANGH 583
|
570
....*....|....*.
gi 490294727 558 PIYW--ILSEVAKRLG 571
Cdd:cd02758 584 PVSMesFLIDLAKALG 599
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-408 |
4.43e-31 |
|
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: 129.35 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 114 RLNYPMKRvgKRGEGKFVRISWQEALDTLADRLKSVVAqygNEAVYinYSSGivggnitRSSPSASPVARL-MNCYG-GS 191
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDP---DRAAF--YTSG-------RASNEAAYLYQLfARAYGtNN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 192 LNQYGTYSTAQIACAMPYTYGSndGNST---SDIENSKLVVMFGNNPAET--RMsgggiTWYLEQARERSnARMIVIDP- 265
Cdd:cd02767 130 LPDCSNMCHEPSSVGLKKSIGV--GKGTvslEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GKIIVINPl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 266 ------RYTDTAAGRE---------DEWIPIRPGTDAALVAGIA-WVLINED----LVDQPFLDKYCVGYDEktlpagap 325
Cdd:cd02767 202 repgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAkHLIERDDepgnVLDHDFIAEHTSGFEE-------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 326 anghYKAYILGEGDDGIaktpqwaSRITGIPTERIIKLAREIGMSKPAYICQGWGPQRQANGELTARAIAMLPILTGNVG 405
Cdd:cd02767 274 ----YVAALRALSWDEI-------ERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIG 342
|
...
gi 490294727 406 ING 408
Cdd:cd02767 343 RPG 345
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-810 |
1.20e-30 |
|
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: 116.97 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPLQLFGFHYKARTHSSYGNVDVLQAAC---RQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMG 764
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKvqgREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490294727 765 QGAWHDANMTGDRID---HGaCMNTLTTHRP-SPLAKGNPQHTNLVDIEK 810
Cdd:cd02793 81 TGAWYDPDDPGEPGPlckHG-NPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
690-805 |
1.12e-28 |
|
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: 110.44 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 690 LQLFGFHYKARTHSSYGNVDVLQAACRQE--VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGA 767
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 490294727 768 WHDAnmtgdridHGACMNTLTTHRPSPLAKGNPQHTNL 805
Cdd:pfam01568 81 WYEP--------RGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
697-802 |
5.27e-28 |
|
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: 108.56 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 697 YKARTHSSY-GNVDVLQAACRQE-VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHdanmt 774
Cdd:cd02775 1 LRDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH----- 75
|
90 100
....*....|....*....|....*...
gi 490294727 775 gdRIDHGACMNTLTTHRPSPLAKGNPQH 802
Cdd:cd02775 76 --RGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
98-769 |
1.24e-24 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 110.47 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 98 ACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFVRISWQEALDTLA-----------DRLKSVVA----------QYG-- 154
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVeggdlfgeghvDGLRAIRDldtpidaknpEYGpk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 155 -NEAVYINyssgivGGNITRsspsASPVARLMNCYGGSLN--QYGTYstaqiaCAMPYTYGSN------DGNS--TSDIE 223
Cdd:PRK14991 221 aNQLLVTN------ASDEGR----DAFIKRFAFNSFGTRNfgNHGSY------CGLAYRAGSGalmgdlDKNPhvKPDWD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 224 NSKLVVMFGNNPAEtrmSGGGitwYLEQARERSNARM------IVIDPR---YTDTAAGREDEWIPIRPGTDAALVAG-I 293
Cdd:PRK14991 285 NVEFALFIGTSPAQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAMGmI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 294 AWVLINED----------------------------LVDQP-------FL------------------DKYCV-GYDEKT 319
Cdd:PRK14991 359 RWIIDNQRynadylaqpgvaamqaageaswtnathlVIADPghprygqFLrasdlglpfegeargdgeDTLVVdAADGEL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 320 LPAGA--PANGHYKAYILGEGDDGIA--------------KTPQWASRITGIPTERIIKLAREI---GmSKPAYICQgwG 380
Cdd:PRK14991 439 VPATQaqPARLFVEQYVTLADGQRVRvksslqllkeaarkLSLAEYSEQCGVPEAQIIALAEEFtshG-RKAAVISH--G 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 381 PQRQANGELTARAIAMLPILTGNVGINGGNS-----------GARestYtiTIERLPVLENPVKTAIS--CFTW------ 441
Cdd:PRK14991 516 GTMSGNGFYNAWAIMMLNALIGNLNLKGGVVvgggkfpgfgdGPR---Y--NLASFAGKVKPKGVSLSrsKFPYekssey 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 442 --------TDAIARGP----------EMTASrdGVRGkekLDVPIKFLWNYAGNTIINQHSDINKTHEILQDESKCETIV 503
Cdd:PRK14991 591 rrkveagqSPYPAKAPwypfvaglltEMLTA--ALEG---YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFI 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 504 VIDNFMTSSAKYADLLLPDLMTVEQEDIIPnDYAGNM-----GYLIFIQPATSAKFERKPIYW--ILSEVAKRLG----D 572
Cdd:PRK14991 666 SIDAFINETTALADYIVPDTHTYESWGFTA-PWGGVPtkastARWPVVEPRTAKTADGQPVCMesFLIAVAKRLQlpgfG 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 573 DVHQRFTEGRTQ-----EQWlqYLYA----KMVAKDPALPAY-EDLKRMG----------------------IYKRkdpN 620
Cdd:PRK14991 745 DNAIKDAQGNTHplnraEDF--YLRGaaniAYLGKTPVADASdEDIALTGvsrilpalqatlkpdevrrvafIYAR---G 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 621 GHFVAYRDFRRDPEAHP-LKTPsgkIEIYSSRLAeiAARWQLeKDEVISPLPVYASTFEGWDDPLRSQY-----PLQLFG 694
Cdd:PRK14991 820 GRFAPAESAYDEERMGNrWKKP---LQIWNEDVA--AARHSM-TGERYSGCPTWYPPRLADGTPLREQFpesqwPLLLIS 893
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490294727 695 FhyKARTHSSYGN-VDVLQAACRQE-VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWH 769
Cdd:PRK14991 894 F--KSNLMSSMSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGH 968
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
688-808 |
3.80e-21 |
|
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: 89.26 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPLQLFGFHYKARTHSSYGNVDVL-QAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQG 766
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELrAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490294727 767 AWHDANMTGDRIdhgacmNTLTTHRPSPLAKGNPQHTNLVDI 808
Cdd:cd02786 81 WWREHSPDGRGV------NALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
687-811 |
1.31e-20 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 88.19 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 687 QYPLQLFGFHYKARTHSSYGNVDVLQAACRQ-EVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQ 765
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490294727 766 GAWHDANMTGDridhgacMNTLTTHRPSPLAKGNPQ-----HTNLVDIEKV 811
Cdd:cd02785 81 GWWSRYFQEGS-------LQDLTSPFVNPVHEYIYGpnsafYDTLVEVRKA 124
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
10-747 |
4.43e-19 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 92.27 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 10 VSRRALLKSTALGSLALAAGgLTLPFTLRRAAAAvqqatgDTTRIVW--GACSVnCGSRCALRLHVRDDEVVYVETD--- 84
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAAG-LSLPAVANAVVGS------AQTAIKWdkAPCRF-CGTGCGVLVGTKDGRVVATQGDpda 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 85 --NTGDDrygdhqvraCLRGRSIRRRINHPDRLNYPMKRVgKRGE----GKFVRISWQEALDTLADRLKSVVAQYGNEAV 158
Cdd:PRK13532 75 pvNRGLN---------CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 159 YInYSSG---IVGG--------------NItrsSPSA-----SPVARLMNCYGgslnqygtystaqiacaMPYTYGSNDg 216
Cdd:PRK13532 145 GM-FGSGqwtIWEGyaasklmkagfrsnNI---DPNArhcmaSAVVGFMRTFG-----------------IDEPMGCYD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 nstsDIENSKLVVMFGNNPAEtrMSGggITWYLEQARERSN--ARMIVIDP---RYTDTAagreDEWIPIRPGTDAALVA 291
Cdd:PRK13532 203 ----DIEAADAFVLWGSNMAE--MHP--ILWSRVTDRRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 292 GIAWVLINEDLVDQPFLDKYCV--------GYD-------EKTLPAGAPANGH-------YKAYIlgegddgiAK-TPQW 348
Cdd:PRK13532 271 YIANYIIQNNAVNWDFVNKHTNfrkgatdiGYGlrpthplEKAAKNPGTAGKSepisfeeFKKFV--------APyTLEK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 349 ASRITGIPTERIIKLArEIGMSKPAYICQGW--GPQRQANGELTARAIAMLPILTGNVGINGgNSG------------AR 414
Cdd:PRK13532 343 TAKMSGVPKEQLEQLA-KLYADPNRKVVSFWtmGFNQHTRGVWANNLVYNIHLLTGKISTPG-NGPfsltgqpsacgtAR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 415 E-STYTitiERLP---VLENPVKTAISCFTWtdaiaRGPEMT-----------ASRDGVRGKekldvpIKFLWNYAGNti 479
Cdd:PRK13532 421 EvGTFS---HRLPadmVVTNPKHREIAEKIW-----KLPEGTippkpgyhavaQDRMLKDGK------LNAYWVMCNN-- 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 480 iNQHSDINKTHEILQDESKCET-IVVIDNFMTSSAKYADLLLPDLMTVEQEdiipndyaGNMG----YLIFIQPATSAKF 554
Cdd:PRK13532 485 -NMQAGPNINEERLPGWRNPDNfIVVSDPYPTVSALAADLILPTAMWVEKE--------GAYGnaerRTQFWRQQVKAPG 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 555 ERKPIYWILSEVAKRlgddvhqrFTegrTQEQWLQYLYAKM-----------------VAKDPA---LPAYE--DLKRMG 612
Cdd:PRK13532 556 EAKSDLWQLVEFSKR--------FK---TEEVWPEELLAKKpeyrgktlydvlfangqVDKFPLselAEGYLndEAKHFG 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 613 IYKRKdpnGHFVAYRDFRRDP-----------EAHPLKTP--SGK---------IEIYSSRLAEIAARWQLEKDEVISPL 670
Cdd:PRK13532 625 FYVQK---GLFEEYASFGRGHghdlapfdtyhKVRGLRWPvvDGKetlwryregYDPYVKAGEGFKFYGKPDGKAVIFAL 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 671 PvYASTFEGWDDplrsQYPLQLFG------FH-----------YKArthssygnvdVLQAACrqevWINPLDAEKRGIKN 733
Cdd:PRK13532 702 P-YEPPAESPDE----EYDLWLSTgrvlehWHtgsmtrrvpelYRA----------FPEAVC----FMHPEDAKARGLRR 762
|
890
....*....|....
gi 490294727 734 GDMVRVFNQRGEVR 747
Cdd:PRK13532 763 GDEVKVVSRRGEVK 776
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
62-571 |
8.81e-19 |
|
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: 91.57 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 62 NCGSRCALRLH-VRDDEVVYVETDNTGDDRYgDHQVRACLRGRSIRRRINHPDRLNYPMKRVG-KRGEGK---FVRISWQ 136
Cdd:cd02760 6 NCVAGPDFMAVkVVDGVATEIEPNFAAEDIH-PARGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVPISWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 137 EALDTLADRLKSVVAQ-YGNEAVYINYSSGIVGGNITrsspsaspvARLMNCYGGSLNQYGT----YSTAQIAC--AMPY 209
Cdd:cd02760 85 EALDLVAAKLRRVREKgLLDEKGLPRLAATFGHGGTP---------AMYMGTFPAFLAAWGPidfsFGSGQGVKcvHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 210 TYGSNDGNSTS---DIENSKLVVMFGNNpaeTRMSGGGITWYLE-QARERSnARMIVIDPRYTDTAAgREDEWIPIRPGT 285
Cdd:cd02760 156 LYGEFWHRAFTvaaDTPLANYVISFGSN---VEASGGPCAVTRHaDARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPKT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 286 DAALVAGIAWVLINE---DLVDQPFL-DK----YCVG----------------YDEK--------TLPAGAPANGHYK-- 331
Cdd:cd02760 231 DPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGpdglylrdaatgkplvWDERsgravpfdTRGAVPAVAGDFAvd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 332 -AYILGEGD------------------DGIAK-TPQWASRITGIPTERIIKLARE------IGMS----------KPAYI 375
Cdd:cd02760 311 gAVSVDADDetaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPVAV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 376 CQGWGPQRQANGELTARAIAMLPILTGNVGINGGNSGAR--------------------------ESTYTITIERLPVLE 429
Cdd:cd02760 391 TLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGTTvrlnrphddrlasvkpgedgfmaqgfNPTDKEHWVVKPTGR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 430 NPVKTAISCF---TWTDAIarGPEMTA--SRDGVRGKEKLDVPIK--FLWNYAGNTIINqhsdINKTHEILQDESKCETI 502
Cdd:cd02760 471 NAHRTLVPIVgnsAWSQAL--GPTQLAwmFLREVPLDWKFELPTLpdVWFNYRTNPAIS----FWDTATLVDNIAKFPFT 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490294727 503 VVIDNFMTSSAKYADLLLPDLMTVEQEDII---PNDYAGNMGY---LIFIQPATSAKFERKPIYWILSEVAKRLG 571
Cdd:cd02760 545 VSFAYTEDETNWMADVLLPEATDLESLQMIkvgGTKFVEQFWEhrgVVLRQPAVEPQGEARDFTWISTELAKRTG 619
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
688-797 |
2.13e-18 |
|
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: 81.78 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPL------QLFGFHYKARThssyGNVDVLQAACRQE-VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGV 760
Cdd:cd00508 3 YPLvlttgrLLEHWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGT 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 490294727 761 SAMgqgAWHDANMTGdridhGACMNTLTTHRPSPLAK 797
Cdd:cd00508 79 VFM---PFHWGGEVS-----GGAANALTNDALDPVSG 107
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
691-810 |
1.15e-14 |
|
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: 71.15 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 691 QLFGFHYKA--RTHSSYGNVDVLQAACR-QEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAM--GQ 765
Cdd:cd02778 1 EFRLIYGKSpvHTHGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490294727 766 GAWHDAnmtGDRID-HGACMNTLTTHRPSPLAKGNPQHTNLVDIEK 810
Cdd:cd02778 81 GHWAPA---LSRAYgGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
686-763 |
1.32e-14 |
|
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: 70.73 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 686 SQYPLQLFG----FHYKARTHSsyGNVDVLQAACRQE-VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGV 760
Cdd:cd02790 1 EEYPLVLTTgrvlYHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGV 78
|
...
gi 490294727 761 SAM 763
Cdd:cd02790 79 VFM 81
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
719-789 |
3.74e-14 |
|
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: 69.52 E-value: 3.74e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490294727 719 VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMgqgAWHDANMTGDridhGACMNTLTT 789
Cdd:cd02791 37 VEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFV---PMHWGDQFGR----SGRVNALTL 100
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
689-795 |
3.77e-14 |
|
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. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 70.10 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 689 PLQLFGFHYKARTHSSYGNVDVLQAACRQE--VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQG 766
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGpvVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
90 100 110
....*....|....*....|....*....|.
gi 490294727 767 AWHDANMTGDRI--DHGACMNTLTTHRPSPL 795
Cdd:cd02776 81 QERHVNVPGSKLtgKRGGIHNSVTRVRIKPT 111
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
688-770 |
6.88e-14 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 69.63 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 688 YPLQLFGFHYKARTHSSYGNVDVLQAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAM--GQ 765
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehGY 80
|
....*
gi 490294727 766 GAWHD 770
Cdd:cd02780 81 GHWAY 85
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
52-111 |
8.19e-14 |
|
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: 66.55 E-value: 8.19e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 52 TRIVWGACSvNCGSRCALRLHVRDDEVVYVETDNTGDDRYGdhqvRACLRGRSIRRRINH 111
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
687-810 |
1.58e-13 |
|
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: 68.10 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 687 QYPLQLFgfhYKART----HSSYGNVDVLQAACRQ-EVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVs 761
Cdd:cd02781 1 EYPLILT---TGARSyyyfHSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490294727 762 AMGQGAWHDANMTGDRIDHGACM----NTLTTHRPS-PLAKGNPQHTNLVDIEK 810
Cdd:cd02781 77 VRAEHGWWYPEREAGEPALGGVWesnaNALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
719-810 |
1.95e-12 |
|
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: 64.55 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 719 VWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMgqgAWHDANM---TGDRIdhgacmNTLTTHRPSPL 795
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI---PYHWGGMglvIGDSA------NTLTPYVGDPN 107
|
90
....*....|....*..
gi 490294727 796 AkgNPQHTN--LVDIEK 810
Cdd:cd02792 108 T--QTPEYKafLVNIEK 122
|
|
| 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 ... |
62-521 |
1.99e-12 |
|
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: 70.11 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 62 NCGSRCALRLHVRDDEVVYVETDNTGD-DRYgdhqvRACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFVRISWQEALD 140
Cdd:cd02771 6 HCSVGCNISLGERYGELRRVENRYNGAvNHY-----FLCDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSWNEALD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 141 TLADRLKSVVAQYGneavyinyssGIVGGNITRSSPSAspVARLMNCYGGSLN--QYGTYSTAQIACAMPYTYGSNDgns 218
Cdd:cd02771 77 VAAARLKEAKDKVG----------GIGSPRASNESNYA--LQKLVGAVLGTNNvdHRARRLIAEILRNGPIYIPSLR--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 219 tsDIENSKLVVMFGNNPAETrmsGGGITWYLEQARERSNARMIVIDPRYTDTAAGREDewIPIRPGTDAALVAgiawvli 298
Cdd:cd02771 142 --DIESADAVLVLGEDLTQT---APRIALALRQAARRKAVELAALSGIPKWQDAAVRN--IAQGAKSPLFIVN------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 299 nedlVDQPFLDKYcVGYDEKTLPAGapanghykayILGEGdDGIAK--TPQWASRITGIPTERIIKLAREIGMSKPAYIC 376
Cdd:cd02771 208 ----ALATRLDDI-AAESIRASPGG----------QARLG-AALARavDASAAGVSGLAPKEKAARIAARLTGAKKPLIV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 377 QGWGPQrqanGELTARAIAMLPILTGNVGINGGNSGARESTYTITIerLPVLENPVKTAIScftwTDAIARGPEmtasrd 456
Cdd:cd02771 272 SGTLSG----SLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGL--LLLGGHVTEPGLD----LDGALAALE------ 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490294727 457 gvrgKEKLDVPIkflwnYAGNTIINQHSDInkthEILQDESKCETIVVIDNFMTSSAKYADLLLP 521
Cdd:cd02771 336 ----DGSADALI-----VLGNDLYRSAPER----RVEAALDAAEFVVVLDHFLTETAERADVVLP 387
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
61-312 |
2.39e-12 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 71.00 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 61 VNC-GSrCALRLHVRDDEVVYvETDNT-----GDDRyGDHQVRACLRGRSIRRRINHPDRLNYPMKR------------- 121
Cdd:COG5013 55 VNCtGS-CSWKVYVKDGIITW-ETQQTdyprtGPDL-PNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvllelwrearar 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 122 ---------------------VGKRGEGKFVRISWQEALDTLADRLKSVVAQYGNEAVY----------INYSSGivggn 170
Cdd:COG5013 132 hgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSYAAG----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 171 itrsspsaspvARLMNCYGGS-LNQYGTYstAQIACAMPYTYG-SNDGNSTSDIENSKLVVMFGNNPAETRmsgggiT-- 246
Cdd:COG5013 207 -----------ARFLSLIGGVmLSFYDWY--ADLPPASPQVWGeQTDVPESADWYNSGYLIMWGSNVPQTR------Tpd 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 247 --WYLEqARERSnARMIVIDPRYTDtAAGREDEWIPIRPGTDAALVAGIAWVLINEDLVDQ--PFLDKYC 312
Cdd:COG5013 268 ahFMTE-ARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
60-238 |
2.28e-11 |
|
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: 66.54 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 60 SVNCGSRCALRLHVRDDEVVYVETDNTGD---------DRYG-DHqvraclrgrsirrrINHPDRLNYPMKRVGkrgeGK 129
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEVMRILPRENEAineewisdkGRFGyDG--------------LNSRQRLTQPLIKKG----GK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 130 FVRISWQEALDTLADRLKSVVAqygnEAVyinysSGIVGGNITrsSPSASPVARLMNCYG-GSLNQYGTYSTAQIACAMP 208
Cdd:cd02768 66 LVPVSWEEALKTVAEGLKAVKG----DKI-----GGIAGPRAD--LESLFLLKKLLNKLGsNNIDHRLRQSDLPADNRLR 134
|
170 180 190
....*....|....*....|....*....|
gi 490294727 209 YTYGSNdgNSTSDIENSKLVVMFGNNPAET 238
Cdd:cd02768 135 GNYLFN--TSIAEIEEADAVLLIGSNLRKE 162
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
721-811 |
1.94e-10 |
|
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: 59.33 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 721 INPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWHDA-NMTGDRIDHGACMNTLT--THRpSPLAk 797
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpGVSGAGSRPGVNVNDLTddTQR-DPLS- 114
|
90
....*....|....*
gi 490294727 798 GNPQHTNL-VDIEKV 811
Cdd:cd02782 115 GNAAHNGVpVRLARV 129
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
112-298 |
2.06e-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: 64.05 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 112 PDRLNYPMKRVGkrgEGKFVRISWQEALDTLADRLKSVvAQYGNEAVYinysSGIVGGNITRSSpsaspVARLMNCYGGS 191
Cdd:cd02764 97 PDRAQGPLRRGI---DGAYVASDWADFDAKVAEQLKAV-KDGGKLAVL----SGNVNSPTTEAL-----IGDFLKKYPGA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 192 LN-QYGTYSTAQIACAMPYTYGsNDGNSTSDIENSKLVVMFGNNPAETRMSGGGITWYLEQAR----ERSNARMIVIDPR 266
Cdd:cd02764 164 KHvVYDPLSAEDVNEAWQASFG-KDVVPGYDFDKAEVIVSIDADFLGSWISAIRHRHDFAAKRrlgaEEPMSRLVAAESV 242
|
170 180 190
....*....|....*....|....*....|..
gi 490294727 267 YTDTAAGrEDEWIPIRPGTDAALVAGIAWVLI 298
Cdd:cd02764 243 YTLTGAN-ADVRLAIRPSQEKAFALGLAHKLI 273
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
52-111 |
2.35e-10 |
|
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: 56.49 E-value: 2.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 52 TRIVWGACSVnCGSRCALRLHVRDDEVVYVEtdntGDDRYGDHQVRACLRGRSIRRRINH 111
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
60-148 |
5.21e-10 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 62.55 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 60 SVNCGSRCALRLHVRDDEVVYVE-TDNTGDDRYgdhqvRACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFVRISWQEA 138
Cdd:COG1034 222 CPHCSVGCNIRVDVRGGKVYRVLpRENEAVNEE-----WLCDKGRFGYDGLNSPDRLTRPLVRKD----GELVEASWEEA 292
|
90
....*....|
gi 490294727 139 LDTLADRLKS 148
Cdd:COG1034 293 LAAAAEGLKA 302
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
90-409 |
7.17e-09 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 59.29 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 90 RYGDHQVRAClrgrsirrrinhpDRLNYPMKRvgKRGEGKFVRISWQEALDTLADRLKSvvaqYGNEAVYINYSSGivgg 169
Cdd:PRK09939 97 TWGDHELEAA-------------GRLTQPLKY--DAVSDCYKPLSWQQAFDEIGARLQS----YSDPNQVEFYTSG---- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 170 nitRSSPSASPVARLMNCYGGSLNqygtYSTAQIACAMPYTYGSND----GNST---SDIENSKLVVMFGNNPAET--RM 240
Cdd:PRK09939 154 ---RTSNEAAFLYQLFAREYGSNN----FPDCSNMCHEPTSVGLAAsigvGKGTvllEDFEKCDLVICIGHNPGTNhpRM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 241 SGGgitwylEQARERSNARMIVIDP-------RYT----------DTAAGREDEWIPIRPGTDAALVAGIAWVLINED-- 301
Cdd:PRK09939 227 LTS------LRALVKRGAKMIAINPlqergleRFTapqnpfemltNSETQLASAYYNVRIGGDMALLKGMMRLLIERDda 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 302 --------LVDQPFLDKYCVGYDEktlpagapanghYKAYILGEgddgiaktpQWA--SRITGIPTERIIKLAREIGMSK 371
Cdd:PRK09939 301 asaagrpsLLDDEFIQTHTVGFDE------------LRRDVLNS---------EWKdiERISGLSQTQIAELADAYAAAE 359
|
330 340 350
....*....|....*....|....*....|....*...
gi 490294727 372 PAYICQGWGPQRQANGELTARAIAMLPILTGNVGINGG 409
Cdd:PRK09939 360 RTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGA 397
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
92-409 |
7.68e-09 |
|
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: 59.42 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 92 GDHQVRACLRGRSIRRRINHP--DRLNYPMKRVGkrgeGKFVRISWQEALDTLADRLKSVVAQYGNE-AVY-INYSSGIV 167
Cdd:cd02756 93 GNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDdAVFaSRFDHGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 168 GGNitrsspsaspvarLMNCYGGSLNQYGTYSTAQIACAMPYTYGSN-----------DGNSTSDIENSKLVVMFGNNPA 236
Cdd:cd02756 169 GGG-------------FENNWGVGKFFFMALQTPFVRIHNRPAYNSEvhatremgvgeLNNSYEDARLADTIVLWGNNPY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 237 ETRMS----------GGGITWYLEQARERSN----ARMIVIDPRYTDTAAGREDEWIP-------IRPGTDAALVAGIAw 295
Cdd:cd02756 236 ETQTVyflnhwlpnlRGATVSEKQQWFPPGEpvppGRIIVVDPRRTETVHAAEAAAGKdrvlhlqVNPGTDTALANAIA- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 296 vlinedlvdqpfldkycvgydektlpagapanghykAYILGEGDDGIAKtpqwASRITGIPTERIIKLAREIGMSKP--- 372
Cdd:cd02756 315 ------------------------------------RYIYESLDEVLAE----AEQITGVPRAQIEKAADWIAKPKEggy 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490294727 373 ------AYIcQG--WGPQR-QANGeltarAIAMLPILTGNVGINGG 409
Cdd:cd02756 355 rkrvmfEYE-KGiiWGNDNyRPIY-----SLVNLAIITGNIGRPGT 394
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
720-773 |
7.03e-08 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 51.78 E-value: 7.03e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490294727 720 WINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWhdANM 773
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW--ANA 85
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
706-767 |
1.58e-06 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant 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, 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 and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 46.92 E-value: 1.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490294727 706 GNVDVLQAACRQEVW-INPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVS--AMGQGA 767
Cdd:cd02788 17 QRSPVIAERAPAPYArLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVglPLGAGF 81
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
63-291 |
3.61e-06 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 50.23 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 63 CGSRCalrlhvrDDEVVYVEtdntgddryGDHQV---RACLRGRSIRRRINHPDRLNYPMKRvgkrgegkFVRISWQEAL 139
Cdd:COG1029 13 CGCLC-------DDLEVEVE---------GGKIVvvkNACAIGAAKFERAVSDHRITSPRIR--------GKEVSLEEAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 140 DTLADRLKSVVAqygnEAVYinyssgivGGNITrSSPSASPVARLMNCYGGSLNqygtySTAQIaCAMPYTYGSNDG--- 216
Cdd:COG1029 69 DKAAEILANAKR----PLIY--------GLSST-DCEAMRAGLALAERVGAVVD-----NTASV-CHGPSLLALQDVgwp 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 217 NST-SDIEN-SKLVVMFGNNPAET------RMSgggitWYLE---QARERSNARMIVIDPRYTDTAAgREDEWIPIRPGT 285
Cdd:COG1029 130 TCTlGEVKNrADVIIYWGCNPVHAhprhmsRYS-----VFPRgffTPKGRKDRTVIVVDPRPTDTAK-VADLHLQVKPGR 203
|
....*.
gi 490294727 286 DAALVA 291
Cdd:COG1029 204 DYEVLS 209
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
69-158 |
1.68e-05 |
|
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: 48.12 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 69 LRLHVRDDEVVYV---------ETDNTGDDRYGdHQvraclrgrsirrRINHPDRLNYPMKRVGkrgeGKFVRISWQEAL 139
Cdd:cd02772 13 LVVHVKNNKVMRVvpreneainECWLSDRDRFS-YE------------GLNSEDRLTKPMIKKD----GQWQEVDWETAL 75
|
90
....*....|....*....
gi 490294727 140 DTLADRLKSVVAQYGNEAV 158
Cdd:cd02772 76 EYVAEGLSAIIKKHGADQI 94
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
694-800 |
1.72e-05 |
|
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: 44.34 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 694 GFHYKARTHSSYgnvDVLQAACrqeVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAWhdANM 773
Cdd:cd02789 14 GRIIEGGNKLTY---EVDACAY---CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW--ANV 85
|
90 100
....*....|....*....|....*..
gi 490294727 774 TGDRIDHGACMntltthrpsPLAKGNP 800
Cdd:cd02789 86 VVDPYTDSTGS---------PIFKGVP 103
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
721-768 |
8.08e-05 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase 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.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 42.83 E-value: 8.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490294727 721 INPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVSAMGQGAW 768
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
687-768 |
7.16e-04 |
|
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 40.91 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490294727 687 QYPLQLFGFHYKARTHS-SYGNVDVLQAACRQEVWINPLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGV----S 761
Cdd:cd02783 1 QYPLTAFTQRPMAMYHSwGSQNAWLRQIHTRNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTvwtwN 80
|
....*....
gi 490294727 762 AMGQ--GAW 768
Cdd:cd02783 81 AIGKrpGAW 89
|
|
| MopB_CT_PHLH |
cd02784 |
The MopB_CT_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
719-782 |
9.91e-04 |
|
The MopB_CT_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding proteins. This CD is of the PHLH region homologous to the conserved molybdopterin-binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239185 [Multi-domain] Cd Length: 137 Bit Score: 40.13 E-value: 9.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490294727 719 VWIN-----PLDAEKRGIKNGDMVRVFNQRGEVRLPAKVTPRIMPGVS--AMGQGAWHdANMTGDRIDHGA 782
Cdd:cd02784 35 VWDNaalvsPRTAEALGLLQGDVVRIRRGGRTIELPVWIQPGHAEGVVllALGYGRTH-AGKVGNGVGHNA 104
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| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
114-235 |
1.56e-03 |
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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: 41.48 E-value: 1.56e-03
10 20 30 40 50 60 70 80
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gi 490294727 114 RLNYPMKRvgkrGEGKFVRISWQEALDTLADRLKSVVaqyGNEAVyinyssGIVGGnitrSSPSASPVA--RLMNCYGGs 191
Cdd:cd02773 53 RLDKPYIR----KNGKLKPATWEEALAAIAKALKGVK---PDEIA------AIAGD----LADVESMVAlkDLLNKLGS- 114
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90 100 110 120
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gi 490294727 192 lnqyGTYSTAQIACAMPYTYGSN-DGNST-SDIENSKLVVMFGNNP 235
Cdd:cd02773 115 ----ENLACEQDGPDLPADLRSNyLFNTTiAGIEEADAVLLVGTNP 156
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