|
Name |
Accession |
Description |
Interval |
E-value |
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
14-807 |
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: 1361.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 14 ISRRSLMKTS-ALGSLALASSAFTLPFSQMVRAAEVPV--EEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDV 90
Cdd:TIGR02166 1 ISRRHFLKTSaALGGLAAASGALSLPFSVNAAAEATPTgpDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 91 YGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGN 170
Cdd:TIGR02166 81 YGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 171 ITNSNVPY---RLMNSCGGFLSRYGSYSTAQISAAMSYMFGAN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVE 246
Cdd:TIGR02166 161 MSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYYFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 247 QARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTLPANAPRNAHY 326
Cdd:TIGR02166 241 QALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 327 KAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN 406
Cdd:TIGR02166 321 KDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 SGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:TIGR02166 401 NGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:TIGR02166 481 KILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 567 GpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSE 646
Cdd:TIGR02166 561 G--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 647 RLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARG 726
Cdd:TIGR02166 639 RLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQKRG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 727 IRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:TIGR02166 719 ITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVEK 796
|
.
gi 1434010499 807 V 807
Cdd:TIGR02166 797 A 797
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-807 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1306.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 1 MKIHTTEALMKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAEV----PVEEKAVWSSCTVNCGSRCLLRLHVKDD 76
Cdd:PRK14990 1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSaiptKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 77 TVYWVESDTTGDDVY-GNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGN 155
Cdd:PRK14990 81 EIKYVETDNTGDDNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 156 EAVHVLYGTGVDGGNITNSNVP-----YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGA-NDGNSPDDIANTKLVVMFGN 229
Cdd:PRK14990 161 ESIYLNYGTGTLGGTMTRSWPPgntlvARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 230 NPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCV 309
Cdd:PRK14990 241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 310 GYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRA 389
Cdd:PRK14990 321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 390 IAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWC 469
Cdd:PRK14990 401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 470 YASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAK 549
Cdd:PRK14990 481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 550 FERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDP 629
Cdd:PRK14990 561 FECKTIYEMTSELAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDP 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 630 QANPLKTPSGKIEIYSERLATIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQ 709
Cdd:PRK14990 639 QANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 710 ACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPS 789
Cdd:PRK14990 719 ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPS 796
|
810
....*....|....*...
gi 1434010499 790 PLAKGNPSHSNLVQIEKV 807
Cdd:PRK14990 797 PLAKGNPSHTNLVQVEKV 814
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
56-675 |
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: 947.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 56 WSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISW 135
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-GNS 214
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAAsGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 PDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQAReRSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLI 294
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 295 TENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQG 374
Cdd:cd02770 240 TENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 375 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGV 454
Cdd:cd02770 320 WGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 455 RGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVL-QDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESA 533
Cdd:cd02770 400 KGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRALlDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 534 GNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKK 613
Cdd:cd02770 480 GMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVP 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434010499 614 cPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLATIADTweLKKDEIIHPLPAYTPGFDG 675
Cdd:cd02770 558 -RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEG 616
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
56-675 |
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: 700.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 56 WSSCTvncgsRCLLRLHVKDDTVYWVESDTTgddvygnHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK----------R 125
Cdd:cd02751 1 PTACH-----WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 126 GEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPY-RLMNSCGGFLSRYGSYSTAQISAAMS 204
Cdd:cd02751 69 GEGEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLhRFLNLIGGYLGSYGTYSTGAAQVILP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 205 YMFGA----NDGNSPDDIA-NTKLVVMFGNNPAETRMSGGGV-----TYYVEQARERsNARMIVIDPRYNDTAAGREDEW 274
Cdd:cd02751 149 HVVGSdevyEQGTSWDDIAeHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKDA-GVRFICIDPRYTDTAAVLAAEW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 275 LPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgPDGIAKTPEWAAKITSIPAE 354
Cdd:cd02751 228 IPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLGE-SDGVPKTPEWAAEITGVPAE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 355 KIIHLAREIGSaKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEW--------FPMLEN 426
Cdd:cd02751 295 TIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPrggaggpgLPQGKN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 427 PVKTQISVFTWTDAIDH-GTEMTAtrdgvRGKEKLDVPIKFLWCYASNTLINQHgDINHTHEVLQDDskcEMIVGIDHFM 505
Cdd:cd02751 374 PVKDSIPVARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFW 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 506 TASAKYCDILLPDLMPTEQEDLIShESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIK 585
Cdd:cd02751 445 TASARYADIVLPATTSLERNDIGL-TGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 586 YLHAKTKERN----PEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLATIADTwelkkDe 661
Cdd:cd02751 522 HLYEETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYD-----D- 595
|
650
....*....|....
gi 1434010499 662 iIHPLPAYTPGFDG 675
Cdd:cd02751 596 -CPGHPTWIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
45-807 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 682.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 45 AAEVPVEEKAVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK 124
Cdd:COG0243 14 AALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 125 RGEGKFERISWDEALDTISDNLRRILKDYGNEAVhVLYGTGVDGGNITNSNVPY--RLMNSCG--GFLSRyGSYSTAQIS 200
Cdd:COG0243 89 RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAV-AFYTSGGSAGRLSNEAAYLaqRFARALGtnNLDDN-SRLCHESAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 201 AAMSYMFGANDG-NSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRP 279
Cdd:COG0243 167 AGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEWLPIRP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 280 GTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYIlgegpdgIAKTPEWAAKITSIPAEKIIHL 359
Cdd:COG0243 243 GTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAEDIREL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 360 AREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktqisvftwtD 439
Cdd:COG0243 304 AREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------------------E 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 440 AIdhgtemtatrdgvrgKEKLDVPIKFLWCYASNtLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPDL 519
Cdd:COG0243 358 AI---------------LDGKPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 520 MPTEQEDLIsheSAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHAKTKERNpemP 599
Cdd:COG0243 419 TWLERDDIV---TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFE--EAFPWGRTEEDYLRELLEATRGRG---I 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 600 DYEEMKTTGIFKKKCPEEHyvafrAFREDpqaNPLKTPSGKIEIYSERLAtiadtwelkkdeiIHPLPAYTPGFDgWDDP 679
Cdd:COG0243 491 TFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE-GAEP 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 680 LRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTA 758
Cdd:COG0243 549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1434010499 759 IGQGAWlkadmFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 807
Cdd:COG0243 629 APHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
102-649 |
1.73e-119 |
|
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: 373.52 E-value: 1.73e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 102 GRSIRRRMNHPDRLKYPMKRVG-----------KRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHV-LYGTGvDGG 169
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIFGgSYGWS-SAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 170 NITNSNVP-YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-----GNSPDDIA-NTKLVVMFGNNPAETRMSGGGVT 242
Cdd:cd02769 113 RFHHAQSLlHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEvyteqQTSWPVIAeHTELVVAFGADPLKNAQIAWGGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 243 ------YYVEQARERsNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktl 316
Cdd:cd02769 193 pdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDK--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 317 panaprnahYKAYILGEGpDGIAKTPEWAAKITSIPAEKIIHLAREIgSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVL 396
Cdd:cd02769 269 ---------FLPYLLGES-DGVPKTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 397 TGNVGINGG--------NSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDH-GTEMtaTRDGvrgkEKLDVP-IKF 466
Cdd:cd02769 338 LGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNpGKPF--DYNG----KKLTYPdIKL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 467 LWcYASNTLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPAT 546
Cdd:cd02769 412 VY-WAGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIVAMKQVV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 547 SAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLH----AKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAF 622
Cdd:cd02769 485 EPVGEARDDYDIFADLAERLG--VEEQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPEADFVRL 562
|
570 580
....*....|....*....|....*..
gi 1434010499 623 RAFREDPQANPLKTPSGKIEIYSERLA 649
Cdd:cd02769 563 ADFREDPEANPLGTPSGRIEIFSETIA 589
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
57-649 |
1.05e-109 |
|
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: 344.62 E-value: 1.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 57 SSCTVNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGeGKFERISWD 136
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVE----GDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 137 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgnITNSNVPYRLMNScGGFLSRYGSYSTAQISAAMSYMFGANDGNSPD 216
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMG--LLQRAARGRFFHA-LGASELRGTICSGAGIEAQKYDFGASLGNDPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 217 DIANTKLVVMFGNNPAETRMSGggvTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLITE 296
Cdd:cd02766 154 DMVNADLIVIWGINPAATNIHL---MRIIQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALGVAKVLFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 297 NMVDQPFLDKYCVGYDEktlpanaprnahYKAYILgegpdgiAKTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWG 376
Cdd:cd02766 229 GLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 377 PQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVREGSwdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrg 456
Cdd:cd02766 290 MQRYRNGGQNVRAIDALPALTGNIGVPGG--GAFYSN------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 457 kekLDVPIKFLWCYASNtLINQHGDINHTHEVLQDDskCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIshesaGNM 536
Cdd:cd02766 325 ---SGPPVKALWVYNSN-PVAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY-----ASY 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 537 G--YVILAQPATSAKFERKPIYWMLSEVAKRLGpdvyqtFTEG---RSQHEWIKylhaktKERNPEMPdyeemKTTGIfk 611
Cdd:cd02766 394 WhyYLQYNEPAIPPPGEARSNTEIFRELAKRLG------FGEPpfeESDEEWLD------QALDGTGL-----PLEGI-- 454
|
570 580 590
....*....|....*....|....*....|....*....
gi 1434010499 612 kKCPEEHYVAFRAFREDPQANP-LKTPSGKIEIYSERLA 649
Cdd:cd02766 455 -DLERLLGPRKAGFPLVAWEDRgFPTPSGKFEFYSERAA 492
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
56-566 |
1.43e-103 |
|
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: 323.90 E-value: 1.43e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 56 WSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGegKFERISW 135
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIE----GDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGniTNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNSP 215
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNE--EAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 216 DDIANTKLVVMFGNNPAETRMSgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAiawvlit 295
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 296 enmvdqpfldkycvgydektlpanaprnahykayilgegpdgiaktpEWAAKITSIPAEKIIHLAREIGSAKPAYICQGW 375
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 376 GPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVRegswdlgvewfpmlENPVKTQisvftwtdaidhgtemtatrdgvr 455
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA------------------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 456 gkekldvpikflwcyasntlinqhgdiNHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHesagN 535
Cdd:cd00368 295 ---------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN----T 343
|
490 500 510
....*....|....*....|....*....|.
gi 1434010499 536 MGYVILAQPATSAKFERKPIYWMLSEVAKRL 566
Cdd:cd00368 344 EGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
14-806 |
1.83e-103 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 337.80 E-value: 1.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 14 ISRRSLMK-TSALGSLALASSAFTLPFSQMVRAAEVPvEEKAVWSSCTVNCGSrclLRLHVKDDTvyWVESDTTGDDVYG 92
Cdd:PRK15102 1 ASRRRFLKgLGGLSAAGMLGPSLLTPRSALAAQAAAA-ETTKEWILTGSHWGA---FRAKVKNGR--FVEAKPFELDKYP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 93 NHQVRAclrgrsIRRRMNHPDRLKYPMKRV-----------GKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHvl 161
Cdd:PRK15102 75 TKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALH-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 162 ygTGVDGGNITNSnvpyrlMNSCGG-----------FLSRYGSYSTAQISAAMSYMFGAND----GNS-PDDIANTKLVV 225
Cdd:PRK15102 147 --TGQTGWQSTGQ------FHSATGhmqraigmhgnSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSwPLILENSKTIV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 226 MFGNNP---------AETRMSGGgvtyYVEQARER---SNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVL 293
Cdd:PRK15102 219 LWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYCVGYDEkTLPanaprnahykaYILGEgPDGIAKTPEWAAKITSIPAEKIIHLAREIgSAKPAYICQ 373
Cdd:PRK15102 295 YSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 374 GWGPQRHSNGEQTSRAIAMLSVLTGNVGINGG--------NS-GVRE----------GSWDLGVEwfPMLENP----VKT 430
Cdd:PRK15102 361 GWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhySGiGVPSsggaipggfpGNLDTGQK--PKHDNSdykgYSS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 431 QISVFTWTDAIDH-GTEMTATrdgvrGKEKLDVPIKFLwCYASNTLINQHGDINHTHEVLQddsKCEMIVGIDHFMTASA 509
Cdd:PRK15102 439 TIPVARFIDAILEpGKTINWN-----GKKVTLPPLKMM-IFSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATC 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 510 KYCDILLPDLMPTEQEDLISHESAGNMGyVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHA 589
Cdd:PRK15102 510 RFADIVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGRE--KEYTRGMDEMGWLKRLYQ 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 590 KTKERNP---EMPDYEEMKTTGI--FKKKCPeehYVAFRAFREDPQANPLKTPSGKIEIYSErlaTIAD----------T 654
Cdd:PRK15102 587 ECKQQNKgkfHMPEFDEFWKKGYveFGEGQP---WVRHADFREDPELNPLGTPSGLIEIYSR---KIADmgyddcqghpM 660
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 655 WeLKKDEIIHPlpayTPGFDgwddplrkTYPLQLTGFHYKARTHSsygnidvlqQACPQE-------------VWINPID 721
Cdd:PRK15102 661 W-FEKIERSHG----GPGSD--------KYPLWLQSVHPDKRLHS---------QLCESEelretytvqgrepVYINPQD 718
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 722 AQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGD--RVDHGGSINILTSHRP-SPLAKGNPSH 798
Cdd:PRK15102 719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEigALCTYGDPNTLTLDIGtSQLAQATSAH 798
|
....*...
gi 1434010499 799 SNLVQIEK 806
Cdd:PRK15102 799 TCLVEIEK 806
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
58-671 |
1.36e-99 |
|
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: 317.33 E-value: 1.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 58 SCTVnCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDE 137
Cdd:cd02759 3 TCPG-CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG----RLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 138 ALDTISDNLRRILKDYGNEAVHVLYGTGvDGGNITNS---NVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNS 214
Cdd:cd02759 78 ALDEIAEKLAEIKAEYGPESIATAVGTG-RGTMWQDSlfwIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 pdDIANTKLVVMFGNNPAETrmSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLI 294
Cdd:cd02759 157 --DWENPECIVLWGKNPLNS--NLDLQGHWLVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 295 TENMVDQPFLDKYCVGYDEKtlpanAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQG 374
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEEL-----AERVQEY--------------TPEKVAEITGVPAEKIRKAARLYATAKPACIQWG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 375 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSgvregswdlgveWFPMlenpvktqisvftwtdaidhgtemtatrdgv 454
Cdd:cd02759 292 LAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL------------LIPY------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 455 rgkekldvPIKFLWCYASNTLINQHGDINhtheVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAG 534
Cdd:cd02759 329 --------PVKMLIVFGTNPLASYADTAP----VLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAE 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 535 NMGYVI--LAQPAtsakFERKPIYWMLSEVAKRLGPDvyqtftegrsQHEWIKYlhaKTKERnpempdyeemkttgifkk 612
Cdd:cd02759 397 NFVQLRqkAVEPY----GEAKSDYEIVLELGKRLGPE----------EAEYYKY---EKGLL------------------ 441
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 613 kcpeehyvafrafREDPQAnPLKTPSGKIEIYSERLatiadtWELKKDeiihPLPAYTP 671
Cdd:cd02759 442 -------------RPDGQP-GFNTPTGKVELYSTML------EELGYD----PLPYYRE 476
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
63-793 |
4.08e-93 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 306.43 E-value: 4.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 63 CGSRCLLRLHVKDDTVYWVESDTtgddvygNHQV---RACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEAL 139
Cdd:COG3383 14 CGVGCGIDLEVKDGKIVKVEGDP-------DHPVnrgRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 140 DTISDNLRRILKDYGNEAVHVLYgtgvdGGNITNSNvpYRLMNS-CGGFL--------SRYGSYSTAqisAAMSYMFGAn 210
Cdd:COG3383 83 DLVAERLREIQAEHGPDAVAFYG-----SGQLTNEE--NYLLQKlARGVLgtnnidnnARLCMASAV---AGLKQSFGS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 211 DG--NSPDDIANTKLVVMFGNNPAETrmsgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 288
Cdd:COG3383 152 DAppNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVLITENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKP 368
Cdd:COG3383 227 LLHVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREAARLIAEAKR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 369 AYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGgnSGV---RE-----GSWDLGV--EWFP---MLENP-VKTQISV 434
Cdd:COG3383 288 AMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPG--TGPfplTGqnnvqGGRDMGAlpNVLPgyrDVTDPeHRAKVAD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 435 FTWTDAIDHGTEMTATR--DGVRGKEkldvpIKFLWCYASNTLInQHGDINHTHEVLqddSKCEMIVGIDHFMTASAKYC 512
Cdd:COG3383 366 AWGVPPLPDKPGLTAVEmfDAIADGE-----IKALWIIGENPAV-SDPDANHVREAL---EKLEFLVVQDIFLTETAEYA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 513 DILLPDLMPTEQED-LISHEsagnmGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV-YQT----FTEGRSqhewiky 586
Cdd:COG3383 437 DVVLPAASWAEKDGtFTNTE-----RRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFdYDSpeevFDEIAR------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 587 lhaktkernpEMPD-----YEEMKTTGIFKKKCP-EEHYVAFRAFREDpqanpLKTPSGKIeiyserlatiadtwelkkd 660
Cdd:COG3383 505 ----------LTPDysgisYERLEALGGVQWPCPsEDHPGTPRLFTGR-----FPTPDGKA------------------- 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 661 eIIHPLPAYTPgfdgwDDPLRKTYPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRV 735
Cdd:COG3383 551 -RFVPVEYRPP-----AELPDEEYPLVLtTGrllDQWHTGTRT--RRSPRLNKHAPEPfVEIHPEDAARLGIKDGDLVRV 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 736 FNNNGEMLIAAKVTPRILPGVTAIgqgawlkADMFGDrvdhgGSINILTSHRPSPLAK 793
Cdd:COG3383 623 SSRRGEVVLRARVTDRVRPGTVFM-------PFHWGE-----GAANALTNDALDPVSK 668
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
57-649 |
7.53e-87 |
|
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: 286.30 E-value: 7.53e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 57 SSCTVNCGSRCLLRLHVKDDTVYWVESDttgdDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWD 136
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN----EWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 137 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgniTNSNVPYRLMNScGGFLSRYGSYSTAQ---ISAAMSYMFGANdGN 213
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGA---ILSYLRLALLGG-GLQDALTYGIDTGVgqgFNRVTGGGFMPP-TN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 214 SPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVL 293
Cdd:cd02765 153 EITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYC-----VGYDEKTL--PANAPRNAHYKAYIL---------------------GEGP---------- 335
Cdd:cd02765 228 LEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVwdtnsdspepvaatninpaleGEYTingvkvhtvl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 336 ----DGIAK-TPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVr 410
Cdd:cd02765 308 talrEQAASyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 411 egswdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrgkekldvpIKFLWCYASNtLINQHGDINHTHEVLq 490
Cdd:cd02765 387 -----------------------------------------------------IKFMYFMGSN-FLGNQPDRDRWLKVM- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 491 ddSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNmgYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV 570
Cdd:cd02765 412 --KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLGD 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 571 YQTFTEgrsqHEWIKyLHAKTKERNPEMPDYEEMKTTGIFKKK-CPEEHYVAF--RAFredpqanplKTPSGKIEIYSER 647
Cdd:cd02765 488 YFPKTP----EDYVR-AFMNSDDPALDGITWEALKEEGIIMRLaTPEDPYVAYldQKF---------GTPSGKLEFYNEA 553
|
..
gi 1434010499 648 LA 649
Cdd:cd02765 554 AP 555
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
55-575 |
1.52e-81 |
|
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: 268.78 E-value: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 55 VWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERIS 134
Cdd:cd02755 1 VPSICEM-CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 135 WDEALDTISDNLRRILKDYGNEAVhvLYGTGVDGG--------------NITNSnvpyrlMNSCggFLSRygsystaqiS 200
Cdd:cd02755 76 WDEALQYIASKLKEIKEQHGPESV--LFGGHGGCYspffkhfaaafgspNIFSH------ESTC--LASK---------N 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 201 AAMSYMFGANDGNSPDDIANTKLVVMFGNNPAEtrmsGGGVTYYVEQARERSN-ARMIVIDPRYNDTAAgREDEWLPIRP 279
Cdd:cd02755 137 LAWKLVIDSFGGEVNPDFENARYIILFGRNLAE----AIIVVDARRLMKALENgAKVVVVDPRFSELAS-KADEWIPIKP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 280 GTDGALACAIAWVLITENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIHL 359
Cdd:cd02755 212 GTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLK--------AHVKPY-----------TPEWAAQITDIPADTIRRI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 360 AREIG-SAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsgvregswdlgveWFPmlenpvktqisvftwt 438
Cdd:cd02755 273 AREFAaAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG--------------LYY---------------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 439 daidhgtemtatrdgvrGKEKLDVPIKFLWCYASNTLINQHgDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDILLPD 518
Cdd:cd02755 323 -----------------AGSAKPYPIKALFIYRTNPFHSMP-DRARLIKALK---NLDLVVAIDILPSDTALYADVILPE 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1434010499 519 LMPTEQEDLISHESAGNMGYVIlAQPATSAKFERKPIYWMLSEVAKRLGPdvYQTFT 575
Cdd:cd02755 382 ATYLERDEPFSDKGGPAPAVAT-RQRAIEPLYDTRPGWDILKELARRLGL--FGTPS 435
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
13-807 |
1.25e-79 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 271.93 E-value: 1.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 13 EISRRSLMKTSALGSLALASSAFtLPFS-QMVRAAEVPVEEKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttgddvy 91
Cdd:PRK15488 2 SLSRRDFLKGAGAGCAACALGSL-LPGAlAANEIAQLKGKTKLTPSICEM-CSTRCPIEARVVNGKNVFIQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 92 GNHQV-----RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGV 166
Cdd:PRK15488 71 GNPKAksfgtKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 167 DGGNITNsnvpyrlmnscggFLSRYGS------YSTAQISAAM--SYMFGandGNSPDDIANTKLVVMFGNNPAE-TRMS 237
Cdd:PRK15488 151 LSSHLFH-------------LATAFGSpntfthASTCPAGYAIaaKVMFG---GKLKRDLANSKYIINFGHNLYEgINMS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 238 gggVTYYVEQARERSNARMIVIDPRYNdTAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKYCVGYDEktLP 317
Cdd:PRK15488 215 ---DTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE--LA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 318 ANAprnahyKAYilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQgWGPQRHSNGE--QTSRAIAMLSV 395
Cdd:PRK15488 289 ASV------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRATFTPEefDMRRAIFAANV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 396 LTGNVGINGGNSGVREGSWD---LGVEWFPMLENPVKTQISVFTWT--DAIDHGTEMTATRDGVRGK------EKLDVPI 464
Cdd:PRK15488 351 LLGNIERKGGLYFGKNASVYnklAGEKVAPTLAKPGVKGMPKPTAKriDLVGEQFKYIAAGGGVVQSiidatlTQKPYQI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 465 KFLWCYASNTLINQhgdiNHTHEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVIlAQP 544
Cdd:PRK15488 431 KGWVMSRHNPMQTV----TDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYAL-RQR 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 545 ATSAKFERKPIYWMLSEVAKRLGPDVYQTFtegrsqhEWIKYLHAKTKERNPEMpdYEEMKTTGIFKKKCP----EEHYV 620
Cdd:PRK15488 506 VVEPIGDTKPSWQIFKELGEKMGLGQYYPW-------QDMETLQLYQVNGDHAL--LKELKKKGYVSFGVPlllrEPKMV 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 621 AfrAFRED-PQANP------------LKTPSGKIEIYSERLATIAdtwelkkdeiihplPAY-TPGFDgwDDPLRKTYPL 686
Cdd:PRK15488 577 A--KFVARyPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALA--------------PGYgVPRYR--DVALKKEDEL 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 687 QLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWL 765
Cdd:PRK15488 639 YFIQGKVAVHTNGATQNVPLLANLMSDNaVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFGS 718
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1434010499 766 KADMFGDRVDHGGSINILTSHRPSPLAkGNPSHSNLVQIEKV 807
Cdd:PRK15488 719 KNKELTRATGKGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
53-583 |
3.18e-79 |
|
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: 262.64 E-value: 3.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 53 KAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDT----TGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEG 128
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATdypeTPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 129 KFERISWDEALDTISDNLRRILKDYGNEAV----------HVLYGTGvdggnitnsnvpYRLMNSCGG----FLSRYGSY 194
Cdd:cd02750 81 KWKRISWDEALELIADAIIDTIKKYGPDRVigfspipamsMVSYAAG------------SRFASLIGGvslsFYDWYGDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 195 STAQisaamSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDE 273
Cdd:cd02750 149 PPGS-----PQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 274 WLPIRPGTDGALACAIAWVLITENMVDQPFLDKYcvgydeKTLPanaprnahYKAYilgegpdgiakTPEWAAKITSIPA 353
Cdd:cd02750 219 WVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 354 EKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktQIS 433
Cdd:cd02750 274 ETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG------------------QPR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 434 VFtwtdaidhgtemtatrdgvrgkekldvpikFLWcyaSNTLINQHgdiNHTHEVLQD--DSKCEMIVGIDHFMTASAKY 511
Cdd:cd02750 336 VL------------------------------FVW---RGNLFGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTALY 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 512 CDILLPDLMPTEQEDLISheSAGNMgYVILAQPATSAKFERKPIYWMLSEVAKRLgpdVYQTFTeGRSQ----HEW 583
Cdd:cd02750 380 SDIVLPAATWYEKHDLST--TDMHP-FIHPFSPAVDPLWEAKSDWEIFKALAKKV---PWRTLT-GRQQfyldHDW 448
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-565 |
2.86e-68 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 229.98 E-value: 2.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 114 RLKYPMKRvgkRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGvdGGNITNSNVPY-----RLMNSCGGFL 188
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALkkllnRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 189 SRYGSYSTAQiSAAMSYMFGAN--DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYyveQARERSNARMIVIDPRYNdt 266
Cdd:pfam00384 76 DHNGDLCTAA-AAAFGSDLRSNylFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 267 aAGREDEWLPIRPGTDGALACAIAWVLITENMVDQPFLDKycvgydektlpanaprnahykayilgegpdgiaktpewaa 346
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 347 kitsipaekiihlareigsakpAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNsgvregswdlgveWFPMLEN 426
Cdd:pfam00384 189 ----------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-------------WNGLNIL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 427 PvktqisvftwTDAIDHGTEMTATRDGVRGKEKLDVP----IKFLWcYASNTLINQHGDINHTHEVLQddsKCEMIVGID 502
Cdd:pfam00384 234 Q----------GAASPVGALDLGLVPGIKSVEMINAIkkggIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434010499 503 HFM-TASAKYCDILLPDLMPTEQEDLIShesagNM-GYVILAQPATSAKFERKPIYWMLSEVAKR 565
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYV-----NTeGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
63-640 |
5.42e-67 |
|
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: 232.50 E-value: 5.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 63 CGSRCLLRLHVKDDTVYWVesdtTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRvgkRGEGKFERISWDEALDTI 142
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAV----RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKDYGNEAVHVlYGTGvdggNITNSNvpYRLMNSC--GGFLSRYGSYSTAQI--SAAMSYM--FGAnDG--NS 214
Cdd:cd02754 80 AERFKAIQAEYGPDSVAF-YGSG----QLLTEE--YYAANKLakGGLGTNNIDTNSRLCmaSAVAGYKrsFGA-DGppGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 215 PDDIANTKLVVMFGNNPAETR---MSgggvtyYVEQARE-RSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIA 290
Cdd:cd02754 152 YDDIEHADCFFLIGSNMAECHpilFR------RLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIRPGTDLALLNGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 291 WVLITENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPAY 370
Cdd:cd02754 225 HVLIEEGLIDRDFIDAHTEGFEELK--------AFVADY-----------TPEKVAEITGVPEADIREAARLFGEARKVM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 371 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVG--------ING-GNS-GVREGSWD---LGvewFPM-LENPVKTQISVFT 436
Cdd:cd02754 286 SLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREVGGLanlLP---GHRsVNNPEHRAEVAKF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 437 WtdAIDHGTEMTAT-RDGVRGKEKL-DVPIKFLWCYASN---TLINQhgdiNHTHEVLQddsKCEMIVGIDHF-MTASAK 510
Cdd:cd02754 363 W--GVPEGTIPPKPgLHAVEMFEAIeDGEIKALWVMCTNpavSLPNA----NRVREALE---RLEFVVVQDAFaDTETAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 511 YCDILLPDLMPTEQEdlishesaGNMG----YVILAQPATSAKFERKPIYWMLSEVAKRLGPDVYQTFTegrSQHEWIKY 586
Cdd:cd02754 434 YADLVLPAASWGEKE--------GTMTnserRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYT---SPEEVFEE 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 587 LHAKTKERNPEMP--DYEEMKTTGIfKKKCPEEHYVAFRAFREDPQANplkTPSGK 640
Cdd:cd02754 503 YRRLSRGRGADLSglSYERLRDGGV-QWPCPDGPPEGTRRLFEDGRFP---TPDGR 554
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
54-659 |
6.20e-67 |
|
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: 231.56 E-value: 6.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 54 AVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRG----EGK 129
Cdd:cd02757 1 WVPSTCQ-GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 130 FERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPyRLMNSCGGFlsrygSYSTAQISA---AMSYM 206
Cdd:cd02757 76 FVPISWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILYGRFT-KMIGSPNNI-----SHSSVCAESekfGRYYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 207 FGANDGNSPDdIANTKLVVMFGNNPAETrmsgggvTYYVEQARE-----RSNARMIVIDPRYNDTAAgREDEWLPIRPGT 281
Cdd:cd02757 150 EGGWDYNSYD-YANAKYILFFGADPLES-------NRQNPHAQRiwggkMDQAKVVVVDPRLSNTAA-KADEWLPIKPGE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 282 DGALACAIAWVLITENMVDQPFLDKYCVGYD----EKTLPANAPR-----------NAHYKAYilgegpdgiakTPEWAA 346
Cdd:cd02757 221 DGALALAIAHVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKeksteglvkwwNLELKDY-----------TPEWAA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 347 KITSIPAEKIIHLAREIGSAKPAYICQGW-GPQRHSNGEQTSRAIAMLSVLTGNVGINGG-NSGVREGSWDLGVEWFpml 424
Cdd:cd02757 290 KISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGGlCPNMGVPKIKVYFTYL--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 425 ENPVKTQISVFTWTDAIDhgtemtatrdgvrgkeklDVPIkflwcyasntlinqhgdinHTHevlqddskcemivgIDHF 504
Cdd:cd02757 367 DNPVFSNPDGMSWEEALA------------------KIPF-------------------HVH--------------LSPF 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 505 MTASAKYCDILLPDLMPTEQEDLISHESAGNmGYVILAQPATSAKFERK---PIYWMLsevAKRLGPDvyqtftegrsqh 581
Cdd:cd02757 396 MSETTYFADIVLPDGHHFERWDVMSQENNLH-PWLSIRQPVVKSLGEVReetEILIEL---AKKLDPK------------ 459
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 582 ewikylhaktkernpempDYEEMKTTGIFKKKCPEEHYVAFRAFredpqANPLKTPSGKIEIYSERLATIADTWELKK 659
Cdd:cd02757 460 ------------------GSDGMKRYAPGQFKDPETGKNNRWEF-----ENVFPTETGKFEFYSETLKKYLQNHADKK 514
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
63-567 |
5.41e-65 |
|
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: 225.56 E-value: 5.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 63 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVgkrgEGKFERISWDEALDTI 142
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKDYGNEAVHVLygTGVDGGN-------------ITNSNVpyrlmNSCggflSRYGSYSTAqisAAMSYMFGA 209
Cdd:cd02753 79 ASRLKEIKDKYGPDAIAFF--GSAKCTNeenylfqklaravGGTNNV-----DHC----ARLCHSPTV---AGLAETLGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 210 N-DGNSPDDIANTKLVVMFGNNPAETRMSGGgvtYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 288
Cdd:cd02753 145 GaMTNSIADIEEADVILVIGSNTTEAHPVIA---RRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALLNA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVLITENMVDQPFLDKYCVGYDE--KTLPANaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSA 366
Cdd:cd02753 220 MAHVIIEEGLYDEEFIEERTEGFEElkEIVEKY---------------------TPEYAERITGVPAEDIREAARMYATA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 367 KPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVregswdlgvewfpmleNPVKTQISVftwTDAIDHGTe 446
Cdd:cd02753 279 KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT--GV----------------NPLRGQNNV---QGACDMGA- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 447 mtatrdgvrgkekldVP------IKFLWCYASNTLINqHGDINHTHEVLqddSKCEMIVGIDHFMTASAKYCDILLP--- 517
Cdd:cd02753 337 ---------------LPnvlpgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPaas 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1434010499 518 ------DLMPTEQEdlishesagnmgyVILAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02753 398 faekdgTFTNTERR-------------VQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
684-806 |
3.01e-63 |
|
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: 207.53 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 763
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1434010499 764 WLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02794 81 WYEPD--ANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
684-806 |
6.97e-53 |
|
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: 179.70 E-value: 6.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACP----QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI 759
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKvkgrEPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1434010499 760 GQGAWLKADmFGDRVDHGGSINILTSHRPSP-LAKGNPSHSNLVQIEK 806
Cdd:cd02777 81 PEGAWYDPD-DNGGLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
59-527 |
6.75e-47 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 175.66 E-value: 6.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 59 CTVNCGsrclLRLHVKDDTVYWVESDTtgDDVYGNHQVraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEA 138
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIRGDP--DDPLSKGYI--CPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 139 LDTISDNLRRILKDYGNEAVHVlYGTGVDG---GNITNSNVPYRLMNScggflSRYGSYSTAQI---SAAMSYMFGANDG 212
Cdd:cd02762 75 FDEIAERLRAIRARHGGDAVGV-YGGNPQAhthAGGAYSPALLKALGT-----SNYFSAATADQkpgHFWSGLMFGHPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 213 NSPDDIANTKLVVMFGNNPAETR---MSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAI 289
Cdd:cd02762 149 HPVPDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLFVRPGTDAWLLAAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 290 AWVLITENMVDQPFLDKYCVGYDEkTLPANAPRnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIGSAKPA 369
Cdd:cd02762 227 LAVLLAEGLTDRRFLAEHCDGLDE-VRAALAEF------------------TPEAYAPRCGVPAETIRRLAREFAAAPSA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 370 YICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN---------------SGVREGSWDLGVEWFPmlenPVKTQISV 434
Cdd:cd02762 288 AVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAmfttpaldlvgqtsgRTIGRGEWRSRVSGLP----EIAGELPV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 435 FTWTDAIDhgtemtatRDGvrgkeklDVPIKFLWCYASNTLINQhGDINHTHEVLQddsKCEMIVGIDHFMTASAKYCDI 514
Cdd:cd02762 364 NVLAEEIL--------TDG-------PGRIRAMIVVAGNPVLSA-PDGARLEAALG---GLEFMVSVDVYMTETTRHADY 424
|
490
....*....|...
gi 1434010499 515 LLPDLMPTEQEDL 527
Cdd:cd02762 425 ILPPASQLEKPHA 437
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-567 |
1.12e-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: 162.69 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 63 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI 142
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 143 SDNLRRILKdygNEAVHVLYGTGVDGgnitnsnvpyrlMNSCGGFLSR---------YGSYSTAQISAAMSYMFGAN--D 211
Cdd:cd02763 83 TKRLKAARA---TDPKKFAFFTGRDQ------------MQALTGWFAGqfgtpnyaaHGGFCSVNMAAGGLYSIGGSfwE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 212 GNSPdDIANTKLVVMFG------NNPAETRMsgggvtyyveQARERSNARMIVIDP---RYNDTAagreDEWLPIRPGTD 282
Cdd:cd02763 148 FGGP-DLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPvrtGYAAIA----DEWVPIKPGTD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 283 GALACAIAWVLITENMVDQPFLDKYcvgydektlpANAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIHLARE 362
Cdd:cd02763 213 GAFILALAHELLKAGLIDWEFLKRY----------TNAAELVDY--------------TPEWVEKITGIPADTIRRIAKE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 363 IGSAK-------PAYICQGWGPQR------------------HSNGEQTSRAIAMLSVLTGNVGINGGN----------- 406
Cdd:cd02763 269 LGVTArdqpielPIAWTDVWGRKHekitgrpvsfhamrgiaaHSNGFQTIRALFVLMMLLGTIDRPGGFrhkppyprhip 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 407 ---------SGVREGS--------WDLGVEWFPMLENPVKTQIS-VFTWTDAID-HGTEMTATRDGVRGKEkldVPIKFL 467
Cdd:cd02763 349 plpkppkipSADKPFTplygpplgWPASPDDLLVDEDGNPLRIDkAYSWEYPLAaHGCMQNVITNAWRGDP---YPIDTL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 468 WCYASNTLINQHGDINHTHEVLQD-----DSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIS------HESAGNM 536
Cdd:cd02763 426 MIYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSlldrpiSEADGPV 505
|
570 580 590
....*....|....*....|....*....|.
gi 1434010499 537 GYVilAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02763 506 DAI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
97-651 |
1.49e-38 |
|
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: 153.65 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 97 RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLR-------------RILK--------DYGN 155
Cdd:cd02758 66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDlfgeghveglkaiRDLDtpidpdhpDLGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 156 EAVHVLYGTGVDGGNITNSNvpyRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNsPD---DIANTKLVVMFGNN 230
Cdd:cd02758 146 KANQLLYTFGRDEGRTPFIK---RFANQAFGTVnfGGHGSYCGLSYRAGNGALMNDLDGY-PHvkpDFDNAEFALFIGTS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 231 PAE-----TRMSGggvtyYVEQARERSNARMIVIDPRY--NDTAAGREDEWLPIRPGTDGALACA-IAWvlITENMvdqp 302
Cdd:cd02758 222 PAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAmIRW--IIENE---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 303 fldkycvGYDEKTLpANAPRNAHYKA---------------------YILGEgpDGIAKTPEWAAKITSIPAEKIIHLAR 361
Cdd:cd02758 291 -------RYNAEYL-SIPSKEAAKAAgepswtnathlvitvrvksalQLLKE--EAFSYSLEEYAEICGVPEAKIIELAK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 362 EIGSA--KPAYICQgwGPQRHSNGEQTSRAIAMLSVLTGNV----GINGGNSGVREGSWDLGVEW--FPMLENP------ 427
Cdd:cd02758 361 EFTSHgrAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLnwkgGLLMSGGGFADNSAGPRYDFkkFFGEVKPwgvpid 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 428 ---------------VKTQISVF----TWTD-AIDHGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTH 486
Cdd:cd02758 439 rskkayektseykrkVAAGENPYpakrPWYPlTPELYTEViASAAEG------YPYKLKALILWMANPVYGAPGLVKQVE 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 487 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEqedliSHESAGNMGYVI-LAQ--------PATSAKFERKPIYW 557
Cdd:cd02758 513 EKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYE-----SWGFSTPWGGVPtKAStarwpviaPLTEKTANGHPVSM 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 558 --MLSEVAKRLG---------PDVYqtfteGRS---QHEWIKYLH-----AKTKERNPEMPDYEEMKTTG-------IFK 611
Cdd:cd02758 588 esFLIDLAKALGlpgfgpnaiKDGQ-----GNKfplNRAEDYYLRvaaniAYDGKAPVPDASEEELKLTGvnrpipaLKR 662
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 612 KKCPEE-HYVAF------------RAFREDPQANPLKTPsgkIEIYSERLATI 651
Cdd:cd02758 663 TLKPEEwRKVAYilarggrfapyeESYDGDNLRNRWGKT---LQIWNEKLAKS 712
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
59-420 |
5.82e-38 |
|
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: 151.01 E-value: 5.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 59 CTVNCGsrclLRLHVKDDTVYWVESDTTGDDVYGNHqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrGEGKFERISWDEA 138
Cdd:cd02752 7 CSVGCG----LIAYVQNGVWVHQEGDPDHPVNRGSL----CPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 139 LDTISDNLRRILKD---YGNEAVHVLYGTgvDG----GNITNSNVPYRLMNSCGGFLSRYGSYSTAQI-------SAAMS 204
Cdd:cd02752 77 LDEIARKMKDIRDAsfvEKNAAGVVVNRP--DSiaflGSAKLSNEECYLIRKFARALGTNNLDHQARIuhsptvaGLANT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 205 YMFGANDgNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGA 284
Cdd:cd02752 155 FGRGAMT-NSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRTAA-KADLYVPIRSGTDIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 285 LACAIAWVLItenmvdqpfldKYcvgydektlpanaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIHLAREIG 364
Cdd:cd02752 230 FLGGMINYII-----------RY---------------------------------TPEEVEDICGVPKEDFLKVAEMFA 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 365 S----AKPAYI--CQGWgpQRHSNGEQTSRAIAMLSVLTGNVGING-------GNSGVrEGSWDLGVEW 420
Cdd:cd02752 266 AtgrpDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGggvnalrGHSNV-QGATDLGLLS 331
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
98-762 |
1.43e-30 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 129.73 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 98 ACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIS-----------DNLRRI--LK--------DYGNE 156
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVeggdlfgeghvDGLRAIrdLDtpidaknpEYGPK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 157 AVHVLYGTGVDGGNitnSNVPYRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNS---PDdIANTKLVVMFGNNP 231
Cdd:PRK14991 221 ANQLLVTNASDEGR---DAFIKRFAFNSFGTRnfGNHGSYCGLAYRAGSGALMGDLDKNPhvkPD-WDNVEFALFIGTSP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 232 AEtrmSGGGvtyYVEQARERSNARM------IVIDPR---YNDTAAGREDEWLPIRPGTDGALACA-IAWvlITEN---- 297
Cdd:PRK14991 297 AQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAMGmIRW--IIDNqryn 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 298 --------------------------MVDQP-------FL------------------DKYCV-GYDEKTLPANAPRNAH 325
Cdd:PRK14991 369 adylaqpgvaamqaageaswtnathlVIADPghprygqFLrasdlglpfegeargdgeDTLVVdAADGELVPATQAQPAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 326 --YKAYILGEGPDGIA--------------KTPEWAAKITSIPAEKIIHLAREIGS--AKPAYICQGwGpQRHSNGEQTS 387
Cdd:PRK14991 449 lfVEQYVTLADGQRVRvksslqllkeaarkLSLAEYSEQCGVPEAQIIALAEEFTShgRKAAVISHG-G-TMSGNGFYNA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 388 RAIAMLSVLTGNVGINGG---NSG-------------------VREGSWDLGVEWFPML------------ENPVKTQIS 433
Cdd:PRK14991 527 WAIMMLNALIGNLNLKGGvvvGGGkfpgfgdgprynlasfagkVKPKGVSLSRSKFPYEksseyrrkveagQSPYPAKAP 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 434 VFTWTDAIdhGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKCEMIVGIDHFMTASAKYC 512
Cdd:PRK14991 607 WYPFVAGL--LTEMlTAALEG------YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISIDAFINETTALA 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 513 DILLPDLMPTEQ-------EDLISHESAGNMGYVilaQPATSAKFERKPIYW--MLSEVAKRL-----GPDVYQTfTEGR 578
Cdd:PRK14991 679 DYIVPDTHTYESwgftapwGGVPTKASTARWPVV---EPRTAKTADGQPVCMesFLIAVAKRLqlpgfGDNAIKD-AQGN 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 579 -----SQHEWikYLHAKT------KERNPEMPDyEEMKTTG-------IFKKKCPEE-HYVAF------------RAFRE 627
Cdd:PRK14991 755 thplnRAEDF--YLRGAAniaylgKTPVADASD-EDIALTGvsrilpaLQATLKPDEvRRVAFiyarggrfapaeSAYDE 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 628 DPQANPLKTPsgkIEIYSERLATIADTwelKKDEIIHPLPA-YTPGF-DGwdDPLRKTY-----PLQLTGFhyKARTHSS 700
Cdd:PRK14991 832 ERMGNRWKKP---LQIWNEDVAAARHS---MTGERYSGCPTwYPPRLaDG--TPLREQFpesqwPLLLISF--KSNLMSS 901
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499 701 YGN-IDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:PRK14991 902 MSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
684-806 |
2.75e-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: 115.81 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ---EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIG 760
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQgrePIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1434010499 761 QGAWLkaDMFGDRVDHG----GSINILTSHRP-SPLAKGNPSHSNLVQIEK 806
Cdd:cd02793 81 TGAWY--DPDDPGEPGPlckhGNPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
686-801 |
3.32e-29 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 111.98 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 686 LQLTGFHYKARTHSSYGNIDVLQQACPQE--VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 763
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1434010499 764 WlkadmfgdRVDHGGSINILTSHRPSPLAKGNPSHSNL 801
Cdd:pfam01568 81 W--------YEPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
57-567 |
1.81e-27 |
|
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: 119.30 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 57 SSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNhQVRACLRGRSIRRRMNHPDRLKYPMKRVG-KRGEGK---FER 132
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 133 ISWDEALDTISDNLRRIL-KDYGNEAVHVLYGTGVDGGNItnsnvPYRLMNSCGGFLSRYG----SYSTAQI--SAAMSY 205
Cdd:cd02760 81 ISWDEALDLVAAKLRRVReKGLLDEKGLPRLAATFGHGGT-----PAMYMGTFPAFLAAWGpidfSFGSGQGvkCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 206 MFGANDGNSPDDIANTKL---VVMFGNNpaeTRMSGG--GVTYYVEqARERSnARMIVIDPRYNDTAAgREDEWLPIRPG 280
Cdd:cd02760 156 LYGEFWHRAFTVAADTPLanyVISFGSN---VEASGGpcAVTRHAD-ARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 281 TDGALACAIAWVLITE---NMVDQPFL-DK----YCVG----------------YDEKT-----------LPANAPRNAH 325
Cdd:cd02760 230 TDPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGpdglylrdaatgkplvWDERSgravpfdtrgaVPAVAGDFAV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 326 YKAY-ILGEGP-----------------DGIAK-TPEWAAKITSIPAEKIIHLARE------IGSA----------KPAY 370
Cdd:cd02760 310 DGAVsVDADDEtaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 371 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSG---------------VREGSWDLGVEWF-----------PML 424
Cdd:cd02760 390 VTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGttvrlnrphddrlasVKPGEDGFMAQGFnptdkehwvvkPTG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 425 ENPVKTQISVF---TWTDAIDHGTEMTATRDGVRGKEKLDVPIK--FLWCYASNTLINqhgdINHTHEVLQDDSKCEMIV 499
Cdd:cd02760 470 RNAHRTLVPIVgnsAWSQALGPTQLAWMFLREVPLDWKFELPTLpdVWFNYRTNPAIS----FWDTATLVDNIAKFPFTV 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499 500 GIDHFMTASAKYCDILLPDLMPTEQEDLISH------ESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLG 567
Cdd:cd02760 546 SFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfvEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAKRTG 619
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-577 |
5.91e-26 |
|
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: 113.17 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 114 RLKYPMKRvgKRGEGKFERISWDEALDTISDNLRRILKD----Y-----GNEAVHVL------YGTgvdggnitnSNVPy 178
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDraafYtsgraSNEAAYLYqlfaraYGT---------NNLP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 179 rlmnSCggflSRYGSYSTaqiSAAMSYMFGANDGN-SPDDIANTKLVVMFGNNPAET--RMsgggvTYYVEQARERSnAR 255
Cdd:cd02767 132 ----DC----SNMCHEPS---SVGLKKSIGVGKGTvSLEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 256 MIVIDP-------RYNDTAAGRE---------DEWLPIRPGTDGALACAIAWVLI-----TENMVDQPFLDKYCVGYDEk 314
Cdd:cd02767 195 IIVINPlrepgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAKHLIerddePGNVLDHDFIAEHTSGFEE- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 315 tlpanaprnahYKAYIlgegpdgiaKTPEWA--AKITSIPAEKIIHLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAM 392
Cdd:cd02767 274 -----------YVAAL---------RALSWDeiERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 393 LSVLTGNVGING-------GNSGVrEGSWDLGVEWFPMLENpvKTQIS-VFTWTDAIDHG-TEMTATRDGVRGKekldvp 463
Cdd:cd02767 334 LALLRGNIGRPGaglmpirGHSNV-QGDRTMGITEKPFPEF--LDALEeVFGFTPPRDPGlDTVEAIEAALEGK------ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 464 IKFLWCYASNtLINQHGDINHTHEVLqddSKCEMIVGID------HFMTASakyCDILLPDLMPTEQ------------E 525
Cdd:cd02767 405 VKAFISLGGN-FAEAMPDPAATEEAL---RRLDLTVHVAtklnrsHLVHGE---EALILPCLGRTEIdmqaggaqavtvE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 526 DLIS--HESAG---NMGYVILAQPATSAK-----FERKPIYW-MLSEVAKRLGPDVYQTFTEG 577
Cdd:cd02767 478 DSMSmtHTSRGrlkPASRVLLSEEAIVAGiagarLGEAKPEWeILVEDYDRIRDEIAAVIYEG 540
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
693-798 |
1.68e-23 |
|
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: 95.46 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 693 YKARTHSSY-GNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkadmf 770
Cdd:cd02775 1 LRDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWG------ 74
|
90 100
....*....|....*....|....*...
gi 1434010499 771 gDRVDHGGSINILTSHRPSPLAKGNPSH 798
Cdd:cd02775 75 -HRGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
684-807 |
4.69e-23 |
|
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: 95.13 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:cd02785 2 YPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1434010499 763 AWlkadmfgDRVDHGGSINILTS----HRPSPLAKGNPSHSN-LVQIEKV 807
Cdd:cd02785 82 WW-------SRYFQEGSLQDLTSpfvnPVHEYIYGPNSAFYDtLVEVRKA 124
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
684-804 |
3.08e-20 |
|
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: 86.57 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 762
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGePTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1434010499 763 AWLKAdmFGDrvdhGGSINILTSHRPSPLAKGNPSHSNLVQI 804
Cdd:cd02786 81 WWREH--SPD----GRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
684-806 |
1.65e-14 |
|
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: 70.80 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTgfhYKART----HSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVtA 758
Cdd:cd02781 2 YPLILT---TGARSyyyfHSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV-V 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 759 IGQGAWLKADMFGDRVDHGG----SINILTSHRPS-PLAKGNPSHSNLVQIEK 806
Cdd:cd02781 78 RAEHGWWYPEREAGEPALGGvwesNANALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
13-360 |
2.07e-14 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 77.25 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 13 EISRRSLMKTSALGSLAlASSAFTLPfsqmVRAAEVPVEEKAVW----SSCTVnCGSRCLLRLHVKDDTVYWVESDTTGD 88
Cdd:PRK13532 2 KLSRRDFMKANAAAAAA-AAAGLSLP----AVANAVVGSAQTAIkwdkAPCRF-CGTGCGVLVGTKDGRVVATQGDPDAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 89 DVYG-NhqvraCLRGRSIRRRMNHPDRLKYPMKRVgKRGE----GKFERISWDEALDTISDNLRRILKDYGNEAVHVlYG 163
Cdd:PRK13532 76 VNRGlN-----CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGM-FG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 164 TG---VDGGnitnsnvpY---RLMNscGGFLS-------RYgsystAQISAAMSYM--FGANDgnsP----DDIANTKLV 224
Cdd:PRK13532 149 SGqwtIWEG--------YaasKLMK--AGFRSnnidpnaRH-----CMASAVVGFMrtFGIDE---PmgcyDDIEAADAF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 225 VMFGNNPAE------TRMSGggvtyyveqaRERSN--ARMIVIDP---RYNDTAagreDEWLPIRPGTDGALACAIAWVL 293
Cdd:PRK13532 211 VLWGSNMAEmhpilwSRVTD----------RRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILNYIANYI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 294 ITENMVDQPFLDKYCV--------GY-----DEKTLPANAPRNA---------HYKAYilgegpdgIAK-TPEWAAKITS 350
Cdd:PRK13532 277 IQNNAVNWDFVNKHTNfrkgatdiGYglrptHPLEKAAKNPGTAgksepisfeEFKKF--------VAPyTLEKTAKMSG 348
|
410
....*....|
gi 1434010499 351 IPAEKIIHLA 360
Cdd:PRK13532 349 VPKEQLEQLA 358
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
53-308 |
4.51e-14 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 76.40 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 53 KAVWSSCTVNC-GSrCLLRLHVKDDTVYWvESD-----TTGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKR----- 121
Cdd:COG5013 47 KVVRSTHGVNCtGS-CSWKVYVKDGIITW-ETQqtdypRTGPD-LPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvlle 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 122 -----------------------------VGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVH----------VLY 162
Cdd:COG5013 124 lwreararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 163 GTGVdggnitnsnvpyRLMNSCGG-FLSRYGSYstAQISAAMSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRmsggg 240
Cdd:COG5013 204 AAGA------------RFLSLIGGvMLSFYDWY--ADLPPASPQVWGeQTDVPESADWYNSGYLIMWGSNVPQTR----- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434010499 241 vT----YYVEqARERSnARMIVIDPRYNDtAAGREDEWLPIRPGTDGALACAIAWVLITENMVDQ--PFLDKYC 308
Cdd:COG5013 265 -TpdahFMTE-ARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
52-111 |
2.14e-13 |
|
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: 65.01 E-value: 2.14e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 52 EKAVWSSCTvNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNH 111
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
685-791 |
2.27e-13 |
|
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: 67.79 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 685 PLQLTGFHYKARTHSSYGN---IDVLQQACPqEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI-- 759
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDnllMLRLQRGGP-VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMyh 79
|
90 100 110
....*....|....*....|....*....|..
gi 1434010499 760 GQGAWLKADMFGDRVDHGGSINILTSHRPSPL 791
Cdd:cd02776 80 AQERHVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
682-793 |
9.82e-13 |
|
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: 65.61 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 682 KTYPLQL-TG-----FHYKARThssyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 754
Cdd:cd00508 1 EEYPLVLtTGrllehWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1434010499 755 GVTAIGqgawlkadM-FGDRVDhGGSINILTSHRPSPLAK 793
Cdd:cd00508 77 GTVFMP--------FhWGGEVS-GGAANALTNDALDPVSG 107
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
684-795 |
6.92e-12 |
|
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: 63.85 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 684 YPLQLTGFHYKARTHSSyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--G 760
Cdd:cd02780 1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENpVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1434010499 761 QGAW----LKADMFGDRVDH------GGSINILTSHRPSPLAKGN 795
Cdd:cd02780 80 YGHWaygaVASTIDGKDLPGdawrgaGVNINDIGLVDPSRGGWSL 124
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
92-572 |
9.82e-12 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 68.66 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 92 GNHQVRACLRGRSIRRRMNHP--DRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNE---AVHVLYGTGV 166
Cdd:cd02756 93 GNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDdavFASRFDHGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 167 DGGNITNSNVpyrlmnscGGFLsrYGSYSTAQIS------------AAMSYMFGAnDGNSPDDIANTKLVVMFGNNPAET 234
Cdd:cd02756 169 GGGFENNWGV--------GKFF--FMALQTPFVRihnrpaynsevhATREMGVGE-LNNSYEDARLADTIVLWGNNPYET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 235 RmsgggVTYYVE---------------QARERSN----ARMIVIDPRYNDT------AAGREDEW-LPIRPGTDGALACA 288
Cdd:cd02756 238 Q-----TVYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRRTETvhaaeaAAGKDRVLhLQVNPGTDTALANA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 289 IAWVlITEnmvdqpfldkycvGYDEktlpanaprnahykayILGEgpdgiaktpewAAKITSIPAEKIIHLA-----REI 363
Cdd:cd02756 313 IARY-IYE-------------SLDE----------------VLAE-----------AEQITGVPRAQIEKAAdwiakPKE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 364 GSAKPAYIC---QG--WGPQRHsngeQTSRAIAMLSVLTGNVGINGGN----SGVREG---SWDLGVEWFPMLENPVKT- 430
Cdd:cd02756 352 GGYRKRVMFeyeKGiiWGNDNY----RPIYSLVNLAIITGNIGRPGTGcvrqGGHQEGyvrPPPPPPPWYPQYQYAPYId 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 431 ------QISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTHEVLQDDSKceMIVGIDHF 504
Cdd:cd02756 428 qllisgKGKVLWVIGCDPYKTTPNAQRLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGDAIQPGGL--FIVVQDIY 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434010499 505 MTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLgPDVYQ 572
Cdd:cd02756 506 PTKLAEDAHVILPAAANGEMNET---SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI-YELYQ 569
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
684-757 |
1.93e-10 |
|
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: 58.79 E-value: 1.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434010499 684 YPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVT 757
Cdd:cd02790 3 YPLVLtTGrvlYHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
683-807 |
2.32e-10 |
|
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: 58.74 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 683 TYPLQL-TG-----FHYKARThssyGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPG 755
Cdd:cd02791 2 EYPLWLnTGrvrdqWHTMTRT----GRVPRLNAHVPEpYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 756 VtaigqgawLKADMF-GDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 807
Cdd:cd02791 78 E--------VFVPMHwGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
53-151 |
1.79e-09 |
|
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: 60.62 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 53 KAVWSSCTvNCGSRCLLRLHVKDDTVYWVESdttGDDVYGNHqVRACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFER 132
Cdd:COG1034 216 KKTPSICP-HCSVGCNIRVDVRGGKVYRVLP---RENEAVNE-EWLCDKGRFGYDGLNSPDRLTRPLVRKD----GELVE 286
|
90
....*....|....*....
gi 1434010499 133 ISWDEALDTISDNLRRILK 151
Cdd:COG1034 287 ASWEEALAAAAEGLKALKK 305
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
52-111 |
2.38e-09 |
|
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: 53.79 E-value: 2.38e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 52 EKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNH 111
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
717-807 |
2.58e-09 |
|
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: 55.86 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 717 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGDRVDHGG-SINILTSHRP-SPLAkG 794
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPGVSGAGSRPGvNVNDLTDDTQrDPLS-G 115
|
90
....*....|....
gi 1434010499 795 NPSHSNL-VQIEKV 807
Cdd:cd02782 116 NAAHNGVpVRLARV 129
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
697-806 |
3.72e-09 |
|
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: 55.36 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 697 THSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--GQGAWLKADMFGDR 773
Cdd:cd02778 13 THGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGFGHWAPALSRAYG 92
|
90 100 110
....*....|....*....|....*....|...
gi 1434010499 774 vdHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02778 93 --GGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
59-289 |
6.42e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 59.09 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 59 CTVnCGSRCllrlhvkDDTVYWVEsdttgddvyGNHQV---RACLRGRSIRRRMNHPDRLKYPMKRvgkrgegkFERISW 135
Cdd:COG1029 10 CPF-CGCLC-------DDLEVEVE---------GGKIVvvkNACAIGAAKFERAVSDHRITSPRIR--------GKEVSL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 136 DEALDTISdnlrRILKdygnEAVHVLYGtgvdGGNITNSN---VPYRLMNSCGGFLSrygsySTAQISAAMSYMFGANDG 212
Cdd:COG1029 65 EEAIDKAA----EILA----NAKRPLIY----GLSSTDCEamrAGLALAERVGAVVD-----NTASVCHGPSLLALQDVG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 213 NSPDDIANTK----LVVMFGNNPAET------RMSGGGVTYYVEQARERSnaRMIVIDPRYNDTAAgREDEWLPIRPGTD 282
Cdd:COG1029 128 WPTCTLGEVKnradVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGRKDR--TVIVVDPRPTDTAK-VADLHLQVKPGRD 204
|
....*..
gi 1434010499 283 GALACAI 289
Cdd:COG1029 205 YEVLSAL 211
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
112-554 |
6.87e-09 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 59.04 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 112 PDRLKYPMKRVGKRGEGKferISWDEALDTISDNLRRIlKDYGNEAVHvlygTGVDGGNITNSNVpyrlmnscGGFLSRY 191
Cdd:cd02764 97 PDRAQGPLRRGIDGAYVA---SDWADFDAKVAEQLKAV-KDGGKLAVL----SGNVNSPTTEALI--------GDFLKKY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 192 GSYSTAQISA--------AMSYMFGaNDGNSPDDIANTKLVVMFGNNPAETRMSG-GGVTYYVEQARERSNA---RMIVI 259
Cdd:cd02764 161 PGAKHVVYDPlsaedvneAWQASFG-KDVVPGYDFDKAEVIVSIDADFLGSWISAiRHRHDFAAKRRLGAEEpmsRLVAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 260 DPRYNDTAAGrEDEWLPIRPGTDGALACAIAWVLItenmvdqpfldkycvgydEKTLPANAPRNahYKAYILgegpdgiA 339
Cdd:cd02764 240 ESVYTLTGAN-ADVRLAIRPSQEKAFALGLAHKLI------------------KKGAGSSLPDF--FRALNL-------A 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 340 KTPEWAAKITSIPAEKIIHLAREIGSAKPAYICQGwgpQRHSNGEQTSRAIAM--LSVLTGNVGinggnSGVREGSwdlg 417
Cdd:cd02764 292 FKPAKVAELTVDLDKALAALAKALAAAGKSLVVAG---SELSQTAGADTQVAVnaLNSLLGNDG-----KTVDHAR---- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 418 vewfPMLENPVKTQISVFTWTDAIDHGTemtatrdgvrgkekldvpikflwcyASNTLINqhgDINHTHEVLQDD----- 492
Cdd:cd02764 360 ----PIKGGELGNQQDLKALASRINAGK-------------------------VSALLVY---DVNPVYDLPQGLgfaka 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 493 -SKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDlishESAGNMGYVILAQPATSAKFERKP 554
Cdd:cd02764 408 lEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWG----DAETPDGTYSICQPVIAPLFDTRS 466
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
682-806 |
7.10e-07 |
|
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: 48.76 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 682 KTYPLQLTG------FHYKARTHSSYGnidvLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 754
Cdd:cd02792 1 EEFPLVLTTgrltehFHGGNMTRNSPY----LAELQPEMfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1434010499 755 GVTAIgqgAWLKADMFGDRvdhGGSINILTSHRPSPLAKGNPSHSNLVQIEK 806
Cdd:cd02792 77 HEVGI---PYHWGGMGLVI---GDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
61-234 |
1.36e-06 |
|
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: 51.51 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 61 VNCGSRCLLRLHVKDDTVYWVESDTtgddvygNHQVRACL---RGR----SIrrrmNHPDRLKYPMKRVGkrgeGKFERI 133
Cdd:cd02768 5 VHDALGSNIRVDVRGGEVMRILPRE-------NEAINEEWisdKGRfgydGL----NSRQRLTQPLIKKG----GKLVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 134 SWDEALDTIsdnlRRILKDYGNEAVHVLYGTGVDggniTNSNVPY-RLMNSCG----GFLSRYGSYSTAQISAAMSYMfg 208
Cdd:cd02768 70 SWEEALKTV----AEGLKAVKGDKIGGIAGPRAD----LESLFLLkKLLNKLGsnniDHRLRQSDLPADNRLRGNYLF-- 139
|
170 180
....*....|....*....|....*.
gi 1434010499 209 andGNSPDDIANTKLVVMFGNNPAET 234
Cdd:cd02768 140 ---NTSIAEIEEADAVLLIGSNLRKE 162
|
|
| 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 ... |
57-149 |
6.39e-06 |
|
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: 49.69 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 57 SSCTvNCGSRCLLRLHVKDDTVYWVESDTTGD-DVYGNhqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISW 135
Cdd:cd02771 2 SICH-HCSVGCNISLGERYGELRRVENRYNGAvNHYFL-----CDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSW 71
|
90
....*....|....
gi 1434010499 136 DEALDTISDNLRRI 149
Cdd:cd02771 72 NEALDVAAARLKEA 85
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
109-161 |
3.31e-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: 46.96 E-value: 3.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1434010499 109 MNHPDRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNEAVHVL 161
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
716-764 |
8.69e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 42.92 E-value: 8.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1434010499 716 WINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 764
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW 82
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
715-796 |
1.63e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 41.64 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434010499 715 VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkADMFGDRVDHGGSiniltshrpSPLAKG 794
Cdd:cd02789 33 CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW--ANVVVDPYTDSTG---------SPIFKG 101
|
..
gi 1434010499 795 NP 796
Cdd:cd02789 102 VP 103
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
717-764 |
3.46e-03 |
|
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: 38.21 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1434010499 717 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 764
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
|
|