|
Name |
Accession |
Description |
Interval |
E-value |
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
14-811 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 1347.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 14 ISRRSLVKTS-AIGSLALASSAFTLPFSRiaHAAADLASGNVAEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGN 92
Cdd:TIGR02166 1 ISRRHFLKTSaALGGLAAASGALSLPFSV--NAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 93 DEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVHVLYGTGVDG 172
Cdd:TIGR02166 79 DEYGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 173 GNITNSNVPY---RLMNACGGYLSRYGSYSTAQISAAMSYMFGGN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYY 248
Cdd:TIGR02166 159 GTMSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 249 VEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDETTLPASAPRNA 328
Cdd:TIGR02166 239 FLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 329 HYKAYILGQGDDGIAKTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGING 408
Cdd:TIGR02166 319 SYKDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 409 GNSGVREGTWDLGVEWFSMLENPVKTQISVFTWTDAIDHGAEMTATRDGVRGKDKLDVPIKFLWCYASNTLINQHGDIAH 488
Cdd:TIGR02166 399 GNNGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 489 THEVLQDDSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILGQPATSPKFERKPIYWTLSEVAK 568
Cdd:TIGR02166 479 THKILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 569 RLGpdVYQTFTEGRTQHEWVKYLHAKTKARNPEMPDYEEMKQTGIFKKKCPEEHYVAFRSFREDPAANPLKTPSGKIEIY 648
Cdd:TIGR02166 559 RLG--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIY 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 649 SERLATLANTWELKKDEIIHPLPAYTPGFDGWDDPLRQRYPLQLTGFHYKARTHSSYGNIDILQQACPQEIWINPIDAQA 728
Cdd:TIGR02166 637 SERLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 729 RGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNADmfGDKVDRGGSINILTSHRPSPLAKGNPSHSNLVQV 808
Cdd:TIGR02166 717 RGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEV 794
|
...
gi 435294959 809 EKA 811
Cdd:TIGR02166 795 EKA 797
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-810 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1303.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 1 MKITNPEALMAASISRRSLVKTSAIGSLALASSAFTLPFSRIAHAAADLASGNVAEKAVWSSCTVNCGSRCLLRLHVKDD 80
Cdd:PRK14990 1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 81 TVYWVESDTTGNDEY-GNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIGDNLKRILKDYGN 159
Cdd:PRK14990 81 EIKYVETDNTGDDNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 160 EAVHVLYGTGVDGGNITNSNVP-----YRLMNACGGYLSRYGSYSTAQISAAMSYMFGG-NDGNSPDDIANTKLVVMFGN 233
Cdd:PRK14990 161 ESIYLNYGTGTLGGTMTRSWPPgntlvARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 234 NPAETRMSGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCI 313
Cdd:PRK14990 241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 314 GYDETTLPASAPRNAHYKAYILGQGDDGIAKTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTARA 393
Cdd:PRK14990 321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 394 IAMLSVLTGNVGINGGNSGVREGTWDLGVEWFSMLENPVKTQISVFTWTDAIDHGAEMTATRDGVRGKDKLDVPIKFLWC 473
Cdd:PRK14990 401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 474 YASNTLINQHGDIAHTHEVLQDDSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILGQPATSPK 553
Cdd:PRK14990 481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 554 FERKPIYWTLSEVAKRLGpdVYQTFTEGRTQHEWVKYLHAKTKARNPEMPDYEEMKQTGIFKKKCPEEHYVAFRSFREDP 633
Cdd:PRK14990 561 FECKTIYEMTSELAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDP 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 634 AANPLKTPSGKIEIYSERLATLANTWELKKDEIIHPLPAYTPGFDGWDDPLRQRYPLQLTGFHYKARTHSSYGNIDILQQ 713
Cdd:PRK14990 639 QANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 714 ACPQEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNADmfGDKVDRGGSINILTSHRPS 793
Cdd:PRK14990 719 ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPS 796
|
810
....*....|....*..
gi 435294959 794 PLAKGNPSHSNLVQVEK 810
Cdd:PRK14990 797 PLAKGNPSHTNLVQVEK 813
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
60-679 |
0e+00 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 950.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 60 WSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISW 139
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 140 DEALDTIGDNLKRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNACGGYLSRYGSYSTAQISAAMSYMFGGND-GNS 218
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAAsGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 219 PDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQAReRSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALAAAIAWVLI 298
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 299 TEDLIDKPFLDKYCIGYDETTLPASAPRNAHYKAYILGQGDDGIAKTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQG 378
Cdd:cd02770 240 TENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 379 WGPQRHSNGEQTARAIAMLSVLTGNVGINGGNSGVREGTWDLGVEWFSMLENPVKTQISVFTWTDAIDHGAEMTATRDGV 458
Cdd:cd02770 320 WGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 459 RGKDKLDVPIKFLWCYASNTLINQHGDIAHTHEVL-QDDSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESA 537
Cdd:cd02770 400 KGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRALlDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 538 GNMGYVILGQPATSPKFERKPIYWTLSEVAKRLGpdVYQTFTEGRTQHEWVKYLHAKTKARNPEMPDYEEMKQTGIFKKK 617
Cdd:cd02770 480 GMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVP 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 435294959 618 cPEEHYVAFRSFREDPAANPLKTPSGKIEIYSERLATLANTweLKKDEIIHPLPAYTPGFDG 679
Cdd:cd02770 558 -RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEG 616
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
60-679 |
0e+00 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 702.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 60 WSSCTvncgsRCLLRLHVKDDTVYWVESDTTgndeygnHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK----------R 129
Cdd:cd02751 1 PTACH-----WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 130 GEGKFERISWDEALDTIGDNLKRILKDYGNEAVHVLYGTGVDGGNITNSNVPY-RLMNACGGYLSRYGSYSTAQISAAMS 208
Cdd:cd02751 69 GEGEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLhRFLNLIGGYLGSYGTYSTGAAQVILP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 209 YMFGG----NDGNSPDDIA-NTKLVVMFGNNPAETRMSGGGV-----TYYVEQARERsNARMIVIDPRYNDTAAGREDEW 278
Cdd:cd02751 149 HVVGSdevyEQGTSWDDIAeHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKDA-GVRFICIDPRYTDTAAVLAAEW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 279 LPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDEttlpasaprnahYKAYILGqGDDGIAKTPQWAAQITSIPAE 358
Cdd:cd02751 228 IPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLG-ESDGVPKTPEWAAEITGVPAE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 359 KIIQLAREIGSaKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNSGVREGTWDLGVEW--------FSMLEN 430
Cdd:cd02751 295 TIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPrggaggpgLPQGKN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 431 PVKTQISVFTWTDAIDH-GAEMTAtrdgvRGKDKLDVPIKFLWCYASNTLINQHgDIAHTHEVLQDDskcEMIVGIEHFM 509
Cdd:cd02751 374 PVKDSIPVARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFW 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 510 TASAKYCDILLPDLMPTEQEDLIShESAGNMGYVILGQPATSPKFERKPIYWTLSEVAKRLGpdVYQTFTEGRTQHEWVK 589
Cdd:cd02751 445 TASARYADIVLPATTSLERNDIGL-TGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 590 YLHAKTKARN----PEMPDYEEMKQTGIFKKKCPEEHYVAFRSFREDPAANPLKTPSGKIEIYSERLATLANTwelkkDe 665
Cdd:cd02751 522 HLYEETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYD-----D- 595
|
650
....*....|....
gi 435294959 666 iIHPLPAYTPGFDG 679
Cdd:cd02751 596 -CPGHPTWIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-811 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 689.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 43 AHAAADLASGNVAEKAVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYP 122
Cdd:COG0243 8 AAGAGAAALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 123 MKRVGKRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVhVLYGTGVDGGNITNSNVPY--RLMNACG-GYLSRYGSYS 199
Cdd:COG0243 83 MKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAV-AFYTSGGSAGRLSNEAAYLaqRFARALGtNNLDDNSRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 200 TAQISAAMSYMFG-GNDGNSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAgREDEW 278
Cdd:COG0243 162 HESAVAGLPRTFGsDKGTVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 279 LPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDEttlpasaprnahYKAYIlgqgddgIAKTPQWAAQITSIPAE 358
Cdd:COG0243 238 LPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 359 KIIQLAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNSGVREGtwdlgvewfsmlenpvktqisv 438
Cdd:COG0243 299 DIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG---------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 439 ftwtDAIdhgaemtatrdgvrgKDKLDVPIKFLWCYASNtLINQHGDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCDI 518
Cdd:COG0243 357 ----EAI---------------LDGKPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 519 LLPDLMPTEQEDLIsheSAGNMGYVILGQPATSPKFERKPIYWTLSEVAKRLGPDvyQTFTEGRTQHEWVKYLHAKTKAR 598
Cdd:COG0243 414 VLPATTWLERDDIV---TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFE--EAFPWGRTEEDYLRELLEATRGR 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 599 NpemPDYEEMKQTGIFKKKCPEEHYvafrsFREDpaaNPLKTPSGKIEIYSERLAtlantwelkkdeiIHPLPAYTPGFD 678
Cdd:COG0243 489 G---ITFEELREKGPVQLPVPPEPA-----FRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 679 gWDDPLRQRYPLQLTGFHYKARTHSSYGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRIL 757
Cdd:COG0243 545 -GAEPLDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIR 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 435294959 758 PGVTAIGQGAWlnadmFGDKVDRGGSINILTSHRPSPLAKGNPSHSNLVQVEKA 811
Cdd:COG0243 624 PGVVFAPHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
106-653 |
1.08e-118 |
|
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: 371.60 E-value: 1.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 106 GRSIRRRMNHPDRLKYPMKRVG-----------KRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVHV-LYGTGvDGG 173
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIFGgSYGWS-SAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 174 NITNSNVP-YRLMNACGGYLSRYGSYSTAQISAAMSYMFGGND-----GNSPDDIA-NTKLVVMFGNNPAETRMSGGGVT 246
Cdd:cd02769 113 RFHHAQSLlHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEvyteqQTSWPVIAeHTELVVAFGADPLKNAQIAWGGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 247 ------YYVEQARERsNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDEttl 320
Cdd:cd02769 193 pdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDK--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 321 pasaprnahYKAYILGqGDDGIAKTPQWAAQITSIPAEKIIQLAREIgSAKPAYICQGWGPQRHSNGEQTARAIAMLSVL 400
Cdd:cd02769 269 ---------FLPYLLG-ESDGVPKTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 401 TGNVGINGG--------NSGVREGTWDLGVEWFSMLENPVKTQISVFTWTDAIDH-GAEMtaTRDGVRgkdkLDVP-IKF 470
Cdd:cd02769 338 LGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNpGKPF--DYNGKK----LTYPdIKL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 471 LWcYASNTLINQHGDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILGQPAT 550
Cdd:cd02769 412 VY-WAGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIVAMKQVV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 551 SPKFERKPIYWTLSEVAKRLGpdVYQTFTEGRTQHEWVKYLH----AKTKARNPEMPDYEEMKQTGIFKKKCPEEHYVAF 626
Cdd:cd02769 485 EPVGEARDDYDIFADLAERLG--VEEQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPEADFVRL 562
|
570 580
....*....|....*....|....*..
gi 435294959 627 RSFREDPAANPLKTPSGKIEIYSERLA 653
Cdd:cd02769 563 ADFREDPEANPLGTPSGRIEIFSETIA 589
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-653 |
9.61e-112 |
|
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: 350.01 E-value: 9.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 61 SSCTVNCGSRCLLRLHVKDDTVYWVESD-----TTGNdeygnhqvrACLRGRSIRRRMNHPDRLKYPMKRVGKRGeGKFE 135
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVEGDpahpyTRGF---------ICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 136 RISWDEALDTIGDNLKRILKDYGNEAVHVLYGTGVDGgnITNSNVPYRLMNAcGGYLSRYGSYSTAQISAAMSYMFGGND 215
Cdd:cd02766 72 RISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMG--LLQRAARGRFFHA-LGASELRGTICSGAGIEAQKYDFGASL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 216 GNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIAW 295
Cdd:cd02766 149 GNDPEDMVNADLIVIWGINPAATNIHL---MRIIQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALGVAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 296 VLITEDLIDKPFLDKYCIGYDEttlpasaprnahYKAYILgqgddgiAKTPQWAAQITSIPAEKIIQLAREIGSAKPAYI 375
Cdd:cd02766 224 VLFREGLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKPPSI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 376 CQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGnsGVRegtwdlgvewFSMLENPVktqisvftwtdaidhgaemtatr 455
Cdd:cd02766 285 RLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGG--GAF----------YSNSGPPV----------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 456 dgvrgkdkldvpiKFLWCYASNtLINQHGDiahTHEVLQDDS-KCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLIsh 534
Cdd:cd02766 330 -------------KALWVYNSN-PVAQAPD---SNKVRKGLArEDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY-- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 535 esaGNMG--YVILGQPATSPKFERKPIYWTLSEVAKRLGpdvyqtFTEG---RTQHEWVKylhaktKARNPEMPDYEEMk 609
Cdd:cd02766 391 ---ASYWhyYLQYNEPAIPPPGEARSNTEIFRELAKRLG------FGEPpfeESDEEWLD------QALDGTGLPLEGI- 454
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 435294959 610 qtgifkkKCPEEHYVAFRSFREDPAANP-LKTPSGKIEIYSERLA 653
Cdd:cd02766 455 -------DLERLLGPRKAGFPLVAWEDRgFPTPSGKFEFYSERAA 492
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
60-570 |
4.27e-105 |
|
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: 328.13 E-value: 4.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 60 WSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGegKFERISW 139
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIE----GDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 140 DEALDTIGDNLKRILKDYGNEAVHVLYGTGVDGGniTNSNVPYRLMNACGGYLSRYGSYSTAQISAAMSYMFGGNDGNSP 219
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNE--EAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 220 DDIANTKLVVMFGNNPAETRMSgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAiawvlit 299
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 300 edlidkpfldkycigydettlpasaprnahykayilgqgddgiaktpQWAAQITSIPAEKIIQLAREIGSAKPAYICQGW 379
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 380 GPQRHSNGEQTARAIAMLSVLTGNVGINGGNSGVRegtwdlgvewfsmlENPVKTQisvftwtdaidhgaemtatrdgvr 459
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA------------------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 460 gkdkldvpikflwcyasntlinqhgdiAHTHEVLQDDSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHesagN 539
Cdd:cd00368 295 ---------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN----T 343
|
490 500 510
....*....|....*....|....*....|.
gi 435294959 540 MGYVILGQPATSPKFERKPIYWTLSEVAKRL 570
Cdd:cd00368 344 EGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
62-675 |
1.84e-101 |
|
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: 322.33 E-value: 1.84e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 62 SCTVnCGSRCLLRLHVKDDTVYWVESDTTGNDEYGnhqvRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDE 141
Cdd:cd02759 3 TCPG-CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG----RLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 142 ALDTIGDNLKRILKDYGNEAVHVLYGTGvDGGNITNSNVPYRLMNACG---GYLSRYGSYSTAQISAAMSYMFGGNDGNS 218
Cdd:cd02759 78 ALDEIAEKLAEIKAEYGPESIATAVGTG-RGTMWQDSLFWIRFVRLFGspnLFLSGESCYWPRDMAHALTTGFGLGYDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 219 pdDIANTKLVVMFGNNPAETrmSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIAWVLI 298
Cdd:cd02759 157 --DWENPECIVLWGKNPLNS--NLDLQGHWLVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 299 TEDLIDKPFLDKYCIGYDETtlpasAPRNAHYkayilgqgddgiakTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQG 378
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEEL-----AERVQEY--------------TPEKVAEITGVPAEKIRKAARLYATAKPACIQWG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 379 WGPQRHSNGEQTARAIAMLSVLTGNVGINGGNsgvregtwdLGVEWfsmlenpvktqisvftwtdaidhgaemtatrdgv 458
Cdd:cd02759 292 LAIDQQKNGTQTSRAIAILRAITGNLDVPGGN---------LLIPY---------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 459 rgkdkldvPIKFLWCYASNTLINQhGDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESAG 538
Cdd:cd02759 329 --------PVKMLIVFGTNPLASY-ADTAPVLEALK---ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAE 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 539 NMGYviLGQPATSPKFERKPIYWTLSEVAKRLGPDvyqtftegrtQHEWVKYlhaktkarnpEMPDYEEMKQTGifkkkc 618
Cdd:cd02759 397 NFVQ--LRQKAVEPYGEAKSDYEIVLELGKRLGPE----------EAEYYKY----------EKGLLRPDGQPG------ 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 435294959 619 peehyvafrsfredpaanpLKTPSGKIEIYSERLatlantWELKKDeiihPLPAYTP 675
Cdd:cd02759 449 -------------------FNTPTGKVELYSTML------EELGYD----PLPYYRE 476
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
14-810 |
3.65e-101 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 331.64 E-value: 3.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 14 ISRRSLVKtsaigSLALASSAFTLPFSRIAHAAADLASGNVAE-KAVWSSCTVNCGSrclLRLHVKDDTvyWVESDTTGN 92
Cdd:PRK15102 1 ASRRRFLK-----GLGGLSAAGMLGPSLLTPRSALAAQAAAAEtTKEWILTGSHWGA---FRAKVKNGR--FVEAKPFEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 93 DEYGNHQVRAclrgrsIRRRMNHPDRLKYPMKRV-----------GKRGEGKFERISWDEALDTIGDNLKRILKDYGNEA 161
Cdd:PRK15102 71 DKYPTKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 162 VHvlygTGVDGGNITN-----SNVPYRLMNACGGYLSRYGSYSTAQISAAMSYMFGGND----GNS-PDDIANTKLVVMF 231
Cdd:PRK15102 145 LH----TGQTGWQSTGqfhsaTGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSwPLILENSKTIVLW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 232 GNNP---------AETRMSGGgvtyYVEQARER---SNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALAAAIAWVLIT 299
Cdd:PRK15102 221 GSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTLYS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 300 EDLIDKPFLDKYCIGYDEtTLPasaprnahykaYILGQgDDGIAKTPQWAAQITSIPAEKIIQLAREIgSAKPAYICQGW 379
Cdd:PRK15102 297 ENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIAGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 380 GPQRHSNGEQTARAIAMLSVLTGNVGINGG--------NS-GVRE----------GTWDLGVE--WFSMLENPVKTQISV 438
Cdd:PRK15102 363 CIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhySGiGVPSsggaipggfpGNLDTGQKpkHDNSDYKGYSSTIPV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 439 FTWTDAIDH-GAEMTATrdgvrGKDKLDVPIKFLwCYASNTLINQHGDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCD 517
Cdd:PRK15102 443 ARFIDAILEpGKTINWN-----GKKVTLPPLKMM-IFSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATCRFAD 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 518 ILLPDLMPTEQEDLISHESAGNMGyVILGQPATSPKFERKPIYWTLSEVAKRLGPDvyQTFTEGRTQHEWVKYLHAKTKA 597
Cdd:PRK15102 514 IVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGRE--KEYTRGMDEMGWLKRLYQECKQ 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 598 RNP---EMPDYEEMKQTGI--FKKKCPeehYVAFRSFREDPAANPLKTPSGKIEIYSERLATLA-------NTWeLKKDE 665
Cdd:PRK15102 591 QNKgkfHMPEFDEFWKKGYveFGEGQP---WVRHADFREDPELNPLGTPSGLIEIYSRKIADMGyddcqghPMW-FEKIE 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 666 IIHPlpayTPGFDgwddplrqRYPLQLTGFHYKARTHSsygnidilqQACPQE-------------IWINPIDAQARGIQ 732
Cdd:PRK15102 667 RSHG----GPGSD--------KYPLWLQSVHPDKRLHS---------QLCESEelretytvqgrepVYINPQDAKARGIK 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 733 HGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNADMfGDKV---DRGGSINILTSHRP-SPLAKGNPSHSNLVQV 808
Cdd:PRK15102 726 DGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDK-GGEIgalCTYGDPNTLTLDIGtSQLAQATSAHTCLVEI 804
|
..
gi 435294959 809 EK 810
Cdd:PRK15102 805 EK 806
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
67-797 |
1.05e-90 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 299.88 E-value: 1.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 67 CGSRCLLRLHVKDDTVYWVESDTtgndeygNHQV---RACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEAL 143
Cdd:COG3383 14 CGVGCGIDLEVKDGKIVKVEGDP-------DHPVnrgRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 144 DTIGDNLKRILKDYGNEAVHVLYgtgvdGGNITNSNVpY---RLMNACGG-----YLSRYGSYSTAqisAAMSYMFG-GN 214
Cdd:COG3383 83 DLVAERLREIQAEHGPDAVAFYG-----SGQLTNEEN-YllqKLARGVLGtnnidNNARLCMASAV---AGLKQSFGsDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 215 DGNSPDDIANTKLVVMFGNNPAETrmsgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIA 294
Cdd:COG3383 154 PPNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNGLL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 295 WVLITEDLIDKPFLDKYCIGYDEttlpasaprnahYKAYILGQgddgiakTPQWAAQITSIPAEKIIQLAREIGSAKPAY 374
Cdd:COG3383 229 HVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREAARLIAEAKRAM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 375 ICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGgnSGV---RE-----GTWDLGV--EWFS---MLENP-VKTQISVFT 440
Cdd:COG3383 290 ILWGMGVNQHTQGTDNVNAIINLALATGNIGRPG--TGPfplTGqnnvqGGRDMGAlpNVLPgyrDVTDPeHRAKVADAW 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 441 WTDAIDHGAEMTATR--DGV-RGKdkldvpIKFLWCYASNTLInQHGDIAHTHEVLqddSKCEMIVGIEHFMTASAKYCD 517
Cdd:COG3383 368 GVPPLPDKPGLTAVEmfDAIaDGE------IKALWIIGENPAV-SDPDANHVREAL---EKLEFLVVQDIFLTETAEYAD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 518 ILLPDLMPTEQED-LISHEsagnmGYVILGQPATSPKFERKPIYWTLSEVAKRLGPDV-YQT----FTEgrtqhewvkyl 591
Cdd:COG3383 438 VVLPAASWAEKDGtFTNTE-----RRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFdYDSpeevFDE----------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 592 HAKtkarnpEMPD-----YEEMKQTGIFKKKCP-EEHYVAFRSFREDPAanplkTPSGKIeiyserlatlantwelkkde 665
Cdd:COG3383 502 IAR------LTPDysgisYERLEALGGVQWPCPsEDHPGTPRLFTGRFP-----TPDGKA-------------------- 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 666 IIHPLPAYTPgfdgwDDPLRQRYPLQL-TG---FHYKARTHSsyGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVF 740
Cdd:COG3383 551 RFVPVEYRPP-----AELPDEEYPLVLtTGrllDQWHTGTRT--RRSPRLNKHAPEPfVEIHPEDAARLGIKDGDLVRVS 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 435294959 741 NQNGEMLILAKVTPRILPGVTAIgqgawlnADMFGDkvdrgGSINILTSHRPSPLAK 797
Cdd:COG3383 624 SRRGEVVLRARVTDRVRPGTVFM-------PFHWGE-----GAANALTNDALDPVSK 668
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-656 |
2.01e-90 |
|
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: 295.93 E-value: 2.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 61 SSCTVNCGSRCLLRLHVKDDTVYWVESDTTGNDEYGnhqvRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWD 140
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYK----RGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 141 EALDTIGDNLKRILKDYGNEAVHVLYGTGVDGgniTNSNVPYRLMNAcGGYLSRYGSYSTAQISAAMSYMFGGN--DGNS 218
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGA---ILSYLRLALLGG-GLQDALTYGIDTGVGQGFNRVTGGGFmpPTNE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 219 PDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIAWVLI 298
Cdd:cd02765 154 ITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINYIL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 299 TEDLIDKPFLDKYC-----IGYDETTL--PASAPRNAHYKAYILGQGDDG------------------------------ 341
Cdd:cd02765 229 EHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVWDTNSDspepvaatninpalegeytingvkvhtvlt 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 342 -----IAK-TPQWAAQITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNSGVre 415
Cdd:cd02765 309 alreqAASyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 416 gtwdlgvewfsmlenpvktqisvftwtdaidhgaemtatrdgvrgkdkldvpIKFLWcyasNTLINQHGDIAHTHEVLQD 495
Cdd:cd02765 387 ----------------------------------------------------IKFMY----FMGSNFLGNQPDRDRWLKV 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 496 DSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESAGNmgYVILGQPATSPKFERKPIYWTLSEVAKRLGPDVY 575
Cdd:cd02765 411 MKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDY 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 576 QTFTEGRTQHEWVKYLHAKTKARNpempdYEEMKQTGIFKKK-CPEEHYVAFrsfrEDPAanpLKTPSGKIEIYSERLAT 654
Cdd:cd02765 489 FPKTPEDYVRAFMNSDDPALDGIT-----WEALKEEGIIMRLaTPEDPYVAY----LDQK---FGTPSGKLEFYNEAAPE 556
|
..
gi 435294959 655 LA 656
Cdd:cd02765 557 LE 558
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
59-579 |
3.98e-82 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 270.32 E-value: 3.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 59 VWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERIS 138
Cdd:cd02755 1 VPSICEM-CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 139 WDEALDTIGDNLKRILKDYGNEAvhVLYGTGVDGgnitNSNVPYRLMNACG--GYLSRYGS--YSTAQISAAMSYMFGgn 214
Cdd:cd02755 76 WDEALQYIASKLKEIKEQHGPES--VLFGGHGGC----YSPFFKHFAAAFGspNIFSHESTclASKNLAWKLVIDSFG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 215 dGNSPDDIANTKLVVMFGNNPAEtrmsGGGVTYYVEQARERSN-ARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAI 293
Cdd:cd02755 148 -GEVNPDFENARYIILFGRNLAE----AIIVVDARRLMKALENgAKVVVVDPRFSELAS-KADEWIPIKPGTDLAFVLAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 294 AWVLITEDLIDKPFLDKYCIGYDETTlpasaprnAHYKAYilgqgddgiakTPQWAAQITSIPAEKIIQLAREIG-SAKP 372
Cdd:cd02755 222 IHVLISENLYDAAFVEKYTNGFELLK--------AHVKPY-----------TPEWAAQITDIPADTIRRIAREFAaAAPH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 373 AYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGnsgvregtwdlgveWFSmlenpvktqisvftwtdaidhgaemt 452
Cdd:cd02755 283 AVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG--------------LYY-------------------------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 453 atrdgvrGKDKLDVPIKFLWCYASNTLINQHgDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLI 532
Cdd:cd02755 323 -------AGSAKPYPIKALFIYRTNPFHSMP-DRARLIKALK---NLDLVVAIDILPSDTALYADVILPEATYLERDEPF 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 435294959 533 SHESAGNMGYVILgQPATSPKFERKPIYWTLSEVAKRLGPdvYQTFT 579
Cdd:cd02755 392 SDKGGPAPAVATR-QRAIEPLYDTRPGWDILKELARRLGL--FGTPS 435
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
13-758 |
1.97e-80 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 274.24 E-value: 1.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 13 SISRRSLVKTSAIGSLALASSAFtLPFSrIAHAAADLASGNvaEKAVWSSCTVnCGSRCLLRLHVKDDTVYWVesdtTGN 92
Cdd:PRK15488 2 SLSRRDFLKGAGAGCAACALGSL-LPGA-LAANEIAQLKGK--TKLTPSICEM-CSTRCPIEARVVNGKNVFI----QGN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 93 DEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVHVLYGTGvdg 172
Cdd:PRK15488 73 PKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSG--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 173 gniTNSNVPYRLMNAcggylsrYGS------YSTAQISAAM--SYMFGGNDGNspdDIANTKLVVMFGNNPAE-TRMSgg 243
Cdd:PRK15488 150 ---SLSSHLFHLATA-------FGSpntfthASTCPAGYAIaaKVMFGGKLKR---DLANSKYIINFGHNLYEgINMS-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 244 gVTYYVEQARERSNARMIVIDPRYNdTAAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDEttLPAS 323
Cdd:PRK15488 215 -DTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE--LAAS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 324 AprnahyKAYilgqgddgiakTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQgWGPQRHSNGE--QTARAIAMLSVLT 401
Cdd:PRK15488 291 V------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRATFTPEefDMRRAIFAANVLL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 402 GNVGINGGNSGVRE-GTWD--LGVEWFSMLENPvktQISVFTWTDA--IDHGAE---MTATRDGVRgKDKLDV------- 466
Cdd:PRK15488 353 GNIERKGGLYFGKNaSVYNklAGEKVAPTLAKP---GVKGMPKPTAkrIDLVGEqfkYIAAGGGVV-QSIIDAtltqkpy 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 467 PIKFLWCYASNTLINQhgdiAHTHEVLQDDSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILg 546
Cdd:PRK15488 429 QIKGWVMSRHNPMQTV----TDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYALR- 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 547 QPATSPKFERKPIYWTLSEVAKRLGPDVYQTFTEGRTqhewvkyLHAKTKARNPEMpdYEEMKQTGIFKKKCP----EEH 622
Cdd:PRK15488 504 QRVVEPIGDTKPSWQIFKELGEKMGLGQYYPWQDMET-------LQLYQVNGDHAL--LKELKKKGYVSFGVPlllrEPK 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 623 YVAfrSFRED-PAANP------------LKTPSGKIEIYSERLATLAntwelkkdeiihplPAY-TPGFDgwDDPLRQRY 688
Cdd:PRK15488 575 MVA--KFVARyPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALA--------------PGYgVPRYR--DVALKKED 636
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 435294959 689 PLQLTGFHYKARTHSSYGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILP 758
Cdd:PRK15488 637 ELYFIQGKVAVHTNGATQNVPLLANLMSDNaVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRP 707
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
57-587 |
7.99e-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: 261.87 E-value: 7.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 57 KAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDT----TGNDeYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEG 132
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATdypeTPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 133 KFERISWDEALDTIGDNLKRILKDYGNEAV----------HVLYGTGvdggnitnsnvpYRLMNACGGY-LSRYGSYstA 201
Cdd:cd02750 81 KWKRISWDEALELIADAIIDTIKKYGPDRVigfspipamsMVSYAAG------------SRFASLIGGVsLSFYDWY--G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 202 QISAAMSYMFG-GNDGNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLP 280
Cdd:cd02750 147 DLPPGSPQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADLWVP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 281 IRPGTDGALAAAIAWVLITEDLIDKPFLDKYcigydeTTLPasaprnahYKAYilgqgddgiakTPQWAAQITSIPAEKI 360
Cdd:cd02750 222 IKPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPRETV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 361 IQLAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNsgvregtWDLGVEWFSMLenpvktqisvft 440
Cdd:cd02750 277 IRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGG-------WAHYVGQPRVL------------ 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 441 wtdaidhgaemtatrdgvrgkdkldvpikFLWcyaSNTLINQHGDiahTHEVLQD--DSKCEMIVGIEHFMTASAKYCDI 518
Cdd:cd02750 338 -----------------------------FVW---RGNLFGSSGK---GHEYFEDapEGKLDLIVDLDFRMDSTALYSDI 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 435294959 519 LLPDLMPTEQEDLISheSAGNMgYVILGQPATSPKFERKPIYWTLSEVAKRLgpdVYQTFTeGRTQ----HEW 587
Cdd:cd02750 383 VLPAATWYEKHDLST--TDMHP-FIHPFSPAVDPLWEAKSDWEIFKALAKKV---PWRTLT-GRQQfyldHDW 448
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
58-653 |
1.07e-71 |
|
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: 244.27 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 58 AVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRG----EGK 133
Cdd:cd02757 1 WVPSTCQ-GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 134 FERISWDEALDTIGDNLKRILKDygNEAVHVLYGTGVDGGNitNSNVPYRLMNACG--GYLSRYGSYSTAQiSAAMSYMF 211
Cdd:cd02757 76 FVPISWDEALDTIADKIRALRKE--NEPHKIMLHRGRYGHN--NSILYGRFTKMIGspNNISHSSVCAESE-KFGRYYTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 212 GGNDGNSPDdIANTKLVVMFGNNPAETrmsgggvTYYVEQARE-----RSNARMIVIDPRYNDTAAgREDEWLPIRPGTD 286
Cdd:cd02757 151 GGWDYNSYD-YANAKYILFFGADPLES-------NRQNPHAQRiwggkMDQAKVVVVDPRLSNTAA-KADEWLPIKPGED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 287 GALAAAIAWVLITEDLIDKPFLDKYCIGYD-----ETTLPASAPR----------NAHYKAYilgqgddgiakTPQWAAQ 351
Cdd:cd02757 222 GALALAIAHVILTEGLWDKDFVGDFVDGKNyfkagETVDEESFKEksteglvkwwNLELKDY-----------TPEWAAK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 352 ITSIPAEKIIQLAREIGSAKPAYICQGW-GPQRHSNGEQTARAIAMLSVLTGNVGINGgnsGVREGTWDLGVE-WFSMLE 429
Cdd:cd02757 291 ISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKG---GLCPNMGVPKIKvYFTYLD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 430 NPVKTQISVFTWTDAIDhgaemtatrdgvrgkdklDVPIkflwcyasntlinqhgdiaHTHevlqddskcemivgIEHFM 509
Cdd:cd02757 368 NPVFSNPDGMSWEEALA------------------KIPF-------------------HVH--------------LSPFM 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 510 TASAKYCDILLPDLMPTEQEDLISHESAGNmGYVILGQPATSPKFERKPIYWTLSEVAKRLGPDvyqtftegrtqhewvk 589
Cdd:cd02757 397 SETTYFADIVLPDGHHFERWDVMSQENNLH-PWLSIRQPVVKSLGEVREETEILIELAKKLDPK---------------- 459
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435294959 590 ylhaktkarnpempDYEEMKQTGIFKKKCPEEHYVAFRSFredpaANPLKTPSGKIEIYSERLA 653
Cdd:cd02757 460 --------------GSDGMKRYAPGQFKDPETGKNNRWEF-----ENVFPTETGKFEFYSETLK 504
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
67-571 |
1.51e-67 |
|
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: 232.87 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 67 CGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVgkrgEGKFERISWDEALDTI 146
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 147 GDNLKRILKDYGNEAVhvlygTGVDGGNITN-SNvpY---RLMNACGG-----YLSRYGSYSTAqisAAMSYMFG-GNDG 216
Cdd:cd02753 79 ASRLKEIKDKYGPDAI-----AFFGSAKCTNeEN--YlfqKLARAVGGtnnvdHCARLCHSPTV---AGLAETLGsGAMT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 217 NSPDDIANTKLVVMFGNNPAETRMSGGgvtYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIAWV 296
Cdd:cd02753 149 NSIADIEEADVILVIGSNTTEAHPVIA---RRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALLNAMAHV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 297 LITEDLIDKPFLDKYCIGYDETTlpasaprnAHYKAYilgqgddgiakTPQWAAQITSIPAEKIIQLAREIGSAKPAYIC 376
Cdd:cd02753 224 IIEEGLYDEEFIEERTEGFEELK--------EIVEKY-----------TPEYAERITGVPAEDIREAARMYATAKSAAIL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 377 QGWGPQRHSNGEQTARAIAMLSVLTGNVGinggnsgvREGTwdlGVewfsmleNPVKTQISVftwTDAIDHGAemtatrd 456
Cdd:cd02753 285 WGMGVTQHSHGTDNVMALSNLALLTGNIG--------RPGT---GV-------NPLRGQNNV---QGACDMGA------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 457 gvrgkdkldVP------IKFLWCYASNTLINqHGDIAHTHEVLqddSKCEMIVGIEHFMTASAKYCDILLP--------- 521
Cdd:cd02753 337 ---------LPnvlpgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPaasfaekdg 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 435294959 522 DLMPTEQEdlishesagnmgyVILGQPATSPKFERKPIYWTLSEVAKRLG 571
Cdd:cd02753 404 TFTNTERR-------------VQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
67-644 |
1.69e-65 |
|
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: 228.65 E-value: 1.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 67 CGSRCLLRLHVKDDTVYWVesdtTGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRvgkRGEGKFERISWDEALDTI 146
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAV----RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 147 GDNLKRILKDYGNEAVHVlYGTG-------------VDGG----NI-TNSnvpyRLMNAcggylsrygsystaqiSAAMS 208
Cdd:cd02754 80 AERFKAIQAEYGPDSVAF-YGSGqllteeyyaanklAKGGlgtnNIdTNS----RLCMA----------------SAVAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 209 YM--FGGnDG--NSPDDIANTKLVVMFGNNPAETRmsggGVTY-YVEQARE-RSNARMIVIDPRYNDTAAgREDEWLPIR 282
Cdd:cd02754 139 YKrsFGA-DGppGSYDDIEHADCFFLIGSNMAECH----PILFrRLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 283 PGTDGALAAAIAWVLITEDLIDKPFLDKYCIGYDETTlpasaprnAHYKAYilgqgddgiakTPQWAAQITSIPAEKIIQ 362
Cdd:cd02754 213 PGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELK--------AFVADY-----------TPEKVAEITGVPEADIRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 363 LAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVG--------ING-GNS-GVRE----GTWDLGVEWFsml 428
Cdd:cd02754 274 AARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREvgglANLLPGHRSV--- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 429 ENPvktqisvftwtdaiDHGAEM-------------TATRDGVRGKDKL-DVPIKFLWCYASNTLINqhgdIAHTHEVLQ 494
Cdd:cd02754 351 NNP--------------EHRAEVakfwgvpegtippKPGLHAVEMFEAIeDGEIKALWVMCTNPAVS----LPNANRVRE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 495 DDSKCEMIVGIEHF-MTASAKYCDILLPDLMPTEQEdlishesaGNMG----YVILGQPATSPKFERKPIYWTLSEVAKR 569
Cdd:cd02754 413 ALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKE--------GTMTnserRVSLLRAAVEPPGEARPDWWILADVARR 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 435294959 570 LGPDVYQTFTegrTQHEWVKYLHAKTKARNPEMP--DYEEMKQTGIfKKKCPEEHYVAFRSFREDPAANplkTPSGK 644
Cdd:cd02754 485 LGFGELFPYT---SPEEVFEEYRRLSRGRGADLSglSYERLRDGGV-QWPCPDGPPEGTRRLFEDGRFP---TPDGR 554
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
118-569 |
2.34e-65 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 222.28 E-value: 2.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 118 RLKYPMKRvgkRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVHVLYGTGvdGGNITNSNVPY-----RLMNACGGYL 192
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALkkllnRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 193 SRYGSYSTAQiSAAMSYMFGGN--DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYyveQARERSNARMIVIDPRYNdt 270
Cdd:pfam00384 76 DHNGDLCTAA-AAAFGSDLRSNylFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 271 aAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDKPFLDKycigydettlpasaprnahykayilgqgddgiaktpqwaa 350
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 351 qitsipaekiiqlareigsakpAYICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNsgvregtwdlgveWFSMLEN 430
Cdd:pfam00384 189 ----------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-------------WNGLNIL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 431 PvktqisvftwTDAIDHGAEMTATRDGVRGKDKLDVP----IKFLWcYASNTLINQHGDIAHTHEVLQddsKCEMIVGIE 506
Cdd:pfam00384 234 Q----------GAASPVGALDLGLVPGIKSVEMINAIkkggIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 435294959 507 HFM-TASAKYCDILLPDLMPTEQEDLIShesagNM-GYVILGQPATSPKFERKPIYWTLSEVAKR 569
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYV-----NTeGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
688-810 |
1.60e-61 |
|
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: 202.91 E-value: 1.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 688 YPLQLTGFHYKARTHSSYGNIDILQQACPQEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGA 767
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 435294959 768 WLNADmfGDKVDRGGSINILTSHRPSPLAKGNPSHSNLVQVEK 810
Cdd:cd02794 81 WYEPD--ANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-810 |
5.74e-51 |
|
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: 174.31 E-value: 5.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 688 YPLQLTGFHYKARTHSSYGNIDILQQACP----QEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAI 763
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKvkgrEPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 435294959 764 GQGAWLNADmFGDKVDRGGSINILTSHRPSP-LAKGNPSHSNLVQVEK 810
Cdd:cd02777 81 PEGAWYDPD-DNGGLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-531 |
4.29e-46 |
|
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: 173.35 E-value: 4.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 63 CTVNCGsrclLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEA 142
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIR----GDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 143 LDTIGDNLKRILKDYGNEAVHVlYGTGVDGGNITNSNVPYRLMNACGGylSRYGSYSTAQI---SAAMSYMFGGNDGNSP 219
Cdd:cd02762 75 FDEIAERLRAIRARHGGDAVGV-YGGNPQAHTHAGGAYSPALLKALGT--SNYFSAATADQkpgHFWSGLMFGHPGLHPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 220 DDIANTKLVVMFGNNPAETR---MSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALAAAIAWV 296
Cdd:cd02762 152 PDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLFVRPGTDAWLLAAMLAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 297 LITEDLIDKPFLDKYCIGYDETTlPASAPRnahykayilgqgddgiakTPQWAAQITSIPAEKIIQLAREIGSAKPAYIC 376
Cdd:cd02762 230 LLAEGLTDRRFLAEHCDGLDEVR-AALAEF------------------TPEAYAPRCGVPAETIRRLAREFAAAPSAAVY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 377 QGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGN----------SGVREGTWDLGvEWFSMLEN--PVKTQISVFTWTDA 444
Cdd:cd02762 291 GRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAmfttpaldlvGQTSGRTIGRG-EWRSRVSGlpEIAGELPVNVLAEE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 445 IDhgaemtatRDGvrgkdklDVPIKFLWCYASNTLINQhGDIAHTHEVLQddsKCEMIVGIEHFMTASAKYCDILLPDLM 524
Cdd:cd02762 370 IL--------TDG-------PGRIRAMIVVAGNPVLSA-PDGARLEAALG---GLEFMVSVDVYMTETTRHADYILPPAS 430
|
....*..
gi 435294959 525 PTEQEDL 531
Cdd:cd02762 431 QLEKPHA 437
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-571 |
6.33e-46 |
|
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: 175.41 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 67 CGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI 146
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 147 GDNLKRILKdygNEAVHVLYGTGVDGgnitnsnvpyrlMNACGGYLSR---------YGSYSTAQISAAMSYMFGGN--D 215
Cdd:cd02763 83 TKRLKAARA---TDPKKFAFFTGRDQ------------MQALTGWFAGqfgtpnyaaHGGFCSVNMAAGGLYSIGGSfwE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 216 GNSPdDIANTKLVVMFG------NNPAETRMsgggvtyyveQARERSNARMIVIDP---RYNDTAagreDEWLPIRPGTD 286
Cdd:cd02763 148 FGGP-DLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPvrtGYAAIA----DEWVPIKPGTD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 287 GALAAAIAWVLITEDLIDKPFLDKYCigydettlpasaprNAHYKayilgqgddgIAKTPQWAAQITSIPAEKIIQLARE 366
Cdd:cd02763 213 GAFILALAHELLKAGLIDWEFLKRYT--------------NAAEL----------VDYTPEWVEKITGIPADTIRRIAKE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 367 IGSAK-------PAYICQGWGPQR------------------HSNGEQTARAIAMLSVLTGNVGINGGN----------- 410
Cdd:cd02763 269 LGVTArdqpielPIAWTDVWGRKHekitgrpvsfhamrgiaaHSNGFQTIRALFVLMMLLGTIDRPGGFrhkppyprhip 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 411 ---------SGVREGT--------WDLGVEWFSMLENPVKTQIS-VFTWTDAID-HGAEMTATRDGVRGKdklDVPIKFL 471
Cdd:cd02763 349 plpkppkipSADKPFTplygpplgWPASPDDLLVDEDGNPLRIDkAYSWEYPLAaHGCMQNVITNAWRGD---PYPIDTL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 472 WCYASNTLINQHGDIAHTHEVLQD-----DSKCEMIVGIEHFMTASAKYCDILLPDLMPTEQEDLIS------HESAGNM 540
Cdd:cd02763 426 MIYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSlldrpiSEADGPV 505
|
570 580 590
....*....|....*....|....*....|.
gi 435294959 541 GYVilGQPATSPKFERKPIYWTLSEVAKRLG 571
Cdd:cd02763 506 DAI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
63-424 |
2.46e-39 |
|
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: 155.25 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 63 CTVNCGsrclLRLHVKDDTVYWVESDTTGNDEYGNHqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrGEGKFERISWDEA 142
Cdd:cd02752 7 CSVGCG----LIAYVQNGVWVHQEGDPDHPVNRGSL----CPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 143 LDTIGDNLKRILKDYGNEAVhvLYGTGVDGGNITNSNVPYRLMNAcGGYLSR-----YGSYST---AQIS-----AAMSY 209
Cdd:cd02752 77 LDEIARKMKDIRDASFVEKN--AAGVVVNRPDSIAFLGSAKLSNE-ECYLIRkfaraLGTNNLdhqARIUhsptvAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 210 MFG-GNDGNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRPGTDga 288
Cdd:cd02752 154 TFGrGAMTNSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRTAA-KADLYVPIRSGTD-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 289 laAAIAWVLItedlidkpfldKYCIGYdettlpasaprnahykayilgqgddgiakTPQWAAQITSIPAEKIIQLAREIG 368
Cdd:cd02752 228 --IAFLGGMI-----------NYIIRY-----------------------------TPEEVEDICGVPKEDFLKVAEMFA 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 435294959 369 S----AKPAYI--CQGWgpQRHSNGEQTARAIAMLSVLTGNVGING-------GNSGVrEGTWDLGVEW 424
Cdd:cd02752 266 AtgrpDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGggvnalrGHSNV-QGATDLGLLS 331
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
101-658 |
1.14e-37 |
|
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: 150.96 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 101 RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI-----------GDNLK--RILK--------DYGN 159
Cdd:cd02758 66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVveggdlfgeghVEGLKaiRDLDtpidpdhpDLGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 160 EAVHVLYGTGVDGGNITNSNvpyRLMNACGGYL--SRYGSYSTAQISAAMSYMFGGNDGNsPD---DIANTKLVVMFGNN 234
Cdd:cd02758 146 KANQLLYTFGRDEGRTPFIK---RFANQAFGTVnfGGHGSYCGLSYRAGNGALMNDLDGY-PHvkpDFDNAEFALFIGTS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 235 PAE-----TRMSGggvtyYVEQARERSNARMIVIDPRY--NDTAAGREDEWLPIRPGTDGALA-AAIAWVLITEdlidkp 306
Cdd:cd02758 222 PAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAmAMIRWIIENE------ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 307 fldkyciGYDETTL----PASAPR-------NAHY-------KAYILGQGDDGIAKT-PQWAAQiTSIPAEKIIQLAREI 367
Cdd:cd02758 291 -------RYNAEYLsipsKEAAKAagepswtNATHlvitvrvKSALQLLKEEAFSYSlEEYAEI-CGVPEAKIIELAKEF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 368 GSA--KPAYICQgwGPQRHSNGEQTARAIAMLSVLTGNV----GINGGNSGVREGTWDLGVEWFSMLENPVKTQISV--- 438
Cdd:cd02758 363 TSHgrAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLnwkgGLLMSGGGFADNSAGPRYDFKKFFGEVKPWGVPIdrs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 439 -FTWTDAIDHGAEMTATRDGVRGK-------------------DKLDVPIKFLWCYASNTLINQHGDIAHTHEVLQDDSK 498
Cdd:cd02758 441 kKAYEKTSEYKRKVAAGENPYPAKrpwypltpelyteviasaaEGYPYKLKALILWMANPVYGAPGLVKQVEEKLKDPKK 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 499 CEMIVGIEHFMTASAKYCDILLPDLMPTEqedliSHESAGNMGYVI-----LGQPATSPKFERK----PIY-WT-LSEVA 567
Cdd:cd02758 521 LPLFIAIDAFINETSAYADYIVPDTTYYE-----SWGFSTPWGGVPtkastARWPVIAPLTEKTanghPVSmESfLIDLA 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 568 KRLG---------PDVYqtfteGRT---QHEWVKYL--------HAKTKarnPEMPDYEEMKQTG-------IFKKKCPE 620
Cdd:cd02758 596 KALGlpgfgpnaiKDGQ-----GNKfplNRAEDYYLrvaaniayDGKAP---VPDASEEELKLTGvnrpipaLKRTLKPE 667
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 435294959 621 E-HYVAF---RSFREDPA-----ANPLKTPSGK-IEIYSERLATLANT 658
Cdd:cd02758 668 EwRKVAYilaRGGRFAPYeesydGDNLRNRWGKtLQIWNEKLAKSRNS 715
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-810 |
9.25e-29 |
|
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: 111.57 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 688 YPLQLTGFHYKARTHSSYGNIDILQQACPQ---EIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIG 764
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQgrePIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 435294959 765 QGAWLNADMFGD--KVDRGGSINILTSHRP-SPLAKGNPSHSNLVQVEK 810
Cdd:cd02793 81 TGAWYDPDDPGEpgPLCKHGNPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
690-805 |
6.78e-28 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 108.51 E-value: 6.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 690 LQLTGFHYKARTHSSYGNIDILQQACPQE--IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGA 767
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 435294959 768 WlnadmfgdKVDRGGSINILTSHRPSPLAKGNPSHSNL 805
Cdd:pfam01568 81 W--------YEPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
102-766 |
1.02e-27 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 120.49 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 102 ACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI---GD--------NLKRI--LK--------DYGNE 160
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVvegGDlfgeghvdGLRAIrdLDtpidaknpEYGPK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 161 AVHVLYGTGVDGGNitnSNVPYRLMNACGGYL--SRYGSYSTAQISAAMSYMFGGNDGNS---PDdIANTKLVVMFGNNP 235
Cdd:PRK14991 221 ANQLLVTNASDEGR---DAFIKRFAFNSFGTRnfGNHGSYCGLAYRAGSGALMGDLDKNPhvkPD-WDNVEFALFIGTSP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 236 AEtrmSGGGvtyYVEQARERSNARM------IVIDPR---YNDTAAGREDEWLPIRPGTDGALA-AAIAWVlITEDLIDK 305
Cdd:PRK14991 297 AQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAmGMIRWI-IDNQRYNA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 306 PFLDK-------------YCigyDETTLPASAP---------RNAH----YKAYILGQGDDGI-----------AKTPQW 348
Cdd:PRK14991 370 DYLAQpgvaamqaageasWT---NATHLVIADPghprygqflRASDlglpFEGEARGDGEDTLvvdaadgelvpATQAQP 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 349 A-------------------------------------AQITSIPAEKIIQLAREIGS--AKPAYICQGwgPQRHSNGEQ 389
Cdd:PRK14991 447 ArlfveqyvtladgqrvrvksslqllkeaarklslaeySEQCGVPEAQIIALAEEFTShgRKAAVISHG--GTMSGNGFY 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 390 TARAIAMLSVLTGNVGINGGNS-----------GVRegtWDL----------GVewfsML-------------------- 428
Cdd:PRK14991 525 NAWAIMMLNALIGNLNLKGGVVvgggkfpgfgdGPR---YNLasfagkvkpkGV----SLsrskfpyeksseyrrkveag 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 429 ENPVKTQISVFTWTDAIdhGAEM-TATRDGvrgkdkLDVPIKFLWCYASNTLINQHGDIAHTHEVLQDDSKCEMIVGIEH 507
Cdd:PRK14991 598 QSPYPAKAPWYPFVAGL--LTEMlTAALEG------YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISIDA 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 508 FMTASAKYCDILLPDLmpteqedlISHES-------AGNMGYVILGQ-PATSPKFER----KPIYWT--LSEVAKRLG-P 572
Cdd:PRK14991 670 FINETTALADYIVPDT--------HTYESwgftapwGGVPTKASTARwPVVEPRTAKtadgQPVCMEsfLIAVAKRLQlP 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 573 DvyqtFTEGR---TQHEWVK-------YLHAKT------KARNPEMPDyEEMKQTG-------IFKKKCPEE-HYVAF-- 626
Cdd:PRK14991 742 G----FGDNAikdAQGNTHPlnraedfYLRGAAniaylgKTPVADASD-EDIALTGvsrilpaLQATLKPDEvRRVAFiy 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 627 -RSFREDPAA---------NPLKTPsgkIEIYSERLATLANTwelKKDEIIHPLPA-YTPGF-DGwdDPLRQRY-----P 689
Cdd:PRK14991 817 aRGGRFAPAEsaydeermgNRWKKP---LQIWNEDVAAARHS---MTGERYSGCPTwYPPRLaDG--TPLREQFpesqwP 888
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 435294959 690 LQLTGFhyKARTHSSYGN-IDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQG 766
Cdd:PRK14991 889 LLLISF--KSNLMSSMSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
118-581 |
8.46e-27 |
|
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: 115.87 E-value: 8.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 118 RLKYPMKRvgKRGEGKFERISWDEALDTIGDNLKRILKD----Y-----GNEAVHVL------YGTgvdggnitnSNVPy 182
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDraafYtsgraSNEAAYLYqlfaraYGT---------NNLP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 183 rlmNAcggylSRYGSYSTaqiSAAMSYMFGGNDGN-SPDDIANTKLVVMFGNNPAET--RMsgggvTYYVEQARERSnAR 259
Cdd:cd02767 132 ---DC-----SNMCHEPS---SVGLKKSIGVGKGTvSLEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 260 MIVIDP-------RYNDTAAGRE---------DEWLPIRPGTDGALAAAIA-WVLITED----LIDKPFLDKYCIGYDEt 318
Cdd:cd02767 195 IIVINPlrepgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAkHLIERDDepgnVLDHDFIAEHTSGFEE- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 319 tlpasaprnahYKAYILGQGDDGIAKtpqwaaqITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTARAIAMLS 398
Cdd:cd02767 274 -----------YVAALRALSWDEIER-------ASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 399 VLTGNVGING-------GNSGVrEGTWDLGVeWFSMLENPVKTQISVFTWTDAIDHGAEMTATRDGVR-GKdkldvpIKF 470
Cdd:cd02767 336 LLRGNIGRPGaglmpirGHSNV-QGDRTMGI-TEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEAALeGK------VKA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 471 LWCYASNtLINQHGDIAHTHEVLqddSKCEMIVGI------EHFMTASakyCDILLPDLMPTEQ------------EDLI 532
Cdd:cd02767 408 FISLGGN-FAEAMPDPAATEEAL---RRLDLTVHVatklnrSHLVHGE---EALILPCLGRTEIdmqaggaqavtvEDSM 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 533 S--HESAG---NMGYVILGQPA-----TSPKFERKPIYW-TLSEVAKRLGPDVYQTFTEG 581
Cdd:cd02767 481 SmtHTSRGrlkPASRVLLSEEAivagiAGARLGEAKPEWeILVEDYDRIRDEIAAVIYEG 540
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
61-571 |
1.84e-25 |
|
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: 112.76 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 61 SSCTVNCGSRCLLRLHVKDDTVYWVESDTTGNDEYGNhQVRACLRGRSIRRRMNHPDRLKYPMKRVG-KRGEGK---FER 136
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 137 ISWDEALDTIGDNLKRIL-KDYGNEAVHVLYGTGVDGGNItnsnvPYRLMNACGGYLSRYG----SYSTAQI--SAAMSY 209
Cdd:cd02760 81 ISWDEALDLVAAKLRRVReKGLLDEKGLPRLAATFGHGGT-----PAMYMGTFPAFLAAWGpidfSFGSGQGvkCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 210 MFGGNDGNSPDDIANTKL---VVMFGNNpaeTRMSGG--GVTYYVEqARERSnARMIVIDPRYNDTAAgREDEWLPIRPG 284
Cdd:cd02760 156 LYGEFWHRAFTVAADTPLanyVISFGSN---VEASGGpcAVTRHAD-ARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 285 TDGALAAAIAWVLITE---DLIDKPFL-DK----YCIGYD---------------------------ETTLPASAPRNAH 329
Cdd:cd02760 230 TDPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGPDglylrdaatgkplvwdersgravpfdtRGAVPAVAGDFAV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 330 YKAYILGQGD------------------DGIAK-TPQWAAQITSIPAEKIIQLARE------IGSA----------KPAY 374
Cdd:cd02760 310 DGAVSVDADDetaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 375 ICQGWGPQRHSNGEQTARAIAMLSVLTGNVGINGGNSG---------------VREGTWDLGVEWFSM-----------L 428
Cdd:cd02760 390 VTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGttvrlnrphddrlasVKPGEDGFMAQGFNPtdkehwvvkptG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 429 ENPVKTQISVF---TWTDAI--DHGAEMTATRDGVRGKDKLDVPIKFLWCYASNTLINqhgdIAHTHEVLQDDSKCEMIV 503
Cdd:cd02760 470 RNAHRTLVPIVgnsAWSQALgpTQLAWMFLREVPLDWKFELPTLPDVWFNYRTNPAIS----FWDTATLVDNIAKFPFTV 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435294959 504 GIEHFMTASAKYCDILLPDLMPTEQEDLISH------ESAGNMGYVILGQPATSPKFERKPIYWTLSEVAKRLG 571
Cdd:cd02760 546 SFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfvEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAKRTG 619
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
687-811 |
3.74e-24 |
|
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: 98.21 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 687 RYPLQLTGFHYKARTHSSYGNIDILQQACPQ-EIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQ 765
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 435294959 766 GAWlnADMFgdkvdRGGSINILTS----HRPSPLAKGNPSHSN-LVQVEKA 811
Cdd:cd02785 81 GWW--SRYF-----QEGSLQDLTSpfvnPVHEYIYGPNSAFYDtLVEVRKA 124
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
697-802 |
9.01e-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: 93.54 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 697 YKARTHSSY-GNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWlnadmf 774
Cdd:cd02775 1 LRDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWG------ 74
|
90 100
....*....|....*....|....*...
gi 435294959 775 gDKVDRGGSINILTSHRPSPLAKGNPSH 802
Cdd:cd02775 75 -HRGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
688-808 |
3.76e-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: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 688 YPLQLTGFHYKARTHSSYGNIDILQQACP-QEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVtAIGQG 766
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGePTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGV-VVAEG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 435294959 767 AWLNADMFGdkvdrGGSINILTSHRPSPLAKGNPSHSNLVQV 808
Cdd:cd02786 80 GWWREHSPD-----GRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
687-810 |
1.62e-15 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 73.88 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 687 RYPLQLTgfhYKART----HSSYGNIDILQQACPQ-EIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVt 761
Cdd:cd02781 1 EYPLILT---TGARSyyyfHSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 435294959 762 AIGQGAWLNADMFGDKVDRGG----SINILTSHRPS-PLAKGNPSHSNLVQVEK 810
Cdd:cd02781 77 VRAEHGWWYPEREAGEPALGGvwesNANALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
13-364 |
7.84e-15 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 78.79 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 13 SISRRSLVKTSAIGSLAlASSAFTLPfsriahAAADLASGNVAEKAVWSS--CTVnCGSRCLLRLHVKDDTVYWVESDTT 90
Cdd:PRK13532 2 KLSRRDFMKANAAAAAA-AAAGLSLP------AVANAVVGSAQTAIKWDKapCRF-CGTGCGVLVGTKDGRVVATQGDPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 91 GNDEYG-NhqvraCLRGRSIRRRMNHPDRLKYPMKRVgKRGE----GKFERISWDEALDTIGDNLKRILKDYGNEAVHVl 165
Cdd:PRK13532 74 APVNRGlN-----CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGM- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 166 YGTG---VDGGnitnsnvpY---RLMNAcgGYLS-------RYgsystAQISAAMSYM--FGGNDgnsP----DDIANTK 226
Cdd:PRK13532 147 FGSGqwtIWEG--------YaasKLMKA--GFRSnnidpnaRH-----CMASAVVGFMrtFGIDE---PmgcyDDIEAAD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 227 LVVMFGNNPAE------TRMSGggvtyyveqaRERSN--ARMIVIDP---RYNDTAagreDEWLPIRPGTDGALAAAIAW 295
Cdd:PRK13532 209 AFVLWGSNMAEmhpilwSRVTD----------RRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILNYIAN 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 296 VLITEDLIDKPFLDKYC--------IGY-----DETTLPASAPRNA---------HYKAYilgqgddgIAK-TPQWAAQI 352
Cdd:PRK13532 275 YIIQNNAVNWDFVNKHTnfrkgatdIGYglrptHPLEKAAKNPGTAgksepisfeEFKKF--------VAPyTLEKTAKM 346
|
410
....*....|..
gi 435294959 353 TSIPAEKIIQLA 364
Cdd:PRK13532 347 SGVPKEQLEQLA 358
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
96-576 |
3.64e-14 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 76.37 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 96 GNHQVRACLRGRSIRRRMNHP--DRLKYPMKRVGkrgeGKFERISWDEALDTIGDNLKRILKDYGNE---AVHVLYGTGV 170
Cdd:cd02756 93 GNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDdavFASRFDHGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 171 DGGNITNSNVPYRLMNACGGYLSR------YGSystaQISAAMSyMFGGNDGNSPDDIANTKLVVMFGNNPAETRmsggg 244
Cdd:cd02756 169 GGGFENNWGVGKFFFMALQTPFVRihnrpaYNS----EVHATRE-MGVGELNNSYEDARLADTIVLWGNNPYETQ----- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 245 VTYYVE---------------QARERSN----ARMIVIDPRYNDT------AAGREDEW-LPIRPGTDGALAAAIAwvli 298
Cdd:cd02756 239 TVYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRRTETvhaaeaAAGKDRVLhLQVNPGTDTALANAIA---- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 299 tedlidkpfldkycigydettlpasaprnahykAYILGQGDDGIAKtpqwAAQITSIPAEKIIQLA-----REIGSAKPA 373
Cdd:cd02756 315 ---------------------------------RYIYESLDEVLAE----AEQITGVPRAQIEKAAdwiakPKEGGYRKR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 374 YIC---QG--WGPQRHsngeQTARAIAMLSVLTGNVGINGGN----SGVREG---TWDLGVEWFSMLENPVKT------- 434
Cdd:cd02756 358 VMFeyeKGiiWGNDNY----RPIYSLVNLAIITGNIGRPGTGcvrqGGHQEGyvrPPPPPPPWYPQYQYAPYIdqllisg 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 435 QISVFTWTDAIDHGAEMTATRDGVRGKDKLDVPIKflwcYASNTLINQHGDIAHTHEVLQD--DSKCEMIVGIEHFMTAS 512
Cdd:cd02756 434 KGKVLWVIGCDPYKTTPNAQRLRETINHRSKLVTD----AVEAALYAGTYDREAMVCLIGDaiQPGGLFIVVQDIYPTKL 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435294959 513 AKYCDILLPDLMPTEQEDLishESAGNMGYVILGQPATSPKFERKPIYWTLSEVAKRLgPDVYQ 576
Cdd:cd02756 510 AEDAHVILPAAANGEMNET---SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI-YELYQ 569
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
689-795 |
1.35e-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: 68.56 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 689 PLQLTGFHYKARTHSSYG-NIDILQ-QACPQEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAI--G 764
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRdNLLMLRlQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMyhA 80
|
90 100 110
....*....|....*....|....*....|.
gi 435294959 765 QGAWLNADMFGDKVDRGGSINILTSHRPSPL 795
Cdd:cd02776 81 QERHVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
57-321 |
3.49e-13 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 73.70 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 57 KAVWSSCTVNC-GSrCLLRLHVKDDTVYWvESD-----TTGNDeYGNHQVRACLRGRSIRRRMNHPDRLKYPMKR----- 125
Cdd:COG5013 47 KVVRSTHGVNCtGS-CSWKVYVKDGIITW-ETQqtdypRTGPD-LPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvlle 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 126 -----------------------------VGKRGEGKFERISWDEALDTIGDNLKRILKDYGNEAVH----------VLY 166
Cdd:COG5013 124 lwreararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 167 GTGVdggnitnsnvpyRLMNACGG-YLSRYGSYstAQISAAMSYMFGgndgnspD--------DIANTKLVVMFGNNPAE 237
Cdd:COG5013 204 AAGA------------RFLSLIGGvMLSFYDWY--ADLPPASPQVWG-------EqtdvpesaDWYNSGYLIMWGSNVPQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 238 TRmsgggvT----YYVEqARERSnARMIVIDPRYNDtAAGREDEWLPIRPGTDGALAAAIAWVLITEDLIDK--PFLDKY 311
Cdd:COG5013 263 TR------TpdahFMTE-ARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDY 333
|
330
....*....|
gi 435294959 312 CIGYdeTTLP 321
Cdd:COG5013 334 ARRY--TDLP 341
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
56-115 |
6.36e-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: 63.85 E-value: 6.36e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 56 EKAVWSSCTvNCGSRCLLRLHVKDDTVYWVESDTTGNDEYGnhqvRACLRGRSIRRRMNH 115
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
688-799 |
2.08e-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: 65.39 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 688 YPLQLTGFHYKARTHSSyGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAI--G 764
Cdd:cd02780 1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENpVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 435294959 765 QGAW---------LNADMFGDK-VDRGGSINILTSHRPSPLAKGN 799
Cdd:cd02780 80 YGHWaygavastiDGKDLPGDAwRGAGVNINDIGLVDPSRGGWSL 124
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
687-797 |
1.27e-11 |
|
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: 62.14 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 687 RYPLQL-TG-----FHYKARThssyGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPG 759
Cdd:cd00508 2 EYPLVLtTGrllehWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPG 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 435294959 760 VtaigqgawLNADMFGDKVDRGGSINILTSHRPSPLAK 797
Cdd:cd00508 78 T--------VFMPFHWGGEVSGGAANALTNDALDPVSG 107
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
57-155 |
7.17e-11 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 65.25 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 57 KAVWSSCTvNCGSRCLLRLHVKDDTVYWVES--DTTGNDEYgnhqvrACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKF 134
Cdd:COG1034 216 KKTPSICP-HCSVGCNIRVDVRGGKVYRVLPreNEAVNEEW------LCDKGRFGYDGLNSPDRLTRPLVRKD----GEL 284
|
90 100
....*....|....*....|.
gi 435294959 135 ERISWDEALDTIGDNLKRILK 155
Cdd:COG1034 285 VEASWEEALAAAAEGLKALKK 305
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
116-558 |
1.23e-10 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 64.82 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 116 PDRLKYPMKRVGKRGEGKferISWDEALDTIGDNLKRIlKDYGNEAVHvlygTGVDGGNITNSnvpyrlmnACGGYLSRY 195
Cdd:cd02764 97 PDRAQGPLRRGIDGAYVA---SDWADFDAKVAEQLKAV-KDGGKLAVL----SGNVNSPTTEA--------LIGDFLKKY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 196 GSYSTAQISA--------AMSYMFGGnDGNSPDDIANTKLVVMFGNNPAETRMSG-GGVTYYVEQARERSNA---RMIVI 263
Cdd:cd02764 161 PGAKHVVYDPlsaedvneAWQASFGK-DVVPGYDFDKAEVIVSIDADFLGSWISAiRHRHDFAAKRRLGAEEpmsRLVAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 264 DPRYNDTAAGrEDEWLPIRPGTDGALAAAIAWVLITEDlidkpfldkycigydettlpASAPRNAHYKAYILgqgddgiA 343
Cdd:cd02764 240 ESVYTLTGAN-ADVRLAIRPSQEKAFALGLAHKLIKKG--------------------AGSSLPDFFRALNL-------A 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 344 KTPQWAAQITSIPAEKIIQLAREIGSAKPAYICQGwgpQRHSNGEQTARAIAM--LSVLTGNVGinggnSGVREGTwdlg 421
Cdd:cd02764 292 FKPAKVAELTVDLDKALAALAKALAAAGKSLVVAG---SELSQTAGADTQVAVnaLNSLLGNDG-----KTVDHAR---- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 422 vewfSMLENPVKTQISVFTWTDAIDHGAemtatrdgvrgkdkldvpIKFLWCYASNtLINQHGDIAHTHEVLqddSKCEM 501
Cdd:cd02764 360 ----PIKGGELGNQQDLKALASRINAGK------------------VSALLVYDVN-PVYDLPQGLGFAKAL---EKVPL 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 435294959 502 IVGIEHFMTASAKYCDILLPDLMPTEQEDlishESAGNMGYVILGQPATSPKFERKP 558
Cdd:cd02764 414 SVSFGDRLDETAMLCDWVAPMSHGLESWG----DAETPDGTYSICQPVIAPLFDTRS 466
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
56-115 |
1.44e-10 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 57.26 E-value: 1.44e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 56 EKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGNDEYGNHQVRACLRGRSIRRRMNH 115
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
687-811 |
4.92e-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: 57.97 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 687 RYPLQL-TG-----FHYKARThssyGNIDILQQACPQ-EIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPG 759
Cdd:cd02791 2 EYPLWLnTGrvrdqWHTMTRT----GRVPRLNAHVPEpYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 435294959 760 VtaigqgawLNADMF-GDKVDRGGSINILTSHRPSPLAKGNPSHSNLVQVEKA 811
Cdd:cd02791 78 E--------VFVPMHwGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
688-761 |
2.52e-09 |
|
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: 55.71 E-value: 2.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 435294959 688 YPLQL-TG---FHYKARTHSsyGNIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVT 761
Cdd:cd02790 3 YPLVLtTGrvlYHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
701-810 |
4.33e-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: 54.97 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 701 THSSYGNIDILQQACP-QEIWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAI--GQGAWlnADMFGDK 777
Cdd:cd02778 13 THGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGFGHW--APALSRA 90
|
90 100 110
....*....|....*....|....*....|...
gi 435294959 778 VDRGGSINILTSHRPSPLAKGNPSHSNLVQVEK 810
Cdd:cd02778 91 YGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
721-811 |
1.18e-08 |
|
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: 53.94 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 721 INPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNA-DMFGDKVDRGGSINILTSHRP-SPLAkG 798
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpGVSGAGSRPGVNVNDLTDDTQrDPLS-G 115
|
90
....*....|....
gi 435294959 799 NPSHSNL-VQVEKA 811
Cdd:cd02782 116 NAAHNGVpVRLARV 129
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
63-303 |
1.66e-08 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 57.55 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 63 CTVnCGSRCllrlhvkDDTVYWVEsdttgndeyGNHQV---RACLRGRSIRRRMNHPDRLKYPMKRvgkrgegkFERISW 139
Cdd:COG1029 10 CPF-CGCLC-------DDLEVEVE---------GGKIVvvkNACAIGAAKFERAVSDHRITSPRIR--------GKEVSL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 140 DEALDTIGdnlkRILKdygnEAVHVLYGtgvdGGNITNSN---VPYRLMNACGGYLSrygsySTAQISAAMSYMFGGNDG 216
Cdd:COG1029 65 EEAIDKAA----EILA----NAKRPLIY----GLSSTDCEamrAGLALAERVGAVVD-----NTASVCHGPSLLALQDVG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 217 NSPDDIANTK----LVVMFGNNPAET------RMSGGGVTYYVEQARERSnaRMIVIDPRYNDTAAgREDEWLPIRPGTD 286
Cdd:COG1029 128 WPTCTLGEVKnradVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGRKDR--TVIVVDPRPTDTAK-VADLHLQVKPGRD 204
|
250
....*....|....*..
gi 435294959 287 GALAAAIAWVLITEDLI 303
Cdd:COG1029 205 YEVLSALRALVRGKELS 221
|
|
| 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 ... |
61-521 |
3.45e-08 |
|
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: 56.63 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 61 SSCTvNCGSRCLLRLHVKDDTVYWVESDTTGN-DEYGNhqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISW 139
Cdd:cd02771 2 SICH-HCSVGCNISLGERYGELRRVENRYNGAvNHYFL-----CDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 140 DEALDTIGDnlkrILKDYGNEAVhvlygtGVDGGNITN-SNvpYRLMNACGGYL--------SRYGSYSTAQISAAMSym 210
Cdd:cd02771 72 NEALDVAAA----RLKEAKDKVG------GIGSPRASNeSN--YALQKLVGAVLgtnnvdhrARRLIAEILRNGPIYI-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 211 fggndgNSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAGREDewLPIRPGTDGALA 290
Cdd:cd02771 138 ------PSLRDIESADAVLVLGEDLTQT---APRIALALRQAARRKAVELAALSGIPKWQDAAVRN--IAQGAKSPLFIV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 291 AAIAWVL--ITEDLIdkpfldkYCIGYDETTLPASAPRnahykayilgqgddgiAKTPQWAAQITSIPAEKIIQLAREIG 368
Cdd:cd02771 207 NALATRLddIAAESI-------RASPGGQARLGAALAR----------------AVDASAAGVSGLAPKEKAARIAARLT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 369 SAKPAYICQGwgpqRHSNGEQTARAIAMLSVLTGNVGINGGNSGVREGTWDLGVewfSMLENPV-KTQISVftwtDAIDH 447
Cdd:cd02771 264 GAKKPLIVSG----TLSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGL---LLLGGHVtEPGLDL----DGALA 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 435294959 448 GAEmtatrDGvrGKDKLDVPIKFLWCYASNTlinqhgdiahthEVLQDDSKCEMIVGIEHFMTASAKYCDILLP 521
Cdd:cd02771 333 ALE-----DG--SADALIVLGNDLYRSAPER------------RVEAALDAAEFVVVLDHFLTETAERADVVLP 387
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
65-238 |
4.65e-07 |
|
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: 53.06 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 65 VNCGSRCLLRLHVKDDTVYWVESDTtgndeygNHQVRACL---RGR----SIrrrmNHPDRLKYPMKRVGkrgeGKFERI 137
Cdd:cd02768 5 VHDALGSNIRVDVRGGEVMRILPRE-------NEAINEEWisdKGRfgydGL----NSRQRLTQPLIKKG----GKLVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 138 SWDEALDTIGDNLKRILKDygneAVHVLYGTGVDggniTNSNVPY-RLMNACG----GYLSRYGSYSTAQISAAMSYMfg 212
Cdd:cd02768 70 SWEEALKTVAEGLKAVKGD----KIGGIAGPRAD----LESLFLLkKLLNKLGsnniDHRLRQSDLPADNRLRGNYLF-- 139
|
170 180
....*....|....*....|....*.
gi 435294959 213 gndGNSPDDIANTKLVVMFGNNPAET 238
Cdd:cd02768 140 ---NTSIAEIEEADAVLLIGSNLRKE 162
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
687-790 |
1.77e-06 |
|
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: 47.60 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 687 RYPLQLTG------FHYKARTHSSYGnidiLQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPG 759
Cdd:cd02792 2 EFPLVLTTgrltehFHGGNMTRNSPY----LAELQPEMfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPH 77
|
90 100 110
....*....|....*....|....*....|.
gi 435294959 760 VTAIgqgAWLNADMFGDKvdrGGSINILTSH 790
Cdd:cd02792 78 EVGI---PYHWGGMGLVI---GDSANTLTPY 102
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
719-771 |
2.66e-06 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 47.15 E-value: 2.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 435294959 719 IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNA 771
Cdd:COG1153 33 CELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPWANA 85
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
719-771 |
3.50e-06 |
|
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: 46.26 E-value: 3.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 435294959 719 IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLNA 771
Cdd:cd02789 33 CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPWANV 85
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
113-165 |
1.35e-05 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 48.50 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 435294959 113 MNHPDRLKYPMKRVGkrgeGKFERISWDEALDTIGDNLKRILKDYGNEAVHVL 165
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
63-414 |
1.93e-04 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 44.63 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 63 CTVnCGSRCllrlhvkDDTVywVESDTTGNDEYGNhqvrACLRGRSIRRRMNHpdRLKYPMKRvgkrgegkFERISWDEA 142
Cdd:cd02761 4 CPF-CGLLC-------DDIE--VEVEDNKITKVRN----ACRIGAAKFARYER--RITTPRID--------GKPVSLEEA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 143 LDTIGdnlkRILKdygnEAVH-VLYGTGVDGGNITNsnVPYRLMNACGGYLSRYGSysTAQISAAMSYMFGGNDGNSPDD 221
Cdd:cd02761 60 IEKAA----EILK----EAKRpLFYGLGTTVCEAQR--AGIELAEKLGAIIDHAAS--VCHGPNLLALQDSGWPTTTLGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 222 IAN-TKLVVMFGNNPAET------RMSGGGVTYYVEQARERSnaRMIVIDPRYNDTAAGReDEWLPIRPGTDGALAAAIA 294
Cdd:cd02761 128 VKNrADVIVYWGTNPMHAhprhmsRYSVFPRGFFREGGREDR--TLIVVDPRKSDTAKLA-DIHLQIDPGSDYELLAALR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435294959 295 WVLITEDLIDKPfldkycigydettlpasaprnahykayilgqgddgiaktpqwaaqITSIPAEKIIQLAREIGSAKPAY 374
Cdd:cd02761 205 ALLRGAGLVPDE---------------------------------------------VAGIPAETILELAERLKNAKFGV 239
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 435294959 375 ICQGWG----PQRHSNGEQTARAIAMLSVLTGNVGIN-GGNSGVR 414
Cdd:cd02761 240 IFWGLGllpsRGAHRNIEAAIRLVKALNEYTKFALLPlRGHYNVR 284
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
707-770 |
2.39e-04 |
|
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: 41.29 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 435294959 707 NIDILQQACPQE-IWINPIDAQARGIQHGDTVRVFNQNGEMLILAKVTPRILPGVTAIGQGAWLN 770
Cdd:cd02779 22 NNSEIAERVPLPyIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPRP 86
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