|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-814 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1852.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
Cdd:PRK14990 1 MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 81 EIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
Cdd:PRK14990 81 EIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 161 ESIYLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGN 240
Cdd:PRK14990 161 ESIYLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCV 320
Cdd:PRK14990 241 NPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
Cdd:PRK14990 321 GYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
Cdd:PRK14990 401 ISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
Cdd:PRK14990 481 YAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 561 FECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQA 640
Cdd:PRK14990 561 FECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 641 NPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAAC 720
Cdd:PRK14990 641 NPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAAC 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 721 RQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCINVLTTQRPSPLAK 800
Cdd:PRK14990 721 RQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCINVLTTQRPSPLAK 800
|
810
....*....|....
gi 90111183 801 GNPSHTNLVQVEKV 814
Cdd:PRK14990 801 GNPSHTNLVQVEKV 814
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
14-814 |
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: 1567.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 14 VSRRGLVKT-TAIGGLAMASSALTLPFSRiaHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNTGD 92
Cdd:TIGR02166 1 ISRRHFLKTsAALGGLAAASGALSLPFSV--NAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 93 DNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTL 172
Cdd:TIGR02166 79 DEY-GNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 173 GGTMTRSWPPgnTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGV 252
Cdd:TIGR02166 158 GGTMSRSWPP--TAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYGISADGSSLDDIENSKLVVMFGNNPAETRMSGGGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 253 TYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEKTLPASAP 332
Cdd:TIGR02166 236 TYYFLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 333 KNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVG 412
Cdd:TIGR02166 316 KNGSYKDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 413 INGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSE 492
Cdd:TIGR02166 396 IKGGNNGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 493 INRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSE 572
Cdd:TIGR02166 476 INRTHKILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 573 LAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEI 652
Cdd:TIGR02166 556 VAKRLGVEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEI 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 653 YSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLDAQ 732
Cdd:TIGR02166 636 YSERLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQ 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 733 KRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVE 812
Cdd:TIGR02166 716 KRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPDKNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVE 795
|
..
gi 90111183 813 KV 814
Cdd:TIGR02166 796 KA 797
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
60-685 |
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: 1082.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 60 WSACTVNCGSRCPLRMHVVDGEIKYVETDNTGDDnYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERIS 139
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDD-DPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 140 WEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTmtrswPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGG 219
Cdd:cd02770 80 WDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGV-----PAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 220 WADGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYYLEQARQkSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNG 299
Cdd:cd02770 155 AASGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAKK-AGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 300 LAYVMITENLVDQAFLDKYCVGYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKP 379
Cdd:cd02770 234 MAYVMITENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 380 AFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMT 459
Cdd:cd02770 314 AAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 460 ALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSEIN-RTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDF 538
Cdd:cd02770 394 ADDGGVKGADKLKSNIKMIWNYAGNTLINQHSDDNnTTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDI 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 539 ALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGI 618
Cdd:cd02770 474 VLTSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGI 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111183 619 FKKRDPqGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATweLPEGDVIDPLPIYTPGFESY 685
Cdd:cd02770 554 YRVPRA-LPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEGP 617
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
60-685 |
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: 804.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 60 WSACTvncgsRCPLRMHVVDGEIKYVETDNTgddnydglHQVRACLRGRSMRRRVYNPDRLKYPMKRVG----------A 129
Cdd:cd02751 1 PTACH-----WGPFKAHVKDGVIVRVEPDDT--------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGwlgngpgsreL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 130 RGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGtmtrSWPPGNTLVARLMNCCGGYLNHYGDYSSAQI 209
Cdd:cd02751 68 RGEGEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAG----RLHHAQSLLHRFLNLIGGYLGSYGTYSTGAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 210 AEGLNYTYGGWAD---GNSPSDI-ENSKLVVLFGNNPGETRMSGGGV-----TYYLEQARQkSNARMIIIDPRYTDTGAG 280
Cdd:cd02751 144 QVILPHVVGSDEVyeqGTSWDDIaEHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKD-AGVRFICIDPRYTDTAAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 281 REDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktlpasapknghYKAYILGEgPDGVAKTPEWASQIT 360
Cdd:cd02751 223 LAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLGE-SDGVPKTPEWAAEIT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 361 GVPADKIIKLAREIGStKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSL--------PFVRM 432
Cdd:cd02751 290 GVPAETIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGggpprggaGGPGL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 433 PTLENPIQTSISMFMWTDAIER-GPEMTAlrdgvRGKDKLDVPIKMIWNYAGNCLINQHSeINRTHEILQDDkkcELIVV 511
Cdd:cd02751 369 PQGKNPVKDSIPVARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQD-LNRLIKALRKD---ETIVV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 512 IDCHMTSSAKYADILLPDCTASEQMDFALDASCgNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEE 591
Cdd:cd02751 440 HDIFWTASARYADIVLPATTSLERNDIGLTGNY-SNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEME 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 592 WMRHLYAQSREAI----PELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAatwelp 667
Cdd:cd02751 519 WLEHLYEETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFG------ 592
|
650
....*....|....*...
gi 90111183 668 eGDVIDPLPIYTPGFESY 685
Cdd:cd02751 593 -YDDCPGHPTWIEPWEGL 609
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
43-814 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 743.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 43 AHAVDSAIPTKSDEKVIWSACTvNCGSRCPLRMHVVDGEIKYVETDNTGDDNydglhQVRACLRGRSMRRRVYNPDRLKY 122
Cdd:COG0243 8 AAGAGAAALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVRGDPDHPVN-----RGRLCAKGAALDERLYSPDRLTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 123 PMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYL-NYGTGTLGGTMTRSWppgntLVARLMNCCgGYLNHY 201
Cdd:COG0243 82 PMKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFyTSGGSAGRLSNEAAY-----LAQRFARAL-GTNNLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 202 --GDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETrmsGGGVTYYLEQARQKSNARMIIIDPRYTDTgA 279
Cdd:COG0243 156 dnSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTET-A 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 280 GREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktlpasapknghYKAYIlgegpdgVAKTPEWASQI 359
Cdd:COG0243 232 AIADEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 360 TGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGsyslpfvrmptlenpi 439
Cdd:COG0243 293 TGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG---------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 440 qtsismfmwtDAIERGpemtalrdgvrgkdkLDVPIKMIWNYAGNCLiNQHSEINRTHEILQddkKCELIVVIDCHMTSS 519
Cdd:COG0243 357 ----------EAILDG---------------KPYPIKALWVYGGNPA-VSAPDTNRVREALR---KLDFVVVIDTFLTET 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 520 AKYADILLPDCTASEQMDFaldASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQ 599
Cdd:COG0243 408 ARYADIVLPATTWLERDDI---VTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLEA 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 600 SReaiPELPTFEEFRKQGIFKKRDPQGHhvaykAFREDpqaNPLTTPSGKIEIYSQALAdiaatwelpegdvIDPLPIYT 679
Cdd:COG0243 485 TR---GRGITFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYA 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 680 PGFESyQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQE-MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVT 758
Cdd:COG0243 541 PPYEG-AEPLDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVT 619
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 90111183 759 PRMMPGVVALGEGAWYDPDAkrvDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
Cdd:COG0243 620 EGIRPGVVFAPHGWWYEPAD---DKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
113-813 |
1.55e-163 |
|
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares sequence similarity and a requirement for a molydenum cofactor as the only prosthetic group. The form of the cofactor is a single molybdenum atom coordinated by two molybdopterin guanine dinucleotide molecules. Members of the family include biotin sulfoxide reductase, dimethylsulfoxide reductase, and trimethylamine-N-oxide reductase, although a single member may show all those activities and related activities; it may not be possible to resolve the primary function for members of this family by sequence comparison alone. A number of similar molybdoproteins in which the N-terminal region contains a CXXXC motif and may bind an iron-sulfur cluster are excluded from this set, including formate dehydrogenases and nitrate reductases. Also excluded is the A chain of a heteromeric, anaerobic DMSO reductase, which also contains the CXXXC motif.
Pssm-ID: 273110 [Multi-domain] Cd Length: 770 Bit Score: 493.51 E-value: 1.55e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 113 RVYNPDRLKYPMKRVG-----------ARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnygtgtlggTMTRSW- 180
Cdd:TIGR00509 38 QVYSESRIKYPMVRKGflengvksdrsGRGREEFVRVSWDEALDLVAEELKRVRKTHGPSAIF----------AGSYGWk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 181 PPG-----NTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNS----PSDIENSKLVVLFGNNPGETRMSGGG 251
Cdd:TIGR00509 108 SAGrlhnaSTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQqttwPVILENSEVLVLWGADPLKTSQIAWG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 252 VT-----YYLEQARqKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEkt 326
Cdd:TIGR00509 188 IPdhggyEYLERLK-AKGKRVISIDPVRTETVEFFGAEWIPPNPQTDVALMLGLAHTLVTEGLYDKDFLAKYTSGFEK-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 327 lpasapknghYKAYILGEGpDGVAKTPEWASQITGVPADKIIKLAREIGSTKpAFISQGWGPQRHANGEIATRAISMLAI 406
Cdd:TIGR00509 265 ----------FLPYLLGET-DGTPKTAEWASKITGVPAETIKELARLFASKR-TMLAAGWSMQRMQHGEQPHWMLVTLAA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 407 LTGNVGINGGNSGAregSYS-----LPF---VRMPTLENPIqtSISMFMWTDA-------IERGPEMTaLRDGVR----G 467
Cdd:TIGR00509 333 MLGQIGLPGGGFGF---SYHysgggTPSasgPALSQGSNSV--SSTAGPEWDDgsasvipVARISDAL-LNPGKEidynG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 468 KDKLDVPIKMIWNYAGNcLINQHSEINRTHEILQddkKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNM 547
Cdd:TIGR00509 407 KELKLPDIKMVYWAGGN-PFHHHQDTNRLIKAWR---KLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTMAGDYSNT 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 548 SyVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLY----AQSREAIPELPTFEEFRKQGIFKKRD 623
Cdd:TIGR00509 483 G-ILAMKQVVPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYekaaKQAKADGVEMPAFDAFWAEGIVEFPV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 624 PQGH-HVAYKAFREDPQANPLTTPSGKIEIYSQALADIA-------ATWELPEgdvidplpiytpgfESYQDPLNKQYPL 695
Cdd:TIGR00509 562 PEGAdFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGyddcpghPTWMEPA--------------EWLGGPRGAKYPL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 696 QLTGFHYKSRVHSTYGNVDVLKA---ACRQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGA 772
Cdd:TIGR00509 628 HLISPHPKYRLHSQLDHTELRQAykvQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGA 707
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 90111183 773 WYDPDAKRV----DKGGCINVLTTQRP-SPLAKGNPSHTNLVQVEK 813
Cdd:TIGR00509 708 WYDPADVREpgglCKYGNPNVLTADIGtSSLAQGNSGNTVLVEIEK 753
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
72-659 |
3.62e-142 |
|
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: 432.84 E-value: 3.62e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 72 PLRMHVVDGEIKYVETDntgDDNYDGLHQvraclrGRSMRRRVYNPDRLKYPMKRVG-----------ARGEGKFERISW 140
Cdd:cd02769 8 AFRARVKDGRIVGVRPF---EEDPDPSPL------LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 141 EEAYDIIATNMQRLIKEYGNESIYL-NYgtgtlggtmtrSW-PPGN-----TLVARLMNCCGGYLNHYGDYSSAQIAEGL 213
Cdd:cd02769 79 DEALDLVAAELKRVRKTYGNEAIFGgSY-----------GWsSAGRfhhaqSLLHRFLNLAGGYVGSVGDYSTGAAQVIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 214 NYTYGGWADGNS-----PSDIENSKLVVLFGNNPGETRMSGGGVT------YYLEQARQKsNARMIIIDPRYTDTGAGRE 282
Cdd:cd02769 148 PHVVGSMEVYTEqqtswPVIAEHTELVVAFGADPLKNAQIAWGGIpdhqaySYLKALKDR-GIRFISISPLRDDTAAELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 283 DEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktlpasapknghYKAYILGEGpDGVAKTPEWASQITGV 362
Cdd:cd02769 227 AEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDK------------FLPYLLGES-DGVPKTPEWAAAICGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 363 PADKIIKLAREIGSTKpAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGG--------NSGAREGSYSLPFVRMPT 434
Cdd:cd02769 294 PAETIRELARRFASKR-TMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 435 LENPIQTSISMFMWTDAIERgPEMTALRDGVRgkdkLDVP-IKMIWNyAGNCLINQHSEINRTHEILQddkKCELIVVID 513
Cdd:cd02769 373 GRNPVSSFIPVARIADMLLN-PGKPFDYNGKK----LTYPdIKLVYW-AGGNPFHHHQDLNRLIRAWQ---KPETVIVHE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 514 CHMTSSAKYADILLPDCTASEQMDFAldaSCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWM 593
Cdd:cd02769 444 PFWTATARHADIVLPATTSLERNDIG---GSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWL 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 594 RHLYAQSREAI----PELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALAD 659
Cdd:cd02769 521 RHLYEESRAQAaargVEMPSFDEFWAQGYVELPIPEADFVRLADFREDPEANPLGTPSGRIEIFSETIAG 590
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
14-813 |
1.32e-122 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 388.65 E-value: 1.32e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 14 VSRRGLVK-TTAIGGLAMASSALTLPFSriAHAVDSAIPTKSDEKVI----WSActvncgsrcpLRMHVVDG---EIKYV 85
Cdd:PRK15102 1 ASRRRFLKgLGGLSAAGMLGPSLLTPRS--ALAAQAAAAETTKEWILtgshWGA----------FRAKVKNGrfvEAKPF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 86 ETDNTGDDNYDGLHQVraclrgrsmrrrVYNPDRLKYPMKRV-----------GARGEGKFERISWEEAYDIIATNMQRL 154
Cdd:PRK15102 69 ELDKYPTKMINGIKGH------------VYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 155 IKEYGNESIYlnygtgtlggtmtrswpPGNT---LVARLMNCC----------GGYLNHYGDYSSAQIAEGLNYTYGG-- 219
Cdd:PRK15102 137 QKTYGPSALH-----------------TGQTgwqSTGQFHSATghmqraigmhGNSVGTVGDYSTGAGQVILPYVLGSte 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 220 -WADGNS-PSDIENSKLVVLFGNNP---------GETRMSGGgvtyYLEQARQK---SNARMIIIDPRYTDTGAGREDEW 285
Cdd:PRK15102 200 vYEQGTSwPLILENSKTIVLWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 286 IPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEkTLPasapknghykaYILGEgPDGVAKTPEWASQITGVPAD 365
Cdd:PRK15102 276 LYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 366 KIIKLAREIGSTKPAFISqGWGPQRHANGEIATRAISMLAILTGNVGINGG---------------NSGAREGSYSLpfv 430
Cdd:PRK15102 343 TIRELARQMAKGRTQIIA-GWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhysgigvpsSGGAIPGGFPG--- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 431 RMPTLENPIQTS---------ISMFMWTDAI-ERGPEMTAlrdgvRGKDKLDVPIKMIWnYAGNCLINQHSEINRTHEIL 500
Cdd:PRK15102 419 NLDTGQKPKHDNsdykgysstIPVARFIDAIlEPGKTINW-----NGKKVTLPPLKMMI-FSGTNPWHRHQDRNRMKEAF 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 501 QddkKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSyVIFNDQVIKPRFECKTIYEMTSELAKRLGVE 580
Cdd:PRK15102 493 R---KLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGRE 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 581 QQFTEGRTQEEWMRHLYAQSR---EAIPELPTFEEFRKQGI--FKKRDPQGHHvayKAFREDPQANPLTTPSGKIEIYSQ 655
Cdd:PRK15102 569 KEYTRGMDEMGWLKRLYQECKqqnKGKFHMPEFDEFWKKGYveFGEGQPWVRH---ADFREDPELNPLGTPSGLIEIYSR 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 656 ALADIAatWELPEGDvidplPIYTPGFE-SYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKA----ACRQEMWINPLD 730
Cdd:PRK15102 646 KIADMG--YDDCQGH-----PMWFEKIErSHGGPGSDKYPLWLQSVHPDKRLHSQLCESEELREtytvQGREPVYINPQD 718
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 731 AQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD----AKRVDKGGCINVLTTQRP-SPLAKGNPSH 805
Cdd:PRK15102 719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDkggeIGALCTYGDPNTLTLDIGtSQLAQATSAH 798
|
....*...
gi 90111183 806 TNLVQVEK 813
Cdd:PRK15102 799 TCLVEIEK 806
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-677 |
4.87e-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: 350.78 E-value: 4.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 61 SACTVNCGSRCPLRMHVVDGEIKYVEtdntGDDNydglHQVRA---CLRGRSMRRRVYNPDRLKYPMKRVGARGeGKFER 137
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVE----GDPA----HPYTRgfiCAKGARYVERVYSPDRLLTPLKRVGRKG-GQWER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 138 ISWEEAYDIIATNMQRLIKEYGNESI-YLNYGtgtlggtmtrswppGN-TLVARLMnccGGYLNHYGDYSSAQ--I---- 209
Cdd:cd02766 73 ISWDEALDTIAAKLKEIKAEYGPESIlPYSYA--------------GTmGLLQRAA---RGRFFHALGASELRgtIcsga 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 210 -AEGLNYTYGGwADGNSPSDIENSKLVVLFGNNPGETRMSGggvTYYLEQARQKsNARMIIIDPRYTDTgAGREDEWIPI 288
Cdd:cd02766 136 gIEAQKYDFGA-SLGNDPEDMVNADLIVIWGINPAATNIHL---MRIIQEARKR-GAKVVVIDPYRTAT-AARADLHIQI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 289 RPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktlpasapknghYKAYILgegpdgvAKTPEWASQITGVPADKII 368
Cdd:cd02766 210 RPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 369 KLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGnsGAREGSYslpfvrmptlenpiqtsismfmw 448
Cdd:cd02766 271 ELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGG--GAFYSNS----------------------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 449 tdaierGPemtalrdgvrgkdkldvPIKMIWNYAGNcLINQHSEINRTHEILQDDkkCELIVVIDCHMTSSAKYADILLP 528
Cdd:cd02766 326 ------GP-----------------PVKALWVYNSN-PVAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLP 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 529 DCTASEQMDfaLDASCGNmSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEgRTQEEWMRHLYaqsreAIPELP 608
Cdd:cd02766 380 ATTFLEHED--VYASYWH-YYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFE-ESDEEWLDQAL-----DGTGLP 450
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 609 TFEEfrkqgifkKRDPQGHHVAyKAFREDPQANP-LTTPSGKIEIYSQaladIAATWELPegdvidPLPI 677
Cdd:cd02766 451 LEGI--------DLERLLGPRK-AGFPLVAWEDRgFPTPSGKFEFYSE----RAAKRGLP------PLPE 501
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
60-577 |
8.28e-102 |
|
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: 319.66 E-value: 8.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 60 WSACTVnCGSRCPLRMHVVDGEIKYVEtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGarGEGKFERIS 139
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIE----GDPNHP-VNEGRLCDKGRAGLDGLYSPDRLKYPLIRVG--GRGKFVPIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 140 WEEAYDIIATNMQRLIKEYGNESIYLNYGtgtlggtmtrSWPPGNTLVA---RLMNCCGGYLNHYGDYSSAQIAEGLNYT 216
Cdd:cd00368 73 WDEALDEIAEKLKEIREKYGPDAIAFYGG----------GGASNEEAYLlqkLLRALGSNNVDSHARLCHASAVAALKAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 217 YGGWaDGNSPSDIENSKLVVLFGNNPGETRMSgggVTYYLEQARQKsNARMIIIDPRYTDTgAGREDEWIPIRPGTDAAL 296
Cdd:cd00368 143 GGGA-PTNTLADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTET-AAKADEWLPIRPGTDAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 297 VNGlayvmitenlvdqafldkycvgydektlpasapknghykayilgegpdgvaktpEWASQITGVPADKIIKLAREIGS 376
Cdd:cd00368 217 ALA------------------------------------------------------EWAAEITGVPAETIRALAREFAA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 377 TKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGARegsyslpfvrmptlENPIQTSismfmwtdaiergp 456
Cdd:cd00368 243 AKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA-------------- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 457 emtalrdgvrgkdkldvpikmiwnyagnclinqhseiNRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQm 536
Cdd:cd00368 295 -------------------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEK- 336
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 90111183 537 dfalDASCGNM-SYVIFNDQVIKPRFECKTIYEMTSELAKRL 577
Cdd:cd00368 337 ----EGTYTNTeGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-668 |
1.51e-95 |
|
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: 309.79 E-value: 1.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 61 SACTVNCGSRCPLRMHVVDGEIKYVETDNTGDDNYDglhqvRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISW 140
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPNEWPDKTYK-----RGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 141 EEAYDIIATNMQRLIKEYGNESIylnygtgtlggtmTRSWPPGN--TLVARLMNCCGGylNHYGDYSSA---QIAEGLNY 215
Cdd:cd02765 77 DEALDTIADKLTEAKREYGGKSI-------------LWMSSSGDgaILSYLRLALLGG--GLQDALTYGidtGVGQGFNR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 216 TYGG--WADGNSPSDIENSKLVVLFGNNPGETRMSGggvTYYLEQARQKSnARMIIIDPRYTDTgAGREDEWIPIRPGTD 293
Cdd:cd02765 142 VTGGgfMPPTNEITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTT-AAKADQWVPIRPGTD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 294 AALVNGLAYVMITENLVDQAFLDKYC-----VGYDEKTL--PASAPKNGHYKAYIL---------------------GE- 344
Cdd:cd02765 217 PALALGMINYILEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVwdtnsdspepvaatninpaleGEy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 345 GPDGV--------------AKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGN 410
Cdd:cd02765 297 TINGVkvhtvltalreqaaSYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 411 VGINGGNSGAregsyslpfvrmptlenpiqtsismfmwtdaiergpemtalrdgvrgkdkldvpIKMIWNyAGNCLINQH 490
Cdd:cd02765 377 IGRVGGGVGQ------------------------------------------------------IKFMYF-MGSNFLGNQ 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 491 SEINRTHEILqddKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNmsYVIFNDQVIKPRFECKTIYEMT 570
Cdd:cd02765 402 PDRDRWLKVM---KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIE 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 571 SELAKRLGVEQQFTEgrTQEEWMRhLYAQSREAIPELPTFEEFRKQGIFKKRD-PQGHHVAYK--AFRedpqanpltTPS 647
Cdd:cd02765 477 KGLAERLGLGDYFPK--TPEDYVR-AFMNSDDPALDGITWEALKEEGIIMRLAtPEDPYVAYLdqKFG---------TPS 544
|
650 660
....*....|....*....|.
gi 90111183 648 GKIEIYSQALADIAATWELPE 668
Cdd:cd02765 545 GKLEFYNEAAPELEEALPLPE 565
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
67-680 |
8.44e-92 |
|
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: 296.91 E-value: 8.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 67 CGSRCPLRMHVVDGEIKYVETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDI 146
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRL-----CMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 147 IATNMQRLIKEYGNESIylnYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLnYTYGGWADGNsp 226
Cdd:cd02759 82 IAEKLAEIKAEYGPESI---ATAVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGESCYWPRDMAHAL-TTGFGLGYDE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 227 SDIENSKLVVLFGNNPgeTRMSGGGVTYYLEQARqKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMIT 306
Cdd:cd02759 156 PDWENPECIVLWGKNP--LNSNLDLQGHWLVAAM-KRGAKLIVVDPRLTWL-AARADLWLPIRPGTDAALALGMLNVIIN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 307 ENLVDQAFLDKYCVGYDEktlpasapknghYKAYilgegpdgVAK-TPEWASQITGVPADKIIKLAREIGSTKPAFISQG 385
Cdd:cd02759 232 EGLYDKDFVENWCYGFEE------------LAER--------VQEyTPEKVAEITGVPAEKIRKAARLYATAKPACIQWG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 386 WGPQRHANGEIATRAISMLAILTGNVGINGGNsgaREGSYslpfvrmptlenpiqtsismfmwtdaiergpemtalrdgv 465
Cdd:cd02759 292 LAIDQQKNGTQTSRAIAILRAITGNLDVPGGN---LLIPY---------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 466 rgkdkldvPIKMIWNYAGNCLINQHSEINrtheILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCG 545
Cdd:cd02759 329 --------PVKMLIVFGTNPLASYADTAP----VLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAE 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 546 NMSYVIfnDQVIKPRFECKTIYEMTSELAKRLGVEQQftegrtqeewmrhlyaqsreaipelptfeEFRKqgiFKKRDPq 625
Cdd:cd02759 397 NFVQLR--QKAVEPYGEAKSDYEIVLELGKRLGPEEA-----------------------------EYYK---YEKGLL- 441
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 90111183 626 ghhvaykafREDPQAnPLTTPSGKIEIYSQALADIAAtwelpegdviDPLPIYTP 680
Cdd:cd02759 442 ---------RPDGQP-GFNTPTGKVELYSTMLEELGY----------DPLPYYRE 476
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
61-800 |
7.73e-91 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 300.26 E-value: 7.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 61 SACTVnCGSRCPLRMHVVDGEIKYVETDNTGDDNyDGlhqvRACLRGRSMRRRVYNPDRLKYPMKRVGargeGKFERISW 140
Cdd:COG3383 9 TVCPY-CGVGCGIDLEVKDGKIVKVEGDPDHPVN-RG----RLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 141 EEAYDIIATNMQRLIKEYGNESIYL----------NYgtgtlggtmtrswppgntLVARLMNCCGGyLNHYgDY------ 204
Cdd:COG3383 79 DEALDLVAERLREIQAEHGPDAVAFygsgqltneeNY------------------LLQKLARGVLG-TNNI-DNnarlcm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 205 SSAqiAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETrmsgggVTYYLEQARQKsNARMIIIDPRYTDTgAGREDE 284
Cdd:COG3383 139 ASA--VAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTET-ARLADL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 285 WIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktlpasapknghYKAYILGEgpdgvakTPEWASQITGVPA 364
Cdd:COG3383 212 HLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 365 DKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING---------GNS-GARE-GSYS--LPFVR 431
Cdd:COG3383 273 EDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGtgpfpltgqNNVqGGRDmGALPnvLPGYR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 432 MptLENPIQTSISMFMW-TDAIERGPEMTA--LRDGV-RGKdkldvpIKMIWNYAGNcLINQHSEINRTHEILqddKKCE 507
Cdd:COG3383 353 D--VTDPEHRAKVADAWgVPPLPDKPGLTAveMFDAIaDGE------IKALWIIGEN-PAVSDPDANHVREAL---EKLE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 508 LIVVIDCHMTSSAKYADILLPDCTASEQ------MDfaldascGNMSYVifnDQVIKPRFECKTIYEMTSELAKRLGVEQ 581
Cdd:COG3383 421 FLVVQDIFLTETAEYADVVLPAASWAEKdgtftnTE-------RRVQRV---RKAVEPPGEARPDWEIIAELARRLGYGF 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 582 QFTegrtqeewmrhlyaqSREAIpelptFEEFRK-----QGIFKKRDPQGHHVAYKAFREDPQANPL------TTPSGKI 650
Cdd:COG3383 491 DYD---------------SPEEV-----FDEIARltpdySGISYERLEALGGVQWPCPSEDHPGTPRlftgrfPTPDGKA 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 651 EIysqaladIAATWELPEgdvidplpiytpgfesyqDPLNKQYPLQL-TG---FHYKSRVHStyGNVDVLKAACRQE-MW 725
Cdd:COG3383 551 RF-------VPVEYRPPA------------------ELPDEEYPLVLtTGrllDQWHTGTRT--RRSPRLNKHAPEPfVE 603
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111183 726 INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWydpdakrvdkGGCINVLTTQRPSPLAK 800
Cdd:COG3383 604 IHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMPFHWG----------EGAANALTNDALDPVSK 668
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
119-576 |
5.63e-90 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 287.76 E-value: 5.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 119 RLKYPMKRvgaRGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYgtGTLGGTMTRSWPPGNTLVARLMNCCGGYL 198
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAING--GSGGLTDVESLYALKKLLNRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 199 NHYGDYSSAQIAE---GLNYTYGGwadGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYyleQARQKSNARMIIIDPRYT 275
Cdd:pfam00384 76 DHNGDLCTAAAAAfgsDLRSNYLF---NSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 276 dtgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKycvgydektlpasapknghykayilgegpdgvaktpew 355
Cdd:pfam00384 150 ---LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK-------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 356 asqitgvpadkiiklareigstkpAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREgsySLPFVRMPT- 434
Cdd:pfam00384 189 ------------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAASPVg 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 435 -LENPIQTSISMFMWTDAIERGPemtalrdgvrgkdkldvpiKMIWNYAGNCLINQHSEINRTHEILQddkKCELIVVID 513
Cdd:pfam00384 242 aLDLGLVPGIKSVEMINAIKKGG-------------------IKVLYLLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111183 514 CHM-TSSAKYADILLPDCTASEQMDFALDASCGNMSyvifNDQVIKPRFECKTIYEMTSELAKR 576
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQS----TKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
67-658 |
3.53e-85 |
|
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: 278.41 E-value: 3.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 67 CGSRCPLRMHVVDGEIKYVEtdntGDDNyDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDI 146
Cdd:cd02755 8 CSSRCGILARVEDGRVVKID----GNPL-SPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 147 IATNMQRLIKEYGNESIYLNygtgtlggtmtrSWPPGN-TLVARLMNCCG--GYLNHYGD-YSSAQIAEGLNYTYGGwad 222
Cdd:cd02755 83 IASKLKEIKEQHGPESVLFG------------GHGGCYsPFFKHFAAAFGspNIFSHESTcLASKNLAWKLVIDSFG--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 223 GNSPSDIENSKLVVLFGNNPGEtrmsGGGVTYYLEQARQKSN-ARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLA 301
Cdd:cd02755 148 GEVNPDFENARYIILFGRNLAE----AIIVVDARRLMKALENgAKVVVVDPRFSEL-ASKADEWIPIKPGTDLAFVLALI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 302 YVMITENLVDQAFLDKYCVGYDEKTlpasapknGHYKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGSTKP-A 380
Cdd:cd02755 223 HVLISENLYDAAFVEKYTNGFELLK--------AHVKPY-----------TPEWAAQITDIPADTIRRIAREFAAAAPhA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 381 FISQGWGPQRHANGEIATRAISMLAILTGNVGINGGnsgaregsysLPFVRMPtlenpiqtsismfmwtdaierGPemta 460
Cdd:cd02755 284 VVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG----------LYYAGSA---------------------KP---- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 461 lrdgvrgkdkldVPIKMIWNYAGNCLINQhSEINRTHEILqddKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAL 540
Cdd:cd02755 329 ------------YPIKALFIYRTNPFHSM-PDRARLIKAL---KNLDLVVAIDILPSDTALYADVILPEATYLERDEPFS 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 541 DASCGNMSYVIfNDQVIKPRFECKTIYEMTSELAKRLGveqqftegrtqeewmrhlyaqsreaipelptfeefrkqgifk 620
Cdd:cd02755 393 DKGGPAPAVAT-RQRAIEPLYDTRPGWDILKELARRLG------------------------------------------ 429
|
570 580 590
....*....|....*....|....*....|....*...
gi 90111183 621 krdpqghhvaykafredpqanPLTTPSGKIEIYSQALA 658
Cdd:cd02755 430 ---------------------LFGTPSGKIELYSPILA 446
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
13-814 |
4.11e-85 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 286.95 E-value: 4.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 13 EVSRRGLVKTTAIGGLAMASSALtLPFSRIAHAVDsaiPTKSDEKVIWSACTVnCGSRCPLRMHVVDGEIKYVeTDNTGD 92
Cdd:PRK15488 2 SLSRRDFLKGAGAGCAACALGSL-LPGALAANEIA---QLKGKTKLTPSICEM-CSTRCPIEARVVNGKNVFI-QGNPKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 93 DNYDGlhqvRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNygtgtl 172
Cdd:PRK15488 76 KSFGT----KVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFS------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 173 ggtmTRSwppgNTLVARLMNCCGGY--LNHYGDYSSAQIAEGL--NYTYGGwadgNSPSDIENSKLVVLFGNNPGE-TRM 247
Cdd:PRK15488 146 ----SKS----GSLSSHLFHLATAFgsPNTFTHASTCPAGYAIaaKVMFGG----KLKRDLANSKYIINFGHNLYEgINM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 248 SgggVTYYLEQARQKSNARMIIIDPRYTdTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEktL 327
Cdd:PRK15488 214 S---DTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE--L 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 328 PASApknghyKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGSTKPAFISQgWG------PQrhangEI-ATRA 400
Cdd:PRK15488 288 AASV------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGhratftPE-----EFdMRRA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 401 ISMLAILTGNVGINGG----------NSGAREGsyslpfvRMPTLENPiqtsismfmwtdAIERGPEMTALRdgvrgKDK 470
Cdd:PRK15488 345 IFAANVLLGNIERKGGlyfgknasvyNKLAGEK-------VAPTLAKP------------GVKGMPKPTAKR-----IDL 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 471 LDVPIKMIWNYAG------NCLINQ-----HSEINRTHEILQ-----DD-----KKCELIVVIDCHMTSSAKYADILLPD 529
Cdd:PRK15488 401 VGEQFKYIAAGGGvvqsiiDATLTQkpyqiKGWVMSRHNPMQtvtdrADvvkalKKLDLVVVCDVYLSESAAYADVVLPE 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 530 CTASEQMDFALDASCGNMSYVIFNdQVIKPRFECKTIYEMTSELAKRLGVEQQFTegrtqeeW--MRHLYAQSREAIPEL 607
Cdd:PRK15488 481 STYLERDEEISDKSGKNPAYALRQ-RVVEPIGDTKPSWQIFKELGEKMGLGQYYP-------WqdMETLQLYQVNGDHAL 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 608 ptFEEFRKQG-----------------IFKKRDPQGHHVAykafrED---PQANPLTTPSGKIEIYSQALADIAATWELP 667
Cdd:PRK15488 553 --LKELKKKGyvsfgvplllrepkmvaKFVARYPNAKAVD-----EDgtyGSQLKFKTPSGKIELFSAKLEALAPGYGVP 625
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 668 egdvidplpiytpgfeSYQD-PLNKQYPLQLTgfHYKSRVHST--YGNVDVL-----KAAcrqeMWINPLDAQKRGIHNG 739
Cdd:PRK15488 626 ----------------RYRDvALKKEDELYFI--QGKVAVHTNgaTQNVPLLanlmsDNA----VWIHPQTAGKLGIKNG 683
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111183 740 DKVRIFNDRGEVHIEAKVTPRMMPGVV--ALGEGAwYDPDAKRVD-KGGCINVLTTQRPSPLAkGNPSHTNLVQVEKV 814
Cdd:PRK15488 684 DEIRLENSVGKEKGKALVTPGIRPDTLfaYMGFGS-KNKELTRATgKGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
57-612 |
2.68e-82 |
|
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: 271.11 E-value: 2.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 57 KVIWSACTVNCGSRCPLRMHVVDGEIKYVE--TD--NTGDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGE 132
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEqaTDypETPPDLPD--YNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 133 GKFERISWEEAYDIIATNMQRLIKEYGNESIYLNygtgtlggtmtrSWPPGNTLV-----ARLMNCCGGYLNH----YGD 203
Cdd:cd02750 80 GKWKRISWDEALELIADAIIDTIKKYGPDRVIGF------------SPIPAMSMVsyaagSRFASLIGGVSLSfydwYGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 204 -YSSAQIaeglnyTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGggvTYYLEQARQKSnARMIIIDPRYTDTgAGRE 282
Cdd:cd02750 148 lPPGSPQ------TWGEQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPS-AKHA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 283 DEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYcvgydeKTLPasapknghYKAYilgegpdgvakTPEWASQITGV 362
Cdd:cd02750 217 DLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 363 PADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSyslpfVRMptlenpiqts 442
Cdd:cd02750 272 PRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQ-----PRV---------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 443 isMFMWtdaiergpemtalrdgvrgkdkldvpikmiwnyAGNcLINQHseiNRTHEILQD--DKKCELIVVIDCHMTSSA 520
Cdd:cd02750 337 --LFVW---------------------------------RGN-LFGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTA 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 521 KYADILLPDCTASEQMDfaLDASCGNmSYVIFNDQVIKPRFECKTIYEMTSELAKRlgVEQQFTEGRTQ----EEWMRHL 596
Cdd:cd02750 378 LYSDIVLPAATWYEKHD--LSTTDMH-PFIHPFSPAVDPLWEAKSDWEIFKALAKK--VPWRTLTGRQQfyldHDWFLEL 452
|
570
....*....|....*.
gi 90111183 597 YAqsreaipELPTFEE 612
Cdd:cd02750 453 GE-------TLPTYKP 461
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
693-813 |
4.98e-74 |
|
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: 236.80 E-value: 4.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGA 772
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 90111183 773 WYDPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEK 813
Cdd:cd02794 81 WYEPDANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
66-659 |
9.69e-68 |
|
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: 233.87 E-value: 9.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 66 NCGSRCPLRMHVVDGEIKYVEtdntGDDNYDGlHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARG----EGKFERISWE 141
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTKVE----GNPLHPG-SRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPKFVPISWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 142 EAYDIIATNMQRLIKEYGNESIYLNYGtgtlggtmtRSWPPGNTLVARLMNCCG--GYLNHYGDYSSAQiAEGLNYTYGG 219
Cdd:cd02757 83 EALDTIADKIRALRKENEPHKIMLHRG---------RYGHNNSILYGRFTKMIGspNNISHSSVCAESE-KFGRYYTEGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 220 WaDGNSPsDIENSKLVVLFGNNPGETrmsgggvTYYLEQARQK-----SNARMIIIDPRYTDTgAGREDEWIPIRPGTDA 294
Cdd:cd02757 153 W-DYNSY-DYANAKYILFFGADPLES-------NRQNPHAQRIwggkmDQAKVVVVDPRLSNT-AAKADEWLPIKPGEDG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 295 ALVNGLAYVMITENLVDQAFLDKYCVGYD----EKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKL 370
Cdd:cd02757 223 ALALAIAHVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKEKSTEGLVKWWNLELKDYTPEWAAKISGIPAETIERV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 371 AREIGSTKPAFISQGW-GPQRHANGEIATRAISMLAILTGNVGINGGnsgaregsySLPFVRMPTLEnpiqtsiSMFMWT 449
Cdd:cd02757 303 AREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGG---------LCPNMGVPKIK-------VYFTYL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 450 DaiergpemtalrdgvrgkdkldvpiKMIWNYagnclinqhseiNRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPD 529
Cdd:cd02757 367 D-------------------------NPVFSN------------PDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPD 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 530 CTASEQMDFaLDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLgveqqftEGRTQEEWMRHLYAQSREAIPELPT 609
Cdd:cd02757 410 GHHFERWDV-MSQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKL-------DPKGSDGMKRYAPGQFKDPETGKNN 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 90111183 610 FEEFrkqgifkkrdpqghhvaykafredpqANPLTTPSGKIEIYSQALAD 659
Cdd:cd02757 482 RWEF--------------------------ENVFPTETGKFEFYSETLKK 505
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
67-578 |
4.00e-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: 231.72 E-value: 4.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 67 CGSRCPLRMHVVDGEIKYVETDNTGDDNydglhQVRACLRGRSMRRRVYNPDRLKYPMKRVgargEGKFERISWEEAYDI 146
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVEPVKGHPVN-----RGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 147 IATNMQRLIKEYGNESIYL----------NYgtgtlggtmtrswppgntLVARLMNCCGGYLN--HYGDYSSAQIAEGLN 214
Cdd:cd02753 78 VASRLKEIKDKYGPDAIAFfgsakctneeNY------------------LFQKLARAVGGTNNvdHCARLCHSPTVAGLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 215 YTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGgvTYYLEQARQKsnARMIIIDPRYTDTgAGREDEWIPIRPGTDA 294
Cdd:cd02753 140 ETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIA--RRIKRAKRNG--AKLIVADPRRTEL-ARFADLHLQLRPGTDV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 295 ALVNGLAYVMITENLVDQAFLDKYCVGYDEktLPASAPKNghykayilgegpdgvakTPEWASQITGVPADKIIKLAREI 374
Cdd:cd02753 215 ALLNAMAHVIIEEGLYDEEFIEERTEGFEE--LKEIVEKY-----------------TPEYAERITGVPAEDIREAARMY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 375 GSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGnsgareGSYSLpfvRMptlENPIQTSISMfmwtdaier 454
Cdd:cd02753 276 ATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT------GVNPL---RG---QNNVQGACDM--------- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 455 gpemtalrdgvrGKDKLDVP--IKMIWNYAGNCLINqHSEINRTHEILqddKKCELIVVIDCHMTSSAKYADILLPDCTA 532
Cdd:cd02753 335 ------------GALPNVLPgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPAASF 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 90111183 533 SEQmdfalDASCGN-MSYVIFNDQVIKPRFECKTIYEMTSELAKRLG 578
Cdd:cd02753 399 AEK-----DGTFTNtERRVQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
693-813 |
7.96e-63 |
|
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: 206.67 E-value: 7.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQLTGFHYKSRVHSTYGNVDVLKAAC----RQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVAL 768
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYkvkgREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 90111183 769 GEGAWYDPDAKR-VDKGGCINVLTTQRPSP-LAKGNPSHTNLVQVEK 813
Cdd:cd02777 81 PEGAWYDPDDNGgLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
67-615 |
1.08e-62 |
|
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: 220.95 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 67 CGSRCPLRMHVVDGEIKYVetdnTGDDNYDGlHQVRACLRGRSMRRRVYNPDRLKYPMKRvgaRGEGKFERISWEEAYDI 146
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAV----RGDPEHPV-NRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 147 IATNMQRLIKEYGNESI-------YLN---YgtgtlggtmtrswppgntLVARLMNccgGYL--NHYgDY------SSAq 208
Cdd:cd02754 79 IAERFKAIQAEYGPDSVafygsgqLLTeeyY------------------AANKLAK---GGLgtNNI-DTnsrlcmASA- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 209 iAEGLNYTYGgwADG--NSPSDIENSKLVVLFGNNPGETRmsggGVTY-YLEQARQKS-NARMIIIDPRYTDTgAGREDE 284
Cdd:cd02754 136 -VAGYKRSFG--ADGppGSYDDIEHADCFFLIGSNMAECH----PILFrRLLDRKKANpGAKIIVVDPRRTRT-ADIADL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 285 WIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEKTLPASAPknghykayilgegpdgvakTPEWASQITGVPA 364
Cdd:cd02754 208 HLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELKAFVADY-------------------TPEKVAEITGVPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 365 DKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVG--------ING-GNS-GAREGSY---SLPFVR 431
Cdd:cd02754 269 ADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREVGGlanLLPGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 432 mpTLENPIQTSISMFMW-----TDAIERGPEMTALRDGV-RGKdkldvpIKMIWNYAGNcliNQHSEINRTHEIlQDDKK 505
Cdd:cd02754 349 --SVNNPEHRAEVAKFWgvpegTIPPKPGLHAVEMFEAIeDGE------IKALWVMCTN---PAVSLPNANRVR-EALER 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 506 CELIVVIDC-HMTSSAKYADILLPDCTASEQmdfalDASCGNMSYVI-FNDQVIKPRFECKTIYEMTSELAKRLGVEQQF 583
Cdd:cd02754 417 LEFVVVQDAfADTETAEYADLVLPAASWGEK-----EGTMTNSERRVsLLRAAVEPPGEARPDWWILADVARRLGFGELF 491
|
570 580 590
....*....|....*....|....*....|..
gi 90111183 584 tegrtqeewmrhlYAQSREAIpelptFEEFRK 615
Cdd:cd02754 492 -------------PYTSPEEV-----FEEYRR 505
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
63-538 |
1.73e-47 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 177.59 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 63 CTVNCGsrcpLRMHVVDGEIKYVEtdntGDDNyDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGargeGKFERISWEE 142
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIR----GDPD-DPLSKGYICPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 143 AYDIIATNMQRLIKEYGNESI--YLNYgtgtlggtmtrswPPGNTLVA--------RLMNCCGGYLNHYGDYSSAQIAEG 212
Cdd:cd02762 74 AFDEIAERLRAIRARHGGDAVgvYGGN-------------PQAHTHAGgayspallKALGTSNYFSAATADQKPGHFWSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 213 LNYtygGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYY--LEQARQKSNARMIIIDPRYTDTgAGREDEWIPIRP 290
Cdd:cd02762 141 LMF---GHPGLHPVPDIDRTDYLLILGANPLQSNGSLRTAPDRvlRLKAAKDRGGSLVVIDPRRTET-AKLADEHLFVRP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 291 GTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEkTLPASApknghykayilgegpdgvAKTPEWASQITGVPADKIIKL 370
Cdd:cd02762 217 GTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDE-VRAALA------------------EFTPEAYAPRCGVPAETIRRL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 371 AREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAregSYSLPFVRMPTLENpiqtsISMFMWTD 450
Cdd:cd02762 278 AREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFT---TPALDLVGQTSGRT-----IGRGEWRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 451 AIERGPEMTALRDGVRGKDKLDVP----IKMIWNYAGNCLinqHS--EINRTHEILQddkKCELIVVIDCHMTSSAKYAD 524
Cdd:cd02762 350 RVSGLPEIAGELPVNVLAEEILTDgpgrIRAMIVVAGNPV---LSapDGARLEAALG---GLEFMVSVDVYMTETTRHAD 423
|
490
....*....|....
gi 90111183 525 ILLPDCTASEQMDF 538
Cdd:cd02762 424 YILPPASQLEKPHA 437
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
57-606 |
9.68e-47 |
|
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: 177.21 E-value: 9.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 57 KVIWSACTVNCGsrcpLRMHVVDGEIKYVETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRVGarGEGKFE 136
Cdd:cd02752 1 RTICPYCSVGCG----LIAYVQNGVWVHQEGDPDHPVNRGSL-----CPKGAALRDFVHSPKRLKYPMYRAP--GSGKWE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 137 RISWEEAYDIIAtnmqRLIKEYGNES-IYLNYGTGTLGGTMTRSWPPGNT-------LVARLMNCCG-GYLNHYGDYSSA 207
Cdd:cd02752 70 EISWDEALDEIA----RKMKDIRDASfVEKNAAGVVVNRPDSIAFLGSAKlsneecyLIRKFARALGtNNLDHQARIUHS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 208 QIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGggvTYYLEQARQKSNARMIIIDPRYTDTgAGREDEWIP 287
Cdd:cd02752 146 PTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRT-AAKADLYVP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 288 IRPGTDAALVNGlayvMItenlvdqafldKYCVGYdektlpasapknghykayilgegpdgvakTPEWASQITGVPADKI 367
Cdd:cd02752 222 IRSGTDIAFLGG----MI-----------NYIIRY-----------------------------TPEEVEDICGVPKEDF 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 368 IKLAREIGST----KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGsyslpfvrmptlENPIQTSi 443
Cdd:cd02752 258 LKVAEMFAATgrpdKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRG------------HSNVQGA- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 444 smfmwTDAierGPEMTALrdgvrgkdkldvPikmiWNYAGNCLINQHSEINRTHEILqddKKCELIVVIDCHMTSSAKYA 523
Cdd:cd02752 325 -----TDL---GLLSHNL------------P----GYLGGQNPNSSFPNANKVRRAL---DKLDWLVVIDPFPTETAAFW 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 524 D-------------ILLPDCTASEQmdfalDASCGNMS-YVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQ 589
Cdd:cd02752 378 KnpgmdpksiqtevFLLPAACQYEK-----EGSITNSGrWLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFP 452
|
570
....*....|....*..
gi 90111183 590 EEWMRHLYAQSREAIPE 606
Cdd:cd02752 453 EPITKWNYGYGDEPTPE 469
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
67-579 |
4.94e-44 |
|
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: 169.63 E-value: 4.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 67 CGSRCPLRMHVVDGEIKYVEtdntGDDNYDgLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDI 146
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNPDHP-LNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 147 IAtnmQRLIKEYGNESIYLNYGTGTLGGTMTRSWPPGNTlvarlmnccgGYLNH--YGDYSSAQIAEGLNYTYGG--WAD 222
Cdd:cd02763 82 AT---KRLKAARATDPKKFAFFTGRDQMQALTGWFAGQF----------GTPNYaaHGGFCSVNMAAGGLYSIGGsfWEF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 223 GNSpsDIENSKLVVLFG------NNPGETRMsgggvtyyleQARQKSNARMIIIDPRYTDTGAgREDEWIPIRPGTDAAL 296
Cdd:cd02763 149 GGP--DLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPVRTGYAA-IADEWVPIKPGTDGAF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 297 VNGLAYVMITENLVDQAFLDKYCvgydektlpasapknghykayilgEGPDGVAKTPEWASQITGVPADKIIKLAREIGS 376
Cdd:cd02763 216 ILALAHELLKAGLIDWEFLKRYT------------------------NAAELVDYTPEWVEKITGIPADTIRRIAKELGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 377 TK-------PAFISQGWGPQR------------------HANGEIATRAISMLAILTGNVGINGGN-------------- 417
Cdd:cd02763 272 TArdqpielPIAWTDVWGRKHekitgrpvsfhamrgiaaHSNGFQTIRALFVLMMLLGTIDRPGGFrhkppyprhipplp 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 418 SGAREGSYSLPFVRMPTLE----------------NPIQTSiSMFMWTDAIE-RGPEMTALRDGVRGkDKLDVPIKMIwn 480
Cdd:cd02763 352 KPPKIPSADKPFTPLYGPPlgwpaspddllvdedgNPLRID-KAYSWEYPLAaHGCMQNVITNAWRG-DPYPIDTLMI-- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 481 YAGNCLINQHSEINRTHEILQD-----DKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFA--LDASCGNMSYVI-- 551
Cdd:cd02763 428 YMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMslLDRPISEADGPVda 507
|
570 580
....*....|....*....|....*...
gi 90111183 552 FNDQVIKPRFECKTIYEMTSELAKRLGV 579
Cdd:cd02763 508 IRVPIVEPKGDVKPFQEVLIELGTRLGL 535
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
693-813 |
8.93e-38 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.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: 137.38 E-value: 8.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQLTGFHYKSRVHSTYGNVDVLKAAC---RQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALG 769
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKvqgREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 90111183 770 EGAWYDPDAKRV----DKGGCINVLTTQRP-SPLAKGNPSHTNLVQVEK 813
Cdd:cd02793 81 TGAWYDPDDPGEpgplCKHGNPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
97-578 |
1.33e-32 |
|
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: 135.16 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 97 GLHQ-VRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIAtNMQRLIKEY---GNESIYL------- 165
Cdd:cd02758 60 GLKArATACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVV-EGGDLFGEGhveGLKAIRDldtpidp 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 166 ---NYGTGTLGGTMTRSWPPGNT-LVARLMNCCGGYLNHYGDYSSAQIA--EGlNYTYGGWADGNS--PSDIENSKLVVL 237
Cdd:cd02758 139 dhpDLGPKANQLLYTFGRDEGRTpFIKRFANQAFGTVNFGGHGSYCGLSyrAG-NGALMNDLDGYPhvKPDFDNAEFALF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 238 FGNNPGE-----TRMSGggvtyYLEQARQKSNARMIIIDPRY--TDTGAGREDEWIPIRPGTDAALVNGLAYVMITENlv 310
Cdd:cd02758 218 IGTSPAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENE-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 311 dqafldkycvGYDEKTLpASAPKNGHYKA---------------------YILGEgpDGVAKT-PEWASQiTGVPADKII 368
Cdd:cd02758 291 ----------RYNAEYL-SIPSKEAAKAAgepswtnathlvitvrvksalQLLKE--EAFSYSlEEYAEI-CGVPEAKII 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 369 KLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGG---NSGAREGSYSLPFVRMPTLEN-------P 438
Cdd:cd02758 357 ELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRMLNALIGNLNWKGGllmSGGGFADNSAGPRYDFKKFFGevkpwgvP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 439 I-------QTSISMFMWTDAIERGPEMTA----LRDGVRGK------DKLDVPIKMIWNYAGNCLINQHSEINRTHEILQ 501
Cdd:cd02758 437 IdrskkayEKTSEYKRKVAAGENPYPAKRpwypLTPELYTEviasaaEGYPYKLKALILWMANPVYGAPGLVKQVEEKLK 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 502 DDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAldascGNMSYVIFNDQ-----VIKPRfECKTI-------YEM 569
Cdd:cd02758 517 DPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFS-----TPWGGVPTKAStarwpVIAPL-TEKTAnghpvsmESF 590
|
....*....
gi 90111183 570 TSELAKRLG 578
Cdd:cd02758 591 LIDLAKALG 599
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
695-808 |
5.30e-30 |
|
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: 114.29 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 695 LQLTGFHYKSRVHSTYGNVDVLKAACRQEM--WINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGA 772
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEvvEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 90111183 773 WYDPdakrvdKGGCINVLTTQRPSPLAKGNPSHTNL 808
Cdd:pfam01568 81 WYEP------RGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
66-583 |
9.18e-28 |
|
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: 120.07 E-value: 9.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 66 NCGSRCPLRMH-VVDGEIKYVETDNTGDDNYDGlhQVRACLRGRSMRRRVYNPDRLKYPMKRV----GARGEGKFERISW 140
Cdd:cd02760 6 NCVAGPDFMAVkVVDGVATEIEPNFAAEDIHPA--RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkGRNEDPGFVPISW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 141 EEAYDIIATN--------------MQRLIKEYGNESIYLNYGTGTLGGTMtrSWPPGNTLVARLMNCCGGYLNH-YGDYS 205
Cdd:cd02760 84 DEALDLVAAKlrrvrekglldekgLPRLAATFGHGGTPAMYMGTFPAFLA--AWGPIDFSFGSGQGVKCVHSEHlYGEFW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 206 SAqiaeglnytygGWAdgnSPSDIENSKLVVLFGNNpgeTRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAgREDEW 285
Cdd:cd02760 162 HR-----------AFT---VAADTPLANYVISFGSN---VEASGGPCAVTRHADARVRGYKRVQVEPHLSVTGA-CSAEW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 286 IPIRPGTDAALVNGLAYVMITE---NLVDQAFL-DK----YCVGYDEKTL--PAS------------APKNGHYKAYILG 343
Cdd:cd02760 224 VPIRPKTDPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGPDGLYLrdAATgkplvwdersgrAVPFDTRGAVPAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 344 EG-----------PDGVAK---------------------TPEWASQITGVPADKIIKLARE------IGST-------- 377
Cdd:cd02760 304 AGdfavdgavsvdADDETAihqgvegttaftmlvehmrkyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtl 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 378 --KPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGS--------------------------YSLPF 429
Cdd:cd02760 384 pyRPVAVTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGTTVRLnrphddrlasvkpgedgfmaqgfnptDKEHW 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 430 VRMPTLENPIQTSISMF---MWTDAIerGPEMTA---LRDgVRGKDKLDVPIKM-IW-NYAGNCLINqhseINRTHEILQ 501
Cdd:cd02760 464 VVKPTGRNAHRTLVPIVgnsAWSQAL--GPTQLAwmfLRE-VPLDWKFELPTLPdVWfNYRTNPAIS----FWDTATLVD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 502 DDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMD------FALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAK 575
Cdd:cd02760 537 NIAKFPFTVSFAYTEDETNWMADVLLPEATDLESLQmikvggTKFVEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAK 616
|
....*...
gi 90111183 576 RLGVEQQF 583
Cdd:cd02760 617 RTGLLADY 624
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
702-805 |
3.32e-26 |
|
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: 103.17 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 702 YKSRVHS-TYGNVDVLKAACRQE-MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYdpdak 779
Cdd:cd02775 1 LRDHFHSgTRTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH----- 75
|
90 100
....*....|....*....|....*.
gi 90111183 780 RVDKGGCINVLTTQRPSPLAKGNPSH 805
Cdd:cd02775 76 RGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
119-649 |
1.55e-25 |
|
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: 112.02 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 119 RLKYPMKRvgARGEGKFERISWEEAYDIIATNMQRLIKE----Y-----GNESIYLnYGtgtlggtmtrswppgntLVAR 189
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDraafYtsgraSNEAAYL-YQ-----------------LFAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 190 LM------NCcgGYLNHYGdySSAqiaeGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGET--RMsgggvTYYLEQARq 261
Cdd:cd02767 124 AYgtnnlpDC--SNMCHEP--SSV----GLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAK- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 262 KSNARMIIIDP-------RYTD--------TGAGR-EDEWIPIRPGTDAALVNGLAYVMI-----TENLVDQAFLDKYCV 320
Cdd:cd02767 190 KRGGKIIVINPlrepgleRFANpqnpesmlTGGTKiADEYFQVRIGGDIALLNGMAKHLIerddePGNVLDHDFIAEHTS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 321 GYDEktlpasapknghYKAYIlgegpdgvaKTPEWAS--QITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIAT 398
Cdd:cd02767 270 GFEE------------YVAAL---------RALSWDEieRASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 399 RAISMLAILTGNVGING-------GNS---GARE-GSYSLPFvrmptlENPIQtSISMFmWTDAIERGPEMT---ALRDG 464
Cdd:cd02767 329 RAIVNLALLRGNIGRPGaglmpirGHSnvqGDRTmGITEKPF------PEFLD-ALEEV-FGFTPPRDPGLDtveAIEAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 465 VRGkdKLDVPIKMIWNYAGnclINQHSEinRTHEILqddKKCELIVVIDCHMTSSA---KYADILLPDCTASEQmdfalD 541
Cdd:cd02767 401 LEG--KVKAFISLGGNFAE---AMPDPA--ATEEAL---RRLDLTVHVATKLNRSHlvhGEEALILPCLGRTEI-----D 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 542 ASCGNMSYVIFND---QVIKPRFECKTI-YEMTSELAKRLGVEQQ-FTEGRTQEEWMRHLYAQSREAIPEL--PTFEEFR 614
Cdd:cd02767 466 MQAGGAQAVTVEDsmsMTHTSRGRLKPAsRVLLSEEAIVAGIAGArLGEAKPEWEILVEDYDRIRDEIAAViyEGFADFN 545
|
570 580 590
....*....|....*....|....*....|....*.
gi 90111183 615 KqgifKKRDPQGHHvaykafREDPQANP-LTTPSGK 649
Cdd:cd02767 546 Q----RGDQPGGFH------LPNGARERkFNTPSGK 571
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
692-814 |
1.13e-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: 99.75 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 692 QYPLQLTGFHYKSRVHSTYGNVDVLKAACRQ-EMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGE 770
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 90111183 771 GAWydpdaKRVDKGGCINVLTTQRPSPLAKGNPS-----HTNLVQVEKV 814
Cdd:cd02785 81 GWW-----SRYFQEGSLQDLTSPFVNPVHEYIYGpnsafYDTLVEVRKA 124
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
693-811 |
4.39e-23 |
|
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: 95.04 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQLTGFHYKSRVHSTYGNVDVL-KAACRQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVaLGEG 771
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELrAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV-VAEG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 90111183 772 AWYDPDAKRvdkGGCINVLTTQRPSPLAKGNPSHTNLVQV 811
Cdd:cd02786 80 GWWREHSPD---GRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
103-771 |
1.53e-22 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 103.92 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 103 ACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWE-------EAYDI--------------IATNMQRLIKEYG-- 159
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEqlveevvEGGDLfgeghvdglrairdLDTPIDAKNPEYGpk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 160 -NESIYLNygtgtlggtmtrSWPPGNT-LVARLMNCCGGYLN--HYGDYSsaqiaeGLNYTYGGWA-----DGNS---Ps 227
Cdd:PRK14991 221 aNQLLVTN------------ASDEGRDaFIKRFAFNSFGTRNfgNHGSYC------GLAYRAGSGAlmgdlDKNPhvkP- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 228 DIENSKLVVLFGNNPGEtrmSGGGvtyYLEQARQKSNARM------IIIDPR---YTDTGAGREDEWIPIRPGTDAALVN 298
Cdd:PRK14991 282 DWDNVEFALFIGTSPAQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 299 GLAYVMITENLVDQAFLDK-------------YC-----VGYDEK-------------TLPASAPKNGHYKAYILGEGPD 347
Cdd:PRK14991 356 GMIRWIIDNQRYNADYLAQpgvaamqaageasWTnathlVIADPGhprygqflrasdlGLPFEGEARGDGEDTLVVDAAD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 348 G--------------VAKTPEWA--------------------------SQITGVPADKIIKLAREIGS--TKPAFISQG 385
Cdd:PRK14991 436 GelvpatqaqparlfVEQYVTLAdgqrvrvksslqllkeaarklslaeySEQCGVPEAQIIALAEEFTShgRKAAVISHG 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 386 wGpQRHANGEIATRAISMLAILTGNVGINGG---NSGAREGSYSLP---FVRMPTLENPIQTSIS--MFMWTDAIE---- 453
Cdd:PRK14991 516 -G-TMSGNGFYNAWAIMMLNALIGNLNLKGGvvvGGGKFPGFGDGPrynLASFAGKVKPKGVSLSrsKFPYEKSSEyrrk 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 454 ----------RGP----------EM-TALRDGvrgkdkLDVPIKMIWNYAGNCLINQHSEINRTHEILQDDKKCELIVVI 512
Cdd:PRK14991 594 veagqspypaKAPwypfvaglltEMlTAALEG------YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 513 DCHMTSSAKYADILLPDCTASEQMDFA-------LDASCGNMSyvifndqVIKPRFEcKT-------IYEMTSELAKRLG 578
Cdd:PRK14991 668 DAFINETTALADYIVPDTHTYESWGFTapwggvpTKASTARWP-------VVEPRTA-KTadgqpvcMESFLIAVAKRLQ 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 579 V------EQQFTEGRTQ-----EEWmrHLYA------QSREAIPE--------------LPTF------EEFRKQGIFKK 621
Cdd:PRK14991 740 LpgfgdnAIKDAQGNTHplnraEDF--YLRGaaniayLGKTPVADasdedialtgvsriLPALqatlkpDEVRRVAFIYA 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 622 R----DPqghhvAYKAFREDPQANPLTTPsgkIEIYSQALADI-----------AATW---ELPEGdvidplpiyTPGFE 683
Cdd:PRK14991 818 RggrfAP-----AESAYDEERMGNRWKKP---LQIWNEDVAAArhsmtgerysgCPTWyppRLADG---------TPLRE 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 684 SYQDplnKQYPLQLTGFhyKSRVHSTYGN-VDVLKAACRQE-MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRM 761
Cdd:PRK14991 881 QFPE---SQWPLLLISF--KSNLMSSMSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGV 955
|
890
....*....|
gi 90111183 762 MPGVVALGEG 771
Cdd:PRK14991 956 MPGVIAIEHG 965
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
13-800 |
1.52e-18 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 90.73 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 13 EVSRRGLVKTTAIGglAMASSA-LTLPfsriahAVDSAIPTKSDEKVIWS--ACTVnCGSRCPLRMHVVDGEIKYVETDN 89
Cdd:PRK13532 2 KLSRRDFMKANAAA--AAAAAAgLSLP------AVANAVVGSAQTAIKWDkaPCRF-CGTGCGVLVGTKDGRVVATQGDP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 90 TGDDNyDGLHqvraCLRGRSMRRRVYNPDRLKYPMKRVgARGE----GKFERISWEEAYDIIATNMQRLIKEYGNESIYL 165
Cdd:PRK13532 73 DAPVN-RGLN----CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 166 nygtgtlggtmtrsWPPGNTLV------ARLMNccGGYLNHYGD----YSSAQIAEGLNYTYG-----GWADgnspsDIE 230
Cdd:PRK13532 147 --------------FGSGQWTIwegyaaSKLMK--AGFRSNNIDpnarHCMASAVVGFMRTFGidepmGCYD-----DIE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 231 NSKLVVLFGNNPGE------TRMSGggvtyyleqaRQKSNARM-IIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYV 303
Cdd:PRK13532 206 AADAFVLWGSNMAEmhpilwSRVTD----------RRLSNPDVkVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 304 MITENLVDQAFLDKYCV--------GY---DEKTLPASAPKNGH-----------YKAYilgegpdgVAK-TPEWASQIT 360
Cdd:PRK13532 276 IIQNNAVNWDFVNKHTNfrkgatdiGYglrPTHPLEKAAKNPGTagksepisfeeFKKF--------VAPyTLEKTAKMS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 361 GVPADKIIKLAREIGSTKPAFISQgW--GPQRHANGEIATRAISMLAILTGNVGINgGNSG------------ARE-GSY 425
Cdd:PRK13532 348 GVPKEQLEQLAKLYADPNRKVVSF-WtmGFNQHTRGVWANNLVYNIHLLTGKISTP-GNGPfsltgqpsacgtAREvGTF 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 426 SLpfvRMP---TLENPIQTSISMFMWtdaieRGPEMT--------------ALRDGVrgkdkldvpIKMIWNYAGNcliN 488
Cdd:PRK13532 426 SH---RLPadmVVTNPKHREIAEKIW-----KLPEGTippkpgyhavaqdrMLKDGK---------LNAYWVMCNN---N 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 489 QHSEINRTHEILQDDKKCE-LIVVIDCHMTSSAKYADILLPdcTAseqMDFALDASCGNMS-YVIFNDQVIKPRFECKT- 565
Cdd:PRK13532 486 MQAGPNINEERLPGWRNPDnFIVVSDPYPTVSALAADLILP--TA---MWVEKEGAYGNAErRTQFWRQQVKAPGEAKSd 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 566 IYEMTsELAKRLGVEQQFTE----------GRTQEEWmrhLYA-------QSREAIPELPT--------------FEEFR 614
Cdd:PRK13532 561 LWQLV-EFSKRFKTEEVWPEellakkpeyrGKTLYDV---LFAngqvdkfPLSELAEGYLNdeakhfgfyvqkglFEEYA 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 615 KQGifkkRDpQGHHVA-----YKA----------------FRE--DPQANPLT------TPSGKIEIYSqaladiaatwe 665
Cdd:PRK13532 637 SFG----RG-HGHDLApfdtyHKVrglrwpvvdgketlwrYREgyDPYVKAGEgfkfygKPDGKAVIFA----------- 700
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 666 LPegdvidplpiYTPGFESyqdPlNKQYPLQL-TGF---HYKS-----RVHSTYgnvdvlKAACRQEMWINPLDAQKRGI 736
Cdd:PRK13532 701 LP----------YEPPAES---P-DEEYDLWLsTGRvleHWHTgsmtrRVPELY------RAFPEAVCFMHPEDAKARGL 760
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111183 737 HNGDKVRIFNDRGEV--HIEAKVTPRMMPGVValgegawYDP--DAKRVdkggcINVLTTQRPSPLAK 800
Cdd:PRK13532 761 RRGDEVKVVSRRGEVksRVETRGRNKPPRGLV-------FVPffDAAQL-----INKLTLDATDPLSK 816
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
56-116 |
2.84e-17 |
|
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: 76.18 E-value: 2.84e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111183 56 EKVIWSACTvNCGSRCPLRMHVVDGEIKYVETDNTGDDNydglhQVRACLRGRSMRRRVYN 116
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVN-----EGRLCVKGRFGYERVYN 55
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
694-798 |
1.40e-14 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 71.25 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 694 PLQLTGFHYKSRVHSTYGNVDVLKAACRQE--MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALgEG 771
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGpvVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YH 79
|
90 100 110
....*....|....*....|....*....|..
gi 90111183 772 AW----YDPDAKRVDKGGCI-NVLTTQRPSPL 798
Cdd:cd02776 80 AQerhvNVPGSKLTGKRGGIhNSVTRVRIKPT 111
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
691-792 |
1.23e-13 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 67.92 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 691 KQYPLQL-TG---FHYKSRVHStyGNVDVLKAAcRQEMW--INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPG 764
Cdd:cd00508 1 EEYPLVLtTGrllEHWHTGTMT--RRSPRLAAL-APEPFveIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPG 77
|
90 100
....*....|....*....|....*...
gi 90111183 765 VVALgegAWYDPDAKRvdkGGCINVLTT 792
Cdd:cd00508 78 TVFM---PFHWGGEVS---GGAANALTN 99
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
693-813 |
1.71e-13 |
|
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: 68.47 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQLTGFhyKSRVHSTY-GNVDVLKAAcRQE--MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVA-- 767
Cdd:cd02780 1 YPFILVTF--KSNLNSHRsANAPWLKEI-KPEnpVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAie 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111183 768 LGEGAW---------YDPDA---KRVDKGGCINVLTTQRPSPLAKGNPS--------HTNLVQVEK 813
Cdd:cd02780 78 HGYGHWaygavastiDGKDLpgdAWRGAGVNINDIGLVDPSRGGWSLVDwvggaaarYDTPVKIEK 143
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
692-813 |
3.19e-13 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 67.33 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 692 QYPLQLT-----GFHYksrvHSTYGNVDVLKAACRQ-EMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGV 765
Cdd:cd02781 1 EYPLILTtgarsYYYF----HSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 90111183 766 VALGEGAWYD-PDAKRVDKGGC----INVLTTQRPS-PLAKGNPSHTNLVQVEK 813
Cdd:cd02781 77 VRAEHGWWYPeREAGEPALGGVwesnANALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
97-433 |
5.25e-13 |
|
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: 72.51 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 97 GLHQVRaclrGRSMRRRVYNPD------RLKYPMKRVGargeGKFERISWEEAYDIIAtnmqRLIKEYGNEsiylnygtg 170
Cdd:cd02756 93 GNYSTR----GGTNAERIWSPDnrvgetRLTTPLVRRG----GQLQPTTWDDAIDLVA----RVIKGILDK--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 171 tlggtmtrsWPPGNTLVARLMN---CCGGYLNHYGD--------------------YSSAQIAEG------LNYTYggwa 221
Cdd:cd02756 152 ---------DGNDDAVFASRFDhggGGGGFENNWGVgkfffmalqtpfvrihnrpaYNSEVHATRemgvgeLNNSY---- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 222 dgnspSDIENSKLVVLFGNNPGETRmsgggVTYYLE---------------QARQKSN----ARMIIIDPRYTDTGAGRE 282
Cdd:cd02756 219 -----EDARLADTIVLWGNNPYETQ-----TVYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRRTETVHAAE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 283 DEWIP-------IRPGTDAALVNGLAYVmITEnlvdqafldkycvGYDEktlpasapknghykayILGEgpdgvaktpew 355
Cdd:cd02756 289 AAAGKdrvlhlqVNPGTDTALANAIARY-IYE-------------SLDE----------------VLAE----------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 356 ASQITGVPADKIIKLAREIGSTKPA-------FISQG---WGPQRHANgeiaTRAISMLAILTGNVGINGGNSGaREGSY 425
Cdd:cd02756 328 AEQITGVPRAQIEKAADWIAKPKEGgyrkrvmFEYEKgiiWGNDNYRP----IYSLVNLAIITGNIGRPGTGCV-RQGGH 402
|
....*...
gi 90111183 426 SLPFVRMP 433
Cdd:cd02756 403 QEGYVRPP 410
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
691-766 |
7.33e-13 |
|
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: 65.72 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 691 KQYPLQL-TG---FHYKSRvhSTYGNVDVLKAACRQE-MWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGV 765
Cdd:cd02790 1 EEYPLVLtTGrvlYHYHTG--TMTRRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGV 78
|
.
gi 90111183 766 V 766
Cdd:cd02790 79 V 79
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
57-319 |
1.60e-12 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 71.39 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 57 KVIWSACTVNC-GSrCPLRMHVVDGEIKYvETDNT-----GDDNYDglHQVRACLRGRSMRRRVYNPDRLKYPMKR---- 126
Cdd:COG5013 47 KVVRSTHGVNCtGS-CSWKVYVKDGIITW-ETQQTdyprtGPDLPN--YEPRGCPRGASFSWYTYSPTRVKYPYVRgvll 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 127 ------------------------------VGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnygtgtlggtm 176
Cdd:COG5013 123 elwreararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVA------------ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 177 TRSWPPGNTLV-----ARLMNCCGG-YLNHYGDY-----SSAQiaeglnyTYGGWADGNSPSDIENSKLVVLFGNNPGET 245
Cdd:COG5013 191 GFSPIPAMSMVsyaagARFLSLIGGvMLSFYDWYadlppASPQ-------VWGEQTDVPESADWYNSGYLIMWGSNVPQT 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111183 246 RmsgggvT---YYLEQARQKSnARMIIIDPRYTDtGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQ--AFLDKYC 319
Cdd:COG5013 264 R------TpdaHFMTEARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
701-813 |
4.01e-12 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 63.83 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 701 HYKSRVHsTYG---NVDVLKAACR-QEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVAL--GEGAWY 774
Cdd:cd02778 6 YGKSPVH-THGhtaNNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGFGHWA 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 90111183 775 DPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEK 813
Cdd:cd02778 85 PALSRAYGGGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| 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 ... |
61-534 |
4.56e-12 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 68.95 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 61 SACTvNCGSRCPLRMHVVDGEIKYVETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRVGargeGKFERISW 140
Cdd:cd02771 2 SICH-HCSVGCNISLGERYGELRRVENRYNGAVNHYFL-----CDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 141 EEAYDIIATNMQRLIKEYG--------NESIYlnygtgtlggtmtrswppgntLVARLMnccGGYL-----NHYGDYSSA 207
Cdd:cd02771 72 NEALDVAAARLKEAKDKVGgigsprasNESNY---------------------ALQKLV---GAVLgtnnvDHRARRLIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 208 QIAEGLNYTyggwadgnSPS--DIENSKLVVLFGNNPGETrmsGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDew 285
Cdd:cd02771 128 EILRNGPIY--------IPSlrDIESADAVLVLGEDLTQT---APRIALALRQAARRKAVELAALSGIPKWQDAAVRN-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 286 IPIRPGTDAALVNGLAyvmitENLVDQAFLDKYCVGYDEKTLPASApknghykAYILGEGPDGVAKT--PEWASQITgvp 363
Cdd:cd02771 195 IAQGAKSPLFIVNALA-----TRLDDIAAESIRASPGGQARLGAAL-------ARAVDASAAGVSGLapKEKAARIA--- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 364 adkiiklAREIGSTKPAFISQGwgpqrHANGEIATRAISMLAILTGNVGINGGNSGAREGSYS---LPFVRMPTlenpiQ 440
Cdd:cd02771 260 -------ARLTGAKKPLIVSGT-----LSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSpglLLLGGHVT-----E 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 441 TSISmfmwTDAIergpeMTALRDGvrGKDKLDVpikmiwnyAGNCLINQHSEInrthEILQDDKKCELIVVIDCHMTSSA 520
Cdd:cd02771 323 PGLD----LDGA-----LAALEDG--SADALIV--------LGNDLYRSAPER----RVEAALDAAEFVVVLDHFLTETA 379
|
490
....*....|....
gi 90111183 521 KYADILLPDCTASE 534
Cdd:cd02771 380 ERADVVLPAASFAE 393
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
721-814 |
6.03e-12 |
|
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: 63.57 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 721 RQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYD---PDAKRVDKGGCINVLT--TQRp 795
Cdd:cd02782 32 RCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDypgVSGAGSRPGVNVNDLTddTQR- 110
|
90 100
....*....|....*....|
gi 90111183 796 SPLAkGNPSHTNL-VQVEKV 814
Cdd:cd02782 111 DPLS-GNAAHNGVpVRLARV 129
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
56-116 |
1.91e-10 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 56.87 E-value: 1.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111183 56 EKVIWSACTVnCGSRCPLRMHVVDGEIKYVEtdntGDDNYDgLHQVRACLRGRSMRRRVYN 116
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHP-VNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
693-814 |
1.44e-09 |
|
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: 56.43 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 693 YPLQL-TG-----FHYKSRVhstyGNVDVLKAAcRQEMW--INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPG 764
Cdd:cd02791 3 YPLWLnTGrvrdqWHTMTRT----GRVPRLNAH-VPEPYveIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 90111183 765 VVALgegAWYDPDakRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
Cdd:cd02791 78 EVFV---PMHWGD--QFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
691-813 |
1.95e-09 |
|
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: 56.08 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 691 KQYPLQLTGFhyksRV--HSTYGN----VDVLKAAcRQEMW--INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMM 762
Cdd:cd02792 1 EEFPLVLTTG----RLteHFHGGNmtrnSPYLAEL-QPEMFveISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 90111183 763 PGVVALgegAWYDPDAKRVdKGGCINVLTTQRPSPLAKGNPSHTNLVQVEK 813
Cdd:cd02792 76 PHEVGI---PYHWGGMGLV-IGDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
16-455 |
2.28e-09 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 60.58 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 16 RRGLVKTTAiGGLAMAS-SALTLPFSRIahaVDSAIPTKSDEKVIWS-ACTVNC--GSRCPLRMHVVDGEIKYVETDNTG 91
Cdd:cd02764 1 RRGFLKLMG-ASLAMASaAACRYPVEKI---VPYVIWPENIVPGETVyYATSLVpaGEGQGVLVKTVDGRPIKIEGNPDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 92 DDNYDGLH-QVRACLRGrsmrrrVYNPDRLKYPMKRVGargEGKFERISWEEAYDIIATNMqRLIKEYGNESIYLNYGTG 170
Cdd:cd02764 77 PASLGGTSaRAQASVLS------LYDPDRAQGPLRRGI---DGAYVASDWADFDAKVAEQL-KAVKDGGKLAVLSGNVNS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 171 tlggtmtrswPPGNTLVARLMNCCGGYLNHYGDYSSAQ-IAEGLNYTYGGwaDGNSPSDIENSKLVVLFGNNPGETRMSG 249
Cdd:cd02764 147 ----------PTTEALIGDFLKKYPGAKHVVYDPLSAEdVNEAWQASFGK--DVVPGYDFDKAEVIVSIDADFLGSWISA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 250 GGVTYYLEQAR----QKSNARMIIIDPRYTDTGAGrEDEWIPIRPGTDAALVNGLAYVMItenlvdqafldkycvgydek 325
Cdd:cd02764 215 IRHRHDFAAKRrlgaEEPMSRLVAAESVYTLTGAN-ADVRLAIRPSQEKAFALGLAHKLI-------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 326 TLPASAPKNGHYKAYILGEGPDGVAKtpewasqITGVPADKIIKLAREIGSTKPAFISQGwgpqrhanGEIATRAISMLA 405
Cdd:cd02764 274 KKGAGSSLPDFFRALNLAFKPAKVAE-------LTVDLDKALAALAKALAAAGKSLVVAG--------SELSQTAGADTQ 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 90111183 406 ILTGNVGINGGNSGAregsySLPFVRmPTLENPIQTSISMFMWTDAIERG 455
Cdd:cd02764 339 VAVNALNSLLGNDGK-----TVDHAR-PIKGGELGNQQDLKALASRINAG 382
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
65-242 |
2.07e-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: 53.83 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 65 VNCGSRCPLRMHVVDGEIKYVETDNTGDDN-----------YDGLhqvraclrgrsmrrrvYNPDRLKYPMKRVGargeG 133
Cdd:cd02768 5 VHDALGSNIRVDVRGGEVMRILPRENEAINeewisdkgrfgYDGL----------------NSRQRLTQPLIKKG----G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 134 KFERISWEEAYDIIATNMQRLIKE----YG-----NESIYlnygtgtlggtmtrswppgntLVARLMNCCG-GYLNHYGD 203
Cdd:cd02768 65 KLVPVSWEEALKTVAEGLKAVKGDkiggIAgpradLESLF---------------------LLKKLLNKLGsNNIDHRLR 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 90111183 204 YSSAQIAEGLNYTYGGwadGNSPSDIENSKLVVLFGNNP 242
Cdd:cd02768 124 QSDLPADNRLRGNYLF---NTSIAEIEEADAVLLIGSNL 159
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
725-766 |
3.83e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 44.07 E-value: 3.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 90111183 725 WINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVV 766
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLV 75
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
63-417 |
1.17e-04 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 45.22 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 63 CTVnCGSRCP-LRMHVVDGEIKYVEtdntgddnydglhqvRACLRGRSMRRRVYNPDRLKYPMKRvgargegkFERISWE 141
Cdd:COG1029 10 CPF-CGCLCDdLEVEVEGGKIVVVK---------------NACAIGAAKFERAVSDHRITSPRIR--------GKEVSLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 142 EAYDIIAtnmqRLIKE------YGNESIYLNygtgtlggtmtrswppGNTLVARLMNCCGGYLNHY---GDYSSAQ-IAE 211
Cdd:COG1029 66 EAIDKAA----EILANakrpliYGLSSTDCE----------------AMRAGLALAERVGAVVDNTasvCHGPSLLaLQD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 212 GlnytygGWAdGNSPSDIEN-SKLVVLFGNNPGET------RMSGGGVTYYLEQARqkSNARMIIIDPRYTDTgAGREDE 284
Cdd:COG1029 126 V------GWP-TCTLGEVKNrADVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGR--KDRTVIVVDPRPTDT-AKVADL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 285 WIPIRPGTDAALVNGLayvmitenlvdqafldkycvgydektlpasapknghyKAYILGEGPDgvaktpewASQITGVPA 364
Cdd:COG1029 196 HLQVKPGRDYEVLSAL-------------------------------------RALVRGKELS--------PEEVAGIPV 230
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111183 365 DKIIKLAREIGSTKPAFISQGWG----PQRHANGEIA----------TRAiSMLAiLTGNVGINGGN 417
Cdd:COG1029 231 EDLEELAERLKNAKYGVIFWGMGltqsPGKHLNVDAAielvrdlnryTKF-SILP-LRGHYNVAGAN 295
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
114-241 |
1.64e-04 |
|
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: 45.04 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111183 114 VYNPDRLKYPMKRVGargeGKFERISWEEAYDIIATNMQRLIKEYGNESI--YLNygtgtlggtmtrswpPGNT-----L 186
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIgaLAS---------------PHSTleelyL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111183 187 VARLMNCCG-GYLNH------YGDYSSAQIAEGLnytyggwadGNSPSDIENSKLVVLFGNN 241
Cdd:cd02772 110 LQKLARGLGsDNIDHrlrqsdFRDDAKASGAPWL---------GMPIAEISELDRVLVIGSN 162
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
726-773 |
1.71e-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: 41.68 E-value: 1.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 90111183 726 INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAW 773
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
708-768 |
2.08e-04 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 41.14 E-value: 2.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111183 708 STYGNVDVLKAACRQEMW-INPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVAL 768
Cdd:cd02788 14 ELSQRSPVIAERAPAPYArLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGL 75
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
725-777 |
6.13e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 40.10 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 90111183 725 WINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAW----YDPD 777
Cdd:cd02789 34 EINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPWanvvVDPY 90
|
|
| |
