|
Name |
Accession |
Description |
Interval |
E-value |
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
5-798 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 1361.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 5 ISRRSLMKTS-ALGSLALASSAFTLPFSQMVRAAEAPV--EEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDV 81
Cdd:TIGR02166 1 ISRRHFLKTSaALGGLAAASGALSLPFSVNAAAEATPTgpDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTGDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 82 YGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGN 161
Cdd:TIGR02166 81 YGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 162 ITNSNVPY---RLMNSCGGFLSRYGSYSTAQISAAMSYMFGAN-DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYYVE 237
Cdd:TIGR02166 161 MSRSWPPTavaRLLNLCGGYLNQYGSYSTAQINEAMPYTYGISaDGSSLDDIENSKLVVMFGNNPAETRMSGGGQTYYFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 238 QARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLISENMVDQPFLDKYCVGYDEKTLPANAPRNAHY 317
Cdd:TIGR02166 241 QALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPKNGSY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 318 KAYILGEGPDGIAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN 397
Cdd:TIGR02166 321 KDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 398 SGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQHGDINHTN 477
Cdd:TIGR02166 401 NGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDINRTH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 478 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRL 557
Cdd:TIGR02166 481 KILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 558 GpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSE 637
Cdd:TIGR02166 561 G--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 638 RLAKIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARG 717
Cdd:TIGR02166 639 RLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDAQKRG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 718 IRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 797
Cdd:TIGR02166 719 ITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLVEVEK 796
|
.
gi 1447699558 798 V 798
Cdd:TIGR02166 797 A 797
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
1-798 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1296.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 1 MKAEISRRSLMKTSALGSLALASSAFTLPFSQMVRAAE----APVEEKAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDT 76
Cdd:PRK14990 10 LAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDsaipTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 77 TGDDVY-GNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGT 155
Cdd:PRK14990 90 TGDDNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 156 GVDGGNITNSNVP-----YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGA-NDGNSPDDIANTKLVVMFGNNPAETRMSG 229
Cdd:PRK14990 170 GTLGGTMTRSWPPgntlvARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGNNPGETRMSG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 230 GGVTYYVEQARERSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLISENMVDQPFLDKYCVGYDEKTLPA 309
Cdd:PRK14990 250 GGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLPA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 310 NAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTG 389
Cdd:PRK14990 330 SAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 390 NVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGVRGKEKLDVPIKFLWCYASNTLINQ 469
Cdd:PRK14990 410 NVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQ 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 470 HGDINHTNEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVILAQPATSAKFERKPIYWM 549
Cdd:PRK14990 490 HSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEM 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 550 LSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPS 629
Cdd:PRK14990 570 TSELAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 630 GKIEIYSERLAKIADTWELKKDEIIHPLPAYTPGFDGWDDPLRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWIN 709
Cdd:PRK14990 648 GKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWIN 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 710 PIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSH 789
Cdd:PRK14990 728 PLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD--AKRVDKGGCINVLTTQRPSPLAKGNPSH 805
|
....*....
gi 1447699558 790 SNLVQIEKV 798
Cdd:PRK14990 806 TNLVQVEKV 814
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
47-666 |
0e+00 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 947.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 47 WSSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISW 126
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 127 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-GNS 205
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAAsGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 206 PDDIANTKLVVMFGNNPAETRMSGGGVTYYVEQAReRSNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLI 285
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 286 SENMVDQPFLDKYCVGYDEKTLPANAPRNAHYKAYILGEGPDGIAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQG 365
Cdd:cd02770 240 TENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAAILQG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 366 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDHGTEMTATRDGV 445
Cdd:cd02770 320 WGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 446 RGKEKLDVPIKFLWCYASNTLINQHGDINHTNEVL-QDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESA 524
Cdd:cd02770 400 KGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRALlDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 525 GNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLHAKTKERNPEMPDYEEMKTTGIFKKK 604
Cdd:cd02770 480 GMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGIYRVP 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699558 605 cPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLAKIADTweLKKDEIIHPLPAYTPGFDG 666
Cdd:cd02770 558 -RALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT--LPEGDEIPAIPKYVPAWEG 616
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
47-666 |
0e+00 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 702.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 47 WSSCTvncgsRCLLRLHVKDDTVYWVESDTTgddvygnHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK----------R 116
Cdd:cd02751 1 PTACH-----WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 117 GEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPY-RLMNSCGGFLSRYGSYSTAQISAAMS 195
Cdd:cd02751 69 GEGEFVRISWDEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLhRFLNLIGGYLGSYGTYSTGAAQVILP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 196 YMFGA----NDGNSPDDIA-NTKLVVMFGNNPAETRMSGGGV-----TYYVEQARERsNARMIVIDPRYNDTAAGREDEW 265
Cdd:cd02751 149 HVVGSdevyEQGTSWDDIAeHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKDA-GVRFICIDPRYTDTAAVLAAEW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 266 LPIRPGTDGALACAIAWVLISENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgPDGIAKTPEWAAKITSIPAE 345
Cdd:cd02751 228 IPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLGE-SDGVPKTPEWAAEITGVPAE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 346 KIIQLAREIGSaKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGSWDLGVEW--------FPMLEN 417
Cdd:cd02751 295 TIRALAREIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPrggaggpgLPQGKN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 418 PVKTQISVFTWTDAIDH-GTEMTAtrdgvRGKEKLDVPIKFLWCYASNTLINQHgDINHTNEVLQDDskcEMIVGIDHFM 496
Cdd:cd02751 374 PVKDSIPVARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFW 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 497 TASAKYCDILLPDLMPTEQEDLIShESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIK 576
Cdd:cd02751 445 TASARYADIVLPATTSLERNDIGL-TGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 577 YLHAKTKERN----PEMPDYEEMKTTGIFKKKCPEEHYVAFRAFREDPQANPLKTPSGKIEIYSERLAKIADTwelkkDe 652
Cdd:cd02751 522 HLYEETRAKAagpgPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYD-----D- 595
|
650
....*....|....
gi 1447699558 653 iIHPLPAYTPGFDG 666
Cdd:cd02751 596 -CPGHPTWIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
36-798 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 683.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 36 AAEAPVEEKAVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGK 115
Cdd:COG0243 14 AALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVR----GDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 116 RGEGKFERISWDEALDTISDNLRRILKDYGNEAVhVLYGTGVDGGNITNSNVPY--RLMNSCG--GFLSRyGSYSTAQIS 191
Cdd:COG0243 89 RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAV-AFYTSGGSAGRLSNEAAYLaqRFARALGtnNLDDN-SRLCHESAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 192 AAMSYMFGANDG-NSPDDIANTKLVVMFGNNPAETrmsGGGVTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRP 270
Cdd:COG0243 167 AGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IADEWLPIRP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 271 GTDGALACAIAWVLISENMVDQPFLDKYCVGYDEktlpanaprnahYKAYIlgegpdgIAKTPEWAAKITSIPAEKIIQL 350
Cdd:COG0243 243 GTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGVPAEDIREL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 351 AREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktqisvftwtD 430
Cdd:COG0243 304 AREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG--------------------------E 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 431 AIdhgtemtatrdgvrgKEKLDVPIKFLWCYASNtLINQHGDINHTNEVLQddsKCEMIVGIDHFMTASAKYCDILLPDL 510
Cdd:COG0243 358 AI---------------LDGKPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 511 MPTEQEDLIsheSAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHAKTKERNpemP 590
Cdd:COG0243 419 TWLERDDIV---TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFE--EAFPWGRTEEDYLRELLEATRGRG---I 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 591 DYEEMKTTGIFKKKCPEEHyvafrAFREDpqaNPLKTPSGKIEIYSERLAkiadtwelkkdeiIHPLPAYTPGFDgWDDP 670
Cdd:COG0243 491 TFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE-GAEP 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 671 LRKTYPLQLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTA 749
Cdd:COG0243 549 LDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVF 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1447699558 750 IGQGAWlkadmFGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 798
Cdd:COG0243 629 APHGWW-----YEPADDKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
93-641 |
3.57e-121 |
|
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: 377.76 E-value: 3.57e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 93 GRSIRRRMNHPDRLKYPMKRVG-----------KRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHV-LYGTGvDGG 160
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIFGgSYGWS-SAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 161 NITNSNVP-YRLMNSCGGFLSRYGSYSTAQISAAMSYMFGAND-----GNSPDDIA-NTKLVVMFGNNPAETRMSGGGVT 233
Cdd:cd02769 113 RFHHAQSLlHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEvyteqQTSWPVIAeHTELVVAFGADPLKNAQIAWGGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 234 ------YYVEQARERsNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVLISENMVDQPFLDKYCVGYDEktl 307
Cdd:cd02769 193 pdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDK--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 308 panaprnahYKAYILGEGpDGIAKTPEWAAKITSIPAEKIIQLAREIgSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVL 387
Cdd:cd02769 269 ---------FLPYLLGES-DGVPKTPEWAAAICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 388 TGNVGINGG--------NSGVREGSWDLGVEWFPMLENPVKTQISVFTWTDAIDH-GTEMtaTRDGvrgkEKLDVP-IKF 457
Cdd:cd02769 338 LGQIGLPGGgfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNpGKPF--DYNG----KKLTYPdIKL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 458 LWcYASNTLINQHGDINHTNEVLQddsKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPAT 537
Cdd:cd02769 412 VY-WAGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIVAMKQVV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 538 SAKFERKPIYWMLSEVAKRLGpdVYQTFTEGRSQHEWIKYLH----AKTKERNPEMPDYEEMKTTGIFKKKCPEEHYVAF 613
Cdd:cd02769 485 EPVGEARDDYDIFADLAERLG--VEEQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPEADFVRL 562
|
570 580
....*....|....*....|....*...
gi 1447699558 614 RAFREDPQANPLKTPSGKIEIYSERLAK 641
Cdd:cd02769 563 ADFREDPEANPLGTPSGRIEIFSETIAG 590
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
48-641 |
1.53e-111 |
|
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: 348.85 E-value: 1.53e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 48 SSCTVNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGeGKFERISWD 127
Cdd:cd02766 2 SVCPLDCPDTCSLLVTVEDGRIVRVE----GDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 128 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgnITNSNVPYRLMNScGGFLSRYGSYSTAQISAAMSYMFGANDGNSPD 207
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMG--LLQRAARGRFFHA-LGASELRGTICSGAGIEAQKYDFGASLGNDPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 208 DIANTKLVVMFGNNPAETRMSGggvTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLISE 287
Cdd:cd02766 154 DMVNADLIVIWGINPAATNIHL---MRIIQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALGVAKVLFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 288 NMVDQPFLDKYCVGYDEktlpanaprnahYKAYILgegpdgiAKTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWG 367
Cdd:cd02766 229 GLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 368 PQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVREGSwdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrg 447
Cdd:cd02766 290 MQRYRNGGQNVRAIDALPALTGNIGVPGG--GAFYSN------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 448 kekLDVPIKFLWCYASNtLINQHGDINHTNEVLQDDskCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIshesaGNM 527
Cdd:cd02766 325 ---SGPPVKALWVYNSN-PVAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY-----ASY 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 528 G--YVILAQPATSAKFERKPIYWMLSEVAKRLGpdvyqtFTEG---RSQHEWIKylhaktKERNPEMPdyeemKTTGIfk 602
Cdd:cd02766 394 WhyYLQYNEPAIPPPGEARSNTEIFRELAKRLG------FGEPpfeESDEEWLD------QALDGTGL-----PLEGI-- 454
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1447699558 603 kKCPEEHYVAFRAFREDPQANP-LKTPSGKIEIYSERLAK 641
Cdd:cd02766 455 -DLERLLGPRKAGFPLVAWEDRgFPTPSGKFEFYSERAAK 493
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
5-797 |
9.15e-105 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 340.88 E-value: 9.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 5 ISRRSLMK-TSALGSLALASSAFTLPFSQMVRAAEAPvEEKAVWSSCTVNCGSrclLRLHVKDDTvyWVESDTTGDDVYG 83
Cdd:PRK15102 1 ASRRRFLKgLGGLSAAGMLGPSLLTPRSALAAQAAAA-ETTKEWILTGSHWGA---FRAKVKNGR--FVEAKPFELDKYP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 84 NHQVRAclrgrsIRRRMNHPDRLKYPMKRV-----------GKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHvl 152
Cdd:PRK15102 75 TKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALH-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 153 ygTGVDGGNITNSnvpyrlMNSCGG-----------FLSRYGSYSTAQISAAMSYMFGAND----GNS-PDDIANTKLVV 216
Cdd:PRK15102 147 --TGQTGWQSTGQ------FHSATGhmqraigmhgnSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSwPLILENSKTIV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 217 MFGNNP---------AETRMSGGgvtyYVEQARER---SNARMIVIDPRYNDTAAGREDEWLPIRPGTDGALACAIAWVL 284
Cdd:PRK15102 219 LWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 285 ISENMVDQPFLDKYCVGYDEkTLPanaprnahykaYILGEgPDGIAKTPEWAAKITSIPAEKIIQLAREIgSAKPAYICQ 364
Cdd:PRK15102 295 YSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 365 GWGPQRHSNGEQTSRAIAMLSVLTGNVGINGG--------NS-GVRE----------GSWDLGVEwfPMLENP----VKT 421
Cdd:PRK15102 361 GWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGgisyghhySGiGVPSsggaipggfpGNLDTGQK--PKHDNSdykgYSS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 422 QISVFTWTDAIDH-GTEMTATrdgvrGKEKLDVPIKFLwCYASNTLINQHGDINHTNEVLQddsKCEMIVGIDHFMTASA 500
Cdd:PRK15102 439 TIPVARFIDAILEpGKTINWN-----GKKVTLPPLKMM-IFSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATC 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 501 KYCDILLPDLMPTEQEDLISHESAGNMGyVILAQPATSAKFERKPIYWMLSEVAKRLGPDvyQTFTEGRSQHEWIKYLHA 580
Cdd:PRK15102 510 RFADIVLPACTQFERNDIDQYGSYSNRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGRE--KEYTRGMDEMGWLKRLYQ 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 581 KTKERNP---EMPDYEEMKTTGI--FKKKCPeehYVAFRAFREDPQANPLKTPSGKIEIYSErlaKIAD----------T 645
Cdd:PRK15102 587 ECKQQNKgkfHMPEFDEFWKKGYveFGEGQP---WVRHADFREDPELNPLGTPSGLIEIYSR---KIADmgyddcqghpM 660
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 646 WeLKKDEIIHPlpayTPGFDgwddplrkTYPLQLTGFHYKARTHSsygnidvlqQACPQE-------------VWINPID 712
Cdd:PRK15102 661 W-FEKIERSHG----GPGSD--------KYPLWLQSVHPDKRLHS---------QLCESEelretytvqgrepVYINPQD 718
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 713 AQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGD--RVDHGGSINILTSHRP-SPLAKGNPSH 789
Cdd:PRK15102 719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEigALCTYGDPNTLTLDIGtSQLAQATSAH 798
|
....*...
gi 1447699558 790 SNLVQIEK 797
Cdd:PRK15102 799 TCLVEIEK 806
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
47-557 |
2.16e-104 |
|
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: 325.82 E-value: 2.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 47 WSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGegKFERISW 126
Cdd:cd00368 1 PSVCPF-CGVGCGILVYVKDGKVVRIE----GDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 127 DEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGniTNSNVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNSP 206
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNE--EAYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 207 DDIANTKLVVMFGNNPAETRMSgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAiawvlis 286
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 287 enmvdqpfldkycvgydektlpanaprnahykayilgegpdgiaktpEWAAKITSIPAEKIIQLAREIGSAKPAYICQGW 366
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 367 GPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVRegswdlgvewfpmlENPVKTQisvftwtdaidhgtemtatrdgvr 446
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPG--------------GNPLVSA------------------------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 447 gkekldvpikflwcyasntlinqhgdiNHTNEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHesagN 526
Cdd:cd00368 295 ---------------------------PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN----T 343
|
490 500 510
....*....|....*....|....*....|.
gi 1447699558 527 MGYVILAQPATSAKFERKPIYWMLSEVAKRL 557
Cdd:cd00368 344 EGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-662 |
3.51e-100 |
|
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: 318.48 E-value: 3.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 49 SCTVnCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDE 128
Cdd:cd02759 3 TCPG-CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG----RLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 129 ALDTISDNLRRILKDYGNEAVHVLYGTGvDGGNITNS---NVPYRLMNSCGGFLSRYGSYSTAQISAAMSYMFGANDGNS 205
Cdd:cd02759 78 ALDEIAEKLAEIKAEYGPESIATAVGTG-RGTMWQDSlfwIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 206 pdDIANTKLVVMFGNNPAETrmSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVLI 285
Cdd:cd02759 157 --DWENPECIVLWGKNPLNS--NLDLQGHWLVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 286 SENMVDQPFLDKYCVGYDEKtlpanAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQG 365
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEEL-----AERVQEY--------------TPEKVAEITGVPAEKIRKAARLYATAKPACIQWG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 366 WGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSgvregswdlgveWFPMlenpvktqisvftwtdaidhgtemtatrdgv 445
Cdd:cd02759 292 LAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL------------LIPY------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 446 rgkekldvPIKFLWCYASNTLINQHGDINhtneVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAG 525
Cdd:cd02759 329 --------PVKMLIVFGTNPLASYADTAP----VLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAE 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 526 NMGYVI--LAQPAtsakFERKPIYWMLSEVAKRLGPDvyqtftegrsQHEWIKYlhaKTKERnpempdyeemkttgifkk 603
Cdd:cd02759 397 NFVQLRqkAVEPY----GEAKSDYEIVLELGKRLGPE----------EAEYYKY---EKGLL------------------ 441
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699558 604 kcpeehyvafrafREDPQAnPLKTPSGKIEIYSERLakiadtWELKKDeiihPLPAYTP 662
Cdd:cd02759 442 -------------RPDGQP-GFNTPTGKVELYSTML------EELGYD----PLPYYRE 476
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
54-784 |
4.49e-93 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 306.04 E-value: 4.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 54 CGSRCLLRLHVKDDTVYWVESDTtgddvygNHQV---RACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEAL 130
Cdd:COG3383 14 CGVGCGIDLEVKDGKIVKVEGDP-------DHPVnrgRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 131 DTISDNLRRILKDYGNEAVHVLYgtgvdGGNITNSNvpYRLMNS-CGGFL--------SRYGSYSTAqisAAMSYMFGAn 201
Cdd:COG3383 83 DLVAERLREIQAEHGPDAVAFYG-----SGQLTNEE--NYLLQKlARGVLgtnnidnnARLCMASAV---AGLKQSFGS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 202 DG--NSPDDIANTKLVVMFGNNPAETrmsgggVTYYVEQARERsNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 279
Cdd:COG3383 152 DAppNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 280 IAWVLISENMVDQPFLDKYCVGYDEktlpanaprnahYKAYILGEgpdgiakTPEWAAKITSIPAEKIIQLAREIGSAKP 359
Cdd:COG3383 227 LLHVIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREAARLIAEAKR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 360 AYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGgnSGV---RE-----GSWDLGV--EWFP---MLENP-VKTQISV 425
Cdd:COG3383 288 AMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPG--TGPfplTGqnnvqGGRDMGAlpNVLPgyrDVTDPeHRAKVAD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 426 FTWTDAIDHGTEMTATR--DGVRGKEkldvpIKFLWCYASNTLInQHGDINHTNEVLqddSKCEMIVGIDHFMTASAKYC 503
Cdd:COG3383 366 AWGVPPLPDKPGLTAVEmfDAIADGE-----IKALWIIGENPAV-SDPDANHVREAL---EKLEFLVVQDIFLTETAEYA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 504 DILLPDLMPTEQED-LISHEsagnmGYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV-YQT----FTEGRSqhewiky 577
Cdd:COG3383 437 DVVLPAASWAEKDGtFTNTE-----RRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFdYDSpeevFDEIAR------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 578 lhaktkernpEMPD-----YEEMKTTGIFKKKCP-EEHYVAFRAFREDpqanpLKTPSGKieiyserlAKiadtwelkkd 651
Cdd:COG3383 505 ----------LTPDysgisYERLEALGGVQWPCPsEDHPGTPRLFTGR-----FPTPDGK--------AR---------- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 652 eiIHPLPAYTPgfdgwDDPLRKTYPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRV 726
Cdd:COG3383 552 --FVPVEYRPP-----AELPDEEYPLVLtTGrllDQWHTGTRT--RRSPRLNKHAPEPfVEIHPEDAARLGIKDGDLVRV 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699558 727 FNNNGEMLIAAKVTPRILPGVTAIgqgawlkADMFGDrvdhgGSINILTSHRPSPLAK 784
Cdd:COG3383 623 SSRRGEVVLRARVTDRVRPGTVFM-------PFHWGE-----GAANALTNDALDPVSK 668
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
48-640 |
7.35e-89 |
|
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: 291.31 E-value: 7.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 48 SSCTVNCGSRCLLRLHVKDDTVYWVESDttgdDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWD 127
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEPN----EWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 128 EALDTISDNLRRILKDYGNEAVHVLYGTGVDGgniTNSNVPYRLMNScGGFLSRYGSYSTAQ---ISAAMSYMFGANdGN 204
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGA---ILSYLRLALLGG-GLQDALTYGIDTGVgqgFNRVTGGGFMPP-TN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 205 SPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIAWVL 284
Cdd:cd02765 153 EITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 285 ISENMVDQPFLDKYC-----VGYDEKTL--PANAPRNAHYKAYIL---------------------GEGP---------- 326
Cdd:cd02765 228 LEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVwdtnsdspepvaatninpaleGEYTingvkvhtvl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 327 ----DGIAK-TPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVr 401
Cdd:cd02765 308 talrEQAASyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 402 egswdlgvewfpmlenpvktqisvftwtdaidhgtemtatrdgvrgkekldvpIKFLWCYASNtLINQHGDINHTNEVLq 481
Cdd:cd02765 387 -----------------------------------------------------IKFMYFMGSN-FLGNQPDRDRWLKVM- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 482 ddSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNmgYVILAQPATSAKFERKPIYWMLSEVAKRLGPDV 561
Cdd:cd02765 412 --KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLGD 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 562 YQTFTEgrsqHEWIKyLHAKTKERNPEMPDYEEMKTTGIFKKK-CPEEHYVAF--RAFredpqanplKTPSGKIEIYSER 638
Cdd:cd02765 488 YFPKTP----EDYVR-AFMNSDDPALDGITWEALKEEGIIMRLaTPEDPYVAYldQKF---------GTPSGKLEFYNEA 553
|
..
gi 1447699558 639 LA 640
Cdd:cd02765 554 AP 555
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
46-641 |
2.26e-82 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 270.71 E-value: 2.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 46 VWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERIS 125
Cdd:cd02755 1 VPSICEM-CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 126 WDEALDTISDNLRRILKDYGNEAVhvLYGTGVDGG--------------NITNSnvpyrlMNSCggFLSRygsystaqiS 191
Cdd:cd02755 76 WDEALQYIASKLKEIKEQHGPESV--LFGGHGGCYspffkhfaaafgspNIFSH------ESTC--LASK---------N 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 192 AAMSYMFGANDGNSPDDIANTKLVVMFGNNPAEtrmsGGGVTYYVEQARERSN-ARMIVIDPRYNDTAAgREDEWLPIRP 270
Cdd:cd02755 137 LAWKLVIDSFGGEVNPDFENARYIILFGRNLAE----AIIVVDARRLMKALENgAKVVVVDPRFSELAS-KADEWIPIKP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 271 GTDGALACAIAWVLISENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIQL 350
Cdd:cd02755 212 GTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLK--------AHVKPY-----------TPEWAAQITDIPADTIRRI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 351 AREIG-SAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsgvregswdlgveWFPmlenpvktqisvftwt 429
Cdd:cd02755 273 AREFAaAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGG--------------LYY---------------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 430 daidhgtemtatrdgvrGKEKLDVPIKFLWCYASNTLINQHgDINHTNEVLQddsKCEMIVGIDHFMTASAKYCDILLPD 509
Cdd:cd02755 323 -----------------AGSAKPYPIKALFIYRTNPFHSMP-DRARLIKALK---NLDLVVAIDILPSDTALYADVILPE 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 510 LMPTEQEDLISHESAGNMGYVIlAQPATSAKFERKPIYWMLSEVAKRLGpdvyqtftegrsqhewikylhaktkernpem 589
Cdd:cd02755 382 ATYLERDEPFSDKGGPAPAVAT-RQRAIEPLYDTRPGWDILKELARRLG------------------------------- 429
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1447699558 590 pdyeemkttgifkkkcpeehyvafrafredpqanPLKTPSGKIEIYSERLAK 641
Cdd:cd02755 430 ----------------------------------LFGTPSGKIELYSPILAK 447
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
4-798 |
7.91e-81 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 275.01 E-value: 7.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 4 EISRRSLMKTSALGSLALASSAFtLPFS-QMVRAAEAPVEEKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttgddvy 82
Cdd:PRK15488 2 SLSRRDFLKGAGAGCAACALGSL-LPGAlAANEIAQLKGKTKLTPSICEM-CSTRCPIEARVVNGKNVFIQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 83 GNHQV-----RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGV 157
Cdd:PRK15488 71 GNPKAksfgtKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 158 DGGNITNsnvpyrlmnscggFLSRYGS------YSTAQISAAM--SYMFGandGNSPDDIANTKLVVMFGNNPAE-TRMS 228
Cdd:PRK15488 151 LSSHLFH-------------LATAFGSpntfthASTCPAGYAIaaKVMFG---GKLKRDLANSKYIINFGHNLYEgINMS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 229 gggVTYYVEQARERSNARMIVIDPRYNdTAAGREDEWLPIRPGTDGALACAIAWVLISENMVDQPFLDKYCVGYDEktLP 308
Cdd:PRK15488 215 ---DTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE--LA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 309 ANAprnahyKAYilgegpdgiakTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQgWGPQRHSNGE--QTSRAIAMLSV 386
Cdd:PRK15488 289 ASV------KEY-----------TPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRATFTPEefDMRRAIFAANV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 387 LTGNVGINGGNSGVREGSWD---LGVEWFPMLENPVKTQISVFTWT--DAIDHGTEMTATRDGVRGK------EKLDVPI 455
Cdd:PRK15488 351 LLGNIERKGGLYFGKNASVYnklAGEKVAPTLAKPGVKGMPKPTAKriDLVGEQFKYIAAGGGVVQSiidatlTQKPYQI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 456 KFLWCYASNTLINQhgdiNHTNEVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLISHESAGNMGYVIlAQP 535
Cdd:PRK15488 431 KGWVMSRHNPMQTV----TDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYAL-RQR 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 536 ATSAKFERKPIYWMLSEVAKRLGPDVYQTFtegrsqhEWIKYLHAKTKERNPEMpdYEEMKTTGIFKKKCP----EEHYV 611
Cdd:PRK15488 506 VVEPIGDTKPSWQIFKELGEKMGLGQYYPW-------QDMETLQLYQVNGDHAL--LKELKKKGYVSFGVPlllrEPKMV 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 612 AfrAFRED-PQANP------------LKTPSGKIEIYSERLAKIAdtwelkkdeiihplPAY-TPGFDgwDDPLRKTYPL 677
Cdd:PRK15488 577 A--KFVARyPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALA--------------PGYgVPRYR--DVALKKEDEL 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 678 QLTGFHYKARTHSSYGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWL 756
Cdd:PRK15488 639 YFIQGKVAVHTNGATQNVPLLANLMSDNaVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFGS 718
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1447699558 757 KADMFGDRVDHGGSINILTSHRPSPLAkGNPSHSNLVQIEKV 798
Cdd:PRK15488 719 KNKELTRATGKGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
44-574 |
6.26e-79 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 261.87 E-value: 6.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 44 KAVWSSCTVNCGSRCLLRLHVKDDTVYWVESDT----TGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEG 119
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATdypeTPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 120 KFERISWDEALDTISDNLRRILKDYGNEAV----------HVLYGTGvdggnitnsnvpYRLMNSCGG----FLSRYGSY 185
Cdd:cd02750 81 KWKRISWDEALELIADAIIDTIKKYGPDRVigfspipamsMVSYAAG------------SRFASLIGGvslsFYDWYGDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 186 STAQisaamSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSnARMIVIDPRYNDTAAgREDE 264
Cdd:cd02750 149 PPGS-----PQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 265 WLPIRPGTDGALACAIAWVLISENMVDQPFLDKYcvgydeKTLPanaprnahYKAYilgegpdgiakTPEWAAKITSIPA 344
Cdd:cd02750 219 WVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 345 EKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSGVREGswdlgvewfpmlenpvktQIS 424
Cdd:cd02750 274 ETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVG------------------QPR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 425 VFtwtdaidhgtemtatrdgvrgkekldvpikFLWcyaSNTLINQHgdiNHTNEVLQD--DSKCEMIVGIDHFMTASAKY 502
Cdd:cd02750 336 VL------------------------------FVW---RGNLFGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTALY 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699558 503 CDILLPDLMPTEQEDLISheSAGNMgYVILAQPATSAKFERKPIYWMLSEVAKRLgpdVYQTFTeGRSQ----HEW 574
Cdd:cd02750 380 SDIVLPAATWYEKHDLST--TDMHP-FIHPFSPAVDPLWEAKSDWEIFKALAKKV---PWRTLT-GRQQfyldHDW 448
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
105-556 |
1.08e-67 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 228.05 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 105 RLKYPMKRvgkRGEGKFERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGvdGGNITNSNVPY-----RLMNSCGGFL 179
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALkkllnRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 180 SRYGSYSTAQiSAAMSYMFGAN--DGNSPDDIANTKLVVMFGNNPAETRMSGGGVTYyveQARERSNARMIVIDPRYNdt 257
Cdd:pfam00384 76 DHNGDLCTAA-AAAFGSDLRSNylFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 258 aAGREDEWLPIRPGTDGALACAIAWVLISENMVDQPFLDKycvgydektlpanaprnahykayilgegpdgiaktpewaa 337
Cdd:pfam00384 150 -LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 338 kitsipaekiiqlareigsakpAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNsgvregswdlgveWFPMLEN 417
Cdd:pfam00384 189 ----------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-------------WNGLNIL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 418 PvktqisvftwTDAIDHGTEMTATRDGVRGKEKLDVP----IKFLWcYASNTLINQHGDINHTNEVLQddsKCEMIVGID 493
Cdd:pfam00384 234 Q----------GAASPVGALDLGLVPGIKSVEMINAIkkggIKVLY-LLGNNPFVTHADENRVVKALQ---KLDLFVVYD 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699558 494 HFM-TASAKYCDILLPDLMPTEQEDLIShesagNM-GYVILAQPATSAKFERKPIYWMLSEVAKR 556
Cdd:pfam00384 300 GHHgDKTAKYADVILPAAAYTEKNGTYV-----NTeGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
45-650 |
1.10e-67 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 233.10 E-value: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 45 AVWSSCTvNCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRG----EGK 120
Cdd:cd02757 1 WVPSTCQ-GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 121 FERISWDEALDTISDNLRRILKDYGNEAVHVLYGTGVDGGNITNSNVPyRLMNSCGGFlsrygSYSTAQISA---AMSYM 197
Cdd:cd02757 76 FVPISWDEALDTIADKIRALRKENEPHKIMLHRGRYGHNNSILYGRFT-KMIGSPNNI-----SHSSVCAESekfGRYYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 198 FGANDGNSPDdIANTKLVVMFGNNPAETrmsgggvTYYVEQARE-----RSNARMIVIDPRYNDTAAgREDEWLPIRPGT 272
Cdd:cd02757 150 EGGWDYNSYD-YANAKYILFFGADPLES-------NRQNPHAQRiwggkMDQAKVVVVDPRLSNTAA-KADEWLPIKPGE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 273 DGALACAIAWVLISENMVDQPFLDKYCVGYD----EKTLPANAPR-----------NAHYKAYilgegpdgiakTPEWAA 337
Cdd:cd02757 221 DGALALAIAHVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKeksteglvkwwNLELKDY-----------TPEWAA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 338 KITSIPAEKIIQLAREIGSAKPAYICQGW-GPQRHSNGEQTSRAIAMLSVLTGNVGINGG-NSGVREGSWDLGVEWFpml 415
Cdd:cd02757 290 KISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGGlCPNMGVPKIKVYFTYL--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 416 ENPVKTQISVFTWTDAIDhgtemtatrdgvrgkeklDVPIkflwcyasntlinqhgdinhtnevlqddskcemIVGIDHF 495
Cdd:cd02757 367 DNPVFSNPDGMSWEEALA------------------KIPF---------------------------------HVHLSPF 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 496 MTASAKYCDILLPDLMPTEQEDLISHESAGNmGYVILAQPATSAKFERK---PIYWMLsevAKRLGPDvyqtftegrsqh 572
Cdd:cd02757 396 MSETTYFADIVLPDGHHFERWDVMSQENNLH-PWLSIRQPVVKSLGEVReetEILIEL---AKKLDPK------------ 459
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699558 573 ewikylhaktkernpempDYEEMKTTGIFKKKCPEEHYVAFRAFredpqANPLKTPSGKIEIYSERLAKIADTWELKK 650
Cdd:cd02757 460 ------------------GSDGMKRYAPGQFKDPETGKNNRWEF-----ENVFPTETGKFEFYSETLKKYLQNHADKK 514
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
54-631 |
1.23e-67 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 234.43 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 54 CGSRCLLRLHVKDDTVYWVesdtTGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRvgkRGEGKFERISWDEALDTI 133
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAV----RGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 134 SDNLRRILKDYGNEAVHVlYGTGvdggNITNSNvpYRLMNSC--GGFLSRYGSYSTAQI--SAAMSYM--FGAnDG--NS 205
Cdd:cd02754 80 AERFKAIQAEYGPDSVAF-YGSG----QLLTEE--YYAANKLakGGLGTNNIDTNSRLCmaSAVAGYKrsFGA-DGppGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 206 PDDIANTKLVVMFGNNPAETR---MSgggvtyYVEQARE-RSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAIA 281
Cdd:cd02754 152 YDDIEHADCFFLIGSNMAECHpilFR------RLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIRPGTDLALLNGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 282 WVLISENMVDQPFLDKYCVGYDEKTlpanaprnAHYKAYilgegpdgiakTPEWAAKITSIPAEKIIQLAREIGSAKPAY 361
Cdd:cd02754 225 HVLIEEGLIDRDFIDAHTEGFEELK--------AFVADY-----------TPEKVAEITGVPEADIREAARLFGEARKVM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 362 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVG--------ING-GNS-GVREGSWD---LGvewFPM-LENPVKTQISVFT 427
Cdd:cd02754 286 SLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsLTGqPNAmGGREVGGLanlLP---GHRsVNNPEHRAEVAKF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 428 WtdAIDHGTEMTAT-RDGVRGKEKL-DVPIKFLWCYASN---TLINQhgdinhtNEVLQDDSKCEMIVGIDHF-MTASAK 501
Cdd:cd02754 363 W--GVPEGTIPPKPgLHAVEMFEAIeDGEIKALWVMCTNpavSLPNA-------NRVREALERLEFVVVQDAFaDTETAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 502 YCDILLPDLMPTEQEdlishesaGNMG----YVILAQPATSAKFERKPIYWMLSEVAKRLGPDVYQTFTegrSQHEWIKY 577
Cdd:cd02754 434 YADLVLPAASWGEKE--------GTMTnserRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYT---SPEEVFEE 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699558 578 LHAKTKERNPEMP--DYEEMKTTGIfKKKCPEEHYVAFRAFREDPQANplkTPSGK 631
Cdd:cd02754 503 YRRLSRGRGADLSglSYERLRDGGV-QWPCPDGPPEGTRRLFEDGRFP---TPDGR 554
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
54-558 |
5.95e-65 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 225.56 E-value: 5.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 54 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVgkrgEGKFERISWDEALDTI 133
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 134 SDNLRRILKDYGNEAVHVLygTGVDGGN-------------ITNSNVpyrlmNSCggflSRYGSYSTAqisAAMSYMFGA 200
Cdd:cd02753 79 ASRLKEIKDKYGPDAIAFF--GSAKCTNeenylfqklaravGGTNNV-----DHC----ARLCHSPTV---AGLAETLGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 201 N-DGNSPDDIANTKLVVMFGNNPAETRMSGGgvtYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACA 279
Cdd:cd02753 145 GaMTNSIADIEEADVILVIGSNTTEAHPVIA---RRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALLNA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 280 IAWVLISENMVDQPFLDKYCVGYDE--KTLPANaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIQLAREIGSA 357
Cdd:cd02753 220 MAHVIIEEGLYDEEFIEERTEGFEElkEIVEKY---------------------TPEYAERITGVPAEDIREAARMYATA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 358 KPAYICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGnsGVregswdlgvewfpmleNPVKTQISVftwTDAIDHGTe 437
Cdd:cd02753 279 KSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT--GV----------------NPLRGQNNV---QGACDMGA- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 438 mtatrdgvrgkekldVP------IKFLWCYASNTLINqHGDINHTNEVLqddSKCEMIVGIDHFMTASAKYCDILLP--- 508
Cdd:cd02753 337 ---------------LPnvlpgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPaas 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699558 509 ------DLMPTEQEdlishesagnmgyVILAQPATSAKFERKPIYWMLSEVAKRLG 558
Cdd:cd02753 398 faekdgTFTNTERR-------------VQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
675-797 |
2.10e-63 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 207.91 E-value: 2.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSYGNIDVLQQACPQEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 754
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1447699558 755 WLKADmfGDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 797
Cdd:cd02794 81 WYEPD--ANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
675-797 |
5.43e-53 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 179.70 E-value: 5.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSYGNIDVLQQACP----QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI 750
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKvkgrEPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1447699558 751 GQGAWLKADmFGDRVDHGGSINILTSHRPSP-LAKGNPSHSNLVQIEK 797
Cdd:cd02777 81 PEGAWYDPD-DNGGLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
50-518 |
4.05e-48 |
|
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: 179.13 E-value: 4.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 50 CTVNCGsrclLRLHVKDDTVYWVESDTtgDDVYGNHQVraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISWDEA 129
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIRGDP--DDPLSKGYI--CPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 130 LDTISDNLRRILKDYGNEAVHVlYGTGVDG---GNITNSNVPYRLMNScggflSRYGSYSTAQI---SAAMSYMFGANDG 203
Cdd:cd02762 75 FDEIAERLRAIRARHGGDAVGV-YGGNPQAhthAGGAYSPALLKALGT-----SNYFSAATADQkpgHFWSGLMFGHPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 204 NSPDDIANTKLVVMFGNNPAETR---MSGGGVTYYVEQARERSnARMIVIDPRYNDTAAgREDEWLPIRPGTDGALACAI 280
Cdd:cd02762 149 HPVPDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLFVRPGTDAWLLAAM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 281 AWVLISENMVDQPFLDKYCVGYDEkTLPANAPRnahykayilgegpdgiakTPEWAAKITSIPAEKIIQLAREIGSAKPA 360
Cdd:cd02762 227 LAVLLAEGLTDRRFLAEHCDGLDE-VRAALAEF------------------TPEAYAPRCGVPAETIRRLAREFAAAPSA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 361 YICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGN---------------SGVREGSWDLGVEWFPmlenPVKTQISV 425
Cdd:cd02762 288 AVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAmfttpaldlvgqtsgRTIGRGEWRSRVSGLP----EIAGELPV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 426 FTWTDAIDhgtemtatRDGvrgkeklDVPIKFLWCYASNTLINQhGDINHTNEVLQddsKCEMIVGIDHFMTASAKYCDI 505
Cdd:cd02762 364 NVLAEEIL--------TDG-------PGRIRAMIVVAGNPVLSA-PDGARLEAALG---GLEFMVSVDVYMTETTRHADY 424
|
490
....*....|...
gi 1447699558 506 LLPDLMPTEQEDL 518
Cdd:cd02762 425 ILPPASQLEKPHA 437
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
54-558 |
8.91e-42 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 162.69 E-value: 8.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 54 CGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTI 133
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAFSIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 134 SDNLRRILKdygNEAVHVLYGTGVDGgnitnsnvpyrlMNSCGGFLSR---------YGSYSTAQISAAMSYMFGAN--D 202
Cdd:cd02763 83 TKRLKAARA---TDPKKFAFFTGRDQ------------MQALTGWFAGqfgtpnyaaHGGFCSVNMAAGGLYSIGGSfwE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 203 GNSPdDIANTKLVVMFG------NNPAETRMsgggvtyyveQARERSNARMIVIDP---RYNDTAagreDEWLPIRPGTD 273
Cdd:cd02763 148 FGGP-DLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPvrtGYAAIA----DEWVPIKPGTD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 274 GALACAIAWVLISENMVDQPFLDKYcvgydektlpANAPRNAHYkayilgegpdgiakTPEWAAKITSIPAEKIIQLARE 353
Cdd:cd02763 213 GAFILALAHELLKAGLIDWEFLKRY----------TNAAELVDY--------------TPEWVEKITGIPADTIRRIAKE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 354 IGSAK-------PAYICQGWGPQR------------------HSNGEQTSRAIAMLSVLTGNVGINGGN----------- 397
Cdd:cd02763 269 LGVTArdqpielPIAWTDVWGRKHekitgrpvsfhamrgiaaHSNGFQTIRALFVLMMLLGTIDRPGGFrhkppyprhip 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 398 ---------SGVREGS--------WDLGVEWFPMLENPVKTQIS-VFTWTDAID-HGTEMTATRDGVRGKEkldVPIKFL 458
Cdd:cd02763 349 plpkppkipSADKPFTplygpplgWPASPDDLLVDEDGNPLRIDkAYSWEYPLAaHGCMQNVITNAWRGDP---YPIDTL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 459 WCYASNTLINQHGDINHTNEVLQD-----DSKCEMIVGIDHFMTASAKYCDILLPDLMPTEQEDLIS------HESAGNM 527
Cdd:cd02763 426 MIYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSlldrpiSEADGPV 505
|
570 580 590
....*....|....*....|....*....|.
gi 1447699558 528 GYVilAQPATSAKFERKPIYWMLSEVAKRLG 558
Cdd:cd02763 506 DAI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
50-411 |
1.63e-38 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 152.55 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 50 CTVNCGsrclLRLHVKDDTVYWVESDTTGDDVYGNHqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrGEGKFERISWDEA 129
Cdd:cd02752 7 CSVGCG----LIAYVQNGVWVHQEGDPDHPVNRGSL----CPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 130 LDTISDNLRRILKD---YGNEAVHVLYGTgvDG----GNITNSNVPYRLMNSCGGFLSRYGSYSTAQI-------SAAMS 195
Cdd:cd02752 77 LDEIARKMKDIRDAsfvEKNAAGVVVNRP--DSiaflGSAKLSNEECYLIRKFARALGTNNLDHQARIuhsptvaGLANT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 196 YMFGANDgNSPDDIANTKLVVMFGNNPAETRMSGggvTYYVEQARERSNARMIVIDPRYNDTAAgREDEWLPIRPGTDGA 275
Cdd:cd02752 155 FGRGAMT-NSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRTAA-KADLYVPIRSGTDIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 276 LACAIAWVLIsenmvdqpfldKYcvgydektlpanaprnahykayilgegpdgiakTPEWAAKITSIPAEKIIQLAREIG 355
Cdd:cd02752 230 FLGGMINYII-----------RY---------------------------------TPEEVEDICGVPKEDFLKVAEMFA 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699558 356 S----AKPAYI--CQGWgpQRHSNGEQTSRAIAMLSVLTGNVGING-------GNSGVrEGSWDLGVEW 411
Cdd:cd02752 266 AtgrpDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGggvnalrGHSNV-QGATDLGLLS 331
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
88-642 |
2.52e-38 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 152.88 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 88 RACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTISDNLR-------------RILK--------DYGN 146
Cdd:cd02758 66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVVEGGDlfgeghveglkaiRDLDtpidpdhpDLGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 147 EAVHVLYGTGVDGGNITNSNvpyRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNsPD---DIANTKLVVMFGNN 221
Cdd:cd02758 146 KANQLLYTFGRDEGRTPFIK---RFANQAFGTVnfGGHGSYCGLSYRAGNGALMNDLDGY-PHvkpDFDNAEFALFIGTS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 222 PAE-----TRMSGggvtyYVEQARERSNARMIVIDPRY--NDTAAGREDEWLPIRPGTDGALACA-IAWvlISENMvdqp 293
Cdd:cd02758 222 PAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAmIRW--IIENE---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 294 fldkycvGYDEKTLpANAPRNAHYKA---------------------YILGEgpDGIAKTPEWAAKITSIPAEKIIQLAR 352
Cdd:cd02758 291 -------RYNAEYL-SIPSKEAAKAAgepswtnathlvitvrvksalQLLKE--EAFSYSLEEYAEICGVPEAKIIELAK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 353 EIGSA--KPAYICQgwGPQRHSNGEQTSRAIAMLSVLTGNV----GINGGNSGVREGSWDLGVEW--FPMLENP------ 418
Cdd:cd02758 361 EFTSHgrAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLnwkgGLLMSGGGFADNSAGPRYDFkkFFGEVKPwgvpid 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 419 ---------------VKTQISVF----TWTD-AIDHGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTN 477
Cdd:cd02758 439 rskkayektseykrkVAAGENPYpakrPWYPlTPELYTEViASAAEG------YPYKLKALILWMANPVYGAPGLVKQVE 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 478 EVLQDDSKCEMIVGIDHFMTASAKYCDILLPDLMPTEqedliSHESAGNMGYVI-LAQ--------PATSAKFERKPIYW 548
Cdd:cd02758 513 EKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYE-----SWGFSTPWGGVPtKAStarwpviaPLTEKTANGHPVSM 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 549 --MLSEVAKRLG---------PDVYqtfteGRS---QHEWIKYLH-----AKTKERNPEMPDYEEMKTTG-------IFK 602
Cdd:cd02758 588 esFLIDLAKALGlpgfgpnaiKDGQ-----GNKfplNRAEDYYLRvaaniAYDGKAPVPDASEEELKLTGvnrpipaLKR 662
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1447699558 603 KKCPEE-HYVAF------------RAFREDPQANPLKTPsgkIEIYSERLAKI 642
Cdd:cd02758 663 TLKPEEwRKVAYilarggrfapyeESYDGDNLRNRWGKT---LQIWNEKLAKS 712
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
89-753 |
5.47e-31 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 130.89 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 89 ACLRGRSIRRRMNHPDRLKYPMKRVGKRGEGKFERISWDEALDTIS-----------DNLRRI--LK--------DYGNE 147
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVeggdlfgeghvDGLRAIrdLDtpidaknpEYGPK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 148 AVHVLYGTGVDGGNitnSNVPYRLMNSCGGFL--SRYGSYSTAQISAAMSYMFGANDGNS---PDdIANTKLVVMFGNNP 222
Cdd:PRK14991 221 ANQLLVTNASDEGR---DAFIKRFAFNSFGTRnfGNHGSYCGLAYRAGSGALMGDLDKNPhvkPD-WDNVEFALFIGTSP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 223 AEtrmSGGGvtyYVEQARERSNARM------IVIDPR---YNDTAAGREDEWLPIRPGTDGALACA-IAWVLisEN---- 288
Cdd:PRK14991 297 AQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAMGmIRWII--DNqryn 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 289 --------------------------MVDQP-------FL------------------DKYCV-GYDEKTLPANAPRNAH 316
Cdd:PRK14991 369 adylaqpgvaamqaageaswtnathlVIADPghprygqFLrasdlglpfegeargdgeDTLVVdAADGELVPATQAQPAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 317 --YKAYILGEGPDGIA--------------KTPEWAAKITSIPAEKIIQLAREIGS--AKPAYICQGwGpQRHSNGEQTS 378
Cdd:PRK14991 449 lfVEQYVTLADGQRVRvksslqllkeaarkLSLAEYSEQCGVPEAQIIALAEEFTShgRKAAVISHG-G-TMSGNGFYNA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 379 RAIAMLSVLTGNVGINGG---NSG-------------------VREGSWDLGVEWFPML------------ENPVKTQIS 424
Cdd:PRK14991 527 WAIMMLNALIGNLNLKGGvvvGGGkfpgfgdgprynlasfagkVKPKGVSLSRSKFPYEksseyrrkveagQSPYPAKAP 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 425 VFTWTDAIdhGTEM-TATRDGvrgkekLDVPIKFLWCYASNTLINQHGDINHTNEVLQDDSKCEMIVGIDHFMTASAKYC 503
Cdd:PRK14991 607 WYPFVAGL--LTEMlTAALEG------YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISIDAFINETTALA 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 504 DILLPDL-------MPTEQEDLISHESAGNMGYVilaQPATSAKFERKPIYW--MLSEVAKRL-----GPDVYQTfTEGR 569
Cdd:PRK14991 679 DYIVPDThtyeswgFTAPWGGVPTKASTARWPVV---EPRTAKTADGQPVCMesFLIAVAKRLqlpgfGDNAIKD-AQGN 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 570 -----SQHEWikYLHAKT------KERNPEMPDyEEMKTTG-------IFKKKCPEE-HYVAF------------RAFRE 618
Cdd:PRK14991 755 thplnRAEDF--YLRGAAniaylgKTPVADASD-EDIALTGvsrilpaLQATLKPDEvRRVAFiyarggrfapaeSAYDE 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 619 DPQANPLKTPsgkIEIYSERLAKIADTwelKKDEIIHPLPA-YTPGF-DGwdDPLRKTY-----PLQLTGFhyKARTHSS 691
Cdd:PRK14991 832 ERMGNRWKKP---LQIWNEDVAAARHS---MTGERYSGCPTwYPPRLaDG--TPLREQFpesqwPLLLISF--KSNLMSS 901
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699558 692 YGN-IDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 753
Cdd:PRK14991 902 MSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
675-797 |
2.63e-30 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 115.81 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ---EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIG 751
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQgrePIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1447699558 752 QGAWLkaDMFGDRVDHG----GSINILTSHRP-SPLAKGNPSHSNLVQIEK 797
Cdd:cd02793 81 TGAWY--DPDDPGEPGPlckhGNPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
677-792 |
2.43e-29 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 112.37 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 677 LQLTGFHYKARTHSSYGNIDVLQQACPQE--VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGA 754
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1447699558 755 WlkadmfgdRVDHGGSINILTSHRPSPLAKGNPSHSNL 792
Cdd:pfam01568 81 W--------YEPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
48-558 |
9.27e-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: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 48 SSCTVNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGNhQVRACLRGRSIRRRMNHPDRLKYPMKRVG-KRGEGK---FER 123
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 124 ISWDEALDTISDNLRRIL-KDYGNEAVHVLYGTGVDGGNItnsnvPYRLMNSCGGFLSRYG----SYSTAQI--SAAMSY 196
Cdd:cd02760 81 ISWDEALDLVAAKLRRVReKGLLDEKGLPRLAATFGHGGT-----PAMYMGTFPAFLAAWGpidfSFGSGQGvkCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 197 MFGANDGNSPDDIANTKL---VVMFGNNpaeTRMSGG--GVTYYVEqARERSnARMIVIDPRYNDTAAgREDEWLPIRPG 271
Cdd:cd02760 156 LYGEFWHRAFTVAADTPLanyVISFGSN---VEASGGpcAVTRHAD-ARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 272 TDGALACAIAWVLISE---NMVDQPFL-DK----YCVG----------------YDEKT-----------LPANAPRNAH 316
Cdd:cd02760 230 TDPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGpdglylrdaatgkplvWDERSgravpfdtrgaVPAVAGDFAV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 317 YKAY-ILGEGP-----------------DGIAK-TPEWAAKITSIPAEKIIQLARE------IGSA----------KPAY 361
Cdd:cd02760 310 DGAVsVDADDEtaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 362 ICQGWGPQRHSNGEQTSRAIAMLSVLTGNVGINGGNSG---------------VREGSWDLGVEWF-----------PML 415
Cdd:cd02760 390 VTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGttvrlnrphddrlasVKPGEDGFMAQGFnptdkehwvvkPTG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 416 ENPVKTQISVF---TWTDAIDHGTEMTATRDGVRGKEKLDVPIK--FLWCYASNTLINqhgdINHTNEVLQDDSKCEMIV 490
Cdd:cd02760 470 RNAHRTLVPIVgnsAWSQALGPTQLAWMFLREVPLDWKFELPTLpdVWFNYRTNPAIS----FWDTATLVDNIAKFPFTV 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699558 491 GIDHFMTASAKYCDILLPDLMPTEQEDLISH------ESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLG 558
Cdd:cd02760 546 SFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfvEQFWEHRGVVLRQPAVEPQGEARDFTWISTELAKRTG 619
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
105-568 |
3.57e-26 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 113.94 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 105 RLKYPMKRvgKRGEGKFERISWDEALDTISDNLRRILKD----Y-----GNEAVHVL------YGTgvdggnitnSNVPy 169
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALDPDraafYtsgraSNEAAYLYqlfaraYGT---------NNLP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 170 rlmnSCggflSRYGSYSTaqiSAAMSYMFGANDGN-SPDDIANTKLVVMFGNNPAET--RMsgggvTYYVEQARERSnAR 246
Cdd:cd02767 132 ----DC----SNMCHEPS---SVGLKKSIGVGKGTvSLEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 247 MIVIDP-------RYNDTAAGRE---------DEWLPIRPGTDGALACAIAWVLI-----SENMVDQPFLDKYCVGYDEk 305
Cdd:cd02767 195 IIVINPlrepgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAKHLIerddePGNVLDHDFIAEHTSGFEE- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 306 tlpanaprnahYKAYIlgegpdgiaKTPEWA--AKITSIPAEKIIQLAREIGSAKPAYICQGWGPQRHSNGEQTSRAIAM 383
Cdd:cd02767 274 -----------YVAAL---------RALSWDeiERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 384 LSVLTGNVGING-------GNSGVrEGSWDLGVEWFPMLENpvKTQIS-VFTWTDAIDHG-TEMTATRDGVRGKekldvp 454
Cdd:cd02767 334 LALLRGNIGRPGaglmpirGHSNV-QGDRTMGITEKPFPEF--LDALEeVFGFTPPRDPGlDTVEAIEAALEGK------ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 455 IKFLWCYASNtLINQHGDINHTNEVLqddSKCEMIVGID------HFMTASakyCDILLPDLMPTEQ------------E 516
Cdd:cd02767 405 VKAFISLGGN-FAEAMPDPAATEEAL---RRLDLTVHVAtklnrsHLVHGE---EALILPCLGRTEIdmqaggaqavtvE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699558 517 DLIS--HESAG---NMGYVILAQPATSAK-----FERKPIYW-MLSEVAKRLGPDVYQTFTEG 568
Cdd:cd02767 478 DSMSmtHTSRGrlkPASRVLLSEEAIVAGiagarLGEAKPEWeILVEDYDRIRDEIAAVIYEG 540
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
684-789 |
1.27e-23 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 95.85 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 684 YKARTHSSY-GNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkadmf 761
Cdd:cd02775 1 LRDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWG------ 74
|
90 100
....*....|....*....|....*...
gi 1447699558 762 gDRVDHGGSINILTSHRPSPLAKGNPSH 789
Cdd:cd02775 75 -HRGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
675-798 |
4.63e-23 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 95.13 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 753
Cdd:cd02785 2 YPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1447699558 754 AWlkadmfgDRVDHGGSINILTS----HRPSPLAKGNPSHSN-LVQIEKV 798
Cdd:cd02785 82 WW-------SRYFQEGSLQDLTSpfvnPVHEYIYGPNSAFYDtLVEVRKA 124
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
675-795 |
2.79e-20 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 86.95 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQG 753
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKEGePTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1447699558 754 AWLKAdmFGDrvdhGGSINILTSHRPSPLAKGNPSHSNLVQI 795
Cdd:cd02786 81 WWREH--SPD----GRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
4-351 |
7.98e-16 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 81.87 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 4 EISRRSLMKTSALGSLAlASSAFTLPFSQMVRAAEApvEEKAVWSS--CTVnCGSRCLLRLHVKDDTVYWVESDTTGDDV 81
Cdd:PRK13532 2 KLSRRDFMKANAAAAAA-AAAGLSLPAVANAVVGSA--QTAIKWDKapCRF-CGTGCGVLVGTKDGRVVATQGDPDAPVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 82 YG-NhqvraCLRGRSIRRRMNHPDRLKYPMKRVgKRGE----GKFERISWDEALDTISDNLRRILKDYGNEAVHVlYGTG 156
Cdd:PRK13532 78 RGlN-----CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGM-FGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 157 ---VDGGnitnsnvpY---RLMNscGGFLS-------RYgsystAQISAAMSYM--FGANDgnsP----DDIANTKLVVM 217
Cdd:PRK13532 151 qwtIWEG--------YaasKLMK--AGFRSnnidpnaRH-----CMASAVVGFMrtFGIDE---PmgcyDDIEAADAFVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 218 FGNNPAE------TRMSGggvtyyveqaRERSN--ARMIVIDP---RYNDTAagreDEWLPIRPGTDGALACAIAWVLIS 286
Cdd:PRK13532 213 WGSNMAEmhpilwSRVTD----------RRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILNYIANYIIQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 287 ENMVDQPFLDKYCV--------GY-----DEKTLPANAPRNA---------HYKAYilgegpdgIAK-TPEWAAKITSIP 343
Cdd:PRK13532 279 NNAVNWDFVNKHTNfrkgatdiGYglrptHPLEKAAKNPGTAgksepisfeEFKKF--------VAPyTLEKTAKMSGVP 350
|
....*...
gi 1447699558 344 AEKIIQLA 351
Cdd:PRK13532 351 KEQLEQLA 358
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
675-797 |
1.58e-14 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 70.80 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTgfhYKART----HSSYGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVtA 749
Cdd:cd02781 2 YPLILT---TGARSyyyfHSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV-V 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1447699558 750 IGQGAWLKADMFGDRVDHGG----SINILTSHRPS-PLAKGNPSHSNLVQIEK 797
Cdd:cd02781 78 RAEHGWWYPEREAGEPALGGvwesNANALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
44-299 |
5.96e-14 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 76.01 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 44 KAVWSSCTVNC-GSrCLLRLHVKDDTVYWvESD-----TTGDDvYGNHQVRACLRGRSIRRRMNHPDRLKYPMKR----- 112
Cdd:COG5013 47 KVVRSTHGVNCtGS-CSWKVYVKDGIITW-ETQqtdypRTGPD-LPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvlle 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 113 -----------------------------VGKRGEGKFERISWDEALDTISDNLRRILKDYGNEAVH----------VLY 153
Cdd:COG5013 124 lwreararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 154 GTGVdggnitnsnvpyRLMNSCGG-FLSRYGSYstAQISAAMSYMFG-ANDGNSPDDIANTKLVVMFGNNPAETRmsggg 231
Cdd:COG5013 204 AAGA------------RFLSLIGGvMLSFYDWY--ADLPPASPQVWGeQTDVPESADWYNSGYLIMWGSNVPQTR----- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699558 232 vT----YYVEqARERSnARMIVIDPRYNDtAAGREDEWLPIRPGTDGALACAIAWVLISENMVDQ--PFLDKYC 299
Cdd:COG5013 265 -TpdahFMTE-ARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
676-782 |
1.79e-13 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 68.17 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 676 PLQLTGFHYKARTHSSYGN---IDVLQQACPqEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI-- 750
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDnllMLRLQRGGP-VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMyh 79
|
90 100 110
....*....|....*....|....*....|..
gi 1447699558 751 GQGAWLKADMFGDRVDHGGSINILTSHRPSPL 782
Cdd:cd02776 80 AQERHVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
43-102 |
2.12e-13 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 65.01 E-value: 2.12e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 43 EKAVWSSCTvNCGSRCLLRLHVKDDTVYWVESDTTGDDVYGnhqvRACLRGRSIRRRMNH 102
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
673-784 |
6.97e-13 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 65.99 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 673 KTYPLQL-TG-----FHYKARThssyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 745
Cdd:cd00508 1 EEYPLVLtTGrllehWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1447699558 746 GVTAIGqgawlkadM-FGDRVDhGGSINILTSHRPSPLAK 784
Cdd:cd00508 77 GTVFMP--------FhWGGEVS-GGAANALTNDALDPVSG 107
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
83-563 |
2.68e-12 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 70.20 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 83 GNHQVRACLRGRSIRRRMNHP--DRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNE---AVHVLYGTGV 157
Cdd:cd02756 93 GNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDdavFASRFDHGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 158 DGGNITNSNVpyrlmnscGGFLsrYGSYSTAQIS------------AAMSYMFGAnDGNSPDDIANTKLVVMFGNNPAET 225
Cdd:cd02756 169 GGGFENNWGV--------GKFF--FMALQTPFVRihnrpaynsevhATREMGVGE-LNNSYEDARLADTIVLWGNNPYET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 226 RmsgggVTYYVE---------------QARERSN----ARMIVIDPRYNDT------AAGREDEW-LPIRPGTDGALACA 279
Cdd:cd02756 238 Q-----TVYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRRTETvhaaeaAAGKDRVLhLQVNPGTDTALANA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 280 IAWVlISEnmvdqpfldkycvGYDEktlpanaprnahykayILGEgpdgiaktpewAAKITSIPAEKIIQLA-----REI 354
Cdd:cd02756 313 IARY-IYE-------------SLDE----------------VLAE-----------AEQITGVPRAQIEKAAdwiakPKE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 355 GSAKPAYIC---QG--WGPQRHsngeQTSRAIAMLSVLTGNVGINGGN----SGVREG---SWDLGVEWFPMLENPVKT- 421
Cdd:cd02756 352 GGYRKRVMFeyeKGiiWGNDNY----RPIYSLVNLAIITGNIGRPGTGcvrqGGHQEGyvrPPPPPPPWYPQYQYAPYId 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 422 ------QISVFTWTDAIDHGTEMTATrdgvRGKEKLDVPIKFLWCYASNTLINQHGDINHTNEVLQD--DSKCEMIVGID 493
Cdd:cd02756 428 qllisgKGKVLWVIGCDPYKTTPNAQ----RLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGDaiQPGGLFIVVQD 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 494 HFMTASAKYCDILLPDLMPTEQEDLishESAGNMGYVILAQPATSAKFERKPIYWMLSEVAKRLgPDVYQ 563
Cdd:cd02756 504 IYPTKLAEDAHVILPAAANGEMNET---SMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRI-YELYQ 569
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
675-786 |
6.39e-12 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 63.85 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 675 YPLQLTGFHYKARTHSSyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--G 751
Cdd:cd02780 1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENpVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1447699558 752 QGAW----LKADMFGDRVDH------GGSINILTSHRPSPLAKGN 786
Cdd:cd02780 80 YGHWaygaVASTIDGKDLPGdawrgaGVNINDIGLVDPSRGGWSL 124
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
675-748 |
1.56e-10 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 59.17 E-value: 1.56e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699558 675 YPLQL-TG---FHYKARTHSsyGNIDVLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVT 748
Cdd:cd02790 3 YPLVLtTGrvlYHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
674-798 |
1.78e-10 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 59.12 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 674 TYPLQL-TG-----FHYKARThssyGNIDVLQQACPQ-EVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPG 746
Cdd:cd02791 2 EYPLWLnTGrvrdqWHTMTRT----GRVPRLNAHVPEpYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1447699558 747 VtaigqgawLKADMF-GDRVDHGGSINILTSHRPSPLAKGNPSHSNLVQIEKV 798
Cdd:cd02791 78 E--------VFVPMHwGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
44-142 |
1.71e-09 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 61.01 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 44 KAVWSSCTvNCGSRCLLRLHVKDDTVYWVESdttGDDVYGNHqVRACLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFER 123
Cdd:COG1034 216 KKTPSICP-HCSVGCNIRVDVRGGKVYRVLP---RENEAVNE-EWLCDKGRFGYDGLNSPDRLTRPLVRKD----GELVE 286
|
90
....*....|....*....
gi 1447699558 124 ISWDEALDTISDNLRRILK 142
Cdd:COG1034 287 ASWEEALAAAAEGLKALKK 305
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-102 |
1.94e-09 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 53.79 E-value: 1.94e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 43 EKAVWSSCTVnCGSRCLLRLHVKDDTVYWVEsdttGDDVYGNHQVRACLRGRSIRRRMNH 102
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVR----GDPDHPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
708-798 |
2.18e-09 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 56.25 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 708 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWLKADMFGDRVDHGG-SINILTSHRP-SPLAkG 785
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPGVSGAGSRPGvNVNDLTDDTQrDPLS-G 115
|
90
....*....|....
gi 1447699558 786 NPSHSNL-VQIEKV 798
Cdd:cd02782 116 NAAHNGVpVRLARV 129
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
688-797 |
3.09e-09 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 55.36 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 688 THSSYGNIDVLQQACP-QEVWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAI--GQGAWLKADMFGDR 764
Cdd:cd02778 13 THGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGFGHWAPALSRAYG 92
|
90 100 110
....*....|....*....|....*....|...
gi 1447699558 765 vdHGGSINILTSHRPSPLAKGNPSHSNLVQIEK 797
Cdd:cd02778 93 --GGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
50-397 |
3.84e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 59.48 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 50 CTVnCGSRCllrlhvkDDTVYWVEsdttgddvyGNHQV---RACLRGRSIRRRMNHPDRLKYPMKRvgkrgegkFERISW 126
Cdd:COG1029 10 CPF-CGCLC-------DDLEVEVE---------GGKIVvvkNACAIGAAKFERAVSDHRITSPRIR--------GKEVSL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 127 DEALDTISdnlrRILKdygnEAVHVLYGtgvdGGNITNSN---VPYRLMNSCGGFLSrygsySTAQISAAMSYMFGANDG 203
Cdd:COG1029 65 EEAIDKAA----EILA----NAKRPLIY----GLSSTDCEamrAGLALAERVGAVVD-----NTASVCHGPSLLALQDVG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 204 NSPDDIANTK----LVVMFGNNPAET------RMSGGGVTYYVEQARERSnaRMIVIDPRYNDTAAgREDEWLPIRPGTD 273
Cdd:COG1029 128 WPTCTLGEVKnradVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGRKDR--TVIVVDPRPTDTAK-VADLHLQVKPGRD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 274 GALACAIawvlisenmvdqpfldkycvgydektlpanaprnahyKAYILGEGPDgiaktpewAAKITSIPAEKIIQLARE 353
Cdd:COG1029 205 YEVLSAL-------------------------------------RALVRGKELS--------PEEVAGIPVEDLEELAER 239
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699558 354 IGSAKPAYICQGWG----PQRHSNGE----------QTSRAIAMlsVLTGNVGINGGN 397
Cdd:COG1029 240 LKNAKYGVIFWGMGltqsPGKHLNVDaaielvrdlnRYTKFSIL--PLRGHYNVAGAN 295
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
103-545 |
7.70e-09 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 59.04 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 103 PDRLKYPMKRVGKRGEGKferISWDEALDTISDNLRRIlKDYGNEAVHvlygTGVDGGNITNSNVpyrlmnscGGFLSRY 182
Cdd:cd02764 97 PDRAQGPLRRGIDGAYVA---SDWADFDAKVAEQLKAV-KDGGKLAVL----SGNVNSPTTEALI--------GDFLKKY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 183 GSYSTAQISA--------AMSYMFGaNDGNSPDDIANTKLVVMFGNNPAETRMSG-GGVTYYVEQARERSNA---RMIVI 250
Cdd:cd02764 161 PGAKHVVYDPlsaedvneAWQASFG-KDVVPGYDFDKAEVIVSIDADFLGSWISAiRHRHDFAAKRRLGAEEpmsRLVAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 251 DPRYNDTAAGrEDEWLPIRPGTDGALACAIAWVLISenmvdqpfldkycvgydektLPANAPRNAHYKAYILgegpdgiA 330
Cdd:cd02764 240 ESVYTLTGAN-ADVRLAIRPSQEKAFALGLAHKLIK--------------------KGAGSSLPDFFRALNL-------A 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 331 KTPEWAAKITSIPAEKIIQLAREIGSAKPAYICQGwgpQRHSNGEQTSRAIAM--LSVLTGNVGinggnSGVREGSwdlg 408
Cdd:cd02764 292 FKPAKVAELTVDLDKALAALAKALAAAGKSLVVAG---SELSQTAGADTQVAVnaLNSLLGNDG-----KTVDHAR---- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 409 vewfPMLENPVKTQISVFTWTDAIDHGtemtatrdgvrgkeklDVPIKFLwcYASNTLINQHGDINHTnEVLqddSKCEM 488
Cdd:cd02764 360 ----PIKGGELGNQQDLKALASRINAG----------------KVSALLV--YDVNPVYDLPQGLGFA-KAL---EKVPL 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699558 489 IVGIDHFMTASAKYCDILLPDLMPTEQEDlishESAGNMGYVILAQPATSAKFERKP 545
Cdd:cd02764 414 SVSFGDRLDETAMLCDWVAPMSHGLESWG----DAETPDGTYSICQPVIAPLFDTRS 466
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
673-797 |
6.19e-07 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 48.76 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 673 KTYPLQLTG------FHYKARTHSSYGnidvLQQACPQE-VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILP 745
Cdd:cd02792 1 EEFPLVLTTgrltehFHGGNMTRNSPY----LAELQPEMfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1447699558 746 GVTAIgqgAWLKADMFGDRvdhGGSINILTSHRPSPLAKGNPSHSNLVQIEK 797
Cdd:cd02792 77 HEVGI---PYHWGGMGLVI---GDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
52-225 |
1.34e-06 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 51.51 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 52 VNCGSRCLLRLHVKDDTVYWVESDTtgddvygNHQVRACL---RGR----SIrrrmNHPDRLKYPMKRVGkrgeGKFERI 124
Cdd:cd02768 5 VHDALGSNIRVDVRGGEVMRILPRE-------NEAINEEWisdKGRfgydGL----NSRQRLTQPLIKKG----GKLVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 125 SWDEALDTIsdnlRRILKDYGNEAVHVLYGTGVDggniTNSNVPY-RLMNSCG----GFLSRYGSYSTAQISAAMSYMfg 199
Cdd:cd02768 70 SWEEALKTV----AEGLKAVKGDKIGGIAGPRAD----LESLFLLkKLLNKLGsnniDHRLRQSDLPADNRLRGNYLF-- 139
|
170 180
....*....|....*....|....*.
gi 1447699558 200 andGNSPDDIANTKLVVMFGNNPAET 225
Cdd:cd02768 140 ---NTSIAEIEEADAVLLIGSNLRKE 162
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
48-140 |
6.30e-06 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 49.69 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 48 SSCTvNCGSRCLLRLHVKDDTVYWVESDTTGD-DVYGNhqvraCLRGRSIRRRMNHPDRLKYPMKRVGkrgeGKFERISW 126
Cdd:cd02771 2 SICH-HCSVGCNISLGERYGELRRVENRYNGAvNHYFL-----CDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSW 71
|
90
....*....|....
gi 1447699558 127 DEALDTISDNLRRI 140
Cdd:cd02771 72 NEALDVAAARLKEA 85
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
100-152 |
3.26e-05 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 46.96 E-value: 3.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1447699558 100 MNHPDRLKYPMKRVGkrgeGKFERISWDEALDTISDNLRRILKDYGNEAVHVL 152
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
707-755 |
8.50e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 42.92 E-value: 8.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1447699558 707 WINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 755
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW 82
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
706-787 |
1.65e-04 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 41.64 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699558 706 VWINPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAWlkADMFGDRVDHGGSiniltshrpSPLAKG 785
Cdd:cd02789 33 CEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW--ANVVVDPYTDSTG---------SPIFKG 101
|
..
gi 1447699558 786 NP 787
Cdd:cd02789 102 VP 103
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
708-755 |
3.56e-03 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 37.82 E-value: 3.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1447699558 708 INPIDAQARGIRHGDTVRVFNNNGEMLIAAKVTPRILPGVTAIGQGAW 755
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
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| |
